|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
18-122 |
2.44e-76 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 248.86 E-value: 2.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 18 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 97
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 2462619853 98 RNDDIADGNPKLTLGLIWTIILHFQ 122
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
15-133 |
1.77e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 241.47 E-value: 1.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 15 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 94
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462619853 95 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 133
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
6-131 |
4.46e-72 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 237.58 E-value: 4.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 6 GRGTLRSGEDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALD 85
Cdd:cd21236 3 YENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALD 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462619853 86 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 131
Cdd:cd21236 83 YLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
135-240 |
1.04e-71 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 235.69 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 135 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 2462619853 215 PEDVDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
136-240 |
2.92e-66 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 219.96 E-value: 2.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 215
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 2462619853 216 EDVDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
15-132 |
2.20e-63 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 212.59 E-value: 2.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 15 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 94
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462619853 95 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 132
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
136-240 |
2.99e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.43 E-value: 2.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 215
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 2462619853 216 EDVDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
134-240 |
1.78e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 177.93 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 134 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 213
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 2462619853 214 DPEDVDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
20-123 |
1.19e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 175.65 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 20 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 98
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 2462619853 99 NDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
7-119 |
1.01e-47 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 167.54 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 7 RGTLRSGEDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALD 85
Cdd:cd21246 3 RSRIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQ 82
|
90 100 110
....*....|....*....|....*....|....
gi 2462619853 86 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 119
Cdd:cd21246 83 FLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
136-236 |
9.01e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 161.43 E-value: 9.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 215
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 2462619853 216 EDVDVPQPDEKSIITYVSSLY 236
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
14-236 |
4.05e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.90 E-value: 4.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 14 EDERDRVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHR 90
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 91 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRL 169
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 170 FNAIIHRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 236
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
7-119 |
1.54e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 158.23 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 7 RGTLRSGEDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALD 85
Cdd:cd21193 3 KGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALA 82
|
90 100 110
....*....|....*....|....*....|....
gi 2462619853 86 YLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 119
Cdd:cd21193 83 FL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
16-123 |
2.40e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.54 E-value: 2.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 16 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 91
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 2462619853 92 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
136-236 |
6.14e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 6.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 215
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2462619853 216 EDVDVPQPDEKSIITYVSSLY 236
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
16-123 |
9.31e-44 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 156.19 E-value: 9.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 16 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 88
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2462619853 89 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
135-240 |
3.95e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 148.24 E-value: 3.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 135 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 2462619853 215 PEDVDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
123-238 |
7.12e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 147.89 E-value: 7.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 123 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 202
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 203 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1291-1870 |
5.15e-40 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 163.95 E-value: 5.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1291 QEYVDLRTHYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---LAEAHAQAKAQAERE 1366
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1367 AKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG 1446
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1447 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAE 1526
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1527 RRLR--QAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQeehvavAQLREEAERRAQQQAEAERAREEA 1604
Cdd:COG1196 449 EEEAelEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE------AEADYEGFLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1605 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1684
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1685 RLAAEQELIRLRAETEQGEqqrqLLEEELARLQREAAAATQKRqeLEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1764
Cdd:COG1196 603 LVASDLREADARYYVLGDT----LLGRTLVAARLEAALRRAVT--LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1765 RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1844
Cdd:COG1196 677 AEAELE----ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
570 580
....*....|....*....|....*.
gi 2462619853 1845 RLAEDEAFQRRRLEEQAAQHKADIEE 1870
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
15-119 |
5.67e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 146.32 E-value: 5.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 15 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 93
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 2462619853 94 LVNIRNDDIADGNPKLTLGLIWTIIL 119
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
7-119 |
7.43e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 145.58 E-value: 7.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 7 RGTLRSGEDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALD 85
Cdd:cd21317 18 RSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQ 97
|
90 100 110
....*....|....*....|....*....|....
gi 2462619853 86 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 119
Cdd:cd21317 98 FLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
18-119 |
1.07e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 141.37 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 18 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 96
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 2462619853 97 IRNDDIADGNPKLTLGLIWTIIL 119
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
16-123 |
1.41e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 141.12 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 16 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 93
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 2462619853 94 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
132-236 |
1.82e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.91 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 132 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 211
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 2462619853 212 LLDPEDVDVPQPDEKSIITYVSSLY 236
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
20-121 |
1.88e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 20 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 97
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 2462619853 98 RNDDIADGNPKLTLGLIWTIILHF 121
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
132-236 |
6.68e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.42 E-value: 6.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 132 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 211
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 2462619853 212 LLDPEDVDVPQPDEKSIITYVSSLY 236
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1328-1950 |
1.56e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 155.87 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1328 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAKELQQRMQEevvRREEAAVdaqQQKRSIQEELQQLrqss 1406
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELKEELKE---LEAELLL---LKLRELEAELEEL---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1407 EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1486
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1487 KRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALEtaQRSAEAELQSKRASFAEKT 1566
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1567 AQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEA 1646
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1647 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQREAAAA 1723
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1724 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAkRQRQLAEEDAAR 1803
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL-LGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1804 QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSEL 1883
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1884 ERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSnaEDTLRsKEQAELEAARQR 1950
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD--LEELE-RELERLEREIEA 778
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
135-236 |
3.52e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 137.30 E-value: 3.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 135 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 2462619853 215 PEDVDVPQPDEKSIITYVSSLY 236
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1658-2226 |
5.01e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 154.32 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1737
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEE---DAARQRAEAERVLAE 1814
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1815 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKgLVEDTL 1894
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1895 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE 1974
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1975 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2049
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2050 QSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQA 2129
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2130 EQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFS 2209
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 2462619853 2210 VRVQMEELSKLKARIEA 2226
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
15-123 |
9.85e-37 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 135.82 E-value: 9.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 15 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 93
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 2462619853 94 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1418-2026 |
2.62e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.01 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1418 EAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASR 1497
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1498 VKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEH 1577
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1578 VAVAQLreeaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE 1657
Cdd:COG1196 341 ELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1737
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLAskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL--AEEAKRQRQLAEEDAARQRAEAERVLAEK 1815
Cdd:COG1196 490 AARLLLLLE--AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1816 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLR 1895
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1896 QRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEE 1975
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 1976 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2026
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1455-2090 |
5.43e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 150.86 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1455 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQRKRqaevelasrVKAEAEAAREKQRALQALEE-------LRLQAEE 1524
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKEleaelllLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1525 AERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEA 1604
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1605 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1684
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELEELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1685 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1764
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1765 RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAiGEATRLKTEAEIALKEKEAENERLR 1844
Cdd:COG1196 468 LLEEAA----LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA-GLRGLAGAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1845 RLAEDEAFQRRRLEEQAAQhkadIEERLAQLRkasdseLERQKGLVEDTLRQRRQVEEEILALKASFekAAAGKAELELE 1924
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAA----AIEYLKAAK------AGRATFLPLDKIRARAALAAALARGAIGA--AVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1925 LGRIRSNAEDTL--RSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2002
Cdd:COG1196 611 ADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2003 ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAA 2082
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
....*...
gi 2462619853 2083 QSRRQVEE 2090
Cdd:COG1196 771 RLEREIEA 778
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
139-240 |
1.18e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 132.55 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 139 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 217
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2462619853 218 VDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1316-2028 |
2.64e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.91 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1395
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1396 Q----EELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEATERQRGGAEGELQALRA--RAEEAEAQKRQA 1469
Cdd:PTZ00121 1192 ElrkaEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeEARMAHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1470 QEEAERLRRQVQ-DESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQ 1548
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK-KKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1549 rsAEAELQSKRASFAEKTAQLERSLQEEHvavaqlreeaerraqqqaeaerareeaerelerwQLKANEAlrlRLQAEEV 1628
Cdd:PTZ00121 1350 --AEAEAAADEAEAAEEKAEAAEKKKEEA----------------------------------KKKADAA---KKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1629 AQQKSLAQaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQ 1707
Cdd:PTZ00121 1391 KKADEAKK------------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1708 LLEEelarlQREAAAATQKRQEL-EAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEaEAGRFRELAEEAARLRAl 1786
Cdd:PTZ00121 1452 KAEE-----AKKAEEAKKKAEEAkKADEAKKKAE-------EAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK- 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1787 AEEAKRQRQLAEEDAARQRAEA----ERVLAEKLAAIGEATRL--KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1860
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAkkaeEKKKADELKKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1861 AAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRrqveEEILALKASFEKAAAGKAELELELGRIRS-----NAEDT 1935
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1936 LRSKEQA--ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQES 2009
Cdd:PTZ00121 1674 KKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDE 1753
|
730
....*....|....*....
gi 2462619853 2010 ARQLQLAQEAAQKRLQAEE 2028
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEE 1772
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
120-236 |
4.90e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 131.71 E-value: 4.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 120 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQA 199
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 200 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 236
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
19-124 |
8.12e-34 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 127.95 E-value: 8.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 19 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 95
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHFQIS 124
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1682-2314 |
1.15e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.54 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1682 AQQRL-AAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAAtQKRQELEAELAKVRAEMEVLLASKARAEEEsrstse 1760
Cdd:COG1196 177 AERKLeATEENLERLEDILGE-------LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELE------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1761 kskqrleaeagrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1840
Cdd:COG1196 243 --------------ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1841 ERLRRLAEDEA---FQRRRLEEQAAQHKADIEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAG 1917
Cdd:COG1196 309 ERRRELEERLEeleEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1918 KAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE 1997
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1998 ARRLRERAEQESARQLQLAQEAAQKR---LQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEAR 2074
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLlllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2075 VQA---------------EREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQA 2139
Cdd:COG1196 548 LQNivveddevaaaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2140 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSK 2219
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2220 LKARIEAENRALILRDKDNTQRFLQEEAEKMKQvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK----MQA 2295
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnLLA 786
|
650
....*....|....*....
gi 2462619853 2296 VQEATRLKAEAELLQQQKE 2314
Cdd:COG1196 787 IEEYEELEERYDFLSEQRE 805
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
20-123 |
6.74e-33 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 124.71 E-value: 6.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 20 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 97
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 2462619853 98 RNDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
7-119 |
1.52e-32 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 125.54 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 7 RGTLRSGEDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALD 85
Cdd:cd21316 40 RSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQ 119
|
90 100 110
....*....|....*....|....*....|....
gi 2462619853 86 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 119
Cdd:cd21316 120 FLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
135-233 |
1.55e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.69 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 135 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 2462619853 215 PEDVDVPQPDEKSIITYVS 233
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
20-123 |
1.71e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 123.58 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 20 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 98
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 2462619853 99 NDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
136-236 |
1.86e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 123.67 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 215
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2462619853 216 EDVDVPQPDEKSIITYVSSLY 236
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
123-238 |
3.28e-31 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 120.33 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 123 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 202
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 203 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 238
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
139-240 |
5.22e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 119.29 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 139 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 217
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2462619853 218 VDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
139-241 |
1.45e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.49 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 139 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 216
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 2462619853 217 DVDVPQPDEKSIITYVSSLYDAMPR 241
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
135-233 |
1.81e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 135 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 2462619853 215 PEDVDVPQPDEKSIITYVS 233
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
16-125 |
2.07e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 118.07 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 16 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 91
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 2462619853 92 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 125
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
141-236 |
4.13e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 116.68 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 141 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 219
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 2462619853 220 VPQPDEKSIITYVSSLY 236
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
19-121 |
5.47e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 116.43 E-value: 5.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 19 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHF 121
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
871-948 |
1.39e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 114.24 E-value: 1.39e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 871 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 948
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
121-238 |
5.15e-29 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 114.41 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 121 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAF 200
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462619853 201 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1654-2437 |
6.08e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 129.11 E-value: 6.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1654 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1733
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEE--ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1734 LAKvRAEmevllasKARAEEESRSTSEKSKqrleaeagrfrelAEEAARlralAEEAKRQRQLAEEDAARQRAEAERvlA 1813
Cdd:PTZ00121 1174 DAK-KAE-------AARKAEEVRKAEELRK-------------AEDARK----AEAARKAEEERKAEEARKAEDAKK--A 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1814 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRleeqaAQHKADIEERLAQLRKASdselERQKGLVEDT 1893
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ-----AAIKAEEARKADELKKAE----EKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1894 LRQRRQVEEeilalkasfekaAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAA 1973
Cdd:PTZ00121 1298 AEEKKKADE------------AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1974 EEEAARQRKAALEEVERLKAKVEEARR---LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2050
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2051 SvlDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQsaeeqaqaraqaqaaaekLRKEAEQEAARRAQAE 2130
Cdd:PTZ00121 1446 A--DEAK--KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE------------------AKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2131 QAALRQKQAADAEMEKHKKFAEQTlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQrlKAEATEAARQRSQVEEELFSV 2210
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2211 RVQMEELSKL-KARIEAENRALILRDKDNTQRFLQEEAEKMKqvAEEAARlsvaAQEAARLRQLAEEDLAQQRALAEKML 2289
Cdd:PTZ00121 1580 LRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2290 KEKMQAVQEATRLKAEAEllqQQKELAQEqARRLQEDKEQMAQQLAEETQgfqrtlEAERQRQLEMSAEAERLKlrVAEM 2369
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAE---EDKKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK--AEEL 1721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 2370 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvTLVQTLEIQRQQSDHDAERLREAIAELEREKE 2437
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1291-2004 |
2.34e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 126.71 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1291 QEYVDLRTHYSELT-TLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqAKAQAEREAKE 1369
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1370 LQQRMQEEVVRREeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1449
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1450 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1529
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1530 RQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL- 1608
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1609 ---------------ERWQLKANEALRLRLQA----------EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1663
Cdd:TIGR02168 518 lsgilgvlselisvdEGYEAAIEAALGGRLQAvvvenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1664 RELA------------------------------EQELEKQRQL-----------------------AEGTAQQRLAAEQ 1690
Cdd:TIGR02168 598 EGFLgvakdlvkfdpklrkalsyllggvlvvddlDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1691 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRL 1766
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1767 EAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAeialKEKEAENERLRRL 1846
Cdd:TIGR02168 758 ELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1847 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAGKAELELELG 1926
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1927 RIRSNAE--DTLRSKEQAELEAARQR------QLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK----AK 1994
Cdd:TIGR02168 912 ELRRELEelREKLAQLELRLEGLEVRidnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAA 991
|
810
....*....|
gi 2462619853 1995 VEEARRLRER 2004
Cdd:TIGR02168 992 IEEYEELKER 1001
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
139-238 |
3.18e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.22 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 139 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 217
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 2462619853 218 VDVPQPDEKSIITYVSSLYDA 238
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1515-2145 |
4.28e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1515 LEELRLQAEEAERRLRQAEVERARQVQVALeTAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLreeaerraqqq 1594
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAEL----------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1595 aeaerareeaerelerwqlkanEALRLRLQAEEvaqqkslaqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQ 1674
Cdd:COG1196 270 ----------------------EELRLELEELE---------------------------LELEEAQAEEYELLAELARL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1675 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevLLASKARAEEE 1754
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1755 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1834
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1835 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKA 1914
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1915 AAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK 1994
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1995 VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEAR 2074
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 2075 VQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEME 2145
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1083-1793 |
7.31e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.66 E-value: 7.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1083 RAHEEQLKEAQAVpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLl 1162
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1163 erwqavlaqtdvrQRELEQLGRQLRYYRESadplgawLQDARRRQEQIQAmpladsqavreqlrQEQALLEEIERHGEKV 1242
Cdd:COG1196 294 -------------LAELARLEQDIARLEER-------RRELEERLEELEE--------------ELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1243 EECQrfakqyinaikdyelqlvtykaqlepvaspakkpkvqsgsesviqeyvdlrthyselttltsqyikfisETLRRME 1322
Cdd:COG1196 340 EELE---------------------------------------------------------------------EELEEAE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1323 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRREEAAVDAQQQKRSIQEELQQL 1402
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1403 RQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRrqvQD 1482
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE---GF 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1483 ESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1562
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1563 AEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA----NEALRLRLQAEEVAQQKSLAQAE 1638
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGS 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1639 AEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR 1718
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1719 EAAAATQ-------KRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLralaEEAK 1791
Cdd:COG1196 747 LLEEEALeelpeppDLEELERELERLEREIEALGPVNLLAIEE-----------YEELEERYDFLSEQREDL----EEAR 811
|
..
gi 2462619853 1792 RQ 1793
Cdd:COG1196 812 ET 813
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1328-2390 |
1.50e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 124.17 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1328 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAE--REAKELQQRMQEEVVRREEAaVDAQQQKRSIQEELQQLRQ 1404
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAElhTEAVQRRQQLDQELAERRQT-VESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1405 SSEA-----EIQAKARQAEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERLRRQ 1479
Cdd:NF041483 162 ESQArrlldESRAEAEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1480 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQaeEAERRLRQAEVERARQVQVALETAqrsaeaelqSKR 1559
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA---------AKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1560 ASFAEKT-AQLERSLQEEhvaVAQL-REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQA 1637
Cdd:NF041483 296 LASAESAnEQRTRTAKEE---IARLvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1638 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQGEQQRQLLEEELARL 1716
Cdd:NF041483 373 AEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1717 QREAAAATQK-----RQELEAELAKVRAEMEVLLAsKARAE-EESRSTSEKSKQRLEAEAGR----FRELAE-------- 1778
Cdd:NF041483 453 RAEAVAEGERirgeaRREAVQQIEEAARTAEELLT-KAKADaDELRSTATAESERVRTEAIErattLRRQAEetlertra 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1779 EAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLAEKLA-AIGEATRLKTEAE-------IALKEKEAENERLRRLAED 1849
Cdd:NF041483 532 EAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEALADARAEAERIRREAAE 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1850 EAfqrRRLEEQAAqhkadieERLAQLRKASDSELERQKGLVEDTLRQRRqVEEEILALKASFEKAAagkaelelELGRIR 1929
Cdd:NF041483 612 ET---ERLRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAAR-AEGENVAVRLRSEAAA--------EAERLK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1930 SNAEDTlRSKEQAELEAARQRqlaaeeerrrrEAEERVQKSLAAEEEAARQRKaalEEVERLKAKVEEARRLRERAEQES 2009
Cdd:NF041483 673 SEAQES-ADRVRAEAAAAAER-----------VGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERERAREQS 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2010 ARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEaarraaeeaeearvQAEREAAQSRRQVE 2089
Cdd:NF041483 738 EELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQE--------------QAEEEIAGLRSAAE 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2090 EAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEaarraqaeqaalRQKQAADAEMEKHKKFAEQTLRQkAQVEQElttlR 2169
Cdd:NF041483 804 HAAERTRTEAQEEADRVRSDAYAERERASEDAN------------RLRREAQEETEAAKALAERTVSE-AIAEAE----R 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2170 LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR----VQMEELSKLKARIEAENRALILRDKDNTQRFLQE 2245
Cdd:NF041483 867 LRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARA 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2246 EAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavqEATRLKAEAELLQQQKELAQEQARRL 2323
Cdd:NF041483 947 EAERVRADAAAQAEqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEA-----ERVKAEAAAEAERLRTEAREEADRTL 1021
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 2324 QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQrfRKQAEEI 2390
Cdd:NF041483 1022 DEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAA--RKEAERI 1086
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
19-121 |
2.17e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 109.11 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 19 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHF 121
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
123-238 |
2.61e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 109.40 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 123 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 202
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 203 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1699-2583 |
3.28e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1699 TEQGEQQRQLLEEELARLQREAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1776
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1777 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAIGEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 1854
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1855 RRLEEQaaqHKADIEERLAQLRKASDSelerqkglvedtlrqrRQVEEeilalkasfekaaAGKAELELELGRIRsNAED 1934
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1935 TLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2014
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2015 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTlqqeqsvldqlrgeaeaarraaeeaeearVQAEREAAQSRRQVEEAERL 2094
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKK-----------------------------ADAAKKKAEEAKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2095 KQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2174
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2175 TDHQknlldEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARiEAENRALILRDKDNtqrfLQEEAEKMKQVA 2254
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADE----AKKKAEEAKKKA 1499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2255 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeQM 2330
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NM 1578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2331 AQQLAEETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtlvqt 2410
Cdd:PTZ00121 1579 ALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK----- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2411 leiqrqqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLlqetqalqqsflsEKDSLLQRErfiEQEK 2490
Cdd:PTZ00121 1647 ---------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-------------KAAEALKKE---AEEA 1701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2491 AKLEQL---FQDEVAKAQqlreEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEE 2567
Cdd:PTZ00121 1702 KKAEELkkkEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
890
....*....|....*.
gi 2462619853 2568 NQRLREQLQLLEEQHR 2583
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRR 1793
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1-123 |
4.35e-27 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 109.08 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1 MSGLEGRGTLRSGEDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKL 77
Cdd:cd21247 1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462619853 78 QNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21247 81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
19-124 |
1.18e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.81 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 19 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHFQIS 124
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
123-238 |
1.46e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.50 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 123 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 202
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 203 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1376-2093 |
2.72e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 120.25 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1376 EEVVrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL 1455
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1456 RARAEEaEAQKRQAQEEAERLRRqvqdeSQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQ-AEEAERRLRQAEV 1534
Cdd:PTZ00121 1108 TGKAEE-ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1535 ERARQVQVALETaqRSAEaelQSKRASFAEKtAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1614
Cdd:PTZ00121 1182 RKAEEVRKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1615 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1694
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1695 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE-----AE 1769
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkaAA 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1770 AGRFRELAEEAARLRALAEEAKRQRQLAEE-DAARQRAEAERVlAEKLAAIGEATRLKTEAEIALKEKEAENErLRRLAE 1848
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADE-AKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1849 DEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGRI 1928
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKKA 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1929 RSNAEDTLRSKEQA-ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE--EVERLKAKVEE----ARRL 2001
Cdd:PTZ00121 1573 EEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkKVEQLKKKEAEekkkAEEL 1652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2002 RERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREA 2081
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
730
....*....|..
gi 2462619853 2082 AQSRRQVEEAER 2093
Cdd:PTZ00121 1733 EEAKKEAEEDKK 1744
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1461-2443 |
6.29e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 118.77 E-value: 6.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1461 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEVELASRVKAE--AEAAREKQRALQALEELRLQAE-EAERRLR 1530
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1531 QAEVERARQVQVA---LETAQRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeAERAREEAERE 1607
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE--------------------AESARAEAEAI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1608 LERWQLKANEALR-LRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrl 1686
Cdd:NF041483 213 LRRARKDAERLLNaASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAE-- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1687 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKS 1762
Cdd:NF041483 288 AKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1763 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVlAEKLAAIG----------------EATRLK 1826
Cdd:NF041483 368 KAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ-AEQLKGAAkddtkeyraktvelqeEARRLR 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1827 TEAEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIE------------------ERLAQLRKASDSEL 1883
Cdd:NF041483 447 GEAEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADelrstataeservrteaiERATTLRRQAEETL 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1884 ERQKGLVEdtlRQRRQVEEEILALKASFEKAA------------AGKAELELELGRIRSNAEDTLRSKEQAELEaarqrq 1951
Cdd:NF041483 527 ERTRAEAE---RLRAEAEEQAEEVRAAAERAArelreeteraiaARQAEAAEELTRLHTEAEERLTAAEEALAD------ 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1952 laaeeerrrreaeervqkslaAEEEAARQRKAALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEKA 2030
Cdd:NF041483 598 ---------------------ARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAEG 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2031 HAFAVQQKEQELQQTLQQEQSVLDqlrgeaeaarraaeeaEEARVQAEREAAQSRRQVEEAERLKQSAEEQAqaraqaqa 2110
Cdd:NF041483 654 ENVAVRLRSEAAAEAERLKSEAQE----------------SADRVRAEAAAAAERVGTEAAEALAAAQEEAA-------- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2111 aaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAEQTL-RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRL 2189
Cdd:NF041483 710 ------------------------RRRREAEETLGSARAEADQEReRAREQSEELLASARKRVEEAQAEAQRLVEEADRR 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2190 KAEATEAARQRSQ-VEEELFSVRVQM-EELSKLkaRIEAENRAlilrdkDNTQRFLQEEAEKMKqvAEEAARLSVAAQEA 2267
Cdd:NF041483 766 ATELVSAAEQTAQqVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDA 835
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2268 ARLRQLAEEDLAQQRALAEKMLKEkmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA 2347
Cdd:NF041483 836 NRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAA 912
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2348 ERQRQL--EMSAEAERLKLRV-AEMSRAQARAEEDAQRFRKQAEEIGEKL--HRTELATQEKVTLVQTLEIQRQQSDH-- 2420
Cdd:NF041483 913 AQADRLigEATSEAERLTAEArAEAERLRDEARAEAERVRADAAAQAEQLiaEATGEAERLRAEAAETVGSAQQHAERir 992
|
1050 1060
....*....|....*....|....*
gi 2462619853 2421 -DAERLR-EAIAELEREKEKLQQEA 2443
Cdd:NF041483 993 tEAERVKaEAAAEAERLRTEAREEA 1017
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
23-120 |
2.18e-25 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 103.16 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 23 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 98
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 2462619853 99 NDDIADGnPKLTLGLIWTIILH 120
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
141-236 |
2.69e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.00 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 141 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 219
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 2462619853 220 VPQPDEKSIITYVSSLY 236
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
123-238 |
3.68e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 103.23 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 123 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 202
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 203 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1078-1831 |
4.65e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 116.01 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHE-EQLKEAQAVPATLPELEATKASLKKlRAQ----AEAQQPTFDALR-DELRGAQEVGERLQQRHGERDVEV 1151
Cdd:PTZ00121 1136 AEDARKAEEaRKAEDAKRVEIARKAEDARKAEEAR-KAEdakkAEAARKAEEVRKaEELRKAEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1152 ERWR----ERVAQLLERWQAVLAQTD-VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVR--EQ 1224
Cdd:PTZ00121 1215 EEARkaedAKKAEAVKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDE 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1225 LR--QEQALLEEIERHGEKVEECQRFAKQYINAIKDYELqlVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTHYSE 1302
Cdd:PTZ00121 1295 AKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEA-----EAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1303 LTTLTSQYIKFISETLRRMEEEERLAEQ--QRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAKELQQRmQEEVVR 1380
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKK-AEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1381 REEAAVDAQQQKRSiqEELQQlrqsseaeiqaKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGElQALRARAE 1460
Cdd:PTZ00121 1446 ADEAKKKAEEAKKA--EEAKK-----------KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKK 1511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1461 EAEAQKRQAQEEAERLRRqvqdeSQRKRQAEvelasrvkaEAEAAREKQRAlqalEELRlQAEEAERRLRQAEVERARQV 1540
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKK-----AEEAKKAD---------EAKKAEEKKKA----DELK-KAEELKKAEEKKKAEEAKKA 1572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1541 QVALETAQRSAE--AELQSKRASFAEKTAQLERSLQEEHVAvaqlreeaerraqqqaeaerareeaerelerwqlKANEA 1618
Cdd:PTZ00121 1573 EEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAK----------------------------------KAEEA 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1619 lrlRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRElaeqELEKQRQLAEGTAQQRLAAEQELIRLRAE 1698
Cdd:PTZ00121 1619 ---KIKAEELKKAEEEKKKVEQLK------------KKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1699 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakVRAEMEVllaskARAEEESRSTSEKSKQRLEAEAGRFRELAE 1778
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE---KKKAEEL-----KKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1779 EAARLRALAEEAKRQRQLAEEdaarQRAEAERVLAEKLAAIGEATRLKTEAEI 1831
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
135-241 |
1.25e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.21 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 135 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 211
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 2462619853 212 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 241
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1658-2496 |
1.90e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.61 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1737
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1817
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1818 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrRLEEQAAQHKADIEERLAQLrkaSDSELERQKGLVEDTLRQR 1897
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1898 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdtlrsKEQAELEAARQRQLaaeeerrrreaeervqkSLAAEEEA 1977
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1978 ARQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQ 2037
Cdd:TIGR02168 487 LQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2038 KEQELQQTLQQEQSVLDQ-LRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEE-------AERLKQSAEEQAQARAQAQ 2109
Cdd:TIGR02168 567 QNELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2110 AAAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRL 2189
Cdd:TIGR02168 647 IVTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2190 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEnralilrdkdntqrfLQEEAEKMKQVAEEAARLSVAAQEAAR 2269
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2270 LRQLAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleae 2348
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2349 rqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA 2428
Cdd:TIGR02168 849 -----ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 2429 IAELEREKEKLQQEAKLLQlkseemQTVQQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2496
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
139-239 |
2.01e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 100.62 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 139 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 218
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 2462619853 219 DVPQPDEKSIITYVSSLYDAM 239
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
20-123 |
2.20e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 20 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 95
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1380-2225 |
2.51e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.23 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1380 RREEAavdaQQQKRSIQEELQQL---RQSSEAEIQAKARQAEAAERSRlRIEEEIRvvrlqleaterqrggaEGELQALR 1456
Cdd:TIGR02168 173 RRKET----ERKLERTRENLDRLediLNELERQLKSLERQAEKAERYK-ELKAELR----------------ELELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1457 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLR--QAEV 1534
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1535 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLErSLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLK 1614
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELE-----------------------ELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1615 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIR 1694
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1695 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGR 1772
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1773 FRELAEEAARLRALAEEAKRQR--QLAEEDAARQRAEAErvlAEKLAAIGEATRLkteAEIALKEKEAENERLRRLAEDE 1850
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGRlqAVVVENLNAAKKAIA---FLKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1851 AFQR--RRLEEQAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILALKASFEKAAAG----KAELELE 1924
Cdd:TIGR02168 599 GFLGvaKDLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1925 LGRI-RSNAEDTLRSK-EQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2002
Cdd:TIGR02168 670 SSILeRRREIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2003 ERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAA 2082
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2083 QSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVE 2162
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 2163 QELTTLRLQLEETDHQKNLLDEELQRLKAEA---TEAARQRSQVEEELFSVRVQMEELSKLKARIE 2225
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIdnlQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1832-2496 |
3.75e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1832 ALKEKEAENERLRRLaEDEAF----QRRRLEEQAAQ------HKADIEERLAQLRKASDSELERQKGLVEdtlRQRRQVE 1901
Cdd:COG1196 177 AERKLEATEENLERL-EDILGelerQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELE---AELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1902 EEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 1981
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1982 KAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQkeqelqqtlqqeqsvldqlrgeae 2061
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL------------------------ 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2062 aarraaeeaeearVQAEREAAQSRRQVEEAERLKQSAeeqaqaraqaqaaaeklrkeaeqeaarraqaeqaaLRQKQAAD 2141
Cdd:COG1196 389 -------------LEALRAAAELAAQLEELEEAEEAL-----------------------------------LERLERLE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2142 AEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2221
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2222 ARIEAENRA-LILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2300
Cdd:COG1196 501 ADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2301 RLKAEAELLQQQKELAQEQARRL----QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARA 2376
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2377 EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTV 2456
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2462619853 2457 QQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2496
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERE-LERLEREIEAL 779
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
137-236 |
4.89e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.56 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 137 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 216
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 2462619853 217 D-VDVPQPDEKSIITYVSSLY 236
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1078-1878 |
3.56e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.38 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1157
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1158 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1237
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1238 hgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQyikfISET 1317
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1318 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-------------------EAKE--LQQRMQE 1376
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegyeAAIEaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1377 EVVRREEAAVDAQQ---QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQ 1453
Cdd:TIGR02168 550 VVVENLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKLRKALSYLLG 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1454 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevelASRVKAEAEAAREKQRalQALEELRLQAEEAERRLR--Q 1531
Cdd:TIGR02168 624 GVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSSILERR--REIEELEEKIEELEEKIAelE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1532 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEehvaVAQLREEAERRAQQQAEAERAREEAERELERW 1611
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1612 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1691
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1692 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEA 1768
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEG 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1769 EAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIGEATRLkteaeiALKEKEAENERLRRLa 1847
Cdd:TIGR02168 934 LEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL- 1005
|
810 820 830
....*....|....*....|....*....|.
gi 2462619853 1848 edeafqrrrleeqaAQHKADIEERLAQLRKA 1878
Cdd:TIGR02168 1006 --------------TAQKEDLTEAKETLEEA 1022
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
136-240 |
3.56e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.17 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 215
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 2462619853 216 EDVDVPQPDEKSIITYVSSLYDAMP 240
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
136-236 |
3.89e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 96.73 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 215
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 2462619853 216 EDVDVPQ-PDEKSIITYVSSLY 236
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
136-234 |
4.14e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 93.84 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 2462619853 215 PEDVDVPQPDEKSIITYVSS 234
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
993-1561 |
4.29e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 993 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1072
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1073 RGTQGAEEVLRAHEEQLKEAQAvpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVE 1152
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1153 RWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAmpladsqAVREQLRQEQALL 1232
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1233 EEIERHGEKVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLtsqyik 1312
Cdd:COG1196 470 EEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1313 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvrreEAAVDAQQQK 1392
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI----GAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1393 RSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1472
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1473 AERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALE--TAQRS 1550
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdlEELER 767
|
570
....*....|.
gi 2462619853 1551 AEAELQSKRAS 1561
Cdd:COG1196 768 ELERLEREIEA 778
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
19-124 |
4.89e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.77 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 19 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHFQIS 124
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
19-124 |
5.01e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.76 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 19 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHFQIS 124
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
770-836 |
6.22e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.94 E-value: 6.22e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 770 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 836
Cdd:pfam17902 1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2053-2665 |
1.01e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2053 LDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERlkqsaeeqaqaraQAQAAAEKLRKEAEQEAARRAQAEQA 2132
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-------------AELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2133 ALRQKQAADAEMEKHKKFAEQtlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRV 2212
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2213 QMEELsklkARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2292
Cdd:COG1196 366 ALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2293 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtLEAERQRQLEMSAEAERLklrvaemsRA 2372
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLLEAEADYEGF--------LE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2373 QARAEEDAQRFRKQAEEIGEKLHRTELAtqEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2452
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAY--EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2453 MQTVQQEQLLQETQALQQSFLSEKDSLLQReRFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 2532
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYY-VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2533 RRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATK------TLPNG 2606
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEReelleeLLEEE 745
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 2607 RDALDGPAAEAEPEHSFDGLRRKVSA--QRLQEAG---ILSAEELQRLAQGHTTVDElaRREDV 2665
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERleREIEALGpvnLLAIEEYEELEERYDFLSE--QREDL 807
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1080-2363 |
1.19e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.44 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1080 EVLRAheeQLKEAQAVPATLPELEAT----KASLKKLRAQAEAQQPTFDALRdELRGAQEVGERLQQRHGERDVeverwr 1155
Cdd:NF041483 46 EVLRA---KLHEARRSLASRPAYDGAdigyQAEQLLRNAQIQADQLRADAER-ELRDARAQTQRILQEHAEHQA------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1156 ervaqlleRWQAVLAQTDV--RQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQ----LRQEQ 1229
Cdd:NF041483 116 --------RLQAELHTEAVqrRQQLDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQalaaARAEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1230 ALLEEIERH--GEKVEECQRFAKQYI-NAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTHYSELTTL 1306
Cdd:NF041483 188 ERLAEEARQrlGSEAESARAEAEAILrRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESD-----QARRQAAELSRA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1307 TSQyikfisetlrRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqAKAQAEREAKELQQRMQEEVVRREEAav 1386
Cdd:NF041483 263 AEQ----------RMQEAEEALREARAEAEKVVAEAKEAAAKQLASAES---ANEQRTRTAKEEIARLVGEATKEAEA-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1387 daqqqkrsIQEELQQLRQSSEAEiqAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQK 1466
Cdd:NF041483 328 --------LKAEAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1467 RQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRA--LQALEELRLQAEEAE--RRLRQAEVER----AR 1538
Cdd:NF041483 389 RAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAktVELQEEARRLRGEAEqlRAEAVAEGERirgeAR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1539 QVQVA-LETAQRSAEAELQSKRASFAE----KTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQl 1613
Cdd:NF041483 469 REAVQqIEEAARTAEELLTKAKADADElrstATAESERVRTEAIERATTLRRQAEET-----------------LERTR- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1614 kaNEALRLRLQAEEVAQqkslAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAegTAQQRLA-AEQEL 1692
Cdd:NF041483 531 --AEAERLRAEAEEQAE----EVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLT--AAEEALAdARAEA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1693 IRLRAET-EQGEQQRQLLEEELARLQREAAAATQK-RQELEAELAKVRAEME---VLLASKARAE-EESRSTSEKSKQRL 1766
Cdd:NF041483 603 ERIRREAaEETERLRTEAAERIRTLQAQAEQEAERlRTEAAADASAARAEGEnvaVRLRSEAAAEaERLKSEAQESADRV 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1767 EAEAGRFRE-LAEEAAR-LRALAEEAKRQRQLAEE--DAARQRAEAERVLA-----EKLA--------AIGEATRLKTEA 1829
Cdd:NF041483 683 RAEAAAAAErVGTEAAEaLAAAQEEAARRRREAEEtlGSARAEADQERERAreqseELLAsarkrveeAQAEAQRLVEEA 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1830 E------IALKEKEAENER-----LRRLAEDEAFQRRrleeQAAQHKADIEERLAQL---RKASDSELERQKGlVEDTLR 1895
Cdd:NF041483 763 DrratelVSAAEQTAQQVRdsvagLQEQAEEEIAGLR----SAAEHAAERTRTEAQEeadRVRSDAYAERERA-SEDANR 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1896 QRRQVEEEILALKASFEKAAAG--------KAELELELGRIRSNAEDTLRSKEQ--------AELEAARQRQLAAEEERR 1959
Cdd:NF041483 838 LRREAQEETEAAKALAERTVSEaiaeaerlRSDASEYAQRVRTEASDTLASAEQdaartradAREDANRIRSDAAAQADR 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1960 RREAEERVQKSLAAE--EEAARQRKAALEEVERLKAK--------VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2029
Cdd:NF041483 918 LIGEATSEAERLTAEarAEAERLRDEARAEAERVRADaaaqaeqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEAER 997
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2030 AHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQAraqaq 2109
Cdd:NF041483 998 VKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQA----- 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2110 aaaeklrkeaeqeaarraqaeqaalrQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTlrlqleetdhqknlLDEELQRL 2189
Cdd:NF041483 1073 --------------------------DTMVGAARKEAERIVAEATVEGNSLVEKARTD--------------ADELLVGA 1112
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2190 KAEATeAARQRSQveeelfsvrvqmeelsKLKARIEAENRALilrdkdnTQRFLQEEAEKMKQVAEEAARLSVAAQEaar 2269
Cdd:NF041483 1113 RRDAT-AIRERAE----------------ELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE--- 1165
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2270 lrQLAEEDLAQQRALAE---KMLKEKMQAVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLAEETqgfQRTLE 2346
Cdd:NF041483 1166 --QLAEAEAKAKELVSDansEASKVRIAAVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELD 1237
|
1370
....*....|....*..
gi 2462619853 2347 AERQRQLEMSAEAERLK 2363
Cdd:NF041483 1238 VLVRRREDINAEISRVQ 1254
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
140-237 |
3.72e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.56 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 140 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 218
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2462619853 219 DVPQPDEKSIITYVSSLYD 237
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1078-1878 |
4.24e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 99.36 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHE--EQLKEAQAVPATLpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDveverwr 1155
Cdd:TIGR02168 209 AEKAERYKElkAELRELELALLVL-RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1156 ERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQALLEEi 1235
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE-LAELEEKLEELKEELESLEA- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1236 erhgeKVEECQrfakqyiNAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDlrthySELTTLTSQYIKFIS 1315
Cdd:TIGR02168 359 -----ELEELE-------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevVRREEAAvdAQQQKRSI 1395
Cdd:TIGR02168 422 EIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQ--LQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1396 QEELQQLRQSSEAEIQAKArqaeaaerSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALRARAEEAEAQKRQAQE 1471
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLK--------NQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1472 EAERLRR-------------QVQDESQRKRQAEVE--LASRVKAEAEAarekQRALQALEELRLQAEEAERRLRQAEVER 1536
Cdd:TIGR02168 567 QNELGRVtflpldsikgteiQGNDREILKNIEGFLgvAKDLVKFDPKL----RKALSYLLGGVLVVDDLDNALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1537 ARQVQVALET-----------AQRSAEAELQSKRASFAE---KTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERARE 1602
Cdd:TIGR02168 643 PGYRIVTLDGdlvrpggvitgGSAKTNSSILERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1603 EAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTA 1682
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1683 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKS 1762
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1763 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAE--- 1839
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidn 940
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 2462619853 1840 -NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1878
Cdd:TIGR02168 941 lQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
136-236 |
5.17e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 88.17 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 215
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 2462619853 216 EDVDV--PQPDEKSIITYVSSLY 236
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1308-2038 |
7.28e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 98.51 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1308 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVD 1387
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1388 AQQQKRSIQEELQQLRQSSEAEIQA-----KARQAEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAE 1460
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESskqeiEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1461 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQALEELRLQAEEAE-RRLRQAEVERA 1537
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKkKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1538 RQVQVALETAQR-SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1616
Cdd:pfam02463 391 KLKEEELELKSEeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1617 EALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELI 1693
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1694 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG-R 1772
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIlK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1773 FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAF 1852
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1853 QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA 1932
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1933 EDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2012
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740
....*....|....*....|....*....
gi 2462619853 2013 LQLAQE---AAQKRLQAEEKAHAFAVQQK 2038
Cdd:pfam02463 871 ELLLKEeelEEQKLKDELESKEEKEKEEK 899
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1316-1875 |
9.58e-20 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 98.06 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDA 1388
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1389 QQQKRSIQEELQQLRQ-----------SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1446
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1447 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELrLQAEEAE 1526
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1527 RRLRQAeVERA----------------------------RQVQVALETAQRSAEAELQSKRASFAEK--------TAQLE 1570
Cdd:COG4913 474 ERWRGA-IERVlggfaltllvppehyaaalrwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfRAWLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1571 RSLQEE--HVAV---AQLREEA----ERRAQQQAEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKSLAQAEAE 1640
Cdd:COG4913 553 AELGRRfdYVCVdspEELRRHPraitRAGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1641 KQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQ 1717
Cdd:COG4913 633 LEAL----------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1718 REAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1797
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1798 EEDAARQRAEAERVLAE--------------KLAAIGE-ATRLKTEAEIALKEKEAENERLRRLAEDEAFQrrRLEEQAA 1862
Cdd:COG4913 779 RARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVA--DLLSKLR 856
|
650
....*....|...
gi 2462619853 1863 QHKADIEERLAQL 1875
Cdd:COG4913 857 RAIREIKERIDPL 869
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
136-235 |
3.06e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 85.61 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 215
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 2462619853 216 ED-VDVPQPDEKSIITYVSSL 235
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
132-237 |
3.47e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 85.77 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 132 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 211
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 2462619853 212 LLDPEDV-DVPQPDEKSIITYVSSLYD 237
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
139-235 |
4.63e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.06 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 139 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 214
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2462619853 215 PEDVDVPQPDEKSIITYVSSL 235
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
21-121 |
1.20e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 84.17 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 21 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 96
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 2462619853 97 IRNDDIADGNPKLTLGLIWTIILHF 121
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1282-1930 |
1.45e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.95 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1282 VQSGSESVIQEYVDLRTHySELTTLTSQyIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQ 1351
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLH-ERLNGLESE-LAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1352 laeahaqAKAQAEREAKELQQRMQEEVVRREEaavdaqqqkrsIQEELQQLRQSSE---AEIQAKARQAEAAERSRLRIE 1428
Cdd:PRK02224 266 -------TIAETEREREELAEEVRDLRERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1429 EEIRVVRLQLEATERQRGGAEGELQALRARAEEaeaqkrqAQEEAERLRRQVQdesqrkrqaevelasrvkaEAEAAREK 1508
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEE-------LREEAAELESELE-------------------EAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1509 QRAlqALEELRLQAEEAERRLRQAEVERArqvqvalETAQRSaeAELQSKRASFAEKTAQLERSLQEEHVAVAQlreeae 1588
Cdd:PRK02224 382 RRE--EIEELEEEIEELRERFGDAPVDLG-------NAEDFL--EELREERDELREREAELEATLRTARERVEE------ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1589 rraqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAE 1668
Cdd:PRK02224 445 ---------------------------AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1669 qELEKQRqLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1748
Cdd:PRK02224 483 -ELEDLE-EEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1749 ARAEEEsrstSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAIGEatrLKTE 1828
Cdd:PRK02224 561 AEAEEE----AEEAREEVAELNSKLAELKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1829 AEIALKEKeaeNERLRRLAEDeaFQRRRLEE------QAAQHKADIEERLAQLRKASDsELERQKGLVE------DTLRQ 1896
Cdd:PRK02224 625 RRERLAEK---RERKRELEAE--FDEARIEEaredkeRAEEYLEQVEEKLDELREERD-DLQAEIGAVEneleelEELRE 698
|
650 660 670
....*....|....*....|....*....|....*
gi 2462619853 1897 RR-QVEEEILALKASFEKAaagkAELELELGRIRS 1930
Cdd:PRK02224 699 RReALENRVEALEALYDEA----EELESMYGDLRA 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1766-2599 |
1.68e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 94.35 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1766 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLAEKLAAIGEATRlKTEAE 1830
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1831 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILAL 1907
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1908 KASFEKAAAGKAELELELgrirsnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1987
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1988 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEqelqqtlqqeqsvLDQLRGEAEAARR 2065
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-------------LKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2066 AAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQAraqaqaaaeklrkeaeqeaarraqaeqaaLRQKQAADAEME 2145
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-----------------------------LQARLDSLERLQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2146 KHKKFAEQTLRQKAQVEQELTTLR---LQLEETDHQ-----KNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL 2217
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSGLSGILgvlSELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2218 SKLKARIEAENRALILRDKDNTQRFLqeeaekmKQVAEEAARLSVAAQeaARLRQLA-EEDLAQQRALAEKMLKEKMQAV 2296
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNIEGFLGVA-------KDLVKFDPKLRKALS--YLLGGVLvVDDLDNALELAKKLRPGYRIVT 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2297 QEATRL--------------------KAEAELLQQQKELAQEQARRLQ---EDKEQMAQQLAEETQGFQRTLEAERQRQL 2353
Cdd:TIGR02168 650 LDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQIS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2354 EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELE 2433
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2434 REKEKLQQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQR 2513
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEE 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2514 QQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEqhrAALAHSEEVT 2593
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIE 964
|
....*.
gi 2462619853 2594 ASQVAA 2599
Cdd:TIGR02168 965 DDEEEA 970
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
22-119 |
3.66e-18 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 82.77 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 22 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 97
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 2462619853 98 RNDDI-ADGNPKLTLGLIWTIIL 119
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1865-2666 |
8.23e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1865 KADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAEL 1944
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA--KKTETGKAEEARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1945 EAARQrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQEAAQKRl 2024
Cdd:PTZ00121 1137 EDARK------------------------AEEARKAEDAKRVEIAR---KAEDARKAEEARKAEDAKKAEAARKAEEVR- 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2025 QAEEKAHAFAVQQKEQELQQTLQQEqsvLDQLRgeaeaarraaEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQA 2104
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERK---AEEAR----------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2105 RAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ--KQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEETDHQKnll 2182
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKA--- 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2183 dEELQRlKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAenralilrDKDNTQRfLQEEAEKMKQVAEEAARLSV 2262
Cdd:PTZ00121 1332 -DAAKK-KAEEAKKAAEAAKAEAE-----AAADEAEAAEEKAEA--------AEKKKEE-AKKKADAAKKKAEEKKKADE 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2263 AAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAEllqqQKELAQEQARRLQEDKEqmaqqlAEETQgfQ 2342
Cdd:PTZ00121 1396 AKKKAEEDKKKADE------------LKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKK------ADEAK--K 1451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2343 RTLEAERQRQLEMSAEAERlklrVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvQTLEIQRQQSDHDA 2422
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAK----KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKA 1524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2423 ERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQALQQSFLSEKD---SLLQRERFIEQEKAKLEQLF-- 2497
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMkl 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2498 --QDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL 2575
Cdd:PTZ00121 1601 yeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2576 QLLEEQHR----AALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRlQEAGILSAEELQRLAQ 2651
Cdd:PTZ00121 1681 KKAEEDEKkaaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKI 1759
|
810
....*....|....*
gi 2462619853 2652 GHTTVDELARREDVR 2666
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1334-1878 |
1.01e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 91.52 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1334 EERERLAEVEAALEKQRQLAEAHAQAkaqaeREAKElqqrmQEEVVRREEAAVDAQQQKRSIQEELQQLRqsSEAEIQAK 1413
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEAL-----EDARE-----QIELLEPIRELAERYAAARERLAELEYLR--AALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1414 ARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDESQ 1485
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1486 RKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQV------ALETAQRSAEAELQSKR 1559
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleaeiaSLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1560 ASFAEKTAQLERSLQ--EEHVAVAQLReeaerraqqqaeaerareeaerelERWQLKANEAL---RLRL--------QAE 1626
Cdd:COG4913 447 DALAEALGLDEAELPfvGELIEVRPEE------------------------ERWRGAIERVLggfALTLlvppehyaAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1627 EVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG- 1702
Cdd:COG4913 503 RWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGq 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1703 --------------------------EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1756
Cdd:COG4913 583 vkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1757 STS--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRL 1825
Cdd:COG4913 663 VASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1826 KTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 1878
Cdd:COG4913 743 ARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1316-2084 |
1.39e-17 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 91.04 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEerlAEQQRAEERERLAEV-----EAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQ 1390
Cdd:NF041483 524 ETLERTRAE---AERLRAEAEEQAEEVraaaeRAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARA 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1391 Q----KRSIQEELQQLRQSSEAEIQAKARQAE----------AAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQAL 1455
Cdd:NF041483 601 EaeriRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESAD 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1456 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASrvkAEAEAAREKQRALQALEELrlqAEEAERRLRQAEVE 1535
Cdd:NF041483 681 RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGS---ARAEADQERERAREQSEEL---LASARKRVEEAQAE 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1536 RARQVQvalETAQRSAEAelqskrASFAEKTAQLERSlqeehvAVAQLREEAERraqqqaeaerareeaerelerwqlka 1615
Cdd:NF041483 755 AQRLVE---EADRRATEL------VSAAEQTAQQVRD------SVAGLQEQAEE-------------------------- 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1616 nEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRL 1695
Cdd:NF041483 794 -EIAGLRSAAEHAAER--TRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERL 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1696 RAETEQGEQQ-------------------RQLLEEELARLQREAAA-----ATQKRQELEAELAKVRAEMEVLLASKARA 1751
Cdd:NF041483 868 RSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAE 947
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1752 EEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAERVLAEklaAIGEATRLKTEAEi 1831
Cdd:NF041483 948 AERVRADAAAQAEQLIAEA------TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR- 1014
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1832 alkekeAENERLRRLAEDEAFQRRRleEQAAQHKADIEERLAQLRK-ASDSELERQKGLVE-----DTLRQRRQVEEEIL 1905
Cdd:NF041483 1015 ------EEADRTLDEARKDANKRRS--EAAEQADTLITEAAAEADQlTAKAQEEALRTTTEaeaqaDTMVGAARKEAERI 1086
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1906 ALKASFE------KAAAGKAELELELGR----IRSNAEDtLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEE 1975
Cdd:NF041483 1087 VAEATVEgnslveKARTDADELLVGARRdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEE 1165
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1976 EAARQRKAALEEVERLK--------AKVEEARRLRERAEQESArqlQLAQEAAQKRLQAEEKAHAFAVQQKEQelqqtlq 2047
Cdd:NF041483 1166 QLAEAEAKAKELVSDANseaskvriAAVKKAEGLLKEAEQKKA---ELVREAEKIKAEAEAEAKRTVEEGKRE------- 1235
|
810 820 830
....*....|....*....|....*....|....*..
gi 2462619853 2048 qeqsvLDQLrgeaeAARRAAEEAEEARVQAEREAAQS 2084
Cdd:NF041483 1236 -----LDVL-----VRRREDINAEISRVQDVLEALES 1262
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
136-235 |
5.26e-17 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 79.51 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 215
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 2462619853 216 ED-VDVPQPDEKSIITYVSSL 235
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1462-2344 |
7.18e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1462 AEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQ 1541
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1542 VALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL 1621
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1622 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1701
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1702 GEQQRQLLeEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAA 1781
Cdd:pfam02463 403 EEKEAQLL-LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1782 RLRALAEEAKRQRQlaEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1861
Cdd:pfam02463 482 LQEQLELLLSRQKL--EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1862 AQHKADIEERLAQLRKASDSeLERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 1941
Cdd:pfam02463 560 VEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1942 AELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2021
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2022 KRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQ 2101
Cdd:pfam02463 719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2102 AQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNL 2181
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2182 LDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAarls 2261
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---- 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2262 vaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF 2341
Cdd:pfam02463 955 --------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
...
gi 2462619853 2342 QRT 2344
Cdd:pfam02463 1027 VSI 1029
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
140-237 |
7.91e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.15 E-value: 7.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 140 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 218
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2462619853 219 DVPQPDEKSIITYVSSLYD 237
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1390-2333 |
1.96e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.43 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1390 QQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA----- 1464
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1465 QKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAR------EKQRALQALEELRLQAEEAERrlrQAEVERAR 1538
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEL---EAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1539 QVQVALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwqlka 1615
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL--------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1616 nEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIR 1694
Cdd:TIGR02169 367 -EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1695 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAG 1771
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHG 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1772 RFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAigeatrlktEAEIALKEKEAENER---LRRLAE 1848
Cdd:TIGR02169 526 TVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1849 DEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELeRQKGLVEDTLRQRRQVEEEILALKAS--FEKAAAgkaeleLELG 1926
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGA------MTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1927 RIRSNAEDTLRSKEQAELEAARQRqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2006
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2007 Q-----ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAeeaeearvqAEREA 2081
Cdd:TIGR02169 716 RkigeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---------NDLEA 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2082 AQSRRQVEEAERLKQSAEeqaqaraqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQV 2161
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2162 EQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENraliLRDKDNTQR 2241
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSELKAK 925
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2242 fLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2321
Cdd:TIGR02169 926 -LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
970
....*....|..
gi 2462619853 2322 RLQEDKEQMAQQ 2333
Cdd:TIGR02169 1004 AILERIEEYEKK 1015
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
138-249 |
2.01e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 78.11 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 138 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 217
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 2462619853 218 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 249
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1313-1800 |
4.29e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 85.59 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1313 FISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQ-RMQEEVVRREEAAVDAQQQ 1391
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1392 KRSIQEELQQLRQSSEA------EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG-GAEGELQALRARAEEAEA 1464
Cdd:COG4717 127 LLPLYQELEALEAELAElperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1465 QKRQAQEEAERLRRQVQDESQRKRQAEVELAsRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVAL 1544
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELE-AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1545 ETAqrsAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQ 1624
Cdd:COG4717 286 LAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1625 AEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQ 1704
Cdd:COG4717 363 LQLEELEQEIAALLAEAGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1705 qrqlLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1784
Cdd:COG4717 430 ----LEEELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALK 496
|
490
....*....|....*.
gi 2462619853 1785 ALAEEAKRQRQLAEED 1800
Cdd:COG4717 497 LALELLEEAREEYREE 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
940-1575 |
4.73e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.26 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 940 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEA-CETRTVHRLRLPLDKEPARECAQRIAEQQK-AQAEVEGLGKGV 1017
Cdd:TIGR02168 284 EELQKELYAL---ANEISRLEQQKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEeLKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1018 ARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSlSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVP 1096
Cdd:TIGR02168 361 EELEAElEELESRLEELEEQLETLRSKVAQLELQIASLNN-EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1097 ATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQ----T 1172
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1173 DVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQampLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQY 1252
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA---KKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1253 INAIKDYELQLVTYKAQLEPVASP---------------AKKPKVQSGSESVIQEYVDLRTHYS--------ELTTL-TS 1308
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1309 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAE----AHAQAKAQAEREAKElQQRMQEEVVRREEA 1384
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEelsrQISALRKDLARLEAE-VEQLEERIAQLSKE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1385 AVDAQQQKRSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1464
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEE-----------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1465 QKRQAQEEAERLRRQVQDESQRKRQAEVELASrvkaeaeaarekqrALQALEELRLQAEEAERRLRQAEVERArQVQVAL 1544
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIES--------------LAAEIEELEELIEELESELEALLNERA-SLEEAL 889
|
650 660 670
....*....|....*....|....*....|.
gi 2462619853 1545 ETAqRSAEAELQSKRASFAEKTAQLERSLQE 1575
Cdd:TIGR02168 890 ALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
141-236 |
6.21e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 76.63 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 141 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 219
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 2462619853 220 VPQPDEKSIITYVSSLY 236
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
943-1852 |
7.05e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 943 QQLLQSLEQGAQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1022
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1023 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKEAQ 1093
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1094 AVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1172
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1173 dvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAmpladsqavreqlrqeqalleEIERHGEKVEECQRFAKQY 1252
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1253 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQR 1332
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1333 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKelqQRMQEEVVRREEAAVDAQQQKRS-------------IQEEL 1399
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1400 QQLRQSSEA----------EIQAKARQA-----------EAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1454
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvEFDPKYEPAfkyvfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1455 LRARAEEAEAQKRQAQEEA-ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEE----LRLQAEEAERRL 1529
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeekLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1530 RQAEVERarqvqvaletaqrsaeAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelE 1609
Cdd:TIGR02169 747 SSLEQEI----------------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------S 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1610 RWQLKANEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAE 1689
Cdd:TIGR02169 792 RIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1690 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAE 1769
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDP 939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1770 AGRFRELAEEAARLRALAEEAKR-QRQLAEEDAARQRA--EAERVLAEKLAAIGEATRLKTEAEiALKEKEAENERLRRL 1846
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKRE 1018
|
....*.
gi 2462619853 1847 AEDEAF 1852
Cdd:TIGR02169 1019 VFMEAF 1024
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
138-237 |
8.56e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 76.16 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 138 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 217
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 2462619853 218 VDV--PQPDEKSIITYVSSLYD 237
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
138-241 |
1.39e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 75.47 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 138 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 217
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 2462619853 218 VDV--PQPDEKSIITYVSSLYDAMPR 241
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
18-117 |
2.49e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.87 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 18 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 92
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 2462619853 93 KLVNIRNDDIADGNPKLTLGLIWTI 117
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1351-1721 |
2.71e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 83.25 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1351 QLAEAHAQAKAQAEREAKELQQRMQEEVVRreeaavdaqQQKRSIQEELQQLRQSSEAEiqaKARQAEA-------AERS 1423
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1424 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEVELASRVK-AEA 1502
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1503 EAAREKQRALQALEELRLQAEEA-ERRLRQAEVERARqvqvaletaqrsaeaELQSKRASFAEKTAQLERSLQEEhvava 1581
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1582 qlreeaerraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQa 1660
Cdd:pfam17380 470 ---------------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE- 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1661 vrQRELAEQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1721
Cdd:pfam17380 534 --RRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
14-120 |
3.56e-15 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 74.24 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 14 EDERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIA 83
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYA 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 84 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 120
Cdd:cd21219 71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4019-4057 |
3.83e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 3.83e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 4019 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4057
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
991-1565 |
6.58e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.27 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 991 EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1070
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1071 VIRGTQGAEEvlraheEQLKEaqavpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVE 1150
Cdd:COG4913 331 QIRGNGGDRL------EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1151 VERWRERVAQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVRE--QLRQE 1228
Cdd:COG4913 396 LEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEliEVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1229 QALLEE-IER--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqeyvdlrth 1299
Cdd:COG4913 473 EERWRGaIERvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG------------ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1300 ysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAE 1364
Cdd:COG4913 539 --KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1365 REAKELQQRMQeEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAErsrlrIEEEIRvvrlQLEAterq 1444
Cdd:COG4913 617 AELAELEEELA-EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE-----LEAELE----RLDA---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1445 rggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL-ASRVKAEAEAAREKQRALQALEELRlqAE 1523
Cdd:COG4913 683 ---SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AA 757
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2462619853 1524 EAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEK 1565
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1667-2453 |
6.78e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 82.57 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1667 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQREA-AAATQKRQELEAELAKVRAEMEV 1743
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1744 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLaekLAAIGE 1821
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1822 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRleeQAAQHKADIEERLAQlrkasdselerqkglVEDTLRQRRQVE 1901
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARR---QAAELSRAAEQRMQE---------------AEEALREARAEA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1902 EEILAlkasfekaaagkaelelelgrirsnaedtlrskeQAELEAARQrqlaaeeerrrreaeervqksLAAEEEAARQR 1981
Cdd:NF041483 282 EKVVA----------------------------------EAKEAAAKQ---------------------LASAESANEQR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1982 -KAALEEVERLKAK-VEEARRLRERAEQESArqlQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQlrge 2059
Cdd:NF041483 307 tRTAKEEIARLVGEaTKEAEALKAEAEQALA---DARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK---- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2060 aeaarraaeeaeearvQAEREAAQSRRQVEEAERLkqsaeeqaqaraqaqaaaeklRKeaeqeaarRAQAEQAALRQKQA 2139
Cdd:NF041483 380 ----------------ASEDAKATTRAAAEEAERI---------------------RR--------EAEAEADRLRGEAA 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2140 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEElQRLKAEATEAARQR-----SQVEEELFSVRVQM 2214
Cdd:NF041483 415 DQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEG-ERIRGEARREAVQQieeaaRTAEELLTKAKADA 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2215 EELSKL------KARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRAla 2285
Cdd:NF041483 494 DELRSTataeseRVRTEAIERATTLRRQaEETLERTRAEAERLRAEAEEQAEevRAAAERAARELREETERAIAARQA-- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2286 ekmlkekmQAVQEATRLKAEAELLQQQKELAQEQARrlqEDKEQMAQQLAEETQGfQRTLEAERQRQLEMSAEAERLKLR 2365
Cdd:NF041483 572 --------EAAEELTRLHTEAEERLTAAEEALADAR---AEAERIRREAAEETER-LRTEAAERIRTLQAQAEQEAERLR 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2366 ---VAEMSRAQARAEEDAQRFRKQAEEIGEKLH----------RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAEL 2432
Cdd:NF041483 640 teaAADASAARAEGENVAVRLRSEAAAEAERLKseaqesadrvRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETL 719
|
810 820
....*....|....*....|.
gi 2462619853 2433 EREKEKLQQEAKLLQLKSEEM 2453
Cdd:NF041483 720 GSARAEADQERERAREQSEEL 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3700-3738 |
1.47e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.47e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3700 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3738
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2782-2820 |
1.53e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.53e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 2782 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 2820
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2218-2733 |
1.58e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2218 SKLKARI-EAENR-----------ALILRDKDNTQRFLQEEAEKmkqvAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL 2284
Cdd:COG1196 168 SKYKERKeEAERKleateenlerlEDILGELERQLEPLERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2285 AEKMLKEkmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqRTLEAERQRQLEM------SAE 2358
Cdd:COG1196 244 LEAELEE---LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEerrrelEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2359 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2438
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2439 LQQEAKLLQ------LKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVA-KAQQLREEQ 2511
Cdd:COG1196 398 LAAQLEELEeaeealLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAElLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2512 QRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE 2591
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2592 VTASQVAATKTLPNGRDALDGPAAEAEPEhsfdgLRRKVSAQRLQEAGILSAEELQRLAQGHTTVDELARREDVRhyLQG 2671
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARA-----ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL--VAA 630
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 2672 RSSIAGLLLKATNEKLSVyAALQRQLLSPGTALILLEAQAASGFLLDPVRNRRLTVNEAVKE 2733
Cdd:COG1196 631 RLEAALRRAVTLAGRLRE-VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
595-784 |
1.72e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.56 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 595 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 674
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 675 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 754
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 2462619853 755 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 784
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1078-2026 |
2.16e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.50 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHEEQLKEAQAVpatLPELEATKASLKKLRAQAEaqqpTFDALRDELRGAqEVGERLQQrhgerdveverWRER 1157
Cdd:TIGR02169 175 ALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAE----RYQALLKEKREY-EGYELLKE-----------KEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1158 VAQLlerwQAVLAQTDVRQRELEQLGRQLRyyrESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1237
Cdd:TIGR02169 236 ERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1238 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTHYSELttltsqyikfiset 1317
Cdd:TIGR02169 309 ---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1318 lrrmeeeerlaeqqraeeRERLAEVEAALEKQRQlaeahaqaKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsiqE 1397
Cdd:TIGR02169 370 ------------------RAELEEVDKEFAETRD--------ELKDYREKLEKLKREINELKRELDRLQEELQRLS---E 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1398 ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqrggAEGELQALRARAEEAEAQKRQAQEEAERLR 1477
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKK------------------QEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1478 RqvqdesqRKRQAEVELAsRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQS 1557
Cdd:TIGR02169 483 K-------ELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVV 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1558 KRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQqkslaqa 1637
Cdd:TIGR02169 555 EDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE------- 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1638 eaekqkeeaereARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA------EQELIRLRAETEQGEQQRQLLEE 1711
Cdd:TIGR02169 628 ------------DIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGIlfsrsePAELQRLRERLEGLKRELSSLQS 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1712 ELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1788
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1789 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT-EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1867
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1868 IEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE--QAELE 1945
Cdd:TIGR02169 856 IENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELS 934
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1946 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2021
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
....*
gi 2462619853 2022 KRLQA 2026
Cdd:TIGR02169 1015 KKREV 1019
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
21-121 |
2.37e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.95 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 21 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 92
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 2462619853 93 KLVNIRNDDIADGNPKLTLGLIWTIILHF 121
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
138-239 |
2.44e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 72.04 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 138 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 217
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 2462619853 218 -VDVPQPDEKSIITYVSSLYDAM 239
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3441-3479 |
2.77e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 2.77e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3441 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 3479
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1612-2455 |
2.98e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.11 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1612 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1687
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1688 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1765
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1766 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLAEKLAaigeatrLKTEAEIALKEKEAENERLRR 1845
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINE-------LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1846 LAEDEAFQRRRLEEQAAQHkADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAELELEL 1925
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEY-DRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1926 GRIrsnaedtlRSKEQAELEAARQRQLAAEEERRRREAEERVQksLAAEEEAARqrkAALEEVERLKAKVEEARRLRERA 2005
Cdd:TIGR02169 531 GSV--------GERYATAIEVAAGNRLNNVVVEDDAVAKEAIE--LLKRRKAGR---ATFLPLNKMRDERRDLSILSEDG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2006 EQESARQLqlaqeaaqkrLQAEEK-AHAFAVQQKEQELQQTLQQEQSVLDQLR------------GEAEAARRAAEEAEE 2072
Cdd:TIGR02169 598 VIGFAVDL----------VEFDPKyEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtlegelfeksGAMTGGSRAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2073 ARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAE 2152
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2153 QTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLkaEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENRALi 2232
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKL- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2233 lrdkdNTQRFLQEEAEKMKQVAEEaARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQ 2312
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2313 KELAQEQARRLQEDKEQMAQQlaeetqgfqrtLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGE 2392
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-----EEELSLE 954
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 2393 KLHRTELATQEKvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2455
Cdd:TIGR02169 955 DVQAELQRVEEE---IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
136-236 |
3.18e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.03 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 215
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 2462619853 216 ED-VDVPQPDEKSIITYVSSLY 236
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1082-1558 |
4.34e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.04 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1082 LRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRH---GERDVEVERWRERV 1158
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1159 AQlLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAW-LQDARRRQEQIQamplADSQAVREQLRQEQALLEEIER 1237
Cdd:COG4717 153 ER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ----QRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1238 HGEKVEEcQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpkVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISET 1317
Cdd:COG4717 228 ELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLG-------LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1318 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrrEEAAVDAQQQKRSIQE 1397
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-----LEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1398 ELQQLRQSSEAEIQAKARQAEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1475
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1476 LRRQVQDESQRKRQaevelasrvkaeAEAAREKQRALQALEELRLQAEEAERRLRqaeveRARQVQVALETAQRSAEAEL 1555
Cdd:COG4717 451 LREELAELEAELEQ------------LEEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYREER 513
|
...
gi 2462619853 1556 QSK 1558
Cdd:COG4717 514 LPP 516
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1078-1581 |
5.29e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRaqaeaqqptfDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1157
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1158 VAQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQA 1230
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1231 LLEEIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESVIQEYVDLRTHYSELTTLtsqy 1310
Cdd:PRK02224 385 EIEELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT---- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1311 ikfISETLRRMEEEERLAEQ-------QRAEERERLAEVEAALEKQRQLAEAHAQAKAQaereakelqqrmQEEVVRREE 1383
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------------VEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1384 AAVDAQQQKRSIqEELQQLRQSSEAEIqakARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGELQALRARAEEA 1462
Cdd:PRK02224 500 RAEDLVEAEDRI-ERLEERREDLEELI---AERRETIEEKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1463 EAQKRQAQ--EEAERLRR--QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEA--ERRLRQAEVER 1536
Cdd:PRK02224 576 ELNSKLAElkERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDK 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1537 AR----QVQVALETAQRSAE-AELQSKRASFAEKTAQLErSLQEEHVAVA 1581
Cdd:PRK02224 656 ERaeeyLEQVEEKLDELREErDDLQAEIGAVENELEELE-ELRERREALE 704
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
136-233 |
7.50e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.49 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPgLCPDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 2462619853 215 PEDVDVPQPDEKSIITYVS 233
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1358-2443 |
8.22e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 78.68 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1358 QAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQqlrqsSEAEIQAKARQAEAAERSRLRIEEEIrvvrlq 1437
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1438 leaterqrggaegeLQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEVELASRVKAEAEAAREKQRALQALEE 1517
Cdd:pfam01576 77 --------------LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAARQKLQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1518 LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKT-AQLERSLQEEHVAVAQLREEAERRAQQQAE 1596
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1597 AERAREEAERELE--RWQLKANE----ALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK-AEEQAVRQRELAEQ 1669
Cdd:pfam01576 220 LQEQIAELQAQIAelRAQLAKKEeelqAALARLEEETAQKNNALKKIRELEAQISELQEDLESERaARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1670 ELEKQRQLAEGT-----AQQRLAA--EQELIRLR----AETEQGEQQRQ-----------LLEEELARLQREAAAATQKR 1727
Cdd:pfam01576 300 ELEALKTELEDTldttaAQQELRSkrEQEVTELKkaleEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1728 QELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQRLEA---EAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAAR 1803
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHK-RKKLEGQLQELQArlsESERQRaELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1804 QRAEAERV---LAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdieeRLAQLRKasd 1880
Cdd:pfam01576 459 LSKDVSSLesqLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKK--- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1881 sELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLrskeqaeLEAARQRQLAAEEERRR 1960
Cdd:pfam01576 532 -KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEKKQ 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1961 REAEErvqksLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafavqqkeq 2040
Cdd:pfam01576 604 KKFDQ-----MLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAE------------- 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2041 elqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqAAAEKLRKEAE 2120
Cdd:pfam01576 666 ------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA------------TEDAKLRLEVN 721
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2121 QEAARRAQAeqaalRQKQAADAEMEKHKKfaeQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQR 2200
Cdd:pfam01576 722 MQALKAQFE-----RDLQARDEQGEEKRR---QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR 793
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2201 SQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQ 2280
Cdd:pfam01576 794 EEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIAS 872
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2281 QRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA----ERQRQ---- 2352
Cdd:pfam01576 873 GASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESArqqlERQNKelka 952
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2353 --LEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAI 2429
Cdd:pfam01576 953 klQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRM 1032
|
1130
....*....|....
gi 2462619853 2430 AELEREKEKLQQEA 2443
Cdd:pfam01576 1033 KQLKRQLEEAEEEA 1046
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1046-1575 |
9.17e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1046 LTLGKLEQVRSLSAiylEKLKTISLVIRGTQGAEEVLRAHEEQlKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDA 1125
Cdd:PRK02224 159 LQLGKLEEYRERAS---DARLGVERVLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1126 LRDElrgAQEVGErlqqRHGERDVEVERWRERVAQLlerwQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARR 1205
Cdd:PRK02224 235 TRDE---ADEVLE----EHEERREELETLEAEIEDL----RETIAET---EREREELAEEVRDLRERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1206 RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1285
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1286 SESVIQEYVDlrthySELTTLTSQYiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAER 1365
Cdd:PRK02224 381 DRREEIEELE-----EEIEELRERF-GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE-----RVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1366 EAKELQQRMQE-EVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---------EIQAKARQAEAAERSRLRIEEEIRVVR 1435
Cdd:PRK02224 450 EAGKCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEveerleraeDLVEAEDRIERLEERREDLEELIAERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1436 LQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQ 1513
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIE 609
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1514 ALEELR--LQAEEAERRLRQAEV-ERARQVQVALETAqrsAEAELQSKRASFAEKTAQLERSLQE 1575
Cdd:PRK02224 610 RLREKReaLAELNDERRERLAEKrERKRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1042-1907 |
1.10e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1042 SELELTLGKLEQVRslsaiylEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATK--ASLKKLRAQAEAQ 1119
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1120 QPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLaQTDVR--QRELEQLGRQLRYYRESadplg 1197
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIAEKERE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1198 awLQDARRRQEQIQAmpladsqavreqlrQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPA 1277
Cdd:TIGR02169 317 --LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1278 KKPKvqsgsesviQEYVDLRTHYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA 1357
Cdd:TIGR02169 381 AETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1358 QAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ 1437
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1438 LEATERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDESQRKRQaeVELASRVKA------EAEAAREK 1508
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEA--IELLKRRKAgratflPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1509 QRALQALEE-----LRLQAEEAERRLRQA--EVERARQVQVALETAQR--------SAEAELQSKRA-----SFAEKTAQ 1568
Cdd:TIGR02169 587 RRDLSILSEdgvigFAVDLVEFDPKYEPAfkYVFGDTLVVEDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1569 LERSLQEEHVAVAqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEaer 1648
Cdd:TIGR02169 667 LFSRSEPAELQRL----------------------------RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--- 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1649 earrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQreAAAATQKRQ 1728
Cdd:TIGR02169 716 ------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE--EALNDLEAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1729 ELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1808
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1809 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---ERLAQL--RKASDSEL 1883
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIedPKGEDEEI 946
|
890 900
....*....|....*....|....
gi 2462619853 1884 ERQKGLVEDTLRQRRQVEEEILAL 1907
Cdd:TIGR02169 947 PEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1303-2197 |
1.68e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 77.52 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1303 LTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAKELQQRMQEEV 1378
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1379 VRREEAavdaQQQKRSIQEELQQLRQSSEAEIQAKARqaeaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1458
Cdd:pfam01576 257 AQKNNA----LKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1459 AE-EAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsrvkaeaEAAREKQRALQALEELRlQAEEAERRLRQAEVERA 1537
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1538 RQVQVALETAQRSAEAELQSKRASFAEktAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANE 1617
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1618 ALRlrlqAEEVAQQKSLAQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1697
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1698 ETEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEAG 1771
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQK 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1772 RFRELaeeaarlraLAEEAKRQRQLAEEdaaRQRAEAERVLAEKLA-----AIGEATRLKTEAEIALKEKEAENERLRRL 1846
Cdd:pfam01576 605 KFDQM---------LAEEKAISARYAEE---RDRAEAEAREKETRAlslarALEEALEAKEELERTNKQLRAEMEDLVSS 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1847 AEDEAFQ-------RRRLEEQAAQHKADIEERLAQLRKASDSEL-------------------------ERQKGLVedtl 1894
Cdd:pfam01576 673 KDDVGKNvhelersKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnmqalkaqferdlqardeqgeEKRRQLV---- 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1895 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE 1974
Cdd:pfam01576 749 KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQS 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1975 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSV 2052
Cdd:pfam01576 829 KESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELL 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2053 LDQLRgeaeaARRAAEEAEEARVQAEREAAQSRRQV-EEAERLKQSAEEQAQARAQAQAAAEKLR-KEAEQEAARRAQAE 2130
Cdd:pfam01576 909 NDRLR-----KSTLQVEQLTTELAAERSTSQKSESArQQLERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEEQL 983
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2131 QAALRQKQAADA--------------EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQK---NLLDEELQRLKAEA 2193
Cdd:pfam01576 984 EQESRERQAANKlvrrtekklkevllQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAsraNAARRKLQRELDDA 1063
|
....
gi 2462619853 2194 TEAA 2197
Cdd:pfam01576 1064 TESN 1067
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1036-1789 |
2.27e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.32 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1036 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTIslvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRA 1114
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSL-------HGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1115 QAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQlgRQLRYYRESAD 1194
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1195 PLGAWLQDARRRQEQI---QAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYElQLVTYKAQLE 1271
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1272 pvaspAKKPKVQSGSesviqeyvdlrthySELTTLTSQYIKFISETLRRMEEEERLAeqqRAEERERLAEVEAALekQRQ 1351
Cdd:TIGR00618 390 -----TLTQKLQSLC--------------KELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAEL--CAA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1352 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE-AAERSRLRIEEE 1430
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGP 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1431 IRVVRLQLEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQRKRQAEVELASRVKAEAE 1503
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSeedvYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1504 AAREKQRALQAlEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK--------RASFAEKTAQLERSLQE 1575
Cdd:TIGR00618 606 AEDMLACEQHA-LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehalsiRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1576 EHVAVAQLREEAER---RAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArr 1652
Cdd:TIGR00618 685 MQSEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE-- 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1653 rgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKR 1727
Cdd:TIGR00618 762 ----AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRL 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 1728 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1789
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
136-236 |
2.75e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 68.90 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 215
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 2462619853 216 ED-VDVPQPDEKSIITYVSSLY 236
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1686-2454 |
4.05e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 76.37 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1686 LAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1765
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1766 LEAEAGRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEIAL-KEKEAENERL 1843
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1844 RRL---AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKglvedtlrQRRQVEEEILALKASFEKAAAGKAE 1920
Cdd:pfam01576 162 SEFtsnLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK--------AKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1921 LELELgrirsnaedtlrSKEQAELEAARQRqlaaeeerrrreaeervqkslaAEEEAArQRKAALEEVERLKAKVEEarr 2000
Cdd:pfam01576 234 LRAQL------------AKKEEELQAALAR----------------------LEEETA-QKNNALKKIRELEAQISE--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2001 LRERAEQESArqlQLAQEAAQKRLQAEEkahafavqqkeqelqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAERE 2080
Cdd:pfam01576 276 LQEDLESERA---ARNKAEKQRRDLGEE------------------------LEALKTELEDTLDTTAAQQELRSKREQE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2081 AAQSRRQVEEAERLKQSAEEqaqaraqaqaaaeKLRKEAEQEAARRAQAeqaaLRQKQAADAEMEKHKKFAEQtlrQKAQ 2160
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQ-------------EMRQKHTQALEELTEQ----LEQAKRNKANLEKAKQALES---ENAE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2161 VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALilrDKD--- 2237
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDvss 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2238 ------NTQRFLQEEAekmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLqq 2311
Cdd:pfam01576 466 lesqlqDTQELLQEET---RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL-- 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2312 qkELAQEQARRLQEDKEQMAQQLAEETQGFQR---------------TLEAERQRQLEMSAEAERLKLR--VAEMSRAQA 2374
Cdd:pfam01576 541 --EALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrlqqelddlLVDLDHQRQLVSNLEKKQKKFDqmLAEEKAISA 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2375 RAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA-------IAELEREKEKLQQEAKLLQ 2447
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKRALEQQVEEMK 698
|
....*..
gi 2462619853 2448 LKSEEMQ 2454
Cdd:pfam01576 699 TQLEELE 705
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2152-2447 |
5.13e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.93 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2152 EQTLRQKAQVEQELTTLRLQLEETDHQKNLlDEELQRLKAEATEAARQRSQVEEELFSV--RVQMEELSKLK-------A 2222
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2223 RIEAENRALILRDKDNTQRFLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2302
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2303 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDaQR 2382
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-KR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 2383 FRKQAEEIGEKLHRTELAT--------QEKVTLVQTLEIQRQQSDHDAERLREaiAELEREKEKLQQEAKLLQ 2447
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEErkqamieeERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEERRRIQ 555
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3034-3072 |
5.18e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 5.18e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3034 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 3072
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
39-118 |
6.52e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 39 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 110
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 2462619853 111 LGLIWTII 118
Cdd:cd21223 105 LALLWRII 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1655-1871 |
8.97e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 73.26 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1734
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1735 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1810
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 1811 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1871
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
23-124 |
1.92e-12 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 66.88 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 23 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHFQIS 124
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
138-233 |
3.01e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.87 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 138 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 216
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPgLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 2462619853 217 DVDVPQPDEKSIITYVS 233
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1670-2451 |
3.49e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.46 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1670 ELEKQRQLAEGTAQQRLAAEQELIRLRAE----TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvll 1745
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1746 askaRAEEESRSTSEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLAEKLAAIGEATRL 1825
Cdd:TIGR00618 251 ----AQEEQLKKQQLLKQLRARIE-----ELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1826 KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR-RQVEEEI 1904
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1905 LALKASFEKAAAGKAELELELGRIrsNAEDTLRSKEQAELEAAR-QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1983
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1984 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQEaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQlrgeaEAA 2063
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-----YAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2064 RRAAEEAEEARVQAEREAAQSRRqvEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEqeaarraqaeqaalRQKQAADAE 2143
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLK--EQMQEIQQSFSILTQCDNRSKEDIPNLQNITV--------------RLQDLTEKL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2144 MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQrLKAEATEAARQRsqVEEELFSVRVQMEELSKLKar 2223
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-LHALQLTLTQER--VREHALSIRVLPKELLASR-- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2224 ieaenralilrdkdntQRFLQEEAEKMKQVAEEAARLsvaAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK 2303
Cdd:TIGR00618 679 ----------------QLALQKMQSEKEQLTYWKEML---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2304 AEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRF 2383
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 2384 RKQAEEIGEKLHRTELATQEKVTLVQTLeiqRQQSDHDAERLReaiaeleREKEKLQQEAKLLQLKSE 2451
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEI---THQLLKYEECSK-------QLAQLTQEQAKIIQLSDK 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1290-2037 |
4.17e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.06 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1290 IQEYVDLRTHYSELTTLTSQYikFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKE 1369
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARE-SD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1370 LQQRMQ--EEVVRREEAAVDAQQQKRSIQEELQQL----RQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLeaTER 1443
Cdd:COG3096 325 LEQDYQaaSDHLNLVQTALRQQEKIERYQEDLEELterlEEQEEVVEEAAEQLAEAEARLE-AAEEEVDSLKSQL--ADY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1444 QRGgaegeLQALRARAeeaeAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsRVKAEAEAAREKQRALqaleELRLQ-A 1522
Cdd:COG3096 402 QQA-----LDVQQTRA----IQYQQAVQALEKARALCGLPDLTPENAEDYLA-AFRAKEQQATEEVLEL----EQKLSvA 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1523 EEAERRLRQA---------EVERARQVQVALETAQRSAEAELQSKRAS-FAEKTAQLERSLQEEHVAVAQLRE---EAER 1589
Cdd:COG3096 468 DAARRQFEKAyelvckiagEVERSQAWQTARELLRRYRSQQALAQRLQqLRAQLAELEQRLRQQQNAERLLEEfcqRIGQ 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1590 RAQQQAEAERAREEAERELERWQLKANEAL--RLRLQAEEV---AQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQR 1664
Cdd:COG3096 548 QLDAAEELEELLAELEAQLEELEEQAAEAVeqRSELRQQLEqlrARIKELAARAPAWL------------AAQDALERLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1665 ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRaetEQGEQQRQLLEEELARLQREAAAATQKRQEL-------------- 1730
Cdd:COG3096 616 EQSGEALADSQEVTA-AMQQLLEREREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALaerlggvllseiyd 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1731 ----------EA------------ELAKVRAEMEVLL-----------------ASKARAEEESRSTSEKSKQRlEAEAG 1771
Cdd:COG3096 692 dvtledapyfSAlygparhaivvpDLSAVKEQLAGLEdcpedlyliegdpdsfdDSVFDAEELEDAVVVKLSDR-QWRYS 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1772 RFREL-----AEEAARLRALAEEAKR-QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEnerlRR 1845
Cdd:COG3096 771 RFPEVplfgrAAREKRLEELRAERDElAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQR----RS 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1846 LAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAsdseLERQKGLVEDTLRQRRQVEEEIL--ALKASFEKAAAGKA--EL 1921
Cdd:COG3096 847 ELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL----LPQANLLADETLADRLEELREELdaAQEAQAFIQQHGKAlaQL 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1922 ELELGRIRSNAE--DTLrskeQAELEAARQRQlaAEEERRRREAEERVQKSLA-AEEEAARQRKAALEEVERLKAKVEEA 1998
Cdd:COG3096 923 EPLVAVLQSDPEqfEQL----QADYLQAKEQQ--RRLKQQIFALSEVVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQA 996
|
810 820 830
....*....|....*....|....*....|....*....
gi 2462619853 1999 RRLRERAeQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2037
Cdd:COG3096 997 EEARREA-REQLRQAQAQYSQYNQVLASLKSSRDAKQQT 1034
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4288-4326 |
4.39e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.39e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 4288 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4326
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
138-237 |
4.52e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.05 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 138 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 213
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 2462619853 214 DPEDVdVPQPDEKSIITYVSSLYD 237
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1694-2248 |
5.11e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1694 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1773
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1774 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE---AENERLRRLA 1847
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1848 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAEL 1921
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1922 ELELGRIRSNAEDtLRSKE---QAELEAARQR-----------------QLAAEEERRRREAEERVQKS-LAAEEEAARQ 1980
Cdd:PRK02224 411 EDFLEELREERDE-LREREaelEATLRTARERveeaealleagkcpecgQPVEGSPHVETIEEDRERVEeLEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1981 RKAALEE-VERLKAKVEEARR---LRERAEQESARQLQLAQEAAQKRLQAEEKahafavqqkeqelQQTLQQEQSVLDQL 2056
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRierLEERREDLEELIAERRETIEEKRERAEEL-------------RERAAELEAEAEEK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2057 RGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqaaaeklrkeaeQEAARRAQAEQAALRQ 2136
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-----------------------LAAIADAEDEIERLRE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2137 KQAADAEMEKHKKFAEQTLRQ-KAQVEQELTTLRlqLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQME 2215
Cdd:PRK02224 614 KREALAELNDERRERLAEKRErKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
570 580 590
....*....|....*....|....*....|....
gi 2462619853 2216 ELSKLKARIEA-ENRALILRDkdntqrfLQEEAE 2248
Cdd:PRK02224 692 ELEELRERREAlENRVEALEA-------LYDEAE 718
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
138-238 |
6.05e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 65.07 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 138 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 217
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 2462619853 218 VdVPQPDEKSIITYVSSLYDA 238
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3110-3148 |
6.95e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 6.95e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3110 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 3148
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2706-2744 |
7.74e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.74e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 2706 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2744
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1333-2269 |
8.38e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.29 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1333 AEERERLaeVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVvrreeaavdAQQQKRsiQEELQQLRQSSE---AE 1409
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQL-----AEEQYRLVEMAREL---------EELSAR--ESDLEQDYQAASdhlNL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1410 IQAKARQAEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQ 1489
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1490 AEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAElqskrasfaEKTAQL 1569
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---------AARRQF 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1570 ERSLQeehvAVAQLREEAERRaqqqaeaerareeaerelERWQlKANEALR----LRLQAEEVAQQKSlaqaeaekqkee 1645
Cdd:COG3096 475 EKAYE----LVCKIAGEVERS------------------QAWQ-TARELLRryrsQQALAQRLQQLRA------------ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1646 aerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQREAAAATQ 1725
Cdd:COG3096 520 ------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1726 KRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1795
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1796 LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAE-----------IALKEKEAENERLRRL----------------AE 1848
Cdd:COG3096 666 PGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYfsalygparhaIVVPDLSAVKEQLAGLedcpedlyliegdpdsFD 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1849 DEAFQRRRLEEQAAQHKADI------------------EERLAQLRKASDSELERQKGLVEDTLRQRRQVE--EEILALK 1908
Cdd:COG3096 746 DSVFDAEELEDAVVVKLSDRqwrysrfpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQafSQFVGGH 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1909 ASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAE------LEAARQR---------QLAAEEERRRREAEERVQKSLAA 1973
Cdd:COG3096 826 LAVAFAPDPEAELA-ALRQRRSELERELAQHRAQEqqlrqqLDQLKEQlqllnkllpQANLLADETLADRLEELREELDA 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1974 EEEAAR---QRKAALEEVERLkakveeARRLRERAEQESARQLQLAQ-EAAQKRLQAEEKAHAFAVQQKE----QELQQT 2045
Cdd:COG3096 905 AQEAQAfiqQHGKALAQLEPL------VAVLQSDPEQFEQLQADYLQaKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2046 LQQEQSVLDQLRgeaeaarraaeeaeEARVQAEREAAQSRRQVEEA-ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAA 2124
Cdd:COG3096 979 LGENSDLNEKLR--------------ARLEQAEEARREAREQLRQAqAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2125 RRAqaeqaalrqkqAADAEMEkhkkfaEQTLRQKAQVEQELTTLRLqleetdhQKNLLDEELQRLKAEATEAARQRSQVE 2204
Cdd:COG3096 1045 LGV-----------QADAEAE------ERARIRRDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 2205 EELFSVRvqmEELSKLKARIEAENRalILRDKD-----NTQRFLQEEAEKMKQVAEE---AARLSVAAQEAAR 2269
Cdd:COG3096 1101 RDYKQER---EQVVQAKAGWCAVLR--LARDNDverrlHRRELAYLSADELRSMSDKalgALRLAVADNEHLR 1168
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1078-1809 |
9.12e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 72.29 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQ--RHGERdveVERWR 1155
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK---IERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1156 ERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLRQEQALLEEI 1235
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1236 ERHGEKVEECQRFAKQYINAIKDYELQLVT-------YKAQ-------LEPVASPAKKPKVQSGSESVIQEYVDLRTHYS 1301
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEEVLELEQklsvadaARRQfekayelVCKIAGEVERSQAWQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1302 ELTTLTSQYiKFISETLRRMEEEERLAEQ------QRAEERERLAEVEAALEKQR----QLAEAHAQAKAQAEREAKELQ 1371
Cdd:COG3096 513 RLQQLRAQL-AELEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQLeeleEQAAEAVEQRSELRQQLEQLR 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1372 QRMQEeVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaERSRLRIEEEIRVVRLQLEATER---QRGGA 1448
Cdd:COG3096 592 ARIKE-LAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQALESQIErlsQPGGA 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1449 E-GELQALRAR-----------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQR 1486
Cdd:COG3096 670 EdPRLLALAERlggvllseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVF 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1487 KRQaEVELASRVKAE---------------AEAAREKQralqaLEELRLQAEE-----AERRLRQAEVER---------A 1537
Cdd:COG3096 750 DAE-ELEDAVVVKLSdrqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1538 RQVQVALETaqrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRA-------QQQAEAERAREEAERELER 1610
Cdd:COG3096 824 GHLAVAFAP---DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1611 WQLKANEALR-LRLQAEEVAQ-QKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLA 1687
Cdd:COG3096 901 ELDAAQEAQAfIQQHGKALAQlEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLG 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1688 AEQELI-RLRAETEQGEQQRQLLEEELARLQREAAAATQKR--------------QELEAELakvrAEMEVLLAskARAE 1752
Cdd:COG3096 981 ENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAE 1054
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1753 EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1809
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3943-3981 |
1.02e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.02e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3943 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3981
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3776-3814 |
1.08e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.08e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3776 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3814
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1583 |
2.99e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 68.64 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1383 EAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA 1462
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1463 EAQKRQAQEEAERLRRQVQdesQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEVERA 1537
Cdd:COG4942 96 RAELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462619853 1538 RQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1583
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2135-2337 |
3.07e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 68.64 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2135 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEEL---FSVR 2211
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2212 VQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2291
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462619853 2292 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEE 2337
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1450-2028 |
3.15e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1450 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevELASRVKAEAEAAREKQRALQALEELRLQAEEA--ER 1527
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1528 RLRQAEVERARQVQVALETA---QRSAEAELQSKRASFAEKTAQLERSLQEehvavaqlreeaerraqqqAEAERAREEA 1604
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------------------LEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1605 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE--REARRRGKAEEQAVRQRELA---EQELEKQRQLAE 1679
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAaelESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1680 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR---AEMEVLLA---------- 1746
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1747 ----SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAARQRAEAERVLAEKLAAIG 1820
Cdd:PRK02224 461 vegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1821 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---------ERLAQLRKASDSELERQKGLVE 1891
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1892 ------DTLRQRRqveEEILALKASFEKAAAGKAELElelgriRSNAEDTLR--SKEQAELEAARQRqlaaeeerrrrea 1963
Cdd:PRK02224 621 lnderrERLAEKR---ERKRELEAEFDEARIEEARED------KERAEEYLEqvEEKLDELREERDD------------- 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1964 eerVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2028
Cdd:PRK02224 679 ---LQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1131-1554 |
3.25e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 70.37 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1131 RGAQEvgERLQQRHGERDVEVERWR---------ERVAQLLERW-------------QAVLAQTDVR----QRELEQLGR 1184
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRrselERELAQHRA 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1185 QLRYYRESADPLGAWLQDARRRQEQiqAMPLADSQAvreqlrqeQALLEEIERHGEKVEECQRFAKQYINAIkdyelqlv 1264
Cdd:COG3096 858 QEQQLRQQLDQLKEQLQLLNKLLPQ--ANLLADETL--------ADRLEELREELDAAQEAQAFIQQHGKAL-------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1265 tykAQLEPVASPAKKPKVQSgsESVIQEYVDLrthySELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEE--R 1336
Cdd:COG3096 920 ---AQLEPLVAVLQSDPEQF--EQLQADYLQA----KEQQRRLKQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEklR 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1337 ERLAEVEAALEKQRQLAEAHAQAKAQAereakelQQRMQEEVVRREEAavdaQQQKRSIQEELQQLrqsseaEIQAKARQ 1416
Cdd:COG3096 991 ARLEQAEEARREAREQLRQAQAQYSQY-------NQVLASLKSSRDAK----QQTLQELEQELEEL------GVQADAEA 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1417 AEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQ 1489
Cdd:COG3096 1054 EERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERRL 1133
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1490 AEVELasrvkaeaeaarekqrALQALEELRLQAEEAERRLRQAeVERARQVQVALETAQRSAEAE 1554
Cdd:COG3096 1134 HRREL----------------AYLSADELRSMSDKALGALRLA-VADNEHLRDALRLSEDPRRPE 1181
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1665-2515 |
3.82e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 69.82 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1665 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAeME 1742
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1743 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1822
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1823 TRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQ---------------AAQH--KADIEERLAQLRKASDSELER 1885
Cdd:pfam01576 267 REL--EAQISELQEDLESERAARNKAEK--QRRDLGEElealkteledtldttAAQQelRSKREQEVTELKKALEEETRS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1886 QKGLVEDTLRQRRQVEEEilaLKASFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEAARQRQlaaeeerrrrE 1962
Cdd:pfam01576 343 HEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK----------K 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1963 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARqlqLAQEAAQKRLQaeekahafaVQQKEQEL 2042
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSSLESQ---------LQDTQELL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2043 QQTLQQEQSVLDQLRgeaeaarraaeeaeearvQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQE 2122
Cdd:pfam01576 478 QEETRQKLNLSTRLR------------------QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2123 AARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLeetDHQKNLL----------DEELQRLKAE 2192
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVsnlekkqkkfDQMLAEEKAI 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2193 ATEAARQRSQVEEE-------LFSVRVQMEELSKLKARIEAENRAL------ILRDKDNTQRFLQEeAEKMKQVAEeaar 2259
Cdd:pfam01576 617 SARYAEERDRAEAEareketrALSLARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHE-LERSKRALE---- 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2260 lsvaaQEAARLR-QLAE-EDLAQQRALAEKMLKEKMQAvqeatrLKAEAEL-LQQQKELAQEQARRLQEDKEQMAQQLAE 2336
Cdd:pfam01576 692 -----QQVEEMKtQLEElEDELQATEDAKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLVKQVRELEAELED 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2337 ETQgfQRTLEAERQRQLEMsaEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQ 2416
Cdd:pfam01576 761 ERK--QRAQAVAAKKKLEL--DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLK 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2417 QSDHDAERLREAIAELEREKEKLQQEAKLLQlksEEMQtvqqeqllqetqalqqSFLSEKDSLLQRERFIEQEKAKLEQL 2496
Cdd:pfam01576 837 NLEAELLQLQEDLAASERARRQAQQERDELA---DEIA----------------SGASGKSALQDEKRRLEARIAQLEEE 897
|
890
....*....|....*....
gi 2462619853 2497 FQDEVAKAQQLREEQQRQQ 2515
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKST 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1101-1482 |
3.86e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1101 ELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWqavlAQTDVRQRELE 1180
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI----AQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1181 QLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQAlleEIERHGEKVEECQRFAKQYINAIKDYE 1260
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1261 LQLVTYKAQLEpvaspaKKPKVQSGSESVIQEYvdlrthyselttltsqyikfiSETLRRMEEEERLAEQQRAEERERLA 1340
Cdd:TIGR02168 838 RRLEDLEEQIE------ELSEDIESLAAEIEEL---------------------EELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1341 EVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAA 1420
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1421 ERSRLRIEEEI-RVVRLQLEATErqrggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1482
Cdd:TIGR02168 971 RRRLKRLENKIkELGPVNLAAIE--------EYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1403-2029 |
4.41e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.87 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1403 RQSSEAEIQAKARQAEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1476
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1477 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAeLQ 1556
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1557 SKRASFAEKTAQLERSLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1635
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1636 QAEAEKQKEEAEREARRRGKAEEQAV-RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelA 1714
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE--L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1715 RLQREAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1788
Cdd:pfam12128 526 ELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1789 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1868
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1869 EERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEkaaagkAELELELGRIRSN--AEDTLRSKEQAELEA 1946
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSGAKAELKALET 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1947 ARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAA------------LEEVERLKAKVEEARRLRERAEQESARQl 2013
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREiRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAISELQQQLARL- 833
|
650
....*....|....*.
gi 2462619853 2014 qlaQEAAQKRLQAEEK 2029
Cdd:pfam12128 834 ---IADTKLRRAKLEM 846
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
12-115 |
5.63e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 62.83 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 12 SGEDERD-RVqkktFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQI 82
Cdd:cd21300 2 DAEGEREaRV----FTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 2462619853 83 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 115
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1336-1861 |
9.35e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.73 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1336 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR 1415
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1416 QAEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEV 1492
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1493 ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERS 1572
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1573 LQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARR 1652
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1653 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEA 1732
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1733 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1812
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462619853 1813 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1861
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1765-2496 |
1.13e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1765 RLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIgEATRLKTEAEIALKEK---EAENE 1841
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKeaiERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1842 RLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAEL 1921
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1922 ELELGRIRSNAEDtlrSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR---KAALEEVERLKAKVEE- 1997
Cdd:TIGR02169 328 EAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLKREINEl 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1998 ---ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARraaee 2069
Cdd:TIGR02169 405 kreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD----- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2070 aeearvQAEREAAQSRRQVEEAE-RLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEME--- 2145
Cdd:TIGR02169 480 ------RVEKELSKLQRELAEAEaQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2146 --------------KHKKFAEQTLRQKAQVEQELTTLRLQLEE--TDHQKNLLDEELQRlkAEATEAARQRSQVEEELFS 2209
Cdd:TIGR02169 554 veddavakeaiellKRRKAGRATFLPLNKMRDERRDLSILSEDgvIGFAVDLVEFDPKY--EPAFKYVFGDTLVVEDIEA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2210 VRVQMeelskLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKML 2289
Cdd:TIGR02169 632 ARRLM-----GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL--SSLQSELRRIENRL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2290 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEM 2369
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2370 SRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2449
Cdd:TIGR02169 785 EARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 2462619853 2450 SEEMQTVQQEQLLQETQalqqsfLSEKDSLLQRERfiEQEKAKLEQL 2496
Cdd:TIGR02169 863 KEELEEELEELEAALRD------LESRLGDLKKER--DELEAQLREL 901
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1658-2091 |
1.22e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR--------QLLEEELARLQREAAAATQKRQE 1729
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1730 L--------------EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR----------- 1784
Cdd:COG4913 364 LeallaalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparll 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1785 ----ALAEEAKRQR----------QLAEEDAARQRAeAERVL-------------AEKLAAIGEATRLKTEAEIALKEKE 1837
Cdd:COG4913 444 alrdALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLggfaltllvppehYAAALRWVNRLHLRGRLVYERVRTG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1838 AENERLRRLAED-------------EAFQRRRLEEQAAQHKADIEERLAQLRKA-------SDSELERQKG--------- 1888
Cdd:COG4913 523 LPDPERPRLDPDslagkldfkphpfRAWLEAELGRRFDYVCVDSPEELRRHPRAitragqvKGNGTRHEKDdrrrirsry 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1889 -LVEDTLRQRRQVEEEILALKASFEKAAAGKAELelelgrirsnaedtlrskeQAELEAARQRQLAAEEERRRREAEERV 1967
Cdd:COG4913 603 vLGFDNRAKLAALEAELAELEEELAEAEERLEAL-------------------EAELDALQERREALQRLAEYSWDEIDV 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1968 QkSLAAEEEAARQRKAALE----EVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQ 2043
Cdd:COG4913 664 A-SAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2044 QTLQQEQSVLDQLRGEAEAARRAAEEA--EEARVQAEREAAQSRRQVEEA 2091
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELREnlEERIDALRARLNRAEEELERA 792
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1290-1788 |
1.33e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1290 IQEYVDLRTHYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKE 1369
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1370 LQQRMQeevvrreeAAVDAQQqkrSIQEELQQlrqsSEAEIQAKARQAEAAErsrlRIEEEIRVVRlqlEATERQrggae 1449
Cdd:PRK04863 326 LEQDYQ--------AASDHLN---LVQTALRQ----QEKIERYQADLEELEE----RLEEQNEVVE---EADEQQ----- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1450 gelqalraraEEAEAQKRQAQEEAERLRRQVQD-----ESQRKR----QAEVELASRVKA-------EAEAAREKQRALQ 1513
Cdd:PRK04863 379 ----------EENEARAEAAEEEVDELKSQLADyqqalDVQQTRaiqyQQAVQALERAKQlcglpdlTADNAEDWLEEFQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1514 A-LEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAeAELQSKRASfaEKTAQLERSLQEEHVAVAQLreeaerraq 1592
Cdd:PRK04863 449 AkEQEATEELLSLEQKLSVAQ-AAHSQFEQAYQLVRKIA-GEVSRSEAW--DVARELLRRLREQRHLAEQL--------- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1593 qqaeaeRAREEAERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELE 1672
Cdd:PRK04863 516 ------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---------------------DEDELEQLQEELEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1673 KQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQREAAAATQKRQELEAELAKvraemevlLASKA 1749
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------LLERE 640
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2462619853 1750 RAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1788
Cdd:PRK04863 641 RELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1493-2028 |
1.55e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 67.96 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1493 ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSAEAELQSKRAS---------- 1561
Cdd:COG3899 713 RRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppasa 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1562 FAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1641
Cdd:COG3899 793 RAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLA 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1642 QKEEAEREARRrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1721
Cdd:COG3899 873 LAAAAAAAAAA---AALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAA 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1722 AATQKRQELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1801
Cdd:COG3899 950 AAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALA 1016
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1802 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDS 1881
Cdd:COG3899 1017 AALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAA 1096
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1882 ELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRR 1961
Cdd:COG3899 1097 LAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALA 1176
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1962 EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2028
Cdd:COG3899 1177 ALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1302-1519 |
1.70e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 66.82 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1302 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAEREA 1367
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1368 KELQQRMQEEVVRRE-EAAVDAQQQKRsiQEELQQlrqssEAEIQAKARQAEAAERSRLRIEEEirvvrlqLEATERQRg 1446
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANA--EREVQR-----QLEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1447 gAEGELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1519
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1658-1895 |
1.71e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAaatqkrqELEAELAKV 1737
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELA-------RLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLASKARAEEESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1813
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREierlERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1814 EKLAAIGEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEeqaaQHKADIEERLAQLRKAsdseLERQKGLVEDT 1893
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEA-------EIASLE----RRKSNIPARLLALRDA----LAEALGLDEAE 459
|
..
gi 2462619853 1894 LR 1895
Cdd:COG4913 460 LP 461
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1655-2032 |
1.81e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1734
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELE-AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1735 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE------EDAARQRAEA 1808
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEeeleqlENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1809 ERVLAEKLAAIGEATRLKTEAEIAL------------------------------KEKEAENERLRRLAEDEAFQRRRLE 1858
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSllsliltiagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1859 EQAAQHKADIEERLAQLRKASDSELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTLR 1937
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1938 SKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQL 2015
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQ 476
|
410
....*....|....*..
gi 2462619853 2016 AQEAAQKRLQAEEKAHA 2032
Cdd:COG4717 477 ELEELKAELRELAEEWA 493
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1506-1858 |
1.94e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.46 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1506 REKQRALQALEELRLQaEEAERRLRqaEVERARQvqvaLETAQRSAEAELQSKRASFAEKtaqlERSLQEEHvavaqlre 1585
Cdd:pfam17380 287 RQQQEKFEKMEQERLR-QEKEEKAR--EVERRRK----LEEAEKARQAEMDRQAAIYAEQ----ERMAMERE-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1586 eaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEQAVRQRE 1665
Cdd:pfam17380 348 --------------------RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1666 LaeQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQ-QRQLLEEELARLQREAAAATQKRQ-------ELEAELAKV 1737
Cdd:pfam17380 406 I--LEEERQRKIQQ--------QKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLAE 1814
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462619853 1815 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1858
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1309-1948 |
2.46e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1309 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDA 1388
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1389 QQQKRSIQEELQQLRQ---SSEAEIQA-KARQAEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1458
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1459 --AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEVELASrVKAEAEAAREKQRALQAleelrlQAEEAERRLRQAEVE 1535
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITG-LTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1536 RARQVQvALETAQRSAEAELQSKRASFAEKTAQLERSLQeehVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1615
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1616 NEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1686
Cdd:pfam15921 391 KE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1687 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1762
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1763 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAIGEATRL-KTEAEIALKEK 1836
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1837 EAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASDSELERQKGL--VEDTLRQRRQVEEEILALKAS 1910
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDYEVLKRN 682
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2462619853 1911 F----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAAR 1948
Cdd:pfam15921 683 FrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMK 727
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1854-2591 |
2.59e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 67.30 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1854 RRRLEEQAA--QHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 1931
Cdd:pfam02463 155 RLEIEEEAAgsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1932 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2011
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2012 QLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRgeaeaarraaeeaeearvQAEREAAQSRRQV 2088
Cdd:pfam02463 315 KLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK------------------LQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2089 EEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2168
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2169 RLQLEEtdhqKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAE 2248
Cdd:pfam02463 457 ELKLLK----DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2249 KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAvqeaTRLKAEAELLQQQKELAQEQARRLQEDKE 2328
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK----LRLLIPKLKLPLKSIAVLEIDPILNLAQL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2329 QMAQQLAEETQGFQRTLEAERQRQLEMSaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLV 2408
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2409 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQalQQSFLSEKDSLLQRERFIEQ 2488
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ--KIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2489 EKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGvrrkqEELQQLEQQRRQQEELLAEEN 2568
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL-----EEEQLLIEQEEKIKEEELEEL 838
|
730 740
....*....|....*....|...
gi 2462619853 2569 qRLREQLQLLEEQHRAALAHSEE 2591
Cdd:pfam02463 839 -ALELKEEQKLEKLAEEELERLE 860
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1078-1579 |
2.91e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.28 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHEEQLKEAQAVPATL-PELEATKASLKKLRAQAEAqqptfdalrdeLRGAQEVGERLQQRHGERDVEVERWRE 1156
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPA-----------WLAAQDALERLREQSGEALADSQEVTA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1157 RVAQLLERWQAVLAQTD---VRQRELEQLGRQLRYYRESADP--------LGAWL----------QDA----RRRQEQIQ 1211
Cdd:COG3096 631 AMQQLLEREREATVERDelaARKQALESQIERLSQPGGAEDPrllalaerLGGVLlseiyddvtlEDApyfsALYGPARH 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1212 AMPLADSQAVREQLRQEQALLEE---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKV 1282
Cdd:COG3096 711 AIVVPDLSAVKEQLAGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEEL 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1283 QSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQ 1362
Cdd:COG3096 791 RAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLD 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1363 AEREAKELQQRMQEEVV---------RREEAAVD---AQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERSRLRIE 1428
Cdd:COG3096 868 QLKEQLQLLNKLLPQANlladetladRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAK 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1429 EEIRVVRLQLEATE--RQR------GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKA 1500
Cdd:COG3096 948 EQQRRLKQQIFALSevVQRrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS 1027
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1501 EAEAAREKQRALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--KRASFAEKTAQLER 1571
Cdd:COG3096 1028 RDAKQQTLQELEQELEELGVQAdAEAEERARirrdelHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQER 1107
|
....*...
gi 2462619853 1572 SLQEEHVA 1579
Cdd:COG3096 1108 EQVVQAKA 1115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4364-4402 |
3.24e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.24e-10
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 4364 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 4402
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
22-118 |
3.71e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 60.28 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 22 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 87
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 2462619853 88 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 118
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
897-1517 |
4.43e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 897 EEQRQALHSLELHYQAFLRDSQDAggfgpeDRLMAEREYgscsHHYQQLLQSLEQGAQEESRCQRcisELKDIRLQLEAC 976
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERL------AELEYLRAA----LRLWFAQRRLELLEAELEELRA---ELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 977 ETRtvhrlrlpldkeparecaQRIAEQQKAQAEVEGLGKGVARLSAeaekvlalpepspaaptLRSELELTLGKLEQVRS 1056
Cdd:COG4913 315 EAR------------------LDALREELDELEAQIRGNGGDRLEQ-----------------LEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1057 LSAIYLEKLKTISLVIRGTqgaeevlrahEEQLKEAQA-VPATLPELEATKASLKKLRAQAEAQqptFDALRDELRGAQE 1135
Cdd:COG4913 360 RRARLEALLAALGLPLPAS----------AEEFAALRAeAAALLEALEEELEALEEALAEAEAA---LRDLRRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1136 VGERLQQRHGERDVEVERWRERVAQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----RYYRE 1191
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppEHYAA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1192 SAdplgAWLQDARRRQE-QIQAMPLADSQAVREQLrQEQALLEEIErhgEKVEECQRFAKQYINAIKDYELqlvtykaql 1270
Cdd:COG4913 501 AL----RWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLD---FKPHPFRAWLEAELGRRFDYVC--------- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1271 epVASPAkkpkvqsgsesviqeyvDLRTHYSELTT--LTSQyikfiSETLRRMEEEERL---------AEQQRAEERERL 1339
Cdd:COG4913 564 --VDSPE-----------------ELRRHPRAITRagQVKG-----NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAEL 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1340 AEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmqEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeAEIQAKARQAEA 1419
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1420 AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE--AERLRRQVQDESQRKRQAEVElASR 1497
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERELRENLE-ERI 775
|
650 660
....*....|....*....|
gi 2462619853 1498 VKAEAEAAREKQRALQALEE 1517
Cdd:COG4913 776 DALRARLNRAEEELERAMRA 795
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1715-2452 |
4.86e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.15 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1715 RLQREAAAATQKRQELEAELAKVRAEMEVLLASKA-------RAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL- 1786
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIyrvhrtlRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1787 -------AEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR 1856
Cdd:TIGR00618 133 hdllkldYKTFTRVVLLPQGEFAQflkAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1857 LEEQAAQHKADIEERLAQLRKASDSELERQKGLVE--DTLRQRRQVEEEILALKASFEKAAAGKAELEL---ELGRIRSN 1931
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqeRINRARKA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1932 AEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2011
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRA-----KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2012 QLQLAQeaaqkrlQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEA 2091
Cdd:TIGR00618 368 REISCQ-------QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2092 ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQ------------------ 2153
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscihpnparqdi 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2154 -----TLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEA-------ARQRSQVEEELFSVRVQMEEL---- 2217
Cdd:TIGR00618 521 dnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsfsilTQCDNRSKEDIPNLQNITVRLqdlt 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2218 ---SKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQE---------AARLRQLAEEDLAQQRA 2283
Cdd:TIGR00618 601 eklSEAEDMLACEQHALLrkLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqervrehALSIRVLPKELLASRQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2284 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEdkeqmaQQLAEETQGFQRTLEAERQRQLEMSAEAER-- 2361
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE------IENASSSLGSDLAAREDALNQSLKELMHQArt 754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2362 -LKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAtQEKVTLVQTLEIQRQQ-----------SDHDAERLREAI 2429
Cdd:TIGR00618 755 vLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEIGQeipsdedilnlQCETLVQEEEQF 833
|
810 820
....*....|....*....|...
gi 2462619853 2430 AELEREKEKLQQEAKLLQLKSEE 2452
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEE 856
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
499-688 |
5.42e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.46 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 499 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 575
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 576 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 652
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462619853 653 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 688
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
14-121 |
7.82e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 59.52 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 14 EDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYL 87
Cdd:cd21222 8 DEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 2462619853 88 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 121
Cdd:cd21222 88 EDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1079-1269 |
7.83e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.08 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1079 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1158
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1159 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1237
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|..
gi 2462619853 1238 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1269
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1328-1526 |
8.60e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1328 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREeaavdAQQQKrsiQEELQQLRQSS 1406
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1407 EAEIQAKARQAEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDESQR 1486
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462619853 1487 KRQAEV-ELASRVKAEAEAAREKQRALQALEELRLQAEEAE 1526
Cdd:PRK09510 218 KAAAEAkAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1674-1888 |
1.08e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1674 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEE 1753
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1754 ESRSTSEKSKQRLEA--EAGRFRELA--------EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1823
Cdd:COG4942 98 ELEAQKEELAELLRAlyRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1824 RLKTEAEIALKE----KEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKASDSELERQKG 1888
Cdd:COG4942 178 ALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPA 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1080-1857 |
1.46e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1080 EVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERva 1159
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1160 qlLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLRQEQALLE----EI 1235
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1236 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKK-------PKVQSGSESVIQEYVDLRTHYSELTT 1305
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1306 LTSQYikfisETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQA-------EREAKELQ 1371
Cdd:PRK04863 518 LRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1372 QRMQEEVVRREE--AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATErQRGGAE 1449
Cdd:PRK04863 593 ARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSE 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1450 GE-LQALRARA--------------EEA-------------------EAQKRQAQE-----------------------E 1472
Cdd:PRK04863 672 DPrLNALAERFggvllseiyddvslEDApyfsalygparhaivvpdlSDAAEQLAGledcpedlyliegdpdsfddsvfS 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1473 AERLRRQV-QDESQRK----RQAEVELASRvkaeaeAAREKQralqaLEELRLQAEEAERRLRQAEVERaRQVQVALETA 1547
Cdd:PRK04863 752 VEELEKAVvVKIADRQwrysRFPEVPLFGR------AAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAF 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1548 QR------------SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlKA 1615
Cdd:PRK04863 820 SRfigshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA----DR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1616 NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--------------LAEGT 1681
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahFSYED 975
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1682 AQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRQELEAELAK--VRAEMEVL 1744
Cdd:PRK04863 976 AAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAE 1055
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1745 LASKARAEE---------ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAARQRAEAERV 1811
Cdd:PRK04863 1056 ERARARRDElharlsanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRL 1134
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 1812 LAEKLAAiGEATRLKTEAEI---ALKEKEAENERLR---RLAEDEAFQRRRL 1857
Cdd:PRK04863 1135 HRRELAY-LSADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRPERKV 1185
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1344-1568 |
1.99e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.90 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1344 AALEKQRQLAEAHAQAKAQAEREAKELQQrmQEEVvrREEAAVDAQQQKRSIQEELQ---QLRQSSEAEIQAKARQAEAA 1420
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1421 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEVELASRVK 1499
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1500 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1568
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1318-1538 |
2.03e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1318 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQE 1397
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1398 ---ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1474
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1475 RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1538
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2245-2686 |
2.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2245 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2321
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2322 RLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlRVAEMSRAQ--ARAEE--DAQRFRKQAEEIGEKLHRT 2397
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdaKKAEAvkKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2398 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQalQQSFLSEKD 2477
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKADEAKKKAEEA--KKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2478 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvaSMEEARRRQHEAEEGVRRKQEELQQLEQqr 2557
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK--KKEEAKKKADAAKKKAEEKKKADEAKKK-- 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2558 rqqeellAEENQRLREQLQLLEEQHRAA---LAHSEEVTASQVAATKtlpngrdaldgpaaeAEPEHSFDGLRRKVSAQR 2634
Cdd:PTZ00121 1400 -------AEEDKKKADELKKAAAAKKKAdeaKKKAEEKKKADEAKKK---------------AEEAKKADEAKKKAEEAK 1457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 2635 LQEAGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLLLKATNEK 2686
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
14-120 |
2.79e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 57.51 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 14 EDERDrvqKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLR 88
Cdd:cd21299 1 ETSRE---ERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 2462619853 89 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 120
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
136-238 |
3.16e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.39 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 136 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 214
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPgLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 2462619853 215 PEDVDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1411-1632 |
3.41e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1411 QAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1490
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1491 EVELASRVKAEAEAAREKQR-ALQALEELRLQAEEAERRLRQAE-VERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1568
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1569 LERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQK 1632
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1324-1575 |
3.72e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.04 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1324 EERLAEQQRaEERERLAEVEAALEKQR---QLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQ 1400
Cdd:PRK05035 456 EARQARLER-EKAAREARHKKAAEARAakdKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1401 QLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1480
Cdd:PRK05035 535 AEKQAAAAADPKKAAVAAAIARAKAKKAA-------QQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQV 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1481 QDESQRKrqaevelasrVKAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEVERARQVQVALETAQRSAEAELQSKR 1559
Cdd:PRK05035 608 AEVDPKK----------AAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAEDPKK 677
|
250
....*....|....*.
gi 2462619853 1560 ASFAEKTAQLERSLQE 1575
Cdd:PRK05035 678 AAVAAAIARAKAKKAA 693
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1666-1897 |
3.76e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.79 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1666 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1745
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1746 AsKARAEEESRSTSEKSKQRLEAEAGRFRelAEEAARLRAlAEEAKRQRQLAE---EDAARQRAEAER-VLAEKLAAIGE 1821
Cdd:TIGR02794 124 A-KAKQAAEAKAKAEAEAERKAKEEAAKQ--AEEEAKAKA-AAEAKKKAEEAKkkaEAEAKAKAEAEAkAKAEEAKAKAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1822 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 1897
Cdd:TIGR02794 200 AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1079-1738 |
4.25e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 63.27 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1079 EEVLRAHEEQLKE-----AQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVER 1153
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1154 WRERV-------AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLR 1226
Cdd:pfam01576 417 LQARLseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLR-QLE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1227 QEQALLEEieRHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESVIQEY-------- 1293
Cdd:pfam01576 496 DERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaayd 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1294 -----------------VDLRTHYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAH 1356
Cdd:pfam01576 570 klektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR-AEAEAREKETRALSLAR 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1357 A-----QAKAQAEREAKELQQRMQEEVVRR----------EEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR-----Q 1416
Cdd:pfam01576 644 AleealEAKEELERTNKQLRAEMEDLVSSKddvgknvhelERSKRALEQQVEEMKTQLEELEDELQATEDAKLRlevnmQ 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1417 A-------------EAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAERL 1476
Cdd:pfam01576 724 AlkaqferdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKL 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1477 RRQVQDesqrkRQAEVELASRVKAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEVERAR-QVQVALETAQRS 1550
Cdd:pfam01576 804 QAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGKS 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1551 AeaeLQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELE-----RWQL-KANEALRLRLQ 1624
Cdd:pfam01576 879 A---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQksesaRQQLeRQNKELKAKLQ 955
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1625 AEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIRL 1695
Cdd:pfam01576 956 EMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQL 1035
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2462619853 1696 RAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR 1738
Cdd:pfam01576 1036 KRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1469-2004 |
4.36e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1469 AQEEAERLRRQVQDESQRKR---QAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRqAEVERARQVQVALE 1545
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1546 TAQRSAEAELQSKRAsFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQA 1625
Cdd:PRK03918 242 ELEKELESLEGSKRK-LEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1626 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRA 1697
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1698 ETEQGEQQRQLLEEELAR--LQREAAAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR-----------S 1757
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytaelK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1758 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLAEKLAAIGEAT 1823
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1824 RLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SDSELERQKGLVE 1891
Cdd:PRK03918 543 SLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1892 DTLRQRRQVEEEILALKASFEKAaagKAELElELGRIRSnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSL 1971
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590
....*....|....*....|....*....|...
gi 2462619853 1972 AAEEEAARQRKAALEEVERLKAKVEEARRLRER 2004
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
994-1579 |
4.70e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.05 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 994 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKLEQVRSlsaiyleklktiSLVI 1072
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLSESVS------------EARE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1073 RGTQgaeevLRAHEEQLK-EAQAVPATLPELEATKASLKKLRAQAEAQQPTFDAL-----------------RDELRGAQ 1134
Cdd:PRK04863 580 RRMA-----LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVteymqqllerereltveRDELAARK 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1135 EV----GERLQQRHGERDveverwrERVAQLLERWQAVLAQTDVRQRELEQLGrqlrYYResadplgAWLQDARrrqeqi 1210
Cdd:PRK04863 655 QAldeeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YFS-------ALYGPAR------ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1211 QAMPLADSQAVREQLRQEQALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK-- 1281
Cdd:PRK04863 711 HAIVVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKri 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1282 --VQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRAEERERLAEVEAALEKQRQLAE 1354
Cdd:PRK04863 789 eqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLE 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1355 AHAQAKAQAEREAKE--------LQQRM---QEEVVRREEAAVDAQQQKRSI-------------QEELQQLRQSSEaei 1410
Cdd:PRK04863 869 QAKEGLSALNRLLPRlnlladetLADRVeeiREQLDEAEEAKRFVQQHGNALaqlepivsvlqsdPEQFEQLKQDYQ--- 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1411 QAKARQAEAaeRSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKR 1488
Cdd:PRK04863 946 QAQQTQRDA--KQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYN 1019
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1489 QAEVELASRVKAEAEAAREkqrALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--KR 1559
Cdd:PRK04863 1020 QVLASLKSSYDAKRQMLQE---LKQELQDLGVPAdSGAEERARarrdelHARLSANRSRRNQLEKQLTFCEAEMDNltKK 1096
|
650 660
....*....|....*....|
gi 2462619853 1560 ASFAEKTAQLERSLQEEHVA 1579
Cdd:PRK04863 1097 LRKLERDYHEMREQVVNAKA 1116
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4286-4323 |
5.46e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 5.46e-09
10 20 30
....*....|....*....|....*....|....*...
gi 2462619853 4286 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4323
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1389-1933 |
6.06e-09 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 62.35 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1389 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1466
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1467 RQAQEEAERLRRQVQDESQRKRQAEVELASrVKAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEVERAr 1538
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1539 QVQVALETAQRS-AEAELQSKRASFA--EKTAQLERSLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLKA 1615
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1616 NEALRLRLQAEEVAQQKSlaqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1692
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1693 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1772
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1773 frelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1850
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1851 AFQR-------------RRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAG 1917
Cdd:pfam05701 466 DSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKEG 544
|
570
....*....|....*.
gi 2462619853 1918 KAELELELGRIRSNAE 1933
Cdd:pfam05701 545 KLAAEQELRKWRAEHE 560
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
131-233 |
6.65e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 131 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 209
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPgLCPDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 2462619853 210 TRLLDPEDVDVPQPDEKSIITYVS 233
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1312-1560 |
6.92e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.09 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1312 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQ 1391
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1392 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGEL-QALRARAEEAEAQKRQAQ 1470
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAeKKARQRQELQQAREEQIE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1471 EEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1550
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
250
....*....|
gi 2462619853 1551 AEAELQSKRA 1560
Cdd:pfam13868 327 RRERIEEERQ 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1200-1583 |
7.10e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1200 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK 1279
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1280 PKVQSGSESVIQEYVDLRTHYSELTTLtsqyikfiSETLRRMEEEERLAEQQRAEERERL-AEVEAALEKQRQLAEAHAQ 1358
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELREL--------EEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1359 AKAQAEREAKELQQRMQ--EEVVRREEAAVDAQQQKRSIQEELQQLRQSS------------------------------ 1406
Cdd:COG4717 207 RLAELEEELEEAQEELEelEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1407 --EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDE 1483
Cdd:COG4717 287 alLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLeLLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1484 SQRKRQAEVELASRVKAEaEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFA 1563
Cdd:COG4717 367 ELEQEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420
....*....|....*....|
gi 2462619853 1564 EKTAQLERSLQEEHVAVAQL 1583
Cdd:COG4717 446 EELEELREELAELEAELEQL 465
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1714-1875 |
7.13e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.43 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1714 ARLQREAAAAtQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRalAEEAKRQ 1793
Cdd:COG2268 206 AEAERETEIA-IAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIA--EANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1794 RQLAEEDAARQR------AEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1867
Cdd:COG2268 279 VQRQLEIAEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAI 358
|
....*...
gi 2462619853 1868 IEERLAQL 1875
Cdd:COG2268 359 LLMLIEKL 366
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1693-1998 |
8.12e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.89 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1693 IRLRA-ETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1765
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1766 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlaeklaaigeatrlkteAEIALKEKEAENERLRR 1845
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1846 LAEDEAFQRRrleeqaaqhkadieerlAQLRKASdselerQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELEL 1925
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAA------QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1926 grIRSNAEDTLRSKEQAELEAARQRQLAAeeerrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 1998
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1399-1952 |
1.20e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 61.80 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1399 LQQLRQSSEAEIQAKARQAEAAERSRlrieeeiRVVRLQLEATER--QRGGAEGELQALRaRAEEAEAQKRQAQEEAERL 1476
Cdd:COG3899 677 EARGPEPLEERLFELAHHLNRAGERD-------RAARLLLRAARRalARGAYAEALRYLE-RALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1477 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV-QVALETAQRSAEAEL 1555
Cdd:COG3899 749 LELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFgELALALAERLGDRRL 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1556 QSK-RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1634
Cdd:COG3899 829 EARaLFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAA 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1635 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1714
Cdd:COG3899 909 AAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAA 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1715 RLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR 1794
Cdd:COG3899 989 AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAAL 1068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1795 QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1874
Cdd:COG3899 1069 LAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAA 1148
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1875 LRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 1952
Cdd:COG3899 1149 LLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLL 1226
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1138-1445 |
1.31e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1138 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdvRQRELEqlgRQLRYYRESAdplgawlQDARRRQEQIQAMPLAD 1217
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1218 SQAVREQLRQEQALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1290
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1291 QEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKEL 1370
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1371 QQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAeAAERSRLRIEEEIRVVRLQLEATERQR 1445
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1630-1825 |
1.45e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.21 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1630 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1709
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1710 EEELARLQREAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1789
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462619853 1790 AKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1825
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1329-1562 |
1.52e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1329 EQQRAEERERLAEVEAALEKQrqLAEAHAQAkAQAEREAKELQQrmQEEVVRREEAAVDAQQQKRSIQEELQQLrQSSEA 1408
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQ--LPELRKEL-EEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEA-RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1409 EIQAKARQAEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkr 1488
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1489 qaeveLASRVKAEAEAAREKQRALQALEE------LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1562
Cdd:COG3206 314 -----ILASLEAELEALQAREASLQAQLAqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
131-238 |
1.68e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 131 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 209
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPgLCPDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 2462619853 210 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1496-2093 |
2.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1496 SRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1575
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1576 EHVAVAQLreeaerraqqqaeaerareeaerelerwqlkanEALRLRLQAEEVAQQKSLAqaeaekqkeeaerearrrgK 1655
Cdd:COG4913 318 LDALREEL---------------------------------DELEAQIRGNGGDRLEQLE-------------------R 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1656 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAeteQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1735
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1736 KVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGrfrelaEEAARLRALAEEAkrqrQLAEEDAARQRAeAERVL--- 1812
Cdd:COG4913 423 ELEAEIASLERRKSNIPARL----LALRDALAEALG------LDEAELPFVGELI----EVRPEEERWRGA-IERVLggf 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1813 ----------AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAED-------------EAFQRRRLEEQAAQHKADIE 1869
Cdd:COG4913 488 altllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfRAWLEAELGRRFDYVCVDSP 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1870 ERLAQLRKA-------SDSELERQKG----------LVEDTLRQRRQVEEEILALKASFEKAAAGKAELelelgrirsna 1932
Cdd:COG4913 568 EELRRHPRAitragqvKGNGTRHEKDdrrrirsryvLGFDNRAKLAALEAELAELEEELAEAEERLEAL----------- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1933 edtlrskeQAELEAARQRQLAAEEERRRREAEERVQkslAAEEEAARQRkaalEEVERLKAKVEEARRLRERAE--QESA 2010
Cdd:COG4913 637 --------EAELDALQERREALQRLAEYSWDEIDVA---SAEREIAELE----AELERLDASSDDLAALEEQLEelEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2011 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEE 2090
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAALGDAVERELRENLEERIDALR 779
|
...
gi 2462619853 2091 AER 2093
Cdd:COG4913 780 ARL 782
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1043-1497 |
2.22e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1043 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLK-------KLRAQ 1115
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelperleELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1116 AEAQQPTFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1195
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1196 LGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEecqrfakqyinAIKDYELQLVTYKAQLEPVAS 1275
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL-----------FLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1276 PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEA 1355
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1356 HAQAKAQAEREAKELQQRmQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS-EAEIQAKARQAEAAERSRLRIEEEIRVV 1434
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1435 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAEV-ELASR 1497
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPPVlERASE 523
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1667-1854 |
2.36e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1667 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevllA 1746
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE-----A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1747 SKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVlAEKLAAIGEATRLK 1826
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAEAK 224
|
170 180
....*....|....*....|....*...
gi 2462619853 1827 TEAEIALKEKEAENERLRRLAEDEAFQR 1854
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
140-235 |
2.60e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 55.77 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 140 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNL-----------------------EN 195
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 196 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 235
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1336-1805 |
2.61e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.42 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1336 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAqqqkrsiqeelqQLRQSSEAEIQAKAR 1415
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRA------------ALRWALAHGDAELAL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1416 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELA 1495
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1496 SRvkAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1575
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1576 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1655
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1656 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1735
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1736 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1805
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1828-2277 |
2.70e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1828 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILAL 1907
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1908 KASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEE 1987
Cdd:COG4717 145 PERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSL---------ATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1988 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAA 2067
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2068 EEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAAlRQKQAADAEMEKH 2147
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2148 KKFA------EQTLRQKAQVEQELTTLRLQLEETDHQ-KNLLDEELQRLKAEATEAARQR-SQVEEELFSVRVQMEELSK 2219
Cdd:COG4717 374 ALLAeagvedEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 2220 LKARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEED 2277
Cdd:COG4717 454 ELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
23-117 |
2.80e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 54.65 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 23 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 94
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 2462619853 95 VNIRNDDIADGNPKLTLGLIWTI 117
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2251-2454 |
2.90e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2251 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2326
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2327 KEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2406
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462619853 2407 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2454
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1655-1862 |
2.90e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAel 1734
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1735 akvRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1813
Cdd:COG4942 119 ---QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462619853 1814 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1862
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1319-1580 |
3.20e-08 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 59.28 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1319 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaqakAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1398
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLL-------LQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1399 LQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaEGELQALRARAEEAEaQKRQAQEEAERLRR 1478
Cdd:pfam15558 94 SRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALR---EQNSLQLQERLEEAC-HKRQLKEREEQKKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1479 QVQDESQR-KRQA-EVELASRVKAEAEAARE--KQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1554
Cdd:pfam15558 170 QENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEER 249
|
250 260
....*....|....*....|....*.
gi 2462619853 1555 LQSKRASFAEKTAQLERSLQEEHVAV 1580
Cdd:pfam15558 250 QEHKEALAELADRKIQQARQVAHKTV 275
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1658-2080 |
3.40e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1735
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1736 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--------------- 1800
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1801 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASD 1880
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1881 SELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTLRSKEQAELEAARQRQLAAEEERR 1959
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1960 RREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQlQLAQEAAQKRLQAEEKAHAFAVQQK 2038
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRELAEEWAALKL 497
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2462619853 2039 EQElqqtlqqeqsVLDQLRGeaeaarraaeeaeearvQAERE 2080
Cdd:COG4717 498 ALE----------LLEEARE-----------------EYREE 512
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1316-1569 |
3.49e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.78 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1395
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1396 QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1475
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1476 LRRQVQDESQRKRQAEVELASRVKaEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1555
Cdd:pfam13868 206 LRAKLYQEEQERKERQKEREEAEK-KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
250
....*....|....
gi 2462619853 1556 QSKRASFAEKTAQL 1569
Cdd:pfam13868 285 RMKRLEHRRELEKQ 298
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1389-1570 |
3.93e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1389 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqleaterqrggaegelqalraraEEAEAQKRQ 1468
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1469 AQEEAER-LRRQVQDESQRKRQAEvelASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER---ARQVQVAL 1544
Cdd:PRK09510 120 AEEAAKQaALKQKQAEEAAAKAAA---AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAA 196
|
170 180
....*....|....*....|....*.
gi 2462619853 1545 ETAQRSAEAELQSKRASFAEKTAQLE 1570
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1024-1519 |
4.46e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1024 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEaqaVPATLPELE 1103
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1104 ATKASLKKLRAQAEAQQpTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLG 1183
Cdd:PRK03918 280 EKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1184 RQLRYYRE------------------SADPLGAWLQDARRRQEQIQAmPLADSQAVREQLRQEQALL----EEIERHGEK 1241
Cdd:PRK03918 359 ERHELYEEakakkeelerlkkrltglTPEKLEKELEELEKAKEEIEE-EISKITARIGELKKEIKELkkaiEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1242 VEECQR---------FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTHYSELTTLTSQYIK 1312
Cdd:PRK03918 438 CPVCGRelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES---ELIKLKELAEQLKELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1313 FISETLRRMEEE-----ERLA-----------EQQRAEERE-RLAEVEAAL-EKQRQLAEAHAQAKAQAEREAKELQQRM 1374
Cdd:PRK03918 515 YNLEELEKKAEEyeklkEKLIklkgeikslkkELEKLEELKkKLAELEKKLdELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1375 Q--EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGE 1451
Cdd:PRK03918 595 KelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRE 674
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1452 LQALRARAEEAEAQKRQAQEEAERLRRQVqdESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1519
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1101-1859 |
4.71e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.85 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1101 ELEATKASLKKLRAQAEAQQPTFDALRDELRgaqevgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELE 1180
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1181 Q-LGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEEcqRFAKQYINAikdy 1259
Cdd:pfam12128 333 AfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD--KLAKIREAR---- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1260 ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYvDLRTHYSELTTLTSQYIkFISETLRRMEEEERLAEQQRAEERERL 1339
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQAT-ATPELLLQLENFDERIERAREEQEAAN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1340 AEVEAAlekQRQLAEAHAQAKAQAEReakelqqrmqeevVRREEAAVdaQQQKRSIQEELQQLRQSSEAEIQAKARQAEA 1419
Cdd:pfam12128 485 AEVERL---QSELRQARKRRDQASEA-------------LRQASRRL--EERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1420 AERSRLRIEEEIRVVRLQL--EATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQV-----QDESQRKRQAEV 1492
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLdpEVWDGSVGG-ELNLYGVKLDLKRIDVPEWAASEEELRERLDKaeealQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1493 ELASRVKAEAEAAREKQRALQALEelrlQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQskraSFAEKTAQLERS 1572
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALK----NARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN----SLEAQLKQLDKK 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1573 LQeehvavaqlreeaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQkslaqaeaekqKEEAEREARR 1652
Cdd:pfam12128 698 HQ-------------------------------AWLEEQKEQKREARTEKQAYWQVVEG-----------ALDAQLALLK 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1653 RGKAEEQAVRQRELAEQELEKQRQLAE-GTAQQRLAA-EQELIRLRAETEQGEQQRQLLeEELARLQREaaAATQKRQEL 1730
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASlGVDPDVIAKlKREIRTLERKIERIAVRRQEV-LRYFDWYQE--TWLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1731 EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlaeeakRQRQLAEEDAARQRAEAER 1810
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANSEQAQG 886
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1811 VLAEKLAAiGEATRLKTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 1859
Cdd:pfam12128 887 SIGERLAQ-LEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1655-1810 |
4.76e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.32 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1734
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1735 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EAARLRALAEEAKRQRQLAeedAARQRAEAER 1810
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEAAKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1170-1936 |
5.33e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1170 AQTDVRQRE---LEQLGRQLR---YYRESADPLGA-WLQDARRRQEQIQAMPLAdSQAVREQLRQeqALLEEIERHGEKV 1242
Cdd:pfam15921 128 AMADIRRREsqsQEDLRNQLQntvHELEAAKCLKEdMLEDSNTQIEQLRKMMLS-HEGVLQEIRS--ILVDFEEASGKKI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1243 EECQRFAKQYINA--------IKDYELQLVTYKAQLEPVAS--PAKKPKVQSGSESVIQEYVD-----LRTHYSELTTLT 1307
Cdd:pfam15921 205 YEHDSMSTMHFRSlgsaiskiLRELDTEISYLKGRIFPVEDqlEALKSESQNKIELLLQQHQDrieqlISEHEVEITGLT 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1308 SQ-------------YIKFISET--------LRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQ-AKAQAE 1364
Cdd:pfam15921 285 EKassarsqansiqsQLEIIQEQarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSElTEARTE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1365 REA---------KELQQRMQEEVVRREEAAVDAQQQKR--------SIQ---------------EELQQLRQSSEAEIQA 1412
Cdd:pfam15921 365 RDQfsqesgnldDQLQKLLADLHKREKELSLEKEQNKRlwdrdtgnSITidhlrrelddrnmevQRLEALLKAMKSECQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1413 KARQAEAAERSRLRIEEEIRVVRLQLEATErqrggaegelQALRARAEEAEAqKRQAQEEAERLRRQVQDESQRKRQAeV 1492
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTK----------EMLRKVVEELTA-KKMTLESSERTVSDLTASLQEKERA-I 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1493 ELASrvkaeAEAAREKQRALQALEELR-LQAEEAERRLRQAEVErARQVQVA-----LETAQRSAEAELQ-------SKR 1559
Cdd:pfam15921 513 EATN-----AEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECE-ALKLQMAekdkvIEILRQQIENMTQlvgqhgrTAG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1560 ASFAEKtAQLERSLQEEHVAVAQLreEAERRAQQQAEAERAREEAERELERWQLKANEALRLRlQAEEVAQQ-------- 1631
Cdd:pfam15921 587 AMQVEK-AQLEKEINDRRLELQEF--KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR-AVKDIKQErdqllnev 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1632 KSLAQAEAEKQKEEAEREARRRGKAEEQAVRQREL------AEQELEKQRQL------AEGTAQQ-RLAAEQELIRLRAE 1698
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmqlksAQSELEQTRNTlksmegSDGHAMKvAMGMQKQITAKRGQ 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1699 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVraemevllaskarAEEESRSTSEkskqrLEAEAGRFRELAE 1778
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV-------------ATEKNKMAGE-----LEVLRSQERRLKE 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1779 EAARLRALAEEAkrQRQLAEEDAARQRAEAERVlaeklaaigeatRLKTEAEIALKEKEA----ENERLR-RLAEDEAFQ 1853
Cdd:pfam15921 805 KVANMEVALDKA--SLQFAECQDIIQRQEQESV------------RLKLQHTLDVKELQGpgytSNSSMKpRLLQPASFT 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1854 RRRLEEQAAQHKADIEERLAQlrkasdseleRQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAE---LELELGRIRS 1930
Cdd:pfam15921 871 RTHSNVPSSQSTASFLSHHSR----------KTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEdkgRAPSLGALDD 940
|
....*.
gi 2462619853 1931 NAEDTL 1936
Cdd:pfam15921 941 RVRDCI 946
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1124-1556 |
5.48e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1124 DALRDELRGAQEVGERLQQRHGERDVEVERWRE-----------RVAQLLERWQAV---LAQTDVRQRELEQLGRQLRYY 1189
Cdd:PRK04863 743 DSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgraarekRIEQLRAEREELaerYATLSFDVQKLQRLHQAFSRF 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1190 RES-------ADPLGAWLQDARRRQEQIQAMPLADSQAVR-----EQLRQEQALLEEI---------ERHGEKVEECQ-- 1246
Cdd:PRK04863 823 IGShlavafeADPEAELRQLNRRRVELERALADHESQEQQqrsqlEQAKEGLSALNRLlprlnlladETLADRVEEIReq 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1247 --------RFAKQYINAIkdyelqlvtykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKF 1313
Cdd:PRK04863 903 ldeaeeakRFVQQHGNAL-----------AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHF 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1314 -ISETLRRMEEEERLAEQQRAeereRLAEVEAALEKQRqlaEAHAQAKAQAeREAKELQQRMQEEVVRreeaavdAQQQK 1392
Cdd:PRK04863 972 sYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERTRAR---EQLRQAQAQL-AQYNQVLASLKSSYDA-------KRQML 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1393 RSIQEELQQL--RQSSEAEIQAKARQAEaaersrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1470
Cdd:PRK04863 1037 QELKQELQDLgvPADSGAEERARARRDE--------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1471 EEAE-------RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKqrALQALeelrlqaeeaerRLRQAEVERARQVQVA 1543
Cdd:PRK04863 1109 EQVVnakagwcAVLRLVKDNGVERRLHRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRL 1174
|
490
....*....|...
gi 2462619853 1544 LETAQRsAEAELQ 1556
Cdd:PRK04863 1175 SEDPKR-PERKVQ 1186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1474-1950 |
7.44e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1474 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERArqvqvalETAQRSAEA 1553
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-------ELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1554 ELQSKRASFAEKTAQLERSLQEEHVAVAQLreeaerraqqqaeaERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1633
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEEL--------------EERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1634 LAQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL 1713
Cdd:COG4717 188 LATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1714 ARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ 1793
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1794 RQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEER 1871
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1872 LAQLRKASDSELERQKGLVEDTLRQR-RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR 1950
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1400-1567 |
8.25e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1400 QQLRQSsEAEIQAKARQAEAAERSRLRIEEeiRVVRLQLEATERQrggaegelqalrARAEEAEAQKRQAQEEA-----E 1474
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAARE------------ARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1475 RLR-RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1553
Cdd:PRK05035 494 RVKaKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170
....*....|....
gi 2462619853 1554 ELQSKRASFAEKTA 1567
Cdd:PRK05035 574 EVDPKKAAVAAAIA 587
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4017-4053 |
9.60e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 9.60e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 4017 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4053
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1655-2028 |
9.95e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.96 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1734
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1735 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1812
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1813 AEKLAAIGEatrlKTEAEIALKEKEAENERLRRLaedeafqrrrleeqaaQHKADIEERLAQLRKASDSELERQKGLVED 1892
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFL----------------DQKRGHPEVKSQNGEEEVTKLKVTTKRRQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1893 TLRQRRQVEEEilalkasfekaAAGKAELELELGRIR-SNAEdtlrsKEQAELEAARQRQLAAEEERRRREAEERVQKSL 1971
Cdd:pfam02029 229 GLSQSQEREEE-----------AEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1972 AAEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2028
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1321-1574 |
1.01e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.24 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1321 MEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1399
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1400 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVR-----------LQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1468
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekeeereedERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1469 ---AQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALE 1545
Cdd:pfam13868 188 rlrAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
|
250 260
....*....|....*....|....*....
gi 2462619853 1546 TAQRSAEAELQSKRASFAEKTAQLERSLQ 1574
Cdd:pfam13868 268 RKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
9-123 |
1.16e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 53.85 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 9 TLRSGEDERDRvqkkTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQ 81
Cdd:cd21331 15 TLLEGETREER----TFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCN 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462619853 82 IALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 123
Cdd:cd21331 89 YAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1339-1751 |
1.46e-07 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 58.33 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1339 LAEVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE----------- 1407
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1408 --------AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1479
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1480 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKR 1559
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1560 ASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1639
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1640 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1719
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 2462619853 1720 AAAATQKRQELEAELAKVRAEMEVLLASKARA 1751
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1329-2008 |
1.55e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1329 EQQRAEERERLAEVEAALEKQRQLAE---AHAQAKAQAEREAKELQQRM------------------QEEVVRREEAAVD 1387
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNeikALKSRKKQMEKDNSELELKMekvfqgtdeqlndlyhnhQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1388 AQQQKRSIQEELQQLRQSS---EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG----------------GA 1448
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfhtlvieRQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1449 EGELQALRARAEEAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRlq 1521
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRdekkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1522 aeEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAR 1601
Cdd:TIGR00606 482 --KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHS 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1602 EEAERELERWQLKAnealrlrlQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE-LAEQELEKQRQLAEG 1680
Cdd:TIGR00606 560 DELTSLLGYFPNKK--------QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDV 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1681 TAQQrlAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKAR 1750
Cdd:TIGR00606 632 CGSQ--DEESDLERLKEEIEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1751 AEEESRSTSEKSKQRLEAEAGRF-----------RELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAA 1818
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLApgrqsiidlkeKEIPELRNKLQKVNRDIQRLKNdIEEQETLLGTIMPEEESAKVCLT 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1819 -IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD------------IEERLAQLR--KASDSEL 1883
Cdd:TIGR00606 790 dVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQhlKSKTNEL 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1884 ERQKGLVEDTLRQRRQVEE-------EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEE 1956
Cdd:TIGR00606 870 KSEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEK 949
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 1957 ERRRREAEERVQKSLaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2008
Cdd:TIGR00606 950 VKNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2225-2452 |
1.96e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2225 EAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLS-----VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA 2299
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2300 TRLKAEAELLQQQK-ELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2378
Cdd:COG4913 319 DALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2379 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE-LEREKEKLQQEAKLLQLKSEE 2452
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1753-2038 |
2.07e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1753 EESRSTSEKSKQ----RLEAEagRFRELAEEAARlralaeEAKRQRQLAEEDAARQrAEAERvlaeKLAAIGEATRLKTE 1828
Cdd:pfam17380 279 QHQKAVSERQQQekfeKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1829 AE-----IALKEKEAENERLRR--LAEDEAFQRR--RLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTL----- 1894
Cdd:pfam17380 346 RErelerIRQEERKRELERIRQeeIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVemeqi 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1895 ---------RQRRQVEEEilaLKASFEKAAAGKAELELELGRIRSNAEDtlRSKEQAELEAARQRQLAAEEERRRREAEE 1965
Cdd:pfam17380 426 raeqeearqREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1966 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHAFAVQQK 2038
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMERE 574
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1514-1952 |
2.12e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 57.72 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1514 ALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ---------LR 1584
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1585 EEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1664
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1665 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVL 1744
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1745 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATR 1824
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1825 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEI 1904
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462619853 1905 LALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 1952
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1456-1576 |
2.20e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.80 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1456 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaevELASRVKAEAEAAREKQRAlqaleELRLQAE----EAERRLRQ 1531
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKA-----EERREAEtaraEAEAAYEI 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462619853 1532 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEE 1576
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAE 315
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1408-1540 |
2.29e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 56.21 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1408 AEIQAKARQAEAAersrlrieeeIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------R 1478
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 1479 QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1540
Cdd:COG1566 148 QELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1316-1538 |
2.67e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.01 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQkr 1393
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1394 siqeelqqlrqsseaeiQAKARQAEAAersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE- 1472
Cdd:TIGR02794 146 -----------------EEAAKQAEEE--------------AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1473 ---AERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1538
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1342-1561 |
2.82e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.01 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1342 VEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAE 1421
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKL----EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1422 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEAERLRRQVQDESQRKRQAEVELASRVKAE 1501
Cdd:TIGR02794 114 AEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKA-KAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1502 AEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRAS 1561
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGA 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2144-2447 |
2.90e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2144 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKAR 2223
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2224 IEAENRAL------ILRDKDNTQRFLQEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2295
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2296 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLeaerqrqlemsaeaERLKLRVAEMSRAQAR 2375
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI--------------EELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 2376 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2447
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1667-1882 |
2.93e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1667 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLA 1746
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1747 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1815
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1816 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSE 1882
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
2-129 |
3.19e-07 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 52.75 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2 SGLEGRGTLRSGEDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----E 68
Cdd:cd21325 10 SELSSEGTQHSYSEE----EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 69 KGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 129
Cdd:cd21325 86 KKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1765-1951 |
3.48e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1765 RLEAEAGRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1840
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1841 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAS 1910
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462619853 1911 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 1951
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1323-1507 |
3.49e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1323 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAKELQQRMqeevvrrEEAAVDAQQQKRSIQEELQQL 1402
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRA-------AAAAKKAAAEAKKKAEAEAAK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1403 RQSSEAEIQAKARQAEAAersrlrieeeirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1482
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKA------------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 2462619853 1483 ESQRKRQAEVELASRVKAEAEAARE 1507
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1322-1487 |
3.83e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.62 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1322 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQ 1401
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1402 LRQSSEAEIQAKARQAEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1470
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 2462619853 1471 EEAERLRRQVQDESQRK 1487
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1804-2194 |
4.40e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1804 QRAEAERVLAEKLAAIgEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasDSEL 1883
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1884 ERQKglVEDTLRQRRQVEEEILALKASFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAARQRQLAaeeerrrre 1962
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1963 aeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHafavQQKEQE 2041
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLR----QQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2042 LQQTLQQEQSVLDQLRGEAEAARRAaeeaeearvqaEREAAQSRRQVEEAERlKQSAEEQAQARAQAQAAAEKLRKEAEQ 2121
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEEQRRKIL-----------EKELEERKQAMIEEER-KRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 2122 EaarraqaeqaalRQKQaadAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKNLLDEELQRLKAEAT 2194
Cdd:pfam17380 541 E------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1654-1896 |
4.48e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.11 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1654 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRQEL 1730
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1731 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1810
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1811 VLAEKlaaigeatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASDSELERQKGL 1889
Cdd:pfam15709 447 AEAEK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 2462619853 1890 VEDTLRQ 1896
Cdd:pfam15709 516 AQEQARQ 522
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1703-1878 |
4.69e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1703 EQQRQLLEEELAR-LQREAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1781
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1782 RLRALAEeakrqrQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1861
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 2462619853 1862 AQHKADIEERLAQLRKA 1878
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
2-128 |
4.98e-07 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 51.97 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2 SGLEGRGTLRSGEDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----E 68
Cdd:cd21323 10 SAISSEGTQHSYSEE----EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainK 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 69 KGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 128
Cdd:cd21323 86 KKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2235-2584 |
5.04e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2235 DKDNTQRFLQEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEKmlkEKMQAVQEATRLKAEAELLQQQKE 2314
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDRQ---AAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2315 LAQEQARRLQEDKEQMAQQLAEETQGFQ--RTLEAERQRQlEMSAeAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2392
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQmeRQQKNERVRQ-ELEA-ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2393 -KLHRTELATQEKVTLVQTLEIQRQqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqllqetqaLQQS 2471
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQ---QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-----------LEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2472 FLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAQQLREEQQRQqqqmeqerqrlvasmEEARRRQHEAEEGvRRKQEELQ 2551
Cdd:pfam17380 501 LEERKQAMIEEER-----KRKLLEKEMEERQKAIYEEERRREA---------------EEERRKQQEMEER-RRIQEQMR 559
|
330 340 350
....*....|....*....|....*....|...
gi 2462619853 2552 QLEQQRRQQeellaEENQRLREQLQLLEEQHRA 2584
Cdd:pfam17380 560 KATEERSRL-----EAMEREREMMRQIVESEKA 587
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1374-1542 |
6.60e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 55.92 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1374 MQEEVVRREEAAVDAQQQkrsiqeELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQ 1453
Cdd:COG1193 497 LPEEIIERARELLGEESI------DVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK-------E 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1454 ALRARA-EEAEAQKRQAQEEAERLRRQVQDEsqrkrqaevelasrvKAEAEAAREKQRALQALEElRLQAEEAERRLRQA 1532
Cdd:COG1193 564 EILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAK 627
|
170
....*....|
gi 2462619853 1533 EVERARQVQV 1542
Cdd:COG1193 628 PAKPPEELKV 637
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2280-2581 |
6.78e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2280 QQRALAEKMLKEKMQavqeatrlKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAEETQGfqrTLEAERQR-QLEMSA 2357
Cdd:pfam17380 280 HQKAVSERQQQEKFE--------KMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQA---AIYAEQERmAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2358 EAERLKLRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTELATQEKVTLV-QTLEIQRQQSDHDAERLREaIAELEREK 2436
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVrQELEAARKVKILEEERQRK-IQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2437 EKL---QQEAKLLQLK--SEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQ 2511
Cdd:pfam17380 423 EQIraeQEEARQREVRrlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2512 QRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRrqqeellaEENQRLREQLQLLEEQ 2581
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2156-2452 |
6.83e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2156 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILR- 2234
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERf 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2235 -----DKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAE-------------------------------EDL 2278
Cdd:PRK02224 401 gdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvetieedrervEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2279 AQQRALAE---KMLKEKMQAVQEATRLKAEAELLQQQKELAQE---QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2352
Cdd:PRK02224 481 EAELEDLEeevEEVEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2353 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK-------------QAEEIGEKL-HRTELATQEKVTLVQTLEIQRQ-Q 2417
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKReALAELNDERRERLAEKRERKRElE 640
|
330 340 350
....*....|....*....|....*....|....*
gi 2462619853 2418 SDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2452
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3698-3733 |
7.01e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.01e-07
10 20 30
....*....|....*....|....*....|....*.
gi 2462619853 3698 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3733
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1297-1430 |
7.35e-07 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 53.83 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1297 RTHYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreakelQQ 1372
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEE------LL 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1373 RMQEEVVRREEAAVDAQQQKRSIQEEL----QQLRQSSEAEIQAKARQAEAA-----ERSRLRIEEE 1430
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2140-2340 |
7.40e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2140 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEE--- 2216
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2217 --------LSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2288
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 2289 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQG 2340
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1897-2452 |
7.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1897 RRQVEEEILALKaSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEE 1976
Cdd:PRK03918 147 REKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1977 AARQRKaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL 2056
Cdd:PRK03918 225 KLEKEV---KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2057 RGEAEAARRAAEEAEEARvqaEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ 2136
Cdd:PRK03918 302 YEEYLDELREIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2137 KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE-----LFSVR 2211
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2212 VQMEELSKLKARIEAENRALiLRDKDNTQRFLQEEAE--KMKQVAEEAARLSvaaqeaARLRQLAEEDLAQQRALAEKML 2289
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKL-RKELRELEKVLKKESEliKLKELAEQLKELE------EKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2290 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2368
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2369 msRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2448
Cdd:PRK03918 612 --KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
....
gi 2462619853 2449 KSEE 2452
Cdd:PRK03918 688 RREE 691
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2293-2438 |
9.69e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.41 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2293 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLAEEtQGFQRTLEAERQRQLEMSAEAERLKL 2364
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2365 RVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2438
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4120-4148 |
1.04e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.04e-06
10 20
....*....|....*....|....*....
gi 2462619853 4120 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4148
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1714-2444 |
1.12e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1714 ARLQREAAAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1790
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1791 KRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIalkekEAENERLR---RLAEDEAfQRRRLEEQAAQH 1864
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRV-----QAENARLEmhfKLKEDHE-KIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1865 KADIEERLAQLRKASDSELERQKGL---VEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSkeq 1941
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1942 aeleaarQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV---EEARRLRERAEQESARQLQLAQE 2018
Cdd:pfam05483 312 -------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcslEELLRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2019 AAQKRLQAEEKAHAFAVQQKEQelqqtlqqeqsvLDQLRgeaeaarraaeeaeeaRVQAEREAA-QSRRQVEE-AERLKQ 2096
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE------------LEELK----------------KILAEDEKLlDEKKQFEKiAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2097 SAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEME--KHKKFAEQTLRQKAQVEQELTTLRLQLEE 2174
Cdd:pfam05483 437 KEQELIFLLQA---------------------------REKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2175 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELskLKARIEAENRALILRDKDNTQR--FLQEEAE---K 2249
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--LKQIENLEEKEMNLRDELESVReeFIQKGDEvkcK 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2250 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2329
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2330 MAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQ---------------ARAEEDAQRFRKQAEEIGEKL 2394
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSEL 727
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2395 HRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAK 2444
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2251-2455 |
1.19e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2251 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2330
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2331 AQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2410
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462619853 2411 LEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2455
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1311-1554 |
1.27e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1311 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQ 1390
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1391 QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE----EAEAQK 1466
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1467 RQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALET 1546
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*...
gi 2462619853 1547 AQRSAEAE 1554
Cdd:COG3883 258 AAGSAGAA 265
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1324-1951 |
1.30e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.19 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1324 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAKELQQRMQEEVVRREEA 1384
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1385 AVDAQQQKRSIQEELQQLRQ-SSEAEIQAKARQAEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1459
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1460 EEAEAQKRQAQEEAERLR---RQVQDESQRKRQAEVElasrvKAEAEAAREKQRALQALEELRLQAEEaerrlRQAEVER 1536
Cdd:PRK10246 410 EVAAALAQHAEQRPLRQRlvaLHGQIVPQQKRLAQLQ-----VAIQNVTQEQTQRNAALNEMRQRYKE-----KTQQLAD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1537 ARQVqvaleTAQRSAEAELQSKRASF-AEKTAQLERSlqEEHVAVAQLREEAERRAQQQAEAERAreeaerelERWQLKa 1615
Cdd:PRK10246 480 VKTI-----CEQEARIKDLEAQRAQLqAGQPCPLCGS--TSHPAVEAYQALEPGVNQSRLDALEK--------EVKKLG- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1616 NEALRLRLQAEEVAQQKSlaqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRL 1695
Cdd:PRK10246 544 EEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPW 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1696 RAETEQGEQQRQLLEEELArLQREAAAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAE 1769
Cdd:PRK10246 602 LDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1770 AGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAIGEATrLKTEAEIALKEKEAENERlRRLAE- 1848
Cdd:PRK10246 681 QNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKa 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1849 ----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASDSELERQKGLVEdtlrQRRQVEEEILALKASFEKAAAGKAE 1920
Cdd:PRK10246 751 qaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQ 826
|
650 660 670
....*....|....*....|....*....|....*.
gi 2462619853 1921 LELEL----GRIRSNAEDTLRSKEQAELEA-ARQRQ 1951
Cdd:PRK10246 827 IQQELaqlaQQLRENTTRQGEIRQQLKQDAdNRQQQ 862
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1353-1567 |
1.51e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1353 AEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEI- 1431
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAEIEERREELg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1432 -RVVRLQ------------------------LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1486
Cdd:COG3883 90 eRARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1487 KRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKT 1566
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
.
gi 2462619853 1567 A 1567
Cdd:COG3883 250 G 250
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1011-1578 |
1.72e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1011 EGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLK 1090
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQE--QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1091 EAQAvpaTLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERlqQRHGERDVEVERWRERVAQLLERWQavla 1170
Cdd:TIGR00606 482 KAER---ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL--NHHTTTRTQMEMLTKDKMDKDEQIR---- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1171 qtDVRQRELEQLGRQLRYYRESADpLGAWLQDARRRQEQIQ------AMPLADSQAVREQLR-QEQALLEEIERHGEKVE 1243
Cdd:TIGR00606 553 --KIKSRHSDELTSLLGYFPNKKQ-LEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINnELESKEEQLSSYEDKLF 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1244 EcqrfakqyINAIKDYELQLVTYKAQLEpvaSPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYIKFISETLR 1319
Cdd:TIGR00606 630 D--------VCGSQDEESDLERLKEEIE---KSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1320 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrreeAAVDAQQQKRSIQEEL 1399
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK-------VNRDIQRLKNDIEEQE 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1400 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1479
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1480 VQDESQRKRQAEV---ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAEAELQ 1556
Cdd:TIGR00606 852 IQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAK-EQDSPLETFLEKDQQEKEELIS 930
|
570 580
....*....|....*....|..
gi 2462619853 1557 SKRASfaEKTAQLERSLQEEHV 1578
Cdd:TIGR00606 931 SKETS--NKKAQDKVNDIKEKV 950
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2156-2441 |
1.76e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2156 RQKAQVEQELTTLRLQLeeTDHQknlldeelQRLKAEATEAArQRSQVEEELFSVRVQME----ELSKLKARIEAenraL 2231
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQ--------QALDVQQTRAI-QYQQAVQALERAKQLCGlpdlTADNAEDWLEE----F 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2232 ILRDKDNTQRFLQEE-----AEKMKQVAEEAARL------SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKE 2291
Cdd:PRK04863 448 QAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQ 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2292 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEEtqgfqrtLEAERQRQLEMSAEAERLKLRVAE-MS 2370
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAA 600
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2371 RAQA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLREAIAELEREKEKLQQ 2441
Cdd:PRK04863 601 RAPAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2135-2591 |
1.78e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2135 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQ--LEETDHQKnllDEELQRLKAEATEAARQRSQVEEELFSVRV 2212
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQ---EIHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2213 QMEELSKLKARIEAENRAL-ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2291
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELdILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2292 KMQAVQEATRLKAEAE-LLQQQKELAQEQARRLQEDKEQ------------MAQQLAEETQGFQRTLEAERQRQLEMSAE 2358
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEqIHLQETRKKAVVLARLLELQEEpcplcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2359 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTelaTQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2438
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS---KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2439 LQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDsllqrerfiEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQM 2518
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER---------VREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 2519 EQERQRLVASMEEARRRQHEAEEGVRRkqeELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE 2591
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDR---EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE 761
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1287-1523 |
1.80e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1287 ESVIQEYVDLRThySELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ---RQLAEAHAQ-AKAQ 1362
Cdd:COG3206 155 NALAEAYLEQNL--ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKlllQQLSELESQlAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1363 AEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAtE 1442
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHPDVIALRAQIAALRAQLQQ-E 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1443 RQRGGAEGELQALRARAEEAEAQKRQAQeeaerLRRQVQDESQRkrqaEVELAsRVKAEAEAAREK-QRALQALEELRLQ 1521
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQ-----LEARLAELPEL----EAELR-RLEREVEVARELyESLLQRLEEARLA 380
|
..
gi 2462619853 1522 AE 1523
Cdd:COG3206 381 EA 382
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1669-1826 |
1.87e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 54.25 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1669 QELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqrEAAAATQKRQELEAELAKVRAemevllAS 1747
Cdd:PTZ00491 647 DSLQKSVQLAiEITTKSQEAAARHQAELLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES------SG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1748 KARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLK 1826
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI-EATKFE 791
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3903-3940 |
2.41e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.41e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2462619853 3903 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3940
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1324-1571 |
2.62e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.88 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1324 EERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQAKAQaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR 1403
Cdd:pfam05667 210 ERNAAELAAAQEWEEEWNSQGL---ASRLTPEEYRKRKR-TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1404 QSSEAEIQAK-------------ARQAEAAERS-----------RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1459
Cdd:pfam05667 286 GSSTTDTGLTkgsrfthteklqfTNEAPAATSSpptkveteeelQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1460 EEAEAQKRQAQEEAERLRRQVQ------------DESQRKRQAEVELASRVKAEAEAAREKQRA--LQALEELRL----Q 1521
Cdd:pfam05667 366 KQVEEELEELKEQNEELEKQYKvkkktldllpdaEENIAKLQALVDASAQRLVELAGQWEKHRVplIEEYRALKEaksnK 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1522 AEEAERRLRQAEVERARQVQVAletaqrsaeAELQSKRASFAEKTAQLER 1571
Cdd:pfam05667 446 EDESQRKLEEIKELREKIKEVA---------EEAKQKEELYKQLVAEYER 486
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1314-2221 |
2.66e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1314 ISETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreAKELQQRMQEEVVRREEAAVDaqqqkr 1393
Cdd:TIGR00606 178 IFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQIT--SKEAQLESSREIVKSYENELD------ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1394 siqeelqqlrqsseaEIQAKARQAEAAERSRLRIEEEIRvvrlQLEATERQRGGAEGELQALraRAEEAEAQKRQAQEEA 1473
Cdd:TIGR00606 249 ---------------PLKNRLKEIEHNLSKIMKLDNEIK----ALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLY 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1474 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER-ARQVQVALETAQRSAE 1552
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIqSLATRLELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1553 AELQSKRASFAEKtaqleRSLQEEHVAVAQLREeaerraqqqaeaerareeaerelerwQLKANEALRLRlQAEEVAQQK 1632
Cdd:TIGR00606 388 SERQIKNFHTLVI-----ERQEDEAKTAAQLCA--------------------------DLQSKERLKQE-QADEIRDEK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1633 SLAQAEAEKqkeeaerearrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAE---------TEQGE 1703
Cdd:TIGR00606 436 KGLGRTIEL-------------KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERElskaeknslTETLK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1704 QQRQLLEEELARLQREAAAATQKRQELEAElAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL 1783
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1784 RALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEI----ALKEKEAENERLRRLAEDEAFQRRRLE 1858
Cdd:TIGR00606 580 HSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEKSSKQRAMLA 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1859 EQAAQHKADIEER---------LAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKaaagKAELELELGRIR 1929
Cdd:TIGR00606 660 GATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK----RRDEMLGLAPGR 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1930 SNAEDtLRSKEQAELEAARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2008
Cdd:TIGR00606 736 QSIID-LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2009 SaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2087
Cdd:TIGR00606 815 L-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2088 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEK--------HKKFAEQTLRQKA 2159
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLK 973
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 2160 QVEQELTTLRLQLEETDHQKNLLDEELqRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2221
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDM-RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1303-1540 |
2.70e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1303 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAKELQQrMQEEVVR 1380
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1381 REEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggAEGELQALRAR-A 1459
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1460 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEaAREKQRALQALEELrlqAEEAERRLRQAEVERARQ 1539
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVAREL---YESLLQRLEEARLAEALT 384
|
.
gi 2462619853 1540 V 1540
Cdd:COG3206 385 V 385
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
1-118 |
2.78e-06 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 49.97 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1 MSGLEGRGTLRSGEDErdrvQKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---- 67
Cdd:cd21292 9 TSEASSEGTTHSYSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErain 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 68 EKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 118
Cdd:cd21292 85 KKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2136-2321 |
3.24e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.49 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2136 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKNLLDEELQRLKAEAteaarqrSQVEEELFSVRVQME 2215
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2216 ELSKLKARIEaenRAL-ILRDKDNT----QRFLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2287
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462619853 2288 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2321
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2780-2816 |
4.30e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 4.30e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 2780 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 2816
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1126-1557 |
4.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1126 LRDELRGAQEVGERLQQRHGERDV-EVERWRERVAQLLERwQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAR 1204
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1205 RRQEQIQAMpladsQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLepvaSPAKKPKVQS 1284
Cdd:COG4717 126 QLLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL----SLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1285 GSESVIQEYVDLRTHYSELTTLTSQyIKFISETLRRMEEE-ERLAEQQRAEERERLAEVEAAL----------------- 1346
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEE-LEELEEELEQLENElEAAALEERLKEARLLLLIAAALlallglggsllslilti 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1347 -EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsIQEELQQLRQSSEAEIQAKARQAEAAERSRL 1425
Cdd:COG4717 276 aGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE-LLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1426 RIEEEIRVVRLQLEATERQ----RGGAEGElQALRARAEEAEaQKRQAQEEAERLRRQVQDE-SQRKRQAEVELASRVKA 1500
Cdd:COG4717 355 EAEELEEELQLEELEQEIAallaEAGVEDE-EELRAALEQAE-EYQELKEELEELEEQLEELlGELEELLEALDEEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1501 EAEAAREKQRALQAlEELRLQAEEAERRLRQAEVERARQVQvALETAQRSAEAELQS 1557
Cdd:COG4717 433 ELEELEEELEELEE-ELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRE 487
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2234-2389 |
5.17e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2234 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2310
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2311 QQKELAQEQARRLQEDKE---QMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRaqaRAEEDAQRF---- 2383
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 2462619853 2384 -RKQAEE 2389
Cdd:pfam15709 512 aMKQAQE 518
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1693-2580 |
5.18e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1693 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1770
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1771 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdE 1850
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1851 AFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQkglvedtlrQRRQVEEeilalkasfeKAAAGKAELELELGRIRS 1930
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1931 NAEdtLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2010
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2011 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL-RGEAEAARRAAEEAEEARVQAEREAAQSRRQVE 2089
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2090 EAERLKQSAEEQAQARAQAQAAAEKlRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR 2169
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2170 LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELsklkarieaenralilrdkdntQRFLQEEAEK 2249
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------------------QDLTEKLSEA 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2250 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlkekmqavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQ 2329
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA-----------LKLTALHALQLTLTQERV--REHALSIRVLPKE 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2330 MAQQlaeetqgfqrtleaerqrqlemsaeaerlklrvaemsraQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2409
Cdd:TIGR00618 674 LLAS---------------------------------------RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2410 TLEIQRQQSdhdAERLREAIAELEREKEKLQQEAKLLQlksEEMQTVQQEQLLQETQALQQSFLsekdsLLQRERFIEQE 2489
Cdd:TIGR00618 715 EYDREFNEI---ENASSSLGSDLAAREDALNQSLKELM---HQARTVLKARTEAHFNNNEEVTA-----ALQTGAELSHL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2490 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQ 2569
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
890
....*....|.
gi 2462619853 2570 RLREQLQLLEE 2580
Cdd:TIGR00618 864 LTQEQAKIIQL 874
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1720-1951 |
5.22e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1720 AAAATQKRQELEAELAKVRAEMEVL---LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1796
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1797 AEEDAARQRAEAERVLAeKLAAIGEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRlEEQAAQHKADIEErLAQLR 1876
Cdd:COG4942 95 LRAELEAQKEELAELLR-ALYRLGRQPPLA-----LLLSPEDFLDAVRRLQYLKYLAPAR-REQAEELRADLAE-LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1877 KASDSELERQKglvedtlRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 1951
Cdd:COG4942 167 AELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
943-1482 |
5.27e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 943 QQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRI-AEQQKAQAEVEGLGKGVARLS 1021
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLcKELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1022 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRGTQGAEEVLRAHEEQLKEAQAVpaTLPE 1101
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1102 LEATKASLKKLRAQAEAQQPTFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1172
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1173 DVRQRELEQLGRQLRYYRESADPLGAWLQDARR---RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfa 1249
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1250 kQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAE 1329
Cdd:TIGR00618 643 -LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1330 QQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAEREAKELQQRMQEEVV------RREEAAVDAQQQKRSIQEELQQL 1402
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAalqtgaELSHLAAEIQFFNRLREEDTHLL 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1403 RQsSEAEIQAKARQAEAAersRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1482
Cdd:TIGR00618 802 KT-LEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1655-1949 |
5.40e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRQE 1729
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1730 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1786
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1787 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 1866
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDES 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1867 DIEERlaqlRKASDSELERQKGLVEDtlrqrrqVEEEILALKASFEKAAAGKaelelelgrirsNAEDtLRSKEQAELEA 1946
Cdd:NF012221 1778 DKPNR----QGAAGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG-LTEQEQEALEG 1833
|
...
gi 2462619853 1947 ARQ 1949
Cdd:NF012221 1834 ATN 1836
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1329-1511 |
5.72e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1329 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAavdaqqqkrsiqeELQQLRQSSEA 1408
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-------------EEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1409 EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkr 1488
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE--- 166
|
170 180
....*....|....*....|...
gi 2462619853 1489 qaevELASRVKAEAEAAREKQRA 1511
Cdd:COG1579 167 ----ELAAKIPPELLALYERIRK 185
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3371-3403 |
5.72e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 5.72e-06
10 20 30
....*....|....*....|....*....|...
gi 2462619853 3371 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 3403
Cdd:pfam00681 7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1383-1582 |
5.86e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.77 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1383 EAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvRLQLEATERQrggaeGELQALRARAEEA 1462
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ----RAAAEKAAKQ-----AEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1463 EAQKRQAQEEAErlrrqvqdesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL---RQAEVERARQ 1539
Cdd:TIGR02794 120 QAEEAKAKQAAE-----------AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462619853 1540 VQValETAQRSAEAElQSKRASFAEKTAQLERSLQEEHVAVAQ 1582
Cdd:TIGR02794 189 AKA--EEAKAKAEAA-KAKAAAEAAAKAEAEAAAAAAAEAERK 228
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1729-2386 |
6.01e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1729 ELEAELAKVRAEMEVLLAskaraEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1808
Cdd:pfam15921 246 QLEALKSESQNKIELLLQ-----QHQDRIEQLISEHEVEITG-----LTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1809 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASDSELERQKG 1888
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1889 LVEDTLRQRRQVEEEIlalkasfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAARQrqlaaeeerrrrEAEERVQ 1968
Cdd:pfam15921 393 LSLEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1969 KSLAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQL-AQEAAQKRLQAEEKAHAFAVQQKEQELQQTL 2046
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLeSSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2047 QQEQSVLDQLRgeaeaaRRAAEEAEEARVQAEREAAqsRRQVEEAERLKQsaeeqaqaraqaqaaaeklrkeaeqeaarr 2126
Cdd:pfam15921 524 SRVDLKLQELQ------HLKNEGDHLRNVQTECEAL--KLQMAEKDKVIE------------------------------ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2127 aqaeqaALRQKQAADAEM-EKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQV-- 2203
Cdd:pfam15921 566 ------ILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvn 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2204 --EEELFSVRVQMEELSKLKARIE---------AENRALILRDKDNTQRFLQEEAEKMK------QVAEEAARLSVAAQE 2266
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKtsrnelnslSEDYEVLKRNFRNKSEEMETTTNKLKmqlksaQSELEQTRNTLKSME 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2267 AARLRQLAEEDLAQQRALAEK----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaEETQGF 2341
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKRgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQ 798
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2462619853 2342 QRTLeaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2386
Cdd:pfam15921 799 ERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1687-1782 |
6.10e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.03 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1687 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1766
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 2462619853 1767 EAEAGRFrELAEEAAR 1782
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1349-1477 |
6.22e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.59 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1349 QRQLAEAHAQ-AKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKArQAEAAERSRLRI 1427
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1428 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1477
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1494-1742 |
6.32e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1494 LASRVKAEAEAAREKQRALQALEElRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1573
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1574 QEEHVAVAQLREEAERRAQQQAEAerareeaerelerWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1653
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1654 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlaaeqeliRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1733
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 2462619853 1734 LAKVRAEME 1742
Cdd:COG4942 229 IARLEAEAA 237
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
131-238 |
6.37e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 131 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 209
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPgLCPDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 2462619853 210 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 238
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
8-128 |
7.01e-06 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 48.85 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 8 GTLRSGEDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRF 74
Cdd:cd21324 16 GTQHSYSEE----EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPF 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 75 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 128
Cdd:cd21324 92 TIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1355-1843 |
7.05e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1355 AHAQAKAQAEREAKELQQR------MQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERsrlr 1426
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAkaaktpAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDnfPKLSAELRQQLNNER---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1427 ieEEIRVVRLQLEAterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRrQVQDESQRKRQAEVElASRVKAEAEaar 1506
Cdd:PRK10929 93 --DEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAR-EISDSLSQLPQQQTE-ARRQLNEIE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1507 ekqRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSA--EAELQSKRASFAEK-TAQLERSLQeehvavaql 1583
Cdd:PRK10929 158 ---RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1584 reeaerraqqqaeaerareeaerelerwqlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgkaeeqavRQ 1663
Cdd:PRK10929 226 ----------------------------------ALRNQLNSQ-----------------------------------RQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1664 RElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQK-RQELEA------ELAK 1736
Cdd:PRK10929 237 RE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlreqsqWLGV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1737 VRAEMEVLLASKARAEEESRStsekskQRLEAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAE 1814
Cdd:PRK10929 315 SNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDA 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2462619853 1815 KLAA---------------IGEATRLK---TEAEIALKE-KEAENERL 1843
Cdd:PRK10929 384 QLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1308-2035 |
7.76e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.45 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1308 SQYIKFIS---ETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQAEREA---KELQQRMQEEVVRR 1381
Cdd:pfam07111 62 SQQAELISrqlQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1382 EeaavdAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSrlrieeeirvvrlqLEATERQRGGAEGELQalraraee 1461
Cdd:pfam07111 141 E-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQLA-------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1462 aeaqkrQAQEEAERLRRQVQdESQRKRQAEVELASRVKaeaeaareKQRALQALEELRLQAEEAERRLRQAEVERARQVQ 1541
Cdd:pfam07111 194 ------EAQKEAELLRKQLS-KTQEELEAQVTLVESLR--------KYVGEQVPPEVHSQTWELERQELLDTMQHLQEDR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1542 VALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQLKANeALRL 1621
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSL-----------------LNRWREKVF-ALMV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1622 RLQAEEVAQQKSLAQAEAEKQKEEAEREarrrGKAEEQAVRQRELaeqelekqrqlaegtaqQRLAAEQELIRLRAETEQ 1701
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAELQEQVT----SQSQEQAILQRAL-----------------QDKAAEVEVERMSAKGLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1702 GEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSekskQRLEAEAGRFRELAEEAA 1781
Cdd:pfam07111 380 MELSRA--QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS----NRLSYAVRKVHTIKGLMA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1782 RLRALAEeaKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1861
Cdd:pfam07111 454 RKVALAQ--LRQESCPPPPPAPPVDADLSLELEQLRE--ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1862 AQHKADIEERLAQLRKASDSELERQKGLVED--TLRQRRQVEEEILAlKASFEKAAagkaelELELgRIRSNAEDTLRsk 1939
Cdd:pfam07111 530 EQELQRAQESLASVGQQLEVARQGQQESTEEaaSLRQELTQQQEIYG-QALQEKVA------EVET-RLREQLSDTKR-- 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1940 eqaeleaarqrqlaaeeerRRREAEERVQK---SLAAEEEAARQRKAALEEVERLK--AKVEEARRLRERAEQ-ESARQL 2013
Cdd:pfam07111 600 -------------------RLNEARREQAKavvSLRQIQHRATQEKERNQELRRLQdeARKEEGQRLARRVQElERDKNL 660
|
730 740
....*....|....*....|..
gi 2462619853 2014 QLAQEAAQKRLQAEEKAHAFAV 2035
Cdd:pfam07111 661 MLATLQQEGLLSRYKQQRLLAV 682
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2143-2580 |
8.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2143 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA------EATEAARQRSQVEEELFSVRVQMEE 2216
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2217 LSKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2294
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2295 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2369
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2370 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-EAKL 2445
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2446 LQLKSEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQqrqqqqmeqerqrl 2525
Cdd:PRK03918 542 KSLKKELEK--------------LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER-------------- 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 2526 VASMEEARRRQHE---AEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE 2580
Cdd:PRK03918 594 LKELEPFYNEYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
596-688 |
8.59e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 596 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 675
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 2462619853 676 ALQTQWSWMLQLC 688
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2134-2336 |
8.85e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2134 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQknLLDEELQRLKAEATEAARQRSQVEEELFSVRVQ 2213
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2214 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAArlrqlaeEDLAQQRAlaekmlkekm 2293
Cdd:COG4913 325 LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA-------EEFAALRA---------- 387
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462619853 2294 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE 2336
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3071-3107 |
8.88e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 8.88e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 3071 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 3107
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1658-1949 |
9.48e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.61 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRQEL 1730
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1731 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1809
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1810 rvlaEKLAAIGEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SDSELERQ 1886
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1887 KGLVEDTLRQRRQVEEEILALKASFEKAAagkAELELELGRIRSNaedtlRSKEQAELEAARQ 1949
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQAN---RRLKEELQRERAE-----RALAQGALEIARE 399
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3439-3475 |
1.01e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 1.01e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 3439 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 3475
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1204-1536 |
1.02e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1204 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGE---KVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKP 1280
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1281 KVQSG-SESVIQEYVDlrthysELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERER---LAEVEAALEKQRQLAEAH 1356
Cdd:pfam07888 121 LAQRAaHEARIRELEE------DIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERkqlQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1357 AQAK-AQAEREAKELQqrMQEEVVRREEAAVDAQQQKRSIQEELQQLR------QSSEAEIQAKARQAEAAERSRLRIEE 1429
Cdd:pfam07888 195 QELRnSLAQRDTQVLQ--LQDTITTLTQKLTTAHRKEAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1430 EIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREK 1508
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
330 340
....*....|....*....|....*...
gi 2462619853 1509 QRALQALEELRLQAEEAERRLRQAEVER 1536
Cdd:pfam07888 353 DCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1872-2394 |
1.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1872 LAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELelgrirsnaedtlRSKEQAELEAARQRq 1951
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-------------LEEELEELEAELEE- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1952 laAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2031
Cdd:COG4717 114 --LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2032 AfAVQQKEQELQQTLQQEQSVLDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSA---EEQAQARAQA 2108
Cdd:COG4717 192 E-ELQDLAEELEELQQRLAELEEELE--EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaalLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2109 QAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQR 2188
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2189 LKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAENRALIlrdkdntqRFLQEEAEKMKQVAEEAARLSvaaqeaA 2268
Cdd:COG4717 349 LQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEEL--------RAALEQAEEYQELKEELEELE------E 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2269 RLRQLAEEDLAQQRALAEKMLKEKMQAVQEatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2348
Cdd:COG4717 410 QLEELLGELEELLEALDEEELEEELEELEE-----ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2462619853 2349 RQRQLEmsaEAERLKLRVAEMSRAQARAEEDAQ-RFRKQAEEIGEKL 2394
Cdd:COG4717 485 LRELAE---EWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1746-1945 |
1.20e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1746 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAIGEATRL 1825
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1826 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEIL 1905
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462619853 1906 ALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1945
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3905-3943 |
1.24e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.24e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3905 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3943
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
991-1583 |
1.25e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 991 EPARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISL 1070
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1071 VIRGTQGAEEVLRAHEEQLKEAQAVPATLPELeatkaslkklrAQAEAQQPTFDALRDELRG-----AQEVGERLQQRhg 1145
Cdd:PRK10246 317 NTRLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1146 erdveveRWRERVAQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLQDARRRQEQIQAmplADSQA 1220
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1221 VREQLRQEQALLEEIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1273
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1274 ASPAKKPKVQSGSESVIQEYVDLRthySELTTLTSQYIKFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1353
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1354 EAHAQAKAQAEREAKELQQRMQEEVVRREEAAvdAQQQKRSIQEELQQLRQSSEAEIQAKARQ--AEAAERSRL--RIEE 1429
Cdd:PRK10246 596 DDIQPWLDAQEEHERQLRLLSQRHELQGQIAA--HNQQIIQYQQQIEQRQQQLLTALAGYALTlpQEDEEASWLatRQQE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1430 EIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DESQRKRQAEVE 1493
Cdd:PRK10246 674 AQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQAQ 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1494 LASRVKAEAEAAREKQRALQALEELRLQAEEAERRLrqaevERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1573
Cdd:PRK10246 754 FDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQ 828
|
650
....*....|
gi 2462619853 1574 QEEHVAVAQL 1583
Cdd:PRK10246 829 QELAQLAQQL 838
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1001-1530 |
1.28e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1001 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRGTQGAEE 1080
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1081 VLRAHEEQLKEAQAVPATLPELEATKASLkklraQAEAQQpTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1160
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1161 LLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLQDARRRQEQIqamplADSQAVREQLRQEQALLEE 1234
Cdd:pfam05557 144 LKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI-----PELEKELERLREHNKHLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1235 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQSGSESVIQEYVDLRTHYSE 1302
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlRSPEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1303 LTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL----------------------AEAHAQA 1359
Cdd:pfam05557 299 NSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgyrailesydkeltMSNYSPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1360 KAQAEREAKELQQRMQeevVRREEAAVDAQQQKRSIQEELQQLrQSSEAEIQAKARQAEAAERSRLRIE-----EEIRVV 1434
Cdd:pfam05557 378 LLERIEEAEDMTQKMQ---AHNEEMEAQLSVAEEELGGYKQQA-QTLERELQALRQQESLADPSYSKEEvdslrRKLETL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1435 RLQLEATERQRGGAEGEL--QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRAL 1512
Cdd:pfam05557 454 ELERQRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533
|
570 580
....*....|....*....|....*..
gi 2462619853 1513 ---------QALEELRLQAEEAERRLR 1530
Cdd:pfam05557 534 pettstmnfKEVLDLRKELESAELKNQ 560
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1315-1565 |
1.29e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.41 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1315 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvrREEAAVDAQQQKRS 1394
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSW--EKEEKRDSRLGRYK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1395 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQ---------------------------RGG 1447
Cdd:pfam02029 130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVkdekikkekkvkyeskvfldqkrghpeVKS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1448 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK----RQAEVELASRvkaEAEAAREKQR-ALQALEEL---- 1518
Cdd:pfam02029 210 QNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKleelRRRRQEKESE---EFEKLRQKQQeAELELEELkkkr 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1519 ---RLQAEEAERRLRQAEVERarqvQVALETAQRSAEAELQSKRASFAEK 1565
Cdd:pfam02029 287 eerRKLLEEEEQRRKQEEAER----KLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1314-1519 |
1.32e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.44 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1314 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQK 1392
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1393 RSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1467
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1468 ------QAQEEAERLRRQV-QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1519
Cdd:COG1842 156 sgidsdDATSALERMEEKIeEMEARAEAAAELAAGDSLDDELAELEADSEVEDELAALK 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1281-1496 |
1.37e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1281 KVQSGSESVIQEYVDLRTHYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1355
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1356 --HAQAKAQAEREAKELQQRMQEevvRREEAavdaqQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIrv 1433
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAPA---RREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1434 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS 1496
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1654-2037 |
1.38e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.55 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1654 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1726
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1727 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1801
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1802 ARQRAEAERvlaeklaaiGEATRL---KTEAEIA---------LKEKEAENERLRRLAEDEAFQRRR---LEEQAAQHKA 1866
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAeeeakrradAKLKEAVEKNVATSEQDKPKRRAKrgvLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1867 DIEErlaqlrKASDSELERQKgLVEDTLRQRRQVEEEILALKASFEKAAAGKAE------------LELELgrirsnAED 1934
Cdd:NF033838 280 ENDA------KSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEI------AES 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1935 TLRSKEqAELEAARQRQLAAEEERRRREAEERVQKSLAAE---EEAARQRKAALEEVERlkaKVEEARRLRER-AEQ-ES 2009
Cdd:NF033838 347 DVKVKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKR---KAAEEDKVKEKpAEQpQP 422
|
410 420
....*....|....*....|....*....
gi 2462619853 2010 ARQLQLAQEAAQKRLQAEE-KAHAFAVQQ 2037
Cdd:NF033838 423 APAPQPEKPAPKPEKPAEQpKAEKPADQQ 451
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
18-117 |
1.38e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 47.27 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 18 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 93
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 2462619853 94 LVNIRNDDIADGNPKLTLGLIWTI 117
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1669-2057 |
1.41e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1669 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRQELEAELAKVRAEMEvlla 1746
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1747 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEaervlaeklaaigEATRLK 1826
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA-------------ELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1827 TEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrQVEEEILA 1906
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL--------FLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1907 LKASF---EKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1983
Cdd:COG4717 288 LLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1984 ALEEVERL--KAKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEK-AHAFAVQQKEQELQQTLQQEQSVLDQLR 2057
Cdd:COG4717 368 LEQEIAALlaEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGeLEELLEALDEEELEEELEELEEELEELE 445
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1328-1756 |
1.51e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.06 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1328 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1407
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1408 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1487
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1488 RQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTA 1567
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1568 QLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1647
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1648 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1727
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 2462619853 1728 QELEAELAKVRAEMEVLLASKARAEEESR 1756
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1655-1870 |
1.63e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.10 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ-------------LLEEEL 1713
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVikagarpdnsaviAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1714 ARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1793
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1794 RQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1870
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2246-2405 |
1.70e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2246 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2325
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2326 DKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2405
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1758-2029 |
1.82e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1758 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA-EIALKEK 1836
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1837 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfeKAAA 1916
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1917 GKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK-V 1995
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270
....*....|....*....|....*....|....
gi 2462619853 1996 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2029
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2151-2585 |
2.08e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2151 AEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRLKAEATEAARQRSQVEEELfSVRVQMEELSKLKARIEAENRA 2230
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2231 LI-LRDKDNTQRFLQEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2309
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2310 QQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARAEEDAQRFRKQAE 2388
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2389 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllqETQAL 2468
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---------IAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2469 QQSFLSEKDSLLQRERFIEQEKAKLEQLfqdEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVrrkqe 2548
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL----- 448
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462619853 2549 elqqleqqrrqqeellaeenQRLREQLQLLEEQHRAA 2585
Cdd:COG4717 449 --------------------EELREELAELEAELEQL 465
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2076-2448 |
2.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2076 QAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAAdaemEKHKKFAEQTL 2155
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----ELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2156 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQmEELSKLKARIEAENRALILRD 2235
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2236 KDNTQRFLQEE---------------AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLaqQRALAEKMLKEKMQAVQEAT 2300
Cdd:COG4717 264 LGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEEL--EELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2301 RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfqrTLEAERQRQLEMSAEAERLKLRVAEMSR--AQARAEE 2378
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDEEELRAALEQAEEYQELKEELEELEEqlEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 2379 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTL---------EIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2448
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEEELEELreelaeleaELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1405-1618 |
2.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1405 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1482
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1483 ESQRKRQAEV-------------ELASRVKAEAEAAREKQRALQALEELRLQAEEAerrlrQAEVERARQVQVALETAQR 1549
Cdd:COG3883 93 RALYRSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1550 SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1618
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1339-1433 |
2.25e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1339 LAEVEAALEKQRQLAEAHAQAKAQAEREAkelqQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR-QSSEAEIQAKARQA 1417
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 2462619853 1418 EAAERSRLRI---EEEIRV 1433
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1612-2030 |
2.45e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1612 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1691
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1692 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1771
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1772 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA 1851
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1852 FQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 1931
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1932 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2011
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 2462619853 2012 QLQLAQEAAQKRLQAEEKA 2030
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
16-124 |
2.46e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.52 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 16 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 86
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462619853 87 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 124
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1316-1553 |
2.67e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.98 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAEREAKelqqrmqeevvrreeAAVDAQQ 1390
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAK---------------AAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1391 QKRSIQEELQQLRQSSEAEIQAKARqAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqalRARAEEAEAQKRQAQ 1470
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAK-AKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA------KAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1471 EEAERlrrqvQDESQRKRQAEVELASRVKAEAeAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1550
Cdd:PRK07735 151 EEVTE-----EEEETDKEKAKAKAAAAAKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
...
gi 2462619853 1551 AEA 1553
Cdd:PRK07735 225 QGN 227
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1329-1456 |
2.68e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 49.50 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1329 EQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAKELQQRMQEEVVrreeaavdaQQQKRSIQEELQQLRQSSE 1407
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEaAEQERKLLEEQQRELEQKL---------EDQERSYEEHLRQLKEKME 247
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462619853 1408 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1456
Cdd:cd16269 248 EERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2137-2339 |
2.70e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2137 KQAADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDHQknlldeelqrlkAEATEAARQRSQVEEELF 2208
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2209 SVRVqmeELSKLKARIEA----------------ENRALILRDK-----DNTQRFLQEEAEKMKQ--------VAEEAAR 2259
Cdd:NF012221 1617 AVTK---ELTTLAQGLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2260 LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQ 2339
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1328-1489 |
2.73e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 50.29 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1328 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1407
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1408 AEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDESQRK 1487
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 2462619853 1488 RQ 1489
Cdd:PRK12678 216 EE 217
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1319-1434 |
2.83e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1319 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-EREAKELQQRMQEEVVRREEAAVD---------A 1388
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1389 QQQKR----SIQEELQQLRQSSEAEiqaKARQAEAAERsRLRIEEEIRVV 1434
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAE---EKARLEAEER-RQKEEEAARLA 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2259-2425 |
2.98e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2259 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2335
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2336 ------EETQGFQRTLEAERQRQLEMSAEAERLK-------LRVAEMSRAQAR----------AEEDAQRFRKQAEEIGE 2392
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKeillekveeeARHEAAVLIKEIEEEAK 183
|
170 180 190
....*....|....*....|....*....|....
gi 2462619853 2393 klhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2425
Cdd:PRK12704 184 -----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1976-2320 |
3.07e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1976 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2047
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2048 qeqsvLDQLRgEAEAARRAAEEAEEARVQAEREAAQSR--RQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQeaAr 2125
Cdd:pfam17380 362 -----LERIR-QEEIAMEISRMRELERLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE--A- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2126 raqaeqaalRQKQAADAEMEKhkkfaeqtlrqkaqvEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEE 2205
Cdd:pfam17380 433 ---------RQREVRRLEEER---------------AREMERVRLEEQERQQQ-------VERLRQQEEERKRKKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2206 ElfsvrvqmeelSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALA 2285
Cdd:pfam17380 482 E-----------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
330 340 350
....*....|....*....|....*....|....*....
gi 2462619853 2286 EKMLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2320
Cdd:pfam17380 551 RRRIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2143-2583 |
3.24e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2143 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEelfsVRVQMEELSKLKA 2222
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2223 RIEAENRALILRDKdNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqraLAEKMLKEKMQAVQEATRL 2302
Cdd:PRK03918 249 SLEGSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2303 KAEAELLQQQKELAQEQARRLQE--DKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLK-LRVAEMSRAQARAEED 2379
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEElkKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2380 AQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---------SDHDAERLREAIAELER-EKEKLQQEAKLLQLK 2449
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRiEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2450 SEEMQTvqqeqllqetqalqQSFLSEKDSLLQRERFIEQEKA---KLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLV 2526
Cdd:PRK03918 480 KELREL--------------EKVLKKESELIKLKELAEQLKEleeKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 2527 ASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHR 2583
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1208-1523 |
3.46e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1208 EQIQAMPLADSQAVREQLRQEQALLEEIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE 1287
Cdd:PRK10929 33 EQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1288 SVIQEYVDLRTHYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAer 1365
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1366 eakelqqrMQEEVVRReEAAVDaqqqkrsiQEELQQLRQSSEAEIqakAR-QAEAAERSRLRIEEEIRVVRLQLEaTERQ 1444
Cdd:PRK10929 178 --------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQALRNQLN-SQRQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1445 RggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL---ASRVKAEA----EAAREKQRALQALEE 1517
Cdd:PRK10929 237 R------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQALNT 304
|
....*.
gi 2462619853 1518 LRLQAE 1523
Cdd:PRK10929 305 LREQSQ 310
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1200-1424 |
3.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1200 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakk 1279
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1280 pKVQSGSESVIQEYVD-LRTHY-----SELTTLTSQyiKFISETLRRMEEEERLAEQQRA------EERERLAEVEAALE 1347
Cdd:COG4942 94 -ELRAELEAQKEELAElLRALYrlgrqPPLALLLSP--EDFLDAVRRLQYLKYLAPARREqaeelrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1348 KQRqlaeahaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQsSEAEIQAKARQAEAAERSR 1424
Cdd:COG4942 171 AER-------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAA 239
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1320-1538 |
3.69e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1320 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1399
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1400 QQLRQSSEAEIQAKARQAeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1479
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1480 VQDESQRKRQaevELASRVKAEAEAAREKQR---------ALQALEELRLQAEEAERRLRQAEVERAR 1538
Cdd:pfam05262 333 VAEDLQKTKP---QVEAQPTSLNEDAIDSSNpvyglkvvdPITNLSELVLIDLKTEVRLRESAQQTIR 397
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1624-1800 |
3.78e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.42 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1624 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1699
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1700 EQGEQQRQLLEEELArlQREAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1774
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 2462619853 1775 ELAEEAARLRALAEEAKRQRQLAEED 1800
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1660-2028 |
3.88e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1660 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--REAAAATQKRQELEA 1732
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1733 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvl 1812
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1813 aEKLAAIGEATRLKTEAEIALKEKEAenerlrrlaedeafqrrRLEEQAAQHKADIEERLaqlrkasdsELERQKGLVED 1892
Cdd:PRK04863 418 -QAVQALERAKQLCGLPDLTADNAED-----------------WLEEFQAKEQEATEELL---------SLEQKLSVAQA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1893 TLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR-QLAAEEERRRREAEERVQKSL 1971
Cdd:PRK04863 471 AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1972 AAEEEAARQRKAALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQAEE 2028
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2158-2710 |
3.89e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2158 KAQVEQELTTLRLQLEETDHQKNLLDEELQRlkaEATEAARQRSQVEEELFSVRVQMEELSKLKAriEAENRALILRDKD 2237
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2238 NTQ-RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2312
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2313 ----KELAQEQARRLQEDKEQMaQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQAE 2388
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2389 EIGEKLHRTElatQEKVTLVQT-------LEIQ----RQQSDHDAERLREAIAELEREKEK---LQQEAKLLQLKSEEMq 2454
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQArekeihdLEIQltaiKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKEL- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2455 TVQQEQLLQETQALQQSFLSEKDsllQRERFIEQekakLEQLFQDEVakaqqlreeqqRQQQQMEQERQRLVASMEEARR 2534
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKK---QEERMLKQ----IENLEEKEM-----------NLRDELESVREEFIQKGDEVKC 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2535 RQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE--QHRAALAHSEEVTASQVAATKTLPNGRDaLDG 2612
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLE-LEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2613 PAAEAEPEHSFDGLRRKVSAQRLQEAGIL--------SAEELQRLAQ------GHTTVDELARREDVRH----YLQGRSS 2674
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLeevekakaIADEAVKLQKeidkrcQHKIAEMVALMEKHKHqydkIIEERDS 725
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462619853 2675 IAGLLLKATNEKLSVYAALQRQLLSPGTALILLEAQ 2710
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2183-2389 |
3.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2183 DEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIlRDKDNTQRFLQEEAEKMKQVAEEAARLSV 2262
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2263 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2334
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2335 AEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2389
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2162-2391 |
4.49e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2162 EQELTTLRLQLEE----TDHQKNLLDEELQRLKAEATEAARQRS-----QVEEELFSVRVQMEELSKLKARI-EAENRal 2231
Cdd:COG3096 450 EQQATEEVLELEQklsvADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRLQQLRAQLaELEQR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2232 iLRDKDNTQRFLQEEAEKMKQVAEEAARLsvaaqeaarlrqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2311
Cdd:COG3096 528 -LRQQQNAERLLEEFCQRIGQQLDAAEEL--------------EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2312 Q-KEL---------AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQ 2381
Cdd:COG3096 593 RiKELaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
250
....*....|
gi 2462619853 2382 RFRKQAEEIG 2391
Cdd:COG3096 673 RLLALAERLG 682
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4113-4141 |
4.53e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.53e-05
10 20
....*....|....*....|....*....
gi 2462619853 4113 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4141
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1689-1838 |
4.53e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1689 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1767
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1768 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEatrLKTEAEIALKEKEA 1838
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREE 167
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2743-2779 |
4.66e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.66e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 2743 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 2779
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2248-2609 |
5.07e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2248 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQED 2326
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2327 keqmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2406
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2407 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqQEQLLQETQALQQSFLSEKDSLLQRERFI 2486
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-LEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2487 EQEKAKLEQL------FQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqqRRQQ 2560
Cdd:TIGR02169 395 EKLKREINELkreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-----------LAAD 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462619853 2561 EELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 2609
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1756-1922 |
5.19e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1756 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1834
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1835 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQR--RQVEEEILALKASFE 1912
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 2462619853 1913 KAAAGKAELE 1922
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2255-2596 |
5.20e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2255 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2334
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2335 AEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQ 2409
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2410 TLEIQRQQSDHDAERLREAIAELEREKeKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQE 2489
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2490 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvasmEEARRRQHEAEEGVR-RKQEELQQLEQQRRQQEELLAEEN 2568
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL----EEEEESIELKQGKLTeEKEELEKQELKLLKDELELKKSED 472
|
330 340
....*....|....*....|....*...
gi 2462619853 2569 QRLREQLQLLEEQHRAALAHSEEVTASQ 2596
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1319-1527 |
5.23e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1319 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREakelQQRMQEEVVRREEAAVDAQQQKRSIQEE 1398
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRR-FEEIRLRKQRLEEE----RQRQEEEERKQRLQLQAAQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1399 LQQLRQsseaEIQAKaRQAEAAERSrlrieeeirvvrlqlEATERQRGGAEGELqalraraeeAEAQKRQAQ-EEAERLr 1477
Cdd:pfam15709 428 FRRKLQ----ELQRK-KQQEEAERA---------------EAEKQRQKELEMQL---------AEEQKRLMEmAEEERL- 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1478 rqvqdESQRKRQaEVELASRVKAEAEAAREKQRALQALEELRLQAEEAER 1527
Cdd:pfam15709 478 -----EYQRQKQ-EAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1295-1574 |
5.47e-05 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 49.45 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1295 DLRTHYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-AKAQAERE-A 1367
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1368 KELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE------AAERSRLRIEEEirVVRLQLEAT 1441
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1442 ERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAarekqralqaleelrl 1520
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKA---------------- 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 1521 qaeeaerrlRQAEVERARQ--------VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQ 1574
Cdd:pfam15450 446 ---------REFEVEAMRQelaallssVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
20-121 |
5.68e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.49 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 20 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHF 121
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1380-1733 |
6.00e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1380 RREEAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1459
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1460 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1539
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1540 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1619
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1620 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1699
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 2462619853 1700 EQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1733
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1039-1479 |
6.05e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1039 TLRSELEltlGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQL-----------KEAQAVPATLPE----LE 1103
Cdd:pfam15921 437 AMKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtlesseRTVSDLTASLQEkeraIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1104 ATKASLKKLRAQAEAQQPTFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVAQLLE-------RWQAVLAQTD 1173
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrTAGAMQVEKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1174 VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfaKQYI 1253
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELN 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1254 NAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTHYSELTTLTSqyikfiseTLRRMEEEERLAeqqra 1333
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA----- 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1334 eererlaeVEAALEKQRQLAEAHAQAKAqaereakelqqrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQssEAEIQAK 1413
Cdd:pfam15921 726 --------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ--ELSTVAT 783
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1414 ARQAEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQAlrarAEEAEAQKRQAQEEAeRLRRQ 1479
Cdd:pfam15921 784 EKNKMAGELEVLRSQER----RLKEKVANMEVALDKASLQF----AECQDIIQRQEQESV-RLKLQ 840
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2668-2706 |
6.46e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 42.70 E-value: 6.46e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 2668 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 2706
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1307-1473 |
6.50e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1307 TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQ--AKAQAEREAKELQQRMQEEVVRREE- 1383
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPn 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1384 --AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIR-------VVRLQLEATERQRGGAEGELQA 1454
Cdd:COG3206 290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpELEAELRRLEREVEVARELYES 369
|
170
....*....|....*....
gi 2462619853 1455 LRARAEEAEAQKRQAQEEA 1473
Cdd:COG3206 370 LLQRLEEARLAEALTVGNV 388
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2228-2594 |
6.71e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2228 NRALILRDKDNTQRflQEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2302
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2303 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF--QRTLEAERQRQLEMSAEAERLkLRVAE 2368
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2369 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2448
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2449 KSEEMQtvqqeqllqetqalqqsflsekdslLQRERFIEQEKAKLEQLFQdEVAKAQQLREEQQRQQQQMEQERQRLVAS 2528
Cdd:COG3096 505 RSQQAL-------------------------AQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 2529 MEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR------LREQLQLLEEQHRAALAHSEEVTA 2594
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTA 630
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2215-2342 |
6.77e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 48.34 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2215 EELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQLAEEDLAQQRALAE--KMLKEK 2292
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEK 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2293 MQavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQ 2342
Cdd:cd16269 246 ME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1460-1539 |
6.78e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 49.56 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1460 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL----ASRVKAE--AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1532
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqQELVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 2462619853 1533 EVERARQ 1539
Cdd:PRK11448 218 RKEITDQ 224
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1456-1577 |
6.82e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1456 RARAEEAEAQ------KRQAQEEAERLRrQVQDESQRKRQAEVELASRVKAEAEAAREkqralQALEELRLQAEEAER-- 1527
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQRRLQ-QEQLERAEKMREELELEQQRRFEEIRLRK-----QRLEEERQRQEEEERkq 410
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1528 -RLRQAEVERARQVQVA----LETAQRSAEAELQSKRASFAEKTAQLERSLQEEH 1577
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ 465
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2238-2705 |
7.32e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.20 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2238 NTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2317
Cdd:COG4995 7 LALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2318 EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2397
Cdd:COG4995 87 LALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2398 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLkseemqtvqqeqLLQETQALQQSFLSEKD 2477
Cdd:COG4995 167 ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAA------------LAALLLALLALAAALLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2478 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQR 2557
Cdd:COG4995 235 LLLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2558 RQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQE 2637
Cdd:COG4995 315 LALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 2638 AGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLL-LKATNEKLSVYAALQRQLLSPGTALI 2705
Cdd:COG4995 395 LLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1389-1524 |
7.55e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1389 QQQKRSIQEELQQLRQ---SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQALR 1456
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1457 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEE 1524
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1246-1577 |
7.71e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.86 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1246 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTHY-SELTTLTSQyikfiSETLRRMEEE 1324
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1325 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA--------KELQQRMQEEVVRREEAAVDAQQQKRSIQ 1396
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1397 EELQQLRQsSEAEIQAKarQAEAaerSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA------ 1469
Cdd:NF033838 201 RDEEKIKQ-AKAKVESK--KAEA---TRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1470 --------QEEAERLRRQVQDES----QRKRQAEVELASRVKAEAEAAREKQR-------ALQALEELRLQAEEAERRLR 1530
Cdd:NF033838 272 epatpdkkENDAKSSDSSVGEETlpspSLKPEKKVAEAEKKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKVK 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 1531 QAEVERARQV--QVALETAQRSAEAELQSKRA--SFAEKTAQLERSLQEEH 1577
Cdd:NF033838 352 EAELELVKEEakEPRNEEKIKQAKAKVESKKAeaTRLEKIKTDRKKAEEEA 402
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1336-1746 |
7.76e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1336 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvRREEAAVDAQQQKRSIQEELQQLRQSSEAEiqaKAR 1415
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERL-AELEAKRQAEEEAREAKAEAEQRAAELAAE---AAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1416 QAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELA 1495
Cdd:COG3064 78 KLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1496 SRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1575
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1576 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1655
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1656 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1735
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGI 391
|
410
....*....|.
gi 2462619853 1736 KVRAEMEVLLA 1746
Cdd:COG3064 392 LAAAGGGGLLG 402
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1678-2174 |
7.80e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.09 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1678 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV----------RAEMEVLLAS 1747
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1748 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1827
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1828 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILAL 1907
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1908 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1987
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1988 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAA 2067
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2068 EEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2147
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 2462619853 2148 KKFAEQTLRQKAQVEQELTTLRLQLEE 2174
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2240-2449 |
7.87e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2240 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2319
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2320 ARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2399
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2400 ATQEKvtlvqTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2449
Cdd:pfam13868 191 AQQEK-----AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ 235
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3774-3810 |
8.08e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.08e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 3774 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3810
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1323-2031 |
8.27e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1323 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1398
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1399 LQQLR-QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ-----LEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1472
Cdd:PRK04863 378 QEENEaRAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1473 AERLRRQVQDESQRKRQAEV--ELASRVKAEAEAAREKQRALQALEELRLQAEEAER----RLRQAEVERARQVQVALET 1546
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQayQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1547 AQRSAEaelqsKRASFAEKTAQLERSLQEEHVAvaqlreeaerrAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1626
Cdd:PRK04863 538 LLAEFC-----KRLGKNLDDEDELEQLQEELEA-----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1627 EVAQQKslaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRaetEQGEQQR 1706
Cdd:PRK04863 602 APAWLA-----------------------AQDALARLREQSGEEFEDSQDV-TEYMQQLLERERELTVER---DELAARK 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1707 QLLEEELARL-QREAAAATQKRQ-----------------------ELEAELAKVRAEMEVLLASKAR------------ 1750
Cdd:PRK04863 655 QALDEEIERLsQPGGSEDPRLNAlaerfggvllseiyddvsledapYFSALYGPARHAIVVPDLSDAAeqlagledcped 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1751 -----------------AEEESRSTSEKSKQRlEAEAGRFRE--LAEEAARlRALAEEAKRQRQLAEEDAARQRAE---- 1807
Cdd:PRK04863 735 lyliegdpdsfddsvfsVEELEKAVVVKIADR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDvqkl 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1808 ------AERVLAEKLA---------AIGEATRLKTEAEIALKEKEAENERLR--------------------RLAEDEAF 1852
Cdd:PRK04863 813 qrlhqaFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHESQEQQQRsqleqakeglsalnrllprlNLLADETL 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1853 QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGRIR--- 1929
Cdd:PRK04863 893 ADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQRRahf 971
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1930 --SNAEDTLrSKEQAELEAARQRQLAAEEERRRREAE-----------ERVQKSLAAEEEAARQ-RKAALEEVE----RL 1991
Cdd:PRK04863 972 syEDAAEML-AKNSDLNEKLRQRLEQAEQERTRAREQlrqaqaqlaqyNQVLASLKSSYDAKRQmLQELKQELQdlgvPA 1050
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 2462619853 1992 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2031
Cdd:PRK04863 1051 DSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1316-1511 |
8.47e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEER---LAEQQRAEererlaeveaaLEKQRQLAEAHAQAKAQAEREAKELQQRMQ----------EEVVRRE 1382
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE-----------LDASRALAEKQKHELDTEKRCAEELKEAMQmamegharmlEQYADLE 1120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1383 EAAVDAQQQKRSIQEELQQLRQsseAEIQAKARQAE-------AAERSRLRI--EEEIRVVRLQLEATERQ-RGGAE--- 1449
Cdd:PLN03188 1121 EKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVerEKERRYLRDENKSLQAQlRDTAEavq 1197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1450 --GELQALRARAEEA--EAQKR--QAQEEAERLRRQVqDESQRKRQAEVELASRVKAEAEAAREKQRA 1511
Cdd:PLN03188 1198 aaGELLVRLKEAEEAltVAQKRamDAEQEAAEAYKQI-DKLKRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2186-2399 |
8.69e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2186 LQRLKAEATEAARQRSQVEEElfsvrvQMEELSKLKARIEAENRALilrdkdnTQRFLQEEAEKmKQvAEEAARLSVAAQ 2265
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL-------EKERLAAQEQK-KQ-AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2266 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQGFQRT 2344
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2345 LEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2399
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2145-2623 |
9.03e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2145 EKHKKFAEQTLRQKAQVEQELTTLRLQL-EETDHQKNLLDEELQRLKAEATEAARQRSQV---EEELFSVRVQMEELSKL 2220
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2221 KARIEAENRAlilrdkdntQRFLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2300
Cdd:pfam12128 477 REEQEAANAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2301 RLKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA------ 2372
Cdd:pfam12128 539 FLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsare 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2373 -QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKS 2450
Cdd:pfam12128 619 kQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2451 EEMQTVQQEQLLQETQALQQSFL---SEKDSLLQR-----ERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQER 2522
Cdd:pfam12128 699 QAWLEEQKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREI 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2523 QRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALA----HSEEVTASQVA 2598
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAklemERKASEKQQVR 857
|
490 500 510
....*....|....*....|....*....|...
gi 2462619853 2599 ATKTLPNGRD--------ALDGPAAEAEPEHSF 2623
Cdd:pfam12128 858 LSENLRGLRCemsklatlKEDANSEQAQGSIGE 890
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1316-1810 |
9.13e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.50 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1395
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1396 QEELQQLRQSSEAEIQAKARQAEAAERSRlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1475
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAE------------KAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1476 LRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1555
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1556 QSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1635
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1636 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1715
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1716 LQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1795
Cdd:COG3064 391 ILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVA 470
|
490
....*....|....*
gi 2462619853 1796 LAEEDAARQRAEAER 1810
Cdd:COG3064 471 LDGGAVLADLLLLGG 485
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1769-1888 |
9.66e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.79 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1769 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLAEKLAAIGEATRLKTEAEIA-LKEKEAE 1839
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1840 NERLRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA---SDSE-LERQKG 1888
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKAgweADSKtLRFSKG 261
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2190-2380 |
1.06e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2190 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAAR 2269
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2270 LRQLAEEDLAQQrALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfQRTLEAER 2349
Cdd:TIGR02794 126 AKQAAEAKAKAE-AEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK-AKAEAAKA 203
|
170 180 190
....*....|....*....|....*....|.
gi 2462619853 2350 QRQLEMSAEAERLKLRVAEMsRAQARAEEDA 2380
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAA-EAERKADEAE 233
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1654-1776 |
1.10e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1654 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1727
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1728 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1776
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1658-1979 |
1.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1737
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1817
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1818 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 1897
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1898 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 1977
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 2462619853 1978 AR 1979
Cdd:COG4372 368 AD 369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1380-1718 |
1.15e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1380 RREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1459
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1460 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1539
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1540 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1619
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1620 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1699
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330
....*....|....*....
gi 2462619853 1700 EQGEQQRQLLEEELARLQR 1718
Cdd:COG4372 323 ELAKKLELALAILLAELAD 341
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3327-3361 |
1.15e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.15e-04
10 20 30
....*....|....*....|....*....|....*
gi 2462619853 3327 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3361
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1672-2035 |
1.18e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1672 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRQELEAELAKVRAEM--EVLLAS 1747
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeEAREAKAEAEQRAAELAAEAakKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1748 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1827
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1828 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILAL 1907
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1908 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1987
Cdd:COG3064 244 ALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462619853 1988 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2035
Cdd:COG3064 324 AGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1658-1853 |
1.23e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1734
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1735 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1799
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1800 DAARQRAEAERVLAEKLAAIG-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1853
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4362-4399 |
1.23e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.23e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2462619853 4362 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 4399
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1151-1529 |
1.36e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1151 VERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWL---QDARRRQEQIQAMPLADSQAVREQLRQ 1227
Cdd:pfam07111 333 VKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELsraQEARRRQQQQTASAEEQLKFVVNAMSS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1228 EQALLE-EIERHGEKVEECQRFAKQYINAIKDYEL-------QLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTH 1299
Cdd:pfam07111 413 TQIWLEtTMTRVEQAVARIPSLSNRLSYAVRKVHTikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNR 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1300 YSELTTLTSQYIkfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVV 1379
Cdd:pfam07111 493 LDAELQLSAHLI----------QQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAA 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1380 rreeaavdaqqqkrSIQEELQQlrqssEAEIQAKARQAEAAErSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1459
Cdd:pfam07111 563 --------------SLRQELTQ-----QQEIYGQALQEKVAE-VETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRA 622
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1460 EeaeaqkrQAQEEAERLRRqVQDESqRKRQAEvELASRVKaeaEAAREKQRALQALEELRLQAEEAERRL 1529
Cdd:pfam07111 623 T-------QEKERNQELRR-LQDEA-RKEEGQ-RLARRVQ---ELERDKNLMLATLQQEGLLSRYKQQRL 679
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3943-3977 |
1.37e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.37e-04
10 20 30
....*....|....*....|....*....|....*
gi 2462619853 3943 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3977
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1079-1795 |
1.45e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1079 EEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1157
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1158 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplGAWLQDARRRQEQIQAMpLADSQavrEQLRQEQALLEEIER 1237
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRKQ-LSKTQ---EELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1238 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTHYSELTTLTSQY 1310
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1311 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKeLQQRMQEEvvrreeaAVDAQ 1389
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDK-------AAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1390 QQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1469
Cdd:pfam07111 370 VERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1470 QEEAER--LRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEEL--RLQAEEAERRLRQAEVERARQVQVAle 1545
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVA-- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1546 taqRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1625
Cdd:pfam07111 527 ---QQLEQELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1626 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1700
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1701 QGEQQR-----QLLEEE----LARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1766
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 2462619853 1767 EAEAGRFRELAEEAARLRALAEEAKRQRQ 1795
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2152-2455 |
1.46e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2152 EQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE--------------LFSVRVQMEEL 2217
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDR 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2218 SKLKARIEAENRALILRDKDNTQR---FLQEEAEKMKQVAEEAARLSVAAQeaaRLRQLAEEDLAQQRALAEK------- 2287
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERqmaAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTAKKMTLESSertvsdl 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2288 --MLKEKMQAVQ----EATRLKAEAEL-LQQQKELAQE--QARRLQEDKEQMAQQLAEEtqgfQRTLEAERQRQLEMSAE 2358
Cdd:pfam15921 502 taSLQEKERAIEatnaEITKLRSRVDLkLQELQHLKNEgdHLRNVQTECEALKLQMAEK----DKVIEILRQQIENMTQL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2359 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQR-QQSDHDAERLReAIAELEREKE 2437
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvKLVNAGSERLR-AVKDIKQERD 656
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462619853 2438 KLQQEAKL------------------LQLKSEEMQT 2455
Cdd:pfam15921 657 QLLNEVKTsrnelnslsedyevlkrnFRNKSEEMET 692
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2154-2386 |
1.52e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2154 TLRQKAQVEQELTTLRLQleetdhQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIL 2233
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2234 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2307
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 2308 LLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2386
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1458-1582 |
1.55e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1458 RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRalQALEELRL------QAEEAERRLRQ 1531
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQaalkqkQAEEAAAKAAA 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 1532 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ 1582
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1771-2017 |
1.57e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1771 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDE 1850
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1851 AFQRRRLEEQAAQHKADIEE------RLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELE 1924
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1925 LGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2003
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 2462619853 2004 RAEQESAR-QLQLAQ 2017
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1810-2581 |
1.66e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1810 RVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqHKADIEERLAQLRKASDSELERQKgl 1889
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGYELLKEK-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1890 vEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAED-TLRSKEQAELEAARQRQLAAEEERRRREAEERVQ 1968
Cdd:TIGR02169 233 -EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1969 KSLAAEEEAARQRKAALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFAVQQKE 2039
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2040 QELQQtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE-RLKQSAEEqaqaraqaqaaaeklrke 2118
Cdd:TIGR02169 389 DYREK--------LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEaKINELEEE------------------ 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2119 aeqeaarraqaeqaalrqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEA---TE 2195
Cdd:TIGR02169 443 ------------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQArasEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2196 AARQRSQVEEELFS----VRVQMEELSKLKAR------IEAENR--ALILRDKDNTQR---FLQEEA---------EKMK 2251
Cdd:TIGR02169 505 RVRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMR 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2252 QVAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAE 2305
Cdd:TIGR02169 585 DERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2306 AELLQQQKElaqEQARRLQEDKEQMAQQLAeetqGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK 2385
Cdd:TIGR02169 665 GILFSRSEP---AELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2386 QAEEIGEKLhrtelatqekvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-----EAKLLQLKSEEMQtvQQEQ 2460
Cdd:TIGR02169 738 RLEELEEDL--------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQ--AELS 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2461 LLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAE 2540
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 2462619853 2541 E---GVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQ 2581
Cdd:TIGR02169 882 SrlgDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1679-2083 |
1.74e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.59 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1679 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1758
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1759 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA 1838
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1839 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGK 1918
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1919 AELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 1998
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1999 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAE 2078
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
....*
gi 2462619853 2079 REAAQ 2083
Cdd:COG5278 513 AEAAL 517
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1403-1556 |
1.82e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.03 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1403 RQSSEAEIQAKARQAEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1480
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1481 QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQ 1556
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2134-2436 |
1.84e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.37 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2134 LRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEEELFSVRVQ 2213
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2214 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2292
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2293 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAEETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEM 2369
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 2370 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLREaiaELEREK 2436
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4252-4285 |
1.90e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.90e-04
10 20 30
....*....|....*....|....*....|....
gi 2462619853 4252 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4285
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1645-1808 |
2.03e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1645 EAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQElirlrAETEQGEQQRQL-LEEELARLQREAAAA 1723
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA-----YEIAEANAEREVqRQLEIAEREREIELQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1724 TQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAA 1802
Cdd:COG2268 296 EKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IA 370
|
....*.
gi 2462619853 1803 RQRAEA 1808
Cdd:COG2268 371 EAAAKP 376
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1449-1583 |
2.07e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 46.67 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1449 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERR 1528
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 1529 LRQ--AEVERARQvQVALETAQRSAEAELQSK----RASFAEKTAQLERSLQEEHVAVAQL 1583
Cdd:pfam09787 141 IKDreAEIEKLRN-QLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1328-1459 |
2.24e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.96 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1328 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ-AKAQAERE-AKELQQRMQEEVvrrEEAAVDAQQqkrsiQEELQQLRQS 1405
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlAAAQAQLDlAQRELERYQALY---KKGAVSQQE-----LDEARAALDA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1406 SEAEIQAkARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1459
Cdd:COG1566 160 AQAQLEA-AQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1325-1489 |
2.43e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.21 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1325 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQ 1404
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1405 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1484
Cdd:PRK12678 158 ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
....*
gi 2462619853 1485 QRKRQ 1489
Cdd:PRK12678 237 DARGD 241
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
158-235 |
2.51e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 43.06 E-value: 2.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 158 DNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 235
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2261-2539 |
2.52e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2261 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAEeTQG 2340
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLAA-ISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2341 FQRTLEAERQRQLEMSAEAERlklrvaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2420
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2421 DAE---RLREAIAE--LEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSllqrerfiEQEKAKLEQ 2495
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462619853 2496 LFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRR-QHEA 2539
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1043-1259 |
2.68e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1043 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraqaEAQQPT 1122
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1123 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLGAWLQD 1202
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1203 ARRRQEQIQAMPladsQAVREQLRQEQ-ALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1259
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERIdALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1659-2029 |
2.73e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 46.95 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1659 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQkrqelEAELAKVR 1738
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQ-----DSELAKLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1739 A-EMEVLLASKARAeeESRSTSEKSKQRLEAEAGRFRELAEEaarLRALAEEakRQRQLAEEDAARQRAEaERVLAEKla 1817
Cdd:pfam05701 107 VeEMEQGIADEASV--AAKAQLEVAKARHAAAVAELKSVKEE---LESLRKE--YASLVSERDIAIKRAE-EAVSASK-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1818 AIGEATRLKTEAEIALKEK---------EAENERLR----------------RLAEDEAfqrRRLEEQAA-----QHKAD 1867
Cdd:pfam05701 177 EIEKTVEELTIELIATKESlesahaahlEAEEHRIGaalareqdklnwekelKQAEEEL---QRLNQQLLsakdlKSKLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1868 IEERLAQLRKAS-----DSELERQKGLVEDTLRQRRQVEEEILALKASFE--KAAAGKAELELELGRIrsnAEDTLRS-- 1938
Cdd:pfam05701 254 TASALLLDLKAElaaymESKLKEEADGEGNEKKTSTSIQAALASAKKELEevKANIEKAKDEVNCLRV---AAASLRSel 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1939 -KEQAELEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAArqrKAALEEVERLKAKVEEARRLRERAE---------- 2006
Cdd:pfam05701 331 eKEKAELASLRQREgMASIAVSSLEAELNRTKSEIALVQAKE---KEAREKMVELPKQLQQAAQEAEEAKslaqaareel 407
|
410 420
....*....|....*....|....*.
gi 2462619853 2007 ---QESARQLQLAQEAAQKRLQAEEK 2029
Cdd:pfam05701 408 rkaKEEAEQAKAAASTVESRLEAVLK 433
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1384-1565 |
2.93e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1384 AAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1463
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1464 AQKRQA--QEEAERLRRQVQDESQRKRQAEvELASRVKAEAEAAREKQRALQA-LEELRLQAEEAERRLRQAEVERARQv 1540
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAeLAELEAELEEKKAELDEELAELEAE- 157
|
170 180
....*....|....*....|....*
gi 2462619853 1541 qvaletaqrsaEAELQSKRASFAEK 1565
Cdd:COG1579 158 -----------LEELEAEREELAAK 171
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2249-2598 |
2.95e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2249 KMKQVAEEAarlsvaaqeaarlrqlaeedlaqqralaekmLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2328
Cdd:pfam02463 166 RLKRKKKEA-------------------------------LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2329 QMAQ-QLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL 2407
Cdd:pfam02463 215 LKEKlELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2408 VQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqlLQETQALQQSFLSEKDSLLQRERFIE 2487
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE-----LKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2488 QEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEA-----EEGVRRKQEELQQLEQQRRQQEE 2562
Cdd:pfam02463 370 QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeekkEELEILEEEEESIELKQGKLTEE 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462619853 2563 LLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVA 2598
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1325-1576 |
3.00e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1325 ERLAEQQRAEERERLAEVEaalekqrqlaeahaqakaQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQE---E 1398
Cdd:pfam10174 453 ERLKEQREREDRERLEELE------------------SLKKENKDLKEKvsaLQPELTEKESSLIDLKEHASSLASsglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1399 LQQLRQSSEAEIQA-------------KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1465
Cdd:pfam10174 515 KDSKLKSLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1466 K---------------RQAQEEAERLR--RQVQDESQRKRQAEVELASRVK-AEAEAAREKQRA--LQALEELRLQAEEA 1525
Cdd:pfam10174 595 KndkdkkiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDAT 674
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1526 ERRLRQAEV--------------ERARQVQVALETAQRSAEAELQSKRASFA--EKTAQLERSLQEE 1576
Cdd:pfam10174 675 KARLSSTQQslaekdghltnlraERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE 741
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2136-2409 |
3.07e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2136 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR 2211
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2212 VQMEELSKL-----KARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRAL 2284
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2285 AEKMLKEKMQAVQEATR--------LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMS 2356
Cdd:pfam13868 213 EEQERKERQKEREEAEKkarqrqelQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 2357 AEAERLklrvaEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2409
Cdd:pfam13868 293 RELEKQ-----IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2135-2442 |
3.11e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.34 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2135 RQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQM 2214
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2215 EELSKLKARIEAENRAlilrdkDNTQRflqeeaekmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2294
Cdd:pfam15905 132 LELTRVNELLKAKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2295 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQA 2374
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 2375 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQE 2442
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3662-3697 |
3.17e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.17e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2462619853 3662 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 3697
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3402-3433 |
3.20e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.20e-04
10 20 30
....*....|....*....|....*....|..
gi 2462619853 3402 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 3433
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1668-1899 |
3.26e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1668 EQELeKQRQLAEGTAQ----QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAaaatqkRQELEAELAKVRA---- 1739
Cdd:PRK10929 29 TQEL-EQAKAAKTPAQaeivEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAEL------RQQLNNERDEPRSvppn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1740 ------EMEVLLAS-------------KARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAE----EAKRQRQL 1796
Cdd:PRK10929 102 mstdalEQEILQVSsqlleksrqaqqeQDRAREISDSLSQLPQQQTEAR----RQLNEIERRLQTLGTpntpLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1797 AEEDAARQRAEAERVLAEKLAAIG--EATRLKteAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1874
Cdd:PRK10929 178 LQAESAALKALVDELELAQLSANNrqELARLR--SELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGD 255
|
250 260
....*....|....*....|....*
gi 2462619853 1875 LRKASDSELERQKGLvEDTLRQRRQ 1899
Cdd:PRK10929 256 LPKSIVAQFKINREL-SQALNQQAQ 279
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2076-2442 |
3.34e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2076 QAEREAAQSRRQVEEAERLKQSAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAeQTL 2155
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEE---------------------------KYKELSASSEELSEEKD-ALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2156 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRAL--IL 2233
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2234 RDKDNTQRFLQEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQ 2311
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2312 QKELAQ------EQARRLQEDKEQMAQqlaeETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrk 2385
Cdd:pfam07888 278 RLQAAQltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER--- 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 2386 qaeeigEKLhRTELATQEKVTLVQTLEIQRQQSDhdaerLREAIAELEREKEKLQQE 2442
Cdd:pfam07888 342 ------EKL-EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3327-3361 |
3.60e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.77 E-value: 3.60e-04
10 20 30
....*....|....*....|....*....|....*
gi 2462619853 3327 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3361
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2184-2392 |
3.69e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2184 EELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKM-----KQVAEEAA 2258
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2259 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLA 2335
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 2336 EETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2392
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1579-2034 |
3.72e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.93 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1579 AVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1658
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1659 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR 1738
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1739 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1818
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1819 IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRR 1898
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1899 QVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 1978
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1979 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2034
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2156-2454 |
3.93e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2156 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRD 2235
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2236 KDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKEL 2315
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE--REEEREAEREEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2316 AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLH 2395
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 2396 RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2454
Cdd:pfam13868 262 EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2149-2316 |
4.00e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.00 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2149 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKNLLDEElqrlkAEATEAARQRSQVEEELFSVRVQMEELSKlkarieaen 2228
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALRS--------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2229 ralILRDKDNTQRFLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2306
Cdd:COG3524 243 ---YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 2462619853 2307 EllQQQKELA 2316
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2151-2335 |
4.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2151 AEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAarQRSQVEEELFSVRVQME-ELSKLKARIEAENR 2229
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2230 ALilrdkdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2309
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|....*.
gi 2462619853 2310 QQQKELAQEqarRLQEDKEQMAQQLA 2335
Cdd:COG3206 364 RELYESLLQ---RLEEARLAEALTVG 386
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1654-1801 |
4.25e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1654 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRQELEA 1732
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1733 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDA 1801
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLEH 506
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2218-2452 |
4.25e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2218 SKLKARIEAENRALILRdkdntQRFlqeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQ 2297
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAK-----ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2298 EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV 2366
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2367 -AEMSRAQAR---AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREK-EKLQQ 2441
Cdd:PRK05035 583 aAAIARAKAKkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKaRKAAQ 662
|
250
....*....|.
gi 2462619853 2442 EAKLLQLKSEE 2452
Cdd:PRK05035 663 QQANAEPEEAE 673
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1345-1516 |
4.39e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1345 ALEKQRQLA--------EAHAQAKAQA-EREAKEL--QQRMQEEVvrreeaavDAQQQKRsiqeELQQLRQSSEAEIQAK 1413
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARGRleRQKMHDKA--------KAEEQRT----KLLELQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1414 ARQAEA-AERSRLRIEEEirvvrlqleaterqrggAEGELQALRARAEEAEAQKrqaqeEAERLR-RQVQDESQRKRQAE 1491
Cdd:PTZ00491 716 QSRAEAlAEAEARLIEAE-----------------AEVEQAELRAKALRIEAEA-----ELEKLRkRQELELEYEQAQNE 773
|
170 180
....*....|....*....|....*
gi 2462619853 1492 VELasrvkaeaeaarEKQRALQALE 1516
Cdd:PTZ00491 774 LEI------------AKAKELADIE 786
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1918-2597 |
4.48e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1918 KAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE 1997
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1998 ARRLRERAEQESARQLQLAQEAAQ-KRLQAEEKAHAFAV----QQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEE 2072
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLEETQerinRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2073 ARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAE 2152
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2153 QTLRQKAQVEQELTTLRlqleetdhqknllDEELQRLKAEATEAARQRSQVEEELFSvrvqMEELSKLKARIEAENRAli 2232
Cdd:TIGR00618 404 ILQREQATIDTRTSAFR-------------DLQGQLAHAKKQQELQQRYAELCAAAI----TCTAQCEKLEKIHLQES-- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2233 lrdkdntQRFLQEEAEKMKQVA----EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2308
Cdd:TIGR00618 465 -------AQSLKEREQQLQTKEqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2309 LQQQKELAQEQARrLQEDKEQmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAE 2388
Cdd:TIGR00618 538 AQLETSEEDVYHQ-LTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ---NITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2389 EigekLHRTELATQEKVTLVQTLEIQRQQSdhdaERLREAIAELEREKEKL----QQEAKLLQLKSEEMQTVQQEQLLQE 2464
Cdd:TIGR00618 613 E----QHALLRKLQPEQDLQDVRLHLQQCS----QELALKLTALHALQLTLtqerVREHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2465 TQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVR 2544
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 2545 RKQEELQQLEQQRRQQEELLAEENQRLRE------QLQLLEEQHRAALAHSEEVTASQV 2597
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLreedthLLKTLEAEIGQEIPSDEDILNLQC 823
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1313-1375 |
4.67e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.79 E-value: 4.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1313 FISETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAEREAKELQQRMQ 1375
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1318-1482 |
4.72e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1318 LRRMEEEERLAEQQRAEERERLAEVEAA--LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1395
Cdd:pfam00038 136 LKKNHEEEVRELQAQVSDTQVNVEMDAArkLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1396 QEELQQLR---QSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqRGgaEGELQALRARAEEAEAQKRQAQEE 1472
Cdd:pfam00038 216 KEEITELRrtiQSLEIELQSLKKQKASLERQLAETEE---------------RY--ELQLADYQELISELEAELQETRQE 278
|
170
....*....|
gi 2462619853 1473 AERLRRQVQD 1482
Cdd:pfam00038 279 MARQLREYQE 288
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2152-2409 |
4.83e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2152 EQTLR---QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRS------QVEEELFSVRVQmeeLSKLKA 2222
Cdd:PRK11281 66 EQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQ---LQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2223 RIEAENRALIlrdkdnTQRFLQEEAEkmkqvaeeaARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQEATrl 2302
Cdd:PRK11281 143 DLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALRPS-QRVLLQAEQALL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2303 kaEAELLQQQKELA-----QE--QARRlqEDKEQMAQQLAEETQGFQrtlEAERQRQLEMSAEAerlklrVAEMSRAQAR 2375
Cdd:PRK11281 205 --NAQNDLQRKSLEgntqlQDllQKQR--DYLTARIQRLEHQLQLLQ---EAINSKRLTLSEKT------VQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*
gi 2462619853 2376 AEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVQ 2409
Cdd:PRK11281 272 ARIQANPLVAQELEINLQLSQRLLkATEKLNTLTQ 306
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1322-1583 |
4.87e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1322 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAK-------ELQQRMQEEVVRREEAAVDAQQQKRS 1394
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgqgglDEEEAFLDRTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1395 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEI--RVVRLQLEATE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1471
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1472 EAERLRRQV-----QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQvqvALET 1546
Cdd:pfam02029 165 EAEEVPTENfakeeVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE---EEAE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462619853 1547 AQRSAEAELQSKRASFAEKTAQ----LERSLQEEHVAVAQL 1583
Cdd:pfam02029 242 VFLEAEQKLEELRRRRQEKESEefekLRQKQQEAELELEEL 282
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2706-2739 |
4.88e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.88e-04
10 20 30
....*....|....*....|....*....|....
gi 2462619853 2706 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2739
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1036-1902 |
4.94e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1036 AAPTLRsELELTLGKLEQVRSLSAIYLEKLKTISLVIRGT--------QGAEEVLRAHE-------EQLKEAQAVPATLP 1100
Cdd:TIGR00606 187 ALETLR-QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYEneldplkNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1101 ELEATKASLKKLRAQAEAQQPTFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRERVaqllerwqavlaqtdvrQREL 1179
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDC-----------------QREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1180 EQLGRQLRYYRESADPL----GAWLQDARRRQEQIQAMplaDSQAVREQLRQEQALLEE---IER-----HGEKVEECQR 1247
Cdd:TIGR00606 329 EKLNKERRLLNQEKTELlveqGRLQLQADRHQEHIRAR---DSLIQSLATRLELDGFERgpfSERqiknfHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1248 FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTHYSELTTLT--SQYIKFISETLRRMEE 1323
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLEgsSDRILELDQELRKAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1324 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKELQQRMQEEVVRREEAAVDAQQQK---RSIQEELQ 1400
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKiksRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1401 QLRQSSEAEIQAKARQAEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-----AQKRQAQE-EAE 1474
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTR--DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdVCGSQDEEsDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1475 RLRRQVqdESQRKRQAEVELASRVKAE--AEAAREKQ-------RALQALEELRLQAEEAERRLRQA------------E 1533
Cdd:TIGR00606 643 RLKEEI--EKSSKQRAMLAGATAVYSQfiTQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLApdklksteselkK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1534 VERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQL 1613
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1614 KANEALRlrlqaeEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLaaeQELI 1693
Cdd:TIGR00606 800 ELKDVER------KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT---NELK 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1694 RLRAETEQGEQQRQLLEEELARLQREA----AAATQKRQE---LEAELAKVRAEMEVLLASK----ARAEEESRSTSEKS 1762
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISSKetsnKKAQDKVNDIKEKV 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1763 KQRLEAEAGRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE------AERVLAEKLaaigeaTRL 1825
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNL------TLR 1024
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1826 KTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEE 1902
Cdd:TIGR00606 1025 KRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1235-1575 |
5.02e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.10 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1235 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaSPAKKPKVQSGSESVIQEY-VDLRTHYSELTTLTSQYIKF 1313
Cdd:COG5185 154 GEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGI-SELKKAEPSGTVNSIKESEtGNLGSESTLLEKAKEIINIE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1314 ISETLRRMEEEERLAEQQRAEERERLAEVEAAL--EKQRQLAEAHAQAKAQAEREAKELQQrmQEEVVRREEAAVDAQQQ 1391
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrlEKLGENAESSKRLNENANNLIKQFEN--TKEKIAEYTKSIDIKKA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1392 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEATERQRGGAEGElQALRARAEEAEAQKRQAQE 1471
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTA-EIEQGQESLTENLEAIKEEIENIVGE-VELSKSSEELDSFKDTIES 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1472 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEElrlQAEEAERRLRQAEVERARQVQVA-------L 1544
Cdd:COG5185 389 TKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATS---SNEEVSKLLNELISELNKVMREAdeesqsrL 465
|
330 340 350
....*....|....*....|....*....|.
gi 2462619853 1545 ETAQRSAEAELQSKRASFAEKTAQLERSLQE 1575
Cdd:COG5185 466 EEAYDEINRSVRSKKEDLNEELTQIESRVST 496
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1655-1814 |
5.19e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.82 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRQELEA 1732
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1733 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1808
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....*.
gi 2462619853 1809 ERVLAE 1814
Cdd:COG1842 207 EDELAA 212
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1336-1445 |
5.89e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 45.36 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1336 RERLAEVEAALEKQRQLAEAH-AQAKAQAEREAKELQQRMQEEVVRREEAavDAQQQKRSIQEELQQLRQSSEAEIQAKA 1414
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEkAIEAERAKAEAAEAEQELLREKQKEEEQ--MMEAQERSYQEHVKQLIEKMEAEREQLL 260
|
90 100 110
....*....|....*....|....*....|.
gi 2462619853 1415 RQAEAAERSRLRIEEEIRVVRLQLEATERQR 1445
Cdd:pfam02841 261 AEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1333-1575 |
6.05e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.60 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1333 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLRQSSEAEIQA 1412
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1413 KARqaeaaersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEV 1492
Cdd:pfam12795 74 ILA-------------------SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1493 ELASRVKAEAEAAREKQRALQA--------LEELRLQAEEAERR--LRQAEVERARQVQVALETAQRSAEAELQSKRASF 1562
Cdd:pfam12795 135 RLNGPAPPGEPLSEAQRWALQAelaalkaqIDMLEQELLSNNNRqdLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQE 214
|
250
....*....|....
gi 2462619853 1563 AEKT-AQLERSLQE 1575
Cdd:pfam12795 215 AEQAvAQTEQLAEE 228
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1352-1558 |
6.07e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.61 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1352 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKarqaeaaersrlrieeei 1431
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1432 rvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkrqaeveLASRVKAEAEAarekqRA 1511
Cdd:COG3524 222 -----LIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERAR-------LTGASGGDSLA-----SL 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462619853 1512 LQALEELRLQAEEAERRLRQAeverarqvQVALETAQrsAEAELQSK 1558
Cdd:COG3524 285 LAEYERLELEREFAEKAYTSA--------LAALEQAR--IEAARQQR 321
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2183-2403 |
6.11e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.74 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2183 DEELQRLKAEATEAARQRSQveEELfsVRVQMEELSKLKARIEAENRALILRDKDNTqrflqEEAEKMKQVAEEAARLSV 2262
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEAR--KRL--VAKHGAEISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2263 AAQEAARLRQLAEEDLAQQRALAekmlkekmqavqeATRLKAEAELLQQQKELAQEQARrlQEDKEQMAQQLAEETQGfq 2342
Cdd:PRK07735 75 AKQKREGTEEVTEEEKAKAKAKA-------------AAAAKAKAAALAKQKREGTEEVT--EEEKAAAKAKAAAAAKA-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 2343 RTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2403
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE 198
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3737-3773 |
6.18e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.18e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 3737 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 3773
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2250-2449 |
6.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2250 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE- 2328
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2329 ----QMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2404
Cdd:COG4717 128 lplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462619853 2405 vtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2449
Cdd:COG4717 208 ---LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1320-1679 |
6.57e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1320 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1399
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1400 QQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1479
Cdd:COG4372 83 EELNE----QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1480 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKR 1559
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1560 ASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1639
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462619853 1640 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE 1679
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1672-1947 |
6.63e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 45.62 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1672 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1748
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1749 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1808
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1809 ErvLAEKLAAIG---EATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLRKASDS 1881
Cdd:pfam03148 159 D--LSDKKEALEideKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1882 ELERQKGLVEDTLRQRrqVEEeilalkasFEKAaagKAELELELGRIRSNAEDTlrSKEQAELEAA 1947
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEL--EKNIEALEKA 287
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
14-118 |
7.11e-04 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 42.43 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 14 EDERdrvqkKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGR 71
Cdd:cd21294 5 EDER-----REFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462619853 72 MRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 118
Cdd:cd21294 76 NNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2134-2298 |
7.27e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2134 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQ 2213
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2214 mEELSKLKARIEAENRALILRDKDnTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2293
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 2462619853 2294 QAVQE 2298
Cdd:COG1579 167 ELAAK 171
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
998-1541 |
7.31e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 998 QRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQG 1077
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1078 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQE-------VGERLQQRHGERDVE 1150
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRI 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1151 VERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQA 1230
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1231 LLEEIERHGEKVEECQR---FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLT 1307
Cdd:pfam02463 605 LAQLDKATLEADEDDKRakvVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1308 SQYIKFISETLRRMEEEERlaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEA--- 1384
Cdd:pfam02463 685 AESELAKEEILRRQLEIKK--KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeek 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1385 ---AVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEE 1461
Cdd:pfam02463 763 eeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1462 AEAQKRQ--AQEEAERLrrqvQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1539
Cdd:pfam02463 843 KEEQKLEklAEEELERL----EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
..
gi 2462619853 1540 VQ 1541
Cdd:pfam02463 919 IE 920
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3034-3068 |
7.38e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.38e-04
10 20 30
....*....|....*....|....*....|....*
gi 2462619853 3034 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 3068
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3108-3144 |
7.45e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.45e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2462619853 3108 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 3144
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1358-1573 |
8.03e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1358 QAKAQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQEELQQLRQ------SSEAEIQAK--------ARQAEAA 1420
Cdd:PRK11637 54 QDIAAKEKSVRQQQQQrasLLAQLKKQEEAISQASRKLRETQNTLNQLNKqidelnASIAKLEQQqaaqerllAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1421 ERsrlriEEEIRVVRLQLEATERQRG------------GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1488
Cdd:PRK11637 134 FR-----QGEHTGLQLILSGEESQRGerilayfgylnqARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1489 QAEVELASRVK--AEAEAAREKQRalQALEELRLQaeeaERRLR----QAEVE-RARQVQVALEtAQRSAEAELQSKRAS 1561
Cdd:PRK11637 209 KLEQARNERKKtlTGLESSLQKDQ--QQLSELRAN----ESRLRdsiaRAEREaKARAEREARE-AARVRDKQKQAKRKG 281
|
250
....*....|..
gi 2462619853 1562 FAEKTAQLERSL 1573
Cdd:PRK11637 282 STYKPTESERSL 293
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1405-1539 |
8.25e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1405 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDES 1484
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1485 QRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1539
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2136-2336 |
9.13e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2136 QKQAADAEMEKHKKFAEQT--LRQKAQVEQElttlRLQLEEtdhQKNLLDEELQRLKAEATEAARQRSQVEEElfsVRVQ 2213
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLE---KERLAAQEQKKQAEEAAKQAALKQKQAEE---AAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2214 MEELSKLKAriEAENRALilrdkdntqrflqeeAEKMKQVAEEAARLSVAAQEAarlrQLAEEdlAQQRALAEkmlkEKM 2293
Cdd:PRK09510 141 AAAAAKAKA--EAEAKRA---------------AAAAKKAAAEAKKKAEAEAAK----KAAAE--AKKKAEAE----AAA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462619853 2294 QAVQEAtRLKAEAELLQQQKELAQEQARRlqEDKEQMAQQLAE 2336
Cdd:PRK09510 194 KAAAEA-KKKAEAEAKKKAAAEAKKKAAA--EAKAAAAKAAAE 233
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2138-2391 |
9.30e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2138 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA-----EATEAARQRSQVEEELFSVRV 2212
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2213 QMEELSKLKARI-EAENRaliLRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2291
Cdd:PRK04863 511 LAEQLQQLRMRLsELEQR---LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2292 KMQAVQEATRLKAEAELLQQqkelAQEQARRLQE---DKEQMAQQLaeeTQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2368
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLA----AQDALARLREqsgEEFEDSQDV---TEYMQQLLERERELTVERDELAARKQALDEE 660
|
250 260
....*....|....*....|...
gi 2462619853 2369 MSRAQARAEEDAQRFRKQAEEIG 2391
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAERFG 683
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1073-1524 |
9.47e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1073 RGTQGAEEVLRAHEEQLKEAQAVPA----------------TLPELEATKASLKKLRAQAEAQQP-------TFDALrdE 1129
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqladvkTICEQEARIKDLEAQRAQLQAGQPcplcgstSHPAV--E 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1130 LRGAQEVGERlQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQ 1209
Cdd:PRK10246 519 AYQALEPGVN-QSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDD 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1210 IQamPLADSQAVRE----QLRQEQALLEEIERHGEKVEEcqrfakqyinaikdYELQLVTYKAQLEPVASPAKKPKVQSG 1285
Cdd:PRK10246 598 IQ--PWLDAQEEHErqlrLLSQRHELQGQIAAHNQQIIQ--------------YQQQIEQRQQQLLTALAGYALTLPQED 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1286 SESviqeyvdlrthySELTTltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1365
Cdd:PRK10246 662 EEA------------SWLAT----------------RQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEET 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1366 EAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1445
Cdd:PRK10246 714 VALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1446 GGAegelQALRARAEEAEAQKRQAQEE-------AERLRRQVQDESQRKRQ---AEVELASRVKAEAEAAREKQRALQAL 1515
Cdd:PRK10246 794 QQA----QTLVTQTAQALAQHQQHRPDgldltvtVEQIQQELAQLAQQLREnttRQGEIRQQLKQDADNRQQQQALMQQI 869
|
....*....
gi 2462619853 1516 EELRLQAEE 1524
Cdd:PRK10246 870 AQATQQVED 878
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1655-1848 |
1.01e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1734
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1735 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1814
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 2462619853 1815 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAE 1848
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1073-1367 |
1.08e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1073 RGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEvgERLQQRhgERDVEVE 1152
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQE--EIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1153 RWRE-------------RVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYR----ESADPLGAWLQDARRRQEQIQAMPL 1215
Cdd:pfam17380 376 RMRElerlqmerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRaeqeEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1216 ADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQlVTYKAQLEPVASPAKKPKVQSGSESVIQEYVD 1295
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1296 LRTHYSElttltsqyikfiSETLRRMEEEERLAEQQR--AEERERLAEVEAALEKQRQLAEAHaqaKAQAEREA 1367
Cdd:pfam17380 535 RREAEEE------------RRKQQEMEERRRIQEQMRkaTEERSRLEAMEREREMMRQIVESE---KARAEYEA 593
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1316-1420 |
1.08e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 43.93 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQ-------AEREAKELQQRMQEEVVRREEA-- 1384
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKqkaaesaSKSLAKPERKVSQEEAKEVLQEwe 148
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462619853 1385 -AVDAQQQKRsiQEELQQLRQSSEAEIQAKARQAEAA 1420
Cdd:pfam13904 149 rKKLEQQQRK--REEEQREQLKKEEEEQERKQLAEKA 183
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1462-1910 |
1.09e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.13 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1462 AEAQKRQAQEEAERLRRQVQDES-QRKRQAEVElASRVKAEAEAAREKQRALQALEElrlqAEEAERRLRQAEVERA-RQ 1539
Cdd:pfam09731 73 SAVTGESKEPKEEKKQVKIPRQSgVSSEVAEEE-KEATKDAAEAKAQLPKSEQEKEK----ALEEVLKEAISKAESAtAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1540 VQVALETAQRSAEAELQSKRASFA-EKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1618
Cdd:pfam09731 148 AKEAKDDAIQAVKAHTDSLKEASDtAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1619 LRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQqrLAAEQELIRLRAE 1698
Cdd:pfam09731 228 LDNVEEKVEKAQSLAKLVDQYKEL------------VASERIVFQQELVSIFPDIIPVLKEDNLL--SNDDLNSLIAHAH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1699 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASkaraeeesrstsEKSKQRLEAEagrfrelae 1778
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAA------------DEAQLRLEFE--------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1779 eaarlRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR-RRL 1857
Cdd:pfam09731 353 -----REREEIRESYEEKLRTELERQAEAHEEHLKDVLVE--QEIELQREFLQDIKEKVEEERAGRLLKLNELLANlKGL 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 1858 EEQAAQHKADIEERLA--QLRKASDSelerqkglVEDTLR------QRRQVEEEILALKAS 1910
Cdd:pfam09731 426 EKATSSHSEVEDENRKaqQLWLAVEA--------LRSTLEdgsadsRPRPLVRELKALKEL 478
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2136-2344 |
1.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2136 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRLKAEATEAAR--QRSQVEEELFSVRVQ 2213
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERREELGERARalYRSGGSVSYLDVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2214 MEELSKLKARIEAENRaLILRDKD--NTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2290
Cdd:COG3883 111 SESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKaELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 2291 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRT 2344
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1231-1724 |
1.14e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1231 LLEEIERHGEKVEECQRFAKQYI---NAIKDY---ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELT 1304
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLkelIEKKDHltkELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1305 TLTSQYIKFISE---TLRRMEEEERlAEQQRAEERE-RLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvr 1380
Cdd:pfam05483 342 KAKAAHSFVVTEfeaTTCSLEELLR-TEQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED--- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1381 reEAAVDAQQQKRSIQEELQQ-------LRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-------------- 1439
Cdd:pfam05483 418 --EKLLDEKKQFEKIAEELKGkeqelifLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcd 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1440 --ATERQRGGAEGELQALRARAEEAEAQKRQAQEEA--------ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1509
Cdd:pfam05483 496 klLLENKELTQEASDMTLELKKHQEDIINCKKQEERmlkqienlEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1510 RALQ---------------ALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSA--------EAELQSKRASFAEK 1565
Cdd:pfam05483 576 RSIEyevlkkekqmkilenKCNNLKKQIENKNKNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEI 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1566 TAQLERSLQEEHVAVAQLREEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKslaqaeaekqkEE 1645
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEE---------------------VEKAKAIADEAVKLQKEIDKRCQHK-----------IA 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1646 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1724
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2237-2406 |
1.15e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2237 DNTQRFLQEEAEKMKQVAEEAarlSVAAQEAARLRQlaEEDLAQqrALAEKMLKEKMQAVQEATRLKAEAElLQQQKEla 2316
Cdd:pfam05262 202 DLKERESQEDAKRAQQLKEEL---DKKQIDADKAQQ--KADFAQ--DNADKQRDEVRQKQQEAKNLPKPAD-TSSPKE-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2317 qeqARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRkqaEEIGEKLHR 2396
Cdd:pfam05262 272 ---DKQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR---EPVAEDLQK 339
|
170
....*....|
gi 2462619853 2397 TELATQEKVT 2406
Cdd:pfam05262 340 TKPQVEAQPT 349
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2268-2443 |
1.15e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2268 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLAEETQG 2340
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2341 FQRTLEAERQRQLemsaeAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2420
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 2462619853 2421 DAERLREAIAELEREKEKLQQEA 2443
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1336-1541 |
1.15e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1336 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEelqQLRQSSEAEIQAKAR 1415
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAE---AASAPEAAQARERRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1416 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqaLRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAEVELA 1495
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEE-----EERDERRRRGDREDRQAEAERGERG--RREERGRDGDDRDR 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462619853 1496 SRVKAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEVERARQVQ 1541
Cdd:PRK12678 206 RDRREQGDRREERGRRDGGDRrGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3662-3700 |
1.16e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2462619853 3662 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 3700
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1655-1951 |
1.16e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQAVRQRELAEQelekqrqlaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEE--ELARLQREAAAATQKRQ-ELE 1731
Cdd:COG5185 279 RLNENANNLIKQFEN------------TKEKIAEYTKSIDIKKATESLEEQLAAAEAeqELEESKRETETGIQNLTaEIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1732 AELAKVRAEMEVLLASKARAEEESRstSEKSKQRLEAEAGRFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERV 1811
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVE--LSKSSEELDSFKDTIESTKES---LDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1812 LAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA-----QHKADIEERLAQLRKASDS---EL 1883
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrsvrSKKEDLNEELTQIESRVSTlkaTL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1884 ERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA--EDTLRSKEQAELEAARQRQ 1951
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELiqASNAKTDGQAANLRTAVID 571
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1314-1419 |
1.18e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 44.21 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1314 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAK------AQ--AEREAKELQQRMQEEV-V 1379
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEvakiqmQQkiMEKEAEKKISEIEDEMhL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462619853 1380 RREEAAVDAQQQKRSIQEELQQLRQSSE----AEIQAKARQAEA 1419
Cdd:cd03406 237 AREKARADAEYYRALREAEANKLKLTPEylelKKYQAIANNTKI 280
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1319-1575 |
1.20e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1319 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREakelqqrmqeevvrREEAAVDAQQQKRSIQE 1397
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1398 ELQqLRQSSEAEIQAKARQAEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQAQEEAERLR 1477
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNHEEEVRELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1478 RQVQDESqrkRQAEV------ELAS-----RVKAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEVERA---RQ 1539
Cdd:pfam00038 149 AQVSDTQ---VNVEMdaarklDLTSalaeiRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEITelrRT 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462619853 1540 VQ-------------VALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1575
Cdd:pfam00038 226 IQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1682-1979 |
1.20e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1682 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAA----TQKRQELEAELAKVRAEME----VLLASKARAEE 1753
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErlaeLEAKRQAEEEAREAKAEAEqraaELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1754 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA 1829
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKaeeaKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1830 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKA 1909
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1910 SFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAAR 1979
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2241-2453 |
1.28e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2241 RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2316
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2317 QEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARA----EEDAQRFRKQAEEIG 2391
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 2392 EKLHRTELATQEKVTLVQTLEIQRQQ------SDHDAERLREAIAELErEKEKLQQ------EAKLLQLKSEEM 2453
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldtemaQLRVQRLRYEDL 355
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2149-2603 |
1.34e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2149 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEN 2228
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2229 RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2308
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2309 LQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2388
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2389 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQAL 2468
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2469 QQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQE 2548
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2549 ELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTL 2603
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2246-2381 |
1.35e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2246 EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2321
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 2322 RLQEDKEQmaQQLAEetqgfqrtLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2381
Cdd:PTZ00491 761 QELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2089-2410 |
1.43e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2089 EEAERLKQSAEEQAQARAQAQAAAEKLRkeaeqeAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLrqkaqvEQELTTL 2168
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIA------EYTKSIDIKKATESLEEQLAAAEAEQELEESKR------ETETGIQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2169 RLQlEETDHQKNLLDEELQRLKAEATE--AARQRSQVEEELFSVRVQMEElskLKARIEAENRALilrdKDNTQRFLQEE 2246
Cdd:COG5185 340 NLT-AEIEQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIES---TKESLDEIPQNQ----RGYAQEILATL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2247 AEKMKQVAEEAARLSVAaqeaarLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqARRLQ 2324
Cdd:COG5185 412 EDTLKAADRQIEELQRQ------IEQATSSNEEVSKLLneLISELNKVMREADEESQSRLEEAYDEINRSVRSK-KEDLN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2325 EDKEQMAQQLAEETQGFQrTLEAERQRQLE-----MSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2399
Cdd:COG5185 485 EELTQIESRVSTLKATLE-KLRAKLERQLEgvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAA 563
|
330
....*....|.
gi 2462619853 2400 ATQEKVTLVQT 2410
Cdd:COG5185 564 NLRTAVIDELT 574
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1967-2402 |
1.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1967 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR--QLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQq 2044
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEER- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2045 tlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEA-ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEA 2123
Cdd:COG4717 155 --------LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2124 ARRAQAeqaalrQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQV 2203
Cdd:COG4717 227 EELEQL------ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2204 EEELFSVRVQmEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEA--ARLRQLAEEDLAQQ 2281
Cdd:COG4717 301 GKEAEELQAL-PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2282 RALAEKMLKEKMQAVQEATRLKAEAELLQQQkeLAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAER 2361
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQ--LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2462619853 2362 LKLRVAEMSRAQ--ARAEEDAQRFRKQAEEIGEKLHRTELATQ 2402
Cdd:COG4717 458 LEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1345-1858 |
1.47e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1345 ALEKQRQLAEAHAQA---KAQAEREAKELQQrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---EIQAKARQAE 1418
Cdd:pfam05557 22 ELEHKRARIELEKKAsalKRQLDRESDRNQE-LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEAlnkKLNEKESQLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1419 AAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ---DESQRKRQAEVELA 1495
Cdd:pfam05557 101 DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1496 SRV-------KAEAEAAR--EKQRALQALEE--------------LRLQAEEAERRLRQaeVERARQVQVALETAQRSAE 1552
Cdd:pfam05557 181 SQEqdseivkNSKSELARipELEKELERLREhnkhlnenienkllLKEEVEDLKRKLER--EEKYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1553 AELQSkrasfAEKTAQ---------------LERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQ 1612
Cdd:pfam05557 259 QELQS-----WVKLAQdtglnlrspedlsrrIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLkkiedLNKK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1613 LKANEALRLRLQAEEVAQQKS-------LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA--- 1682
Cdd:pfam05557 334 LKRHKALVRRLQRRVLLLTKErdgyraiLESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1683 -QQRLAAEQELIRLRAETEQGEQQRQllEEELARLQREAaaatqkrQELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1761
Cdd:pfam05557 414 kQQAQTLERELQALRQQESLADPSYS--KEEVDSLRRKL-------ETLELERQRLREQKNELEMELERRCLQGDYDPKK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1762 SK---QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervlAEKLAAIGEATRLKTEAEIA--LKEK 1836
Cdd:pfam05557 485 TKvlhLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDD------------LEQVLRLPETTSTMNFKEVLdlRKEL 552
|
570 580
....*....|....*....|..
gi 2462619853 1837 EAENERLRRLaeDEAFQRRRLE 1858
Cdd:pfam05557 553 ESAELKNQRL--KEVFQAKIQE 572
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1418-1534 |
1.48e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1418 EAAerSRLRIE-----EEIRVVRLQLEATERQRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQdesqrkrqAE 1491
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEIEKEALKKEQdEASFERLAELRDELAELEEELEALKARWE--------AE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462619853 1492 VELASRV---KAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1534
Cdd:COG0542 467 KELIEEIqelKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1658-1801 |
1.50e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1737
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1738 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1801
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1683-1945 |
1.57e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1683 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKS 1762
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1763 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQR--------------AEAERVLAEKLAaigeatRLKTE 1828
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIK------ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1829 AEIALKEKEAENERLRRLAEDEAFQrrrleEQAAQHKADIEERLAQLRKASDS------ELERQKGLVEDTLRQRRQVEE 1902
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELR-----KEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462619853 1903 EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1945
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1328-1521 |
1.64e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1328 AEQQRAEERERlaEVEAALEKQRqlaeahAQAKAQAEREAKELQQrmqeevVRREEAAVDAQQQKRsiqeelqqlrqsSE 1407
Cdd:PTZ00491 667 AARHQAELLEQ--EARGRLERQK------MHDKAKAEEQRTKLLE------LQAESAAVESSGQSR------------AE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1408 AEIQAKARQAEAaersrlriEEEIRVVRLQLEAterQRGGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDESQr 1486
Cdd:PTZ00491 721 ALAEAEARLIEA--------EAEVEQAELRAKA---LRIEAEAELEKLRKRQElELEYEQAQNELEIAKAKELADIEAT- 788
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462619853 1487 KRQAEVELASR--VKAEAEAAREKQRALqaLEELRLQ 1521
Cdd:PTZ00491 789 KFERIVEALGRetLIAIARAGPELQAKL--LGGLGLK 823
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1346-1556 |
1.67e-03 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 44.08 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1346 LEKQRQLAEAHAQAKAqAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKaRQAEAAERSRL 1425
Cdd:pfam08017 31 LERRQRDAENRSQGNV-LERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER-RQRDAENRSQG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1426 RIEEEIR---VVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEA 1502
Cdd:pfam08017 109 NVLERRQrdaENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1503 EAAREKQRAlqalEELRLQAEEAERRLRQAEVERARQVqvaLETAQRSAEAELQ 1556
Cdd:pfam08017 189 NVLERRQRD----AENRSQGNVLERRQRDAENRSQGNV---LERRQRDAENRSQ 235
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1663-2348 |
1.72e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1663 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR---QLLEEELARLQREAAAATQKRQELEAELAKVR- 1738
Cdd:PRK10246 232 EKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpQLAALSLAQPARQLRPHWERIQEQSAALAHTRq 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1739 --AEMEVLLASKARAEEESRSTSEKSKQRLEAEAG----------RFRELAEEAARLRALAEEAKRQRQlaEEDAARQRA 1806
Cdd:PRK10246 312 qiEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslntwlaehdRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1807 EAERvlaEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLaedeafqRRRLEEQAAQHkADIEERLAQLrKASDSELERQ 1886
Cdd:PRK10246 390 THAE---QKLNALPAITLTLTADEVA--AALAQHAEQRPL-------RQRLVALHGQI-VPQQKRLAQL-QVAIQNVTQE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1887 KGLVEDTLRQRRQveeeilALKASFEKAAAGKAELELElGRIRSNAEdtlrskEQAELEAARQRQLAAEEERRRreaeer 1966
Cdd:PRK10246 456 QTQRNAALNEMRQ------RYKEKTQQLADVKTICEQE-ARIKDLEA------QRAQLQAGQPCPLCGSTSHPA------ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1967 VQKSLAAEEEAARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQT 2045
Cdd:PRK10246 517 VEAYQALEPGVNQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2046 LQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQsrRQVEEAErlKQSAEEQAQARAQAQAAAEKLRKEAEQEAAR 2125
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHN--QQIIQYQ--QQIEQRQQQLLTALAGYALTLPQEDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2126 RAqaeqaalrqkQAADAEMEKHKKFAEQTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--ATEAARQRSQ 2202
Cdd:PRK10246 668 AT----------RQQEAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQclSLHSQLQTLQ 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2203 VEEELFSVRVQmeelsKLKARIEAENRALILRDKDNTQRFLQEEaEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2282
Cdd:PRK10246 738 QQDVLEAQRLQ-----KAQAQFDTALQASVFDDQQAFLAALLDE-ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 2283 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2348
Cdd:PRK10246 812 QHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1608-1818 |
1.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1608 LERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAvrQRELAEQELEKQRQLAegTAQQRLA 1687
Cdd:COG4942 43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAELEAQKEELAELLR--ALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1688 AEQELIRLRAET-EQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL 1766
Cdd:COG4942 119 QPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 1767 EAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1818
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1665-1839 |
1.85e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1665 ELAEQELEKQRQLAEGTAqqrLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE-LAKVRAEMEV 1743
Cdd:PHA03247 1552 ERVDQSPVKDTAYAEYVA---FVARRDLAEAKDALVRAKQQRAEATDRVTAALREALAAHERRAQSEAEsLANLKTLLRV 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1744 --LLASKARAEEESRSTSEKSKQrLEAeagrFRELAEEAARLRALA----EEAKRQRQLAEEDAARQRAEAERV-LAEKL 1816
Cdd:PHA03247 1629 aaIPATAAKTLDQARSVAEIVDQ-IEL----LLEQTEKAAELDVAAvdwlEHARRVFEAHPLTAARGGGPDPLArLHARL 1703
|
170 180
....*....|....*....|...
gi 2462619853 1817 AAIGEATRLKTEAEIALKEKEAE 1839
Cdd:PHA03247 1704 DALGETRRRTEALRRSLEAAEAE 1726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
941-1366 |
1.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 941 HYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRIAEQQKAQAEVEGL 1013
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1014 GKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLR------AHEE 1087
Cdd:COG4717 169 EAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEneleaaALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1088 QLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQA 1167
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1168 VLAQTDVRQREleqlgrQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQAL--LEEIERHGEKVEEC 1245
Cdd:COG4717 324 LLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVedEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1246 QRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQyikfisetLRRMEEEE 1325
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE--------LEQLEEDG 469
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2462619853 1326 RLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE 1366
Cdd:COG4717 470 ELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1975-2499 |
1.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1975 EEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSV 2052
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2053 LDQLRGEAEAARRAAEEAEEARVQAEREAAQS-RRQVEEAER----LKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRA 2127
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEReierLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2128 QAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--------------- 2192
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlaealgldeaelpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2193 ------ATEAARQRSQVEEEL----FSVRVQMEELSKLKARIEAENRALILRdkdnTQRFLQEEAEKMKQVAEE---AAR 2259
Cdd:COG4913 464 gelievRPEEERWRGAIERVLggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdslAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2260 LSVAAQEAAR-LRQL-----------AEEDLAQ-QRAL-AEKMLKEKMQAVQEATRLKAEAELL-----QQQKELAQEQA 2320
Cdd:COG4913 540 LDFKPHPFRAwLEAElgrrfdyvcvdSPEELRRhPRAItRAGQVKGNGTRHEKDDRRRIRSRYVlgfdnRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2321 RRLQEDKEQMAQQLAEetqgfqrtLEAERQRQLEMSAEAERLklrvaemsRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2400
Cdd:COG4913 620 AELEEELAEAEERLEA--------LEAELDALQERREALQRL--------AEYSWDEIDVASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2401 TQEkvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLL 2480
Cdd:COG4913 684 SDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
570 580
....*....|....*....|....*....
gi 2462619853 2481 QRERF----------IEQEKAKLEQLFQD 2499
Cdd:COG4913 760 GDAVErelrenleerIDALRARLNRAEEE 788
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1448-1557 |
1.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1448 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEElRLQA 1522
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE-ELEK 114
|
90 100 110
....*....|....*....|....*....|....*
gi 2462619853 1523 EEAERRLRQAEVERARQVqvaLETAQRSAEAELQS 1557
Cdd:PRK12704 115 KEKELEQKQQELEKKEEE---LEELIEEQLQELER 146
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1663-2441 |
1.95e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1663 QRELAEQE-----LEKQRQLAE---GTAQQRLAAEQELIRLRAE----TEQGEQQRQLLE---EELARLQREAAAATQKR 1727
Cdd:PRK04863 313 ARELAELNeaesdLEQDYQAASdhlNLVQTALRQQEKIERYQADleelEERLEEQNEVVEeadEQQEENEARAEAAEEEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1728 QELEAELAKVRAEMEVLlASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ-----RQLAEEDAA 1802
Cdd:PRK04863 393 DELKSQLADYQQALDVQ-QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEllsleQKLSVAQAA 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1803 RQRAEAERVLAEKLAaiGEATRlkTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASD 1880
Cdd:PRK04863 472 HSQFEQAYQLVRKIA--GEVSR--SEAWDVARELLRRLREQRHLAEQLQQLRMRLSelEQRLRQQQRAERLLAEFCKRLG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1881 SELERqkglvEDTLRQ-RRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdTLRSKEQAELEA----ARQRQLAAE 1955
Cdd:PRK04863 548 KNLDD-----EDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ-RLAARAPAWLAAqdalARLREQSGE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1956 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKakvEEARRLRERAEQESARQLQLA-----------------QE 2018
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLERERELTVERDELAARKQALD---EEIERLSQPGGSEDPRLNALAerfggvllseiyddvslED 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2019 AAQKRLQAEEKAHAFAVQQKEQELQQTLQqeqsvLDQLRGEAEAARRAAEEAEEARVQA-EREAAQSRRQVEEAERLKQS 2097
Cdd:PRK04863 699 APYFSALYGPARHAIVVPDLSDAAEQLAG-----LEDCPEDLYLIEGDPDSFDDSVFSVeELEKAVVVKIADRQWRYSRF 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2098 AEEQAQARAQAQAAAEKLRKEAEQEAARRAQAE---QAALRQKQAADAEMEKHKKFAEQtlrqkAQVEQELTTLRLQLEE 2174
Cdd:PRK04863 774 PEVPLFGRAAREKRIEQLRAEREELAERYATLSfdvQKLQRLHQAFSRFIGSHLAVAFE-----ADPEAELRQLNRRRVE 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2175 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEElsKLKARIEaENRALILRDKDNtQRFLQEEAEKMKQVA 2254
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE--TLADRVE-EIREQLDEAEEA-KRFVQQHGNALAQLE 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2255 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQ-----AVQEATRLKAEA----ELLQQQKELAQEQARRL 2323
Cdd:PRK04863 925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfaLTEVVQrrahfSYEDAAEMLAKNsdlnEKLRQRLEQAEQERTRA 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2324 QEDKEQMAQQLAEETQgFQRTLEAERQRQLEMSAEAERlklrvaEMSRAQARAEEDA-QRFRKQAEEIGEKLHRTELATQ 2402
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQ-VLASLKSSYDAKRQMLQELKQ------ELQDLGVPADSGAeERARARRDELHARLSANRSRRN 1077
|
810 820 830
....*....|....*....|....*....|....*....
gi 2462619853 2403 EkvtLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ 2441
Cdd:PRK04863 1078 Q---LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2232-2439 |
1.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2232 ILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2305
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2306 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQR 2382
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 2383 FRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL 2439
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1376-1717 |
2.01e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1376 EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR------QAEAAERSRLRIEEEIRVvrLQLEATERQRGGAE 1449
Cdd:COG3206 97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNvieisyTSPDPELAAAVANALAEA--YLEQNLELRREEAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1450 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESqrkrqaevelasrVKAEAEAAREKQRALQA-LEELRLQAEEAERR 1528
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-------------LSEEAKLLLQQLSELESqLAEARAELAEAEAR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1529 LRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAerraqqqaeaerareeaerel 1608
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI--------------------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1609 erwqlkanEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgKAEEQAVRQRElaeQELEKQRQLAEGTAQQRLAA 1688
Cdd:COG3206 301 --------AALRAQLQQEAQRILASL--------------------EAELEALQARE---ASLQAQLAQLEARLAELPEL 349
|
330 340
....*....|....*....|....*....
gi 2462619853 1689 EQELIRLRAETeqgEQQRQLLEEELARLQ 1717
Cdd:COG3206 350 EAELRRLEREV---EVARELYESLLQRLE 375
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1768-2278 |
2.04e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.46 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1768 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLa 1847
Cdd:COG3899 752 AEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEA- 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1848 edeafQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGR 1927
Cdd:COG3899 831 -----RALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1928 IRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2007
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2008 ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2087
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2088 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfaeqtLRQKAQVEQELTT 2167
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL------------AALALAAAARAAA 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2168 LRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEA 2247
Cdd:COG3899 1134 ALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALA 1213
|
490 500 510
....*....|....*....|....*....|.
gi 2462619853 2248 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2278
Cdd:COG3899 1214 LLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1715-1947 |
2.05e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1715 RLQREAAAATQKRQELEAELAKVRAEMEVLLA--SKARAEEESRSTSEKSKQRLEaeagRFRELAEEAARLRALAEEAKR 1792
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQ----QLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1793 QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIAlkekeaeneRLRRLAEDEAFQRRRLEEQaaqhKADIEERL 1872
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA---------ELSARYTPNHPDVIALRAQ----IAALRAQL 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1873 AQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAA 1947
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2348-2672 |
2.15e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2348 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2408
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2409 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEKDSLLQRERFIEQ 2488
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2489 EKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqQRRQQEELLAEEN 2568
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----------LRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2569 QrLREQLQLLEEQ-HRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQ 2647
Cdd:TIGR02168 397 S-LNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*
gi 2462619853 2648 RLAQGHTTVDELARREDVRHYLQGR 2672
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQEN 500
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2193-2618 |
2.15e-03 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 44.22 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2193 ATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQ 2272
Cdd:COG5281 2 AALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2273 LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2352
Cdd:COG5281 82 AALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAA--AAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2353 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAEL 2432
Cdd:COG5281 160 AAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2433 EREKEKLQQEAKLLQLKSEEmQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQ 2512
Cdd:COG5281 240 ASAAAQALAALAAAAAAAAL-ALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2513 RQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL--QLLEEQHRAALAHSE 2590
Cdd:COG5281 319 AAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWaaGAKAALAEYADSATN 398
|
410 420
....*....|....*....|....*...
gi 2462619853 2591 EVTASQVAATKTLPNGRDALDGPAAEAE 2618
Cdd:COG5281 399 VAAQVAQAATSAFSGLTDALAGAVTTGK 426
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2215-2343 |
2.24e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2215 EELSKLKARIEAENRALILRDKDNTQrfLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2294
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462619853 2295 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAEETQGFQR 2343
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1167-1426 |
2.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1167 AVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVE 1243
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1244 ECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESVIQEYVDLRthyseLTTLTSQYIKFISETLRRMEE 1323
Cdd:COG4942 94 ELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1324 EERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAKELQQRMQEEvvrrEEAAVDAQQQKRSIQEELQQLR 1403
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 2462619853 1404 QSSEAEIQAKARQAEAAERSRLR 1426
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1706-2018 |
2.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1706 RQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1785
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1786 LAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 1865
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1866 ADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1945
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1946 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2018
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1664-2097 |
2.37e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.13 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1664 RELAEQELEKQRQLAEGTAQQRlaaeQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEV 1743
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQQ----ARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1744 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1823
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1824 RLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEE 1903
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1904 ILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1983
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1984 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAA 2063
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430
....*....|....*....|....*....|....
gi 2462619853 2064 RRAAEEAEEARVQAEREAAQSRRQVEEAERLKQS 2097
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAE 514
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
16-124 |
2.37e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.13 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 16 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 86
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462619853 87 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 124
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2183-2335 |
2.42e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2183 DEELQRLKAEATEAARQRSQVEEELfSVRVQMEELSKLKARIEAENRALILR---DKDNTQRFLQEEAEKMKQVAEEAAR 2259
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEAEL-AKKKAEERREAETARAEAEAAYEIAEanaEREVQRQLEIAEREREIELQEKEAE 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 2260 LSVAAQEAA-RLRQLAEEDLAQQRALAE-KMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLA 2335
Cdd:COG2268 301 REEAELEADvRKPAEAEKQAAEAEAEAEaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2134-2355 |
2.45e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2134 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQ-VEEELFSVRV 2212
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2213 QMEELSKLKARIEAENRALILRDKdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--- 2289
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKERQK---EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEdee 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 2290 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEM 2355
Cdd:pfam13868 276 IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1487-1721 |
2.52e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1487 KRQAEVELASRVKAEaeaaREKQRALQAleELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEkt 1566
Cdd:pfam15709 327 KREQEKASRDRLRAE----RAEMRRLEV--ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1567 aqlERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeea 1646
Cdd:pfam15709 399 ---ERQRQEEEERKQRLQLQAAQ-------------------ERARQQQEEFRRKLQELQRKKQQEEAE----------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 1647 erearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1721
Cdd:pfam15709 446 --------RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1349-1508 |
2.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1349 QRQLAEAHAQAK---AQAEREAKELQQRM----QEEVVR-REEAAVDAQQQKRSIQEELQQLRQSSEAEiqakARQAEAA 1420
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAIKKEAlleaKEEIHKlRNEFEKELRERRNELQKLEKRLLQKEENL----DRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1421 ERSrlriEEEIRVVRLQLEATERqrggaegELQALRARAEEAEAQKRQA--------QEEA-ERLRRQVQDESQRkrqae 1491
Cdd:PRK12704 106 EKR----EEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEEARH----- 169
|
170
....*....|....*..
gi 2462619853 1492 vELASRVKAEAEAAREK 1508
Cdd:PRK12704 170 -EAAVLIKEIEEEAKEE 185
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
27-117 |
2.64e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.75 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 27 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 99
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 2462619853 100 DDIADGNPKLTLGLIWTI 117
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1313-1529 |
2.74e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1313 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAKELQQRMQEEVVRREEAAVDAQQQ- 1391
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRLEQQTEQAKKLEEKAQAALTKGNEEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1392 KRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1471
Cdd:pfam04012 85 AREALAEKKSLEKQAEALETQLAQQRSAVEQ-----------LRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1472 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQaLEELRLQAEEAERRL 1529
Cdd:pfam04012 154 LGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2157-2499 |
2.78e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2157 QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENralilrDK 2236
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI------DK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2237 DNTQRFLQEEaekmkqvaeeaaRLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ-K 2313
Cdd:TIGR04523 192 IKNKLLKLEL------------LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2314 ELAQEQarrlQEDKEQMAQQLAEETQGFQRTLEAERQRQlEMSAEAERLKlrvaemsraqaraeedaqrfrKQAEEIGEK 2393
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN---------------------NQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2394 LHRTELATQEKVtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvqqeqllqetqaLQQSFL 2473
Cdd:TIGR04523 311 ELKSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN------------EIEKLK 376
|
330 340
....*....|....*....|....*.
gi 2462619853 2474 SEKDSLLQRERFIEQEKAKLEQLFQD 2499
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN 402
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1448-1531 |
2.92e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1448 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVElasrvKAEAEAAREKQralQALEELRLQAEEAER 1527
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-----EAKEEAERILE---QAKAEIEQEKEKALA 113
|
....
gi 2462619853 1528 RLRQ 1531
Cdd:cd06503 114 ELRK 117
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1346-1524 |
2.99e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1346 LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrl 1425
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1426 rieeeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEVELASRVKAEAEaa 1505
Cdd:PRK12705 100 ------------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180
....*....|....*....|
gi 2462619853 1506 REK-QRALQALEELRLQAEE 1524
Cdd:PRK12705 157 EEKaQRVKKIEEEADLEAER 176
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2310-2591 |
3.05e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2310 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2389
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRK----LEEAEKARQ----AEMDRQAAIYAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2390 I-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDhdaERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQA 2467
Cdd:pfam17380 360 ReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2468 LQQsflsekdslLQRERFIEQEKAKLEQLFQDEvakaqqlREEQQRQQQQMEQERQRlvaSMEEARRRQHEAEEgVRRKQ 2547
Cdd:pfam17380 437 VRR---------LEEERAREMERVRLEEQERQQ-------QVERLRQQEEERKRKKL---ELEKEKRDRKRAEE-QRRKI 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462619853 2548 EELQQLEQQRRQQeellaeENQRLREQLQLLEEQHRAALAHSEE 2591
Cdd:pfam17380 497 LEKELEERKQAMI------EEERKRKLLEKEMEERQKAIYEEER 534
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1521-1918 |
3.11e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1521 QAEEAERRLRQAEVERARQVQvALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEA 1597
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQ-AQEAANRQREKEKErykRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1598 ERAREeaerelerwQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE--EQAVRQRELAEQELEKQR 1675
Cdd:pfam07888 107 SASSE---------ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKEraKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1676 QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1755
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1756 RSTSEKSKQR--LEAEAGRFR-ELAEEAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLkteaE 1830
Cdd:pfam07888 258 EELSSMAAQRdrTQAELHQARlQAAQLTLQLAdaSLALREGRARWAQERETLQQSAEADKDRIEKLSA--ELQRL----E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1831 IALKEKEAENERLR-RLAEDEAFQRRRLEEQaaqhkadieERLAQLRKASDSELERQKglvEDTLRQRRQVEEEILALKA 1909
Cdd:pfam07888 332 ERLQEERMEREKLEvELGREKDCNRVQLSES---------RRELQELKASLRVAQKEK---EQLQAEKQELLEYIRQLEQ 399
|
....*....
gi 2462619853 1910 SFEKAAAGK 1918
Cdd:pfam07888 400 RLETVADAK 408
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1452-1576 |
3.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1452 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELasrvKAEAEaarekQRALQALEELRLQAEEAERRLRQ 1531
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462619853 1532 AEVERARQVqvaletaqrsAEAELQSKRASFAEKTAQLERSLQEE 1576
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1295-1630 |
3.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1295 DLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAKELQQRM 1374
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1375 QEEVVRREEAAvDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQA 1454
Cdd:COG4372 94 AELAQAQEELE-SLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1455 LRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1534
Cdd:COG4372 169 LEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1535 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1614
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|....*.
gi 2462619853 1615 ANEALRLRLQAEEVAQ 1630
Cdd:COG4372 327 KLELALAILLAELADL 342
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1780-1924 |
3.28e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1780 AARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 1859
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1860 QAAQ------HKADIEERLAQLRKASDSELERQKGLVEDTLRQR--RQVEEEILALKASFEKAAAGKAELELE 1924
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1386-1532 |
3.29e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1386 VDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvvrlqleaterqrggAEGELQALRARAEEAEAQ 1465
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1466 KRQAQEEAERLRRQVQDESQRKRQaevelasrvkaeaeaaREKQRALQALEELRLqaEEAERR------LRQA 1532
Cdd:PRK11448 193 QQELEAQLEQLQEKAAETSQERKQ----------------KRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1316-1575 |
3.32e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 43.51 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKelQQRMQEEVVRREEAAVDAqqqkrsi 1395
Cdd:pfam04747 68 EKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHK--QWKAEQERIQKEQEKKEA------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1396 qeELQQLRQSSEAEIQAKARQAEAAERSR-----LRIEEEIRVVRLqleATERQRGGAEGELQALRARAEEAEaqkrQAQ 1470
Cdd:pfam04747 139 --DLKKLQAEKKKEKAVKAEKAEKAEKTKkastpAPVEEEIVVKKV---ANDRSAAPAPEPKTPTNTPAEPAE----QVQ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1471 EEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1550
Cdd:pfam04747 210 EITGKKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPA 289
|
250 260
....*....|....*....|....*
gi 2462619853 1551 AEAELQSKRasfAEKTAQLERSLQE 1575
Cdd:pfam04747 290 SENQKKNKK---DKKKSESEKVVEE 311
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1861-2037 |
3.34e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1861 AAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE 1940
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1941 QAELEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2006
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 2462619853 2007 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2037
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1841-2022 |
3.61e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1841 ERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAE 1920
Cdd:COG1579 7 RALLDLQELDS-ELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEI-------EEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1921 LELELGRIRSNAE-DTLrskeQAELEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 1999
Cdd:COG1579 78 YEEQLGNVRNNKEyEAL----QKEIESLKRRI---------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
170 180
....*....|....*....|...
gi 2462619853 2000 RLRERAEQESARQLQLAQEAAQK 2022
Cdd:COG1579 145 AELDEELAELEAELEELEAEREE 167
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2666-2703 |
3.63e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.63e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2462619853 2666 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 2703
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1703-1913 |
3.64e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1703 EQQRQLLEeeLARLQREAAAATQKRQELEAELAKVRAEMEvllaskaraeeesrstsekskqrleaeagrfrELAEEAAR 1782
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELA--------------------------------ALEARLEA 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1783 LRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIgeatrlKTEAEI-ALKEKEAENERLRRLAEDEAFQRRRLEEQA 1861
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNV------RNNKEYeALQKEIESLKRRISDLEDEILELMERIEEL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 1862 AQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEK 1913
Cdd:COG1579 123 EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1366-1504 |
3.65e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1366 EAKELQQRMQEevVRREEAAVDAQQQKRSiQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1445
Cdd:COG0542 412 ELDELERRLEQ--LEIEKEALKKEQDEAS-FERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619853 1446 GGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEVELASRVKAEAEA 1504
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1319-1408 |
3.67e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1319 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAH-------AQAKAQAEREAKE-LQQRMQEEVVRREEAAVDAQ 1389
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARkqaqaviAEAEAEADKLAAEaLAEAQAEAQASKEKARREIE 111
|
90
....*....|....*....
gi 2462619853 1390 QQKrsiQEELQQLRQSSEA 1408
Cdd:PRK07353 112 QQK---QAALAQLEQQVDA 127
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2134-2398 |
3.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2134 LRQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE 2206
Cdd:COG1340 14 EEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2207 LFSVRVQMEEL-------SKLKARIEA-------------ENRALILRDKDntqrfLQEEAEKMKQVAEEAARLSVAAQE 2266
Cdd:COG1340 94 LDELRKELAELnkaggsiDKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2267 AARLRQLAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaeetqgfqr 2343
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL--------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2344 tleaerqRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2398
Cdd:COG1340 240 -------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1658-1823 |
3.90e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1737
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1817
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 2462619853 1818 AIGEAT 1823
Cdd:COG3883 275 GAAAAS 280
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1663-1756 |
3.93e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.29 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1663 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEME 1742
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 2462619853 1743 VLLASKARAEEESR 1756
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1337-1508 |
3.97e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1337 ERLAEVEAALEK-QRQLAEAHAQAKAQAEREAKELQQRMQ---EEVVRREEAAVDAQQQKrsIQEELQQLRQsseaeiQA 1412
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQkdlEEVRAKLEPYLEELQAK--LGQNVEELRQ------RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1413 KARQAEAAERSRLRIEEEIRVVRlqlEATERQRGGAEGELQALRARAEEAEAQKRQ-----AQEEAERLRRQVQDESQRK 1487
Cdd:pfam01442 76 EPYTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPYAEELRQklaerLEELKESLAPYAEEVQAQL 152
|
170 180
....*....|....*....|.
gi 2462619853 1488 RQAEVELASRVKAEAEAAREK 1508
Cdd:pfam01442 153 SQRLQELREKLEPQAEDLREK 173
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1609-2092 |
4.06e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1609 ERWQLKANEALRLRLQAEEVAQQKSLAQ--AEAEKQKEEAER---------------EARRRGKAEEQAVRQRELAEQEL 1671
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKriRLLEKREAEAEEalreqaelnrlkkkyLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1672 EKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEM 1741
Cdd:pfam05557 108 CLKNELSE-LRRQIQRAELELQSTNSELEELQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1742 EVLLASKarAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLA- 1817
Cdd:pfam05557 187 EIVKNSK--SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSw 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1818 -AIGEATRLKTEAEIALKEK--EAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASDSE---LERQKGLVE 1891
Cdd:pfam05557 265 vKLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1892 DTLRQRRQVEEEILALKA---SFEKAAAGKAELELELGRIRSNAEDTLRSKEQ-AELEAARQRQLAAEEERRRREAEERV 1967
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAEDMTQKMQAHnEEMEAQLSVAEEELGGYKQQAQTLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1968 QKSLAAEEEAARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQEAAQKR---LQAEEKAHAFAVQQK 2038
Cdd:pfam05557 423 ELQALRQQESLADPSYSKEEVDSLRRKLETLElerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAEAYQQR 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 2039 EQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE 2092
Cdd:pfam05557 503 KNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1079-1575 |
4.11e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1079 EEVLRAHEEQLKEAQAVPATL-PELEATKASL-------KKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVE 1150
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLtKELEDIKMSLqrsmstqKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1151 VERWRERVAQLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQA 1230
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKN---EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1231 LLEEIErhgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqEYVDLRTHYSELTTLTSQY 1310
Cdd:pfam05483 430 IAEELK---GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL--KNIELTAHCDKLLLENKEL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1311 IKFISE-TLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRM---QEEVVRREEAAV 1386
Cdd:pfam05483 505 TQEASDmTLELKKHQEDIINCKKQEER-MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLdksEENARSIEYEVL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1387 DAQQQKRSIQEELQQLRQS--------SEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-ATERQRGG-------AEG 1450
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQienknkniEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKFEeiidnyqKEI 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1451 ELQALRARAEEAEAQKRQA-QEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERrl 1529
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAiADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK-- 741
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462619853 1530 rqaeverarqvqVALETAQRSAEAELQSKRASFA---EKTAQLERSLQE 1575
Cdd:pfam05483 742 ------------AALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKE 778
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2136-2504 |
4.13e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2136 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKnlldEELQRLKAEATEAARQrsQVEEELFSVRVQME 2215
Cdd:pfam09731 98 SSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKA----ESATAVAKEAKDDAIQ--AVKAHTDSLKEASD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2216 --ELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA------LAEK 2287
Cdd:pfam09731 172 taEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLaklvdqYKEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2288 MLKEKMQAVQEATRLkaEAELLQQQKELAQEQARRL-------QEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEA 2359
Cdd:pfam09731 252 VASERIVFQQELVSI--FPDIIPVLKEDNLLSNDDLnsliahaHREIDQLSKKLAElKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2360 ERLKLRVAE---MSRAQARAEEDAQRFRkQAEEIGEKLhRTELATQEKV---TLVQTLEIQRQQSDHDAERLREAIAELE 2433
Cdd:pfam09731 330 EELSARLEEvraADEAQLRLEFEREREE-IRESYEEKL-RTELERQAEAheeHLKDVLVEQEIELQREFLQDIKEKVEEE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2434 REKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQ---------SFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 2504
Cdd:pfam09731 408 RAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQlwlavealrSTLEDGSADSRPRPLVRELKALKELASDDEVVKA 487
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2232-2447 |
4.22e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2232 ILRDKDNTQRFLQEeaeKMKQVAEEAARLSVAAQEAARLRQLAE---EDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2308
Cdd:pfam06008 17 INYNLENLTKQLQE---YLSPENAHKIQIEILEKELSSLAQETEelqKKATQTLAKAQQVNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2309 LQQQKELAQEQARRLQEDKEQMA-QQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAE--MSRAQARAEEDAQRFRK 2385
Cdd:pfam06008 94 LIDNIKEINEKVATLGENDFALPsSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQdlLSRIQTWFQSPQEENKA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462619853 2386 QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2447
Cdd:pfam06008 174 LANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLE 235
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1322-1505 |
4.26e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1322 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAV-DAQQQKRSIQEELQ 1400
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIaRAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1401 QLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQAQEEAErlrrqv 1480
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*.
gi 2462619853 1481 QDESQRKrqAEVELA-SRVKAEAEAA 1505
Cdd:PRK05035 671 EAEDPKK--AAVAAAiARAKAKKAAQ 694
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2145-2353 |
4.34e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2145 EKHKKFAEQTLrqkAQVEQELTTLRLQLE-----ETDHQKNLLDEELQRLKAEATEAAR-QRSQVEEElfsVRVQMEELS 2218
Cdd:COG2268 147 EDREKFAEKVQ---EVAGTDLAKNGLELEsvaitDLEDENNYLDALGRRKIAEIIRDARiAEAEAERE---TEIAIAQAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2219 KLKARIEAENRALIL--------RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlK 2290
Cdd:COG2268 221 REAEEAELEQEREIEtariaeaeAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-A 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 2291 EKMQAVQEAT-RLKAEAELLQQQKElAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQL 2353
Cdd:COG2268 300 EREEAELEADvRKPAEAEKQAAEAE-AEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLML 362
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1073-1744 |
4.47e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1073 RGTQGAEEVLRAHEEQLKEAQAVPATLPEleatkaslkklrAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVE 1152
Cdd:NF041483 569 RQAEAAEELTRLHTEAEERLTAAEEALAD------------ARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQEAE 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1153 RWRERVAQLLERWQAVLAQTDVRQR-----ELEQLGRQLRyyrESADPLGAWLQDARRR--QEQIQAMPLADSQAVREQL 1225
Cdd:NF041483 637 RLRTEAAADASAARAEGENVAVRLRseaaaEAERLKSEAQ---ESADRVRAEAAAAAERvgTEAAEALAAAQEEAARRRR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1226 RQEQALL-------EEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESV--IQEYVDl 1296
Cdd:NF041483 714 EAEETLGsaraeadQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVagLQEQAE- 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1297 rthySELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEvEAALEKQRQLAEAHAqAKAQAER----------- 1365
Cdd:NF041483 793 ----EEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASE-DANRLRREAQEETEA-AKALAERtvseaiaeaer 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1366 ---EAKELQQRMQEEVV-RREEAAVDAQQQKRSIQEELQQLRqsSEAEIQAKARQAEAAErsrlrieEEIRVVRLQLEAT 1441
Cdd:NF041483 867 lrsDASEYAQRVRTEASdTLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEATS-------EAERLTAEARAEA 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1442 ERQRGGAEGELQALRARA-EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL---ASRVKAEAEAAREKQRALQALEE 1517
Cdd:NF041483 938 ERLRDEARAEAERVRADAaAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIrteAERVKAEAAAEAERLRTEAREEA 1017
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1518 LRL----QAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASfAEKTAQLERSLQEEHVAVAQLREEAERRAQQ 1593
Cdd:NF041483 1018 DRTldeaRKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT-TEAEAQADTMVGAARKEAERIVAEATVEGNS 1096
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1594 QAEAERAREEAERELERWQLKAN----EALRLRLQAE-----EVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1664
Cdd:NF041483 1097 LVEKARTDADELLVGARRDATAIreraEELRDRITGEieelhERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKE 1176
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1665 ELAEQELE----------KQRQLAEGTAQQRLAAEQELIRLRAETEQgeQQRQLLEEElarlQREAAAATQKRQELEAEL 1734
Cdd:NF041483 1177 LVSDANSEaskvriaavkKAEGLLKEAEQKKAELVREAEKIKAEAEA--EAKRTVEEG----KRELDVLVRRREDINAEI 1250
|
730
....*....|
gi 2462619853 1735 AKVRAEMEVL 1744
Cdd:NF041483 1251 SRVQDVLEAL 1260
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1321-1401 |
4.63e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1321 MEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAH-------AQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQ 1391
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEyEEKLAEARaeaqeiiEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQE 107
|
90
....*....|
gi 2462619853 1392 KRSIQEELQQ 1401
Cdd:cd06503 108 KEKALAELRK 117
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1334-1564 |
4.70e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1334 EERERLAEVEAAL-------EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS 1406
Cdd:pfam13868 3 ENSDELRELNSKLlaakcnkERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1407 EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---------- 1476
Cdd:pfam13868 83 EEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREederileylk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1477 -----RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQaEEAERRLRQAEVERARQVQVALETAQRSA 1551
Cdd:pfam13868 163 ekaerEEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ-EEQERKERQKEREEAEKKARQRQELQQAR 241
|
250
....*....|...
gi 2462619853 1552 EAELQSKRASFAE 1564
Cdd:pfam13868 242 EEQIELKERRLAE 254
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2248-2342 |
4.93e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.27 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2248 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2321
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 2462619853 2322 RLQEDKEQMAQQLAEETQGFQ 2342
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2185-2446 |
4.93e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.97 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2185 ELQRLKAEATEAARQRSQVEEElfsvrvqmEELSKLKARIEAEN-RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVA 2263
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEE--------ANFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2264 AQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQgf 2341
Cdd:pfam15964 397 EREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH-- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2342 qRTLEAERQRQLEMS-AEAERLKL-------RVAEMSRAQARAEEDAQRFrkqAEEIGEKLHRTELATQEKVTLVQTL-- 2411
Cdd:pfam15964 473 -REYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREECLKL---TELLGESEHQLHLTRLEKESIQQSFsn 548
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462619853 2412 --EIQRQQSDHDAERLREAIAELEREKEKLQQEAKLL 2446
Cdd:pfam15964 549 eaKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSL 585
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1400-1880 |
4.99e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1400 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1478
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1479 QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK 1558
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1559 RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAE 1638
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1639 AEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELiRLRAETEQGEQQRQLLEEELARLQR 1718
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGL-VLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1719 EAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1798
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1799 EDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1878
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
..
gi 2462619853 1879 SD 1880
Cdd:COG3064 481 LL 482
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1203-1539 |
5.03e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1203 ARRRQEQIQAMpLADSQAVREQLRQE-QALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVaspakkpk 1281
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDEL-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1282 vqsgsESVIQEYVDLRTHYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1360
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1361 AQ--------AEREAKELQQRMQEEVVRREEAAVD-AQQQKRSIQEELQQLRQSSEAEIQAKArqaeaaersrlRIEEEI 1431
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKK-----------YVEKNL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1432 RVVRLQLEATERQRGGAEGELQALRAR---AEEAEAQKRQAQEEAERLRRQVQDESQR---KRQAEVELASRVKaeaeaa 1505
Cdd:pfam06160 294 PEIEDYLEHAEEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDEIVERleeKEVAYSELQEELE------ 367
|
330 340 350
....*....|....*....|....*....|....
gi 2462619853 1506 rEKQRALQALEELRLQAEEAERRLRQAEvERARQ 1539
Cdd:pfam06160 368 -EILEQLEEIEEEQEEFKESLQSLRKDE-LEARE 399
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1349-1514 |
5.07e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1349 QRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAER-SRLRI 1427
Cdd:pfam00529 53 PTDYQAALDSAEAQL-AKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDlARRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1428 EEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqAEVElASRVKAEAEAAR 1506
Cdd:pfam00529 132 LAPIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQI-AEAE-AELKLAKLDLER 209
|
....*...
gi 2462619853 1507 EKQRALQA 1514
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1523-1859 |
5.08e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.79 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1523 EEAERRLRQAEVERARqvqvaLETAQRSAEAELQSKRASFAE----KTAQLERS---LQEEHVAVAQLREEAERRAQQQA 1595
Cdd:pfam03528 4 EDLQQRVAELEKENAE-----FYRLKQQLEAEFNQKRAKFKElylaKEEDLKRQnavLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1596 EAERAREEAerelERWQLKANEALRLRLQaEEVAqqkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL-EKQ 1674
Cdd:pfam03528 79 NIKAVATVS----ENTKQEAIDEVKSQWQ-EEVA---SLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIaDLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1675 RQLAEGTAQQRLaaEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAelAKVRAEMEVLLASKA-RAEE 1753
Cdd:pfam03528 151 RRLSEGQEEENL--EDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEA--SKMKELNHYLEAEKScRTDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1754 ESR-STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL---AEKLAAIGEATRLKTEA 1829
Cdd:pfam03528 227 EMYvAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLmrdMQRMESVLTSEQLRQVE 306
|
330 340 350
....*....|....*....|....*....|
gi 2462619853 1830 EIALKEKEaENERLRRLAEDEAFQRRRLEE 1859
Cdd:pfam03528 307 EIKKKDQE-EHKRARTHKEKETLKSDREHT 335
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2155-2452 |
5.28e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2155 LRQKAQVEQ-ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFsvrvQMEELSKLKARIEAEnraliL 2233
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2234 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2313
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2314 ELAQEQARRLQEDKEQMAQQLAEET--QGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2391
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2392 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2439
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 2462619853 2440 QQEAKllQLKSEE 2452
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1694-1802 |
5.39e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1694 RLRAETEQGEQQRQLLEEELARLQREAAAAT--------QKRQELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQR 1765
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKkeqdeasfERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462619853 1766 LEAEAGRFRELAEEAARLRALAEEAKRQRQLA--EEDAA 1802
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLREEvtEEDIA 518
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1461-1560 |
5.63e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1461 EAEAQKRQAQEEAERLR--RQVQDESQRK-------RQAEVELASRVKAEAEA-AREKQRALQA-LEELRLQAeEAERRL 1529
Cdd:PTZ00491 671 QAELLEQEARGRLERQKmhDKAKAEEQRTkllelqaESAAVESSGQSRAEALAeAEARLIEAEAeVEQAELRA-KALRIE 749
|
90 100 110
....*....|....*....|....*....|..
gi 2462619853 1530 RQAEVERARQVQVA-LETAQRSAEAELQSKRA 1560
Cdd:PTZ00491 750 AEAELEKLRKRQELeLEYEQAQNELEIAKAKE 781
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2151-2324 |
5.67e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2151 AEQTLRQKAQVEQELTTLRLQL-------EETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKlkar 2223
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA---- 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2224 ieaenRALILRDkdntqrflqeeaekmkqvaeeaarlsvAAQEAARLRQLAEEDLAQQRALAEKMlkekMQAVQEATRLK 2303
Cdd:COG3096 600 -----RAPAWLA---------------------------AQDALERLREQSGEALADSQEVTAAM----QQLLEREREAT 643
|
170 180
....*....|....*....|.
gi 2462619853 2304 AEAELLQQQKELAQEQARRLQ 2324
Cdd:COG3096 644 VERDELAARKQALESQIERLS 664
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1341-1730 |
5.95e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1341 EVEAALEKqrqlaeahaqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeaeiqAKARQAEAA 1420
Cdd:pfam02029 4 EEEAARER---------------RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1421 ERSRLRIEEEIRVVRLQlEATERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKA 1500
Cdd:pfam02029 64 FLDRTAKREERRQKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1501 EAEAAREKqralqalEELRLQAEEAERRLRQAEVERA-RQVQVALETAQRSAEAELQSKRASfaEKTAQLERSLQEEHVA 1579
Cdd:pfam02029 140 YQENKWST-------EVRQAEEEGEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYES--KVFLDQKRGHPEVKSQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1580 VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrlrlqaeevaqqkslaqaeaekqkeeaerearrrgkaEEQ 1659
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKL-------------------------------------EEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1660 AVRQRELAEQELEKQRQlaegtAQQRLAAEQELI--------RLRAETEQG----EQQRQLLEEELAR-----LQREAAA 1722
Cdd:pfam02029 254 RRRRQEKESEEFEKLRQ-----KQQEAELELEELkkkreerrKLLEEEEQRrkqeEAERKLREEEEKRrmkeeIERRRAE 328
|
....*...
gi 2462619853 1723 ATQKRQEL 1730
Cdd:pfam02029 329 AAEKRQKL 336
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1666-1951 |
6.04e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1666 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1745
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1746 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAIGEAtRL 1825
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1826 KTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrqveeeil 1905
Cdd:PRK11637 170 ETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT--------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1906 ALKASFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-------ARQRQ 1951
Cdd:PRK11637 223 GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1323-1583 |
6.12e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1323 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRR-----------EEAAVDAQQQ 1391
Cdd:PRK10811 514 SEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAAAPKAAAATPPA-QPGLLSRffgalkalfsgGEETKPQEQP 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1392 KRSIQE--ELQQLRQSSeaeiqakaRQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1469
Cdd:PRK10811 593 APKAEAkpERQQDRRKP--------RQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEK 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1470 QEEAERLRRQVQDESQRKRQAEVELASrvkAEAEAarekqralQALEELRLQAEEAERRLRQAEVERA-RQV--QVALET 1546
Cdd:PRK10811 665 ARTQDEQQQAPRRERQRRRNDEKRQAQ---QEAKA--------LNVEEQSVQETEQEERVQQVQPRRKqRQLnqKVRIEQ 733
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462619853 1547 AQrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1583
Cdd:PRK10811 734 SV-AEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPL 769
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2232-2394 |
6.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2232 ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQ---EATRLKAEAEL 2308
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2309 LQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleaerqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2388
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEA--------------ELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*.
gi 2462619853 2389 EIGEKL 2394
Cdd:COG1579 167 ELAAKI 172
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1656-1756 |
6.29e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1656 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1735
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 2462619853 1736 KvRAEMEVLLaskarAEEESR 1756
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1289-1556 |
6.46e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1289 VIQEYVDLRThYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEererLAEVEAALEKQRQLAEAHAQAKAQAEREAK 1368
Cdd:COG1538 78 VAQAYFDLLA-AQEQLALAEENLALAEELLELARARYEAGLASRLD----VLQAEAQLAQARAQLAQAEAQLAQARNALA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1369 ELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeAEIQAKARQAEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1448
Cdd:COG1538 153 LLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERR-PDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1449 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1509
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1510 RALQALEEL-------RLQAEEAERRLRQAEVERarqvqVALETAQRSAEAELQ 1556
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1678-1821 |
6.56e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.09 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1678 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS 1757
Cdd:COG4191 1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462619853 1758 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGE 1821
Cdd:COG4191 81 LLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGE 144
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1085-1583 |
6.62e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1085 HEEQLKEAQAVPATLPELEatkaslkklrAQAEAQQPTFDAlRDElrGAQEVGERLQQRHGERDVEVERWrERVAQLLEr 1164
Cdd:pfam10174 125 HERQAKELFLLRKTLEEME----------LRIETQKQTLGA-RDE--SIKKLLEMLQSKGLPKKSGEEDW-ERTRRIAE- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1165 WQAVLAQTDVrqrELEQLGRQLRYYRESAdplgawlqdarRRQEQIQAMPlADSQAVREQLRQEQALLEEIERHGEKVEE 1244
Cdd:pfam10174 190 AEMQLGHLEV---LLDQKEKENIHLREEL-----------HRRNQLQPDP-AKTKALQTVIEMKDTKISSLERNIRDLED 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1245 CQRFAKQyiNAIKDYELQLVTYKaQLEPVASPAK--KPKVQSGSESVIQEYVDLRTHYSELTTLTS------QYIKFISE 1316
Cdd:pfam10174 255 EVQMLKT--NGLLHTEDREEEIK-QMEVYKSHSKfmKNKIDQLKQELSKKESELLALQTKLETLTNqnsdckQHIEVLKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1317 TLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQA-------------EREAKELQQRMQ--EEVVR 1380
Cdd:pfam10174 332 SLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEKSTLAgeirdlkdmldvkERKINVLQKKIEnlQEQLR 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1381 reeaavDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEA-------AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ 1453
Cdd:pfam10174 412 ------DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAlsekeriIERLKEQREREDRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1454 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAER-RLRQA 1532
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQ 565
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1533 EV----ERARQVQVALE---TAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1583
Cdd:pfam10174 566 EVarykEESGKAQAEVErllGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI 623
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
20-122 |
7.08e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 39.59 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 20 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 95
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 2462619853 96 NIRNDDIADGNPKLTLGLIWTIILHFQ 122
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1437-1562 |
7.12e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1437 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQAL 1515
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619853 1516 EELR---------LQAEEAERRLRQAEVER-ARQVQVALetAQRSaeAELQSKRASF 1562
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKIADlGRRLNVAL--AQRV--QELNRYRSEF 199
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1211-1489 |
7.27e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1211 QAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpkvqsgsesvi 1290
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET---------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1291 qeyvdlRTHYSELttltsqyikfiseTLRRMEE--EERLAEQQRAeererlaeveaalekQRQLAEAHAQ---AKAQAER 1365
Cdd:PRK11281 115 ------RETLSTL-------------SLRQLESrlAQTLDQLQNA---------------QNDLAEYNSQlvsLQTQPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1366 EAKEL---QQRMQEevVRREEAAVDAQQqkRSIQEELQQLRQSSEAEIQAKA--RQAEAAERSRLrieeeIRVVRLQLEA 1440
Cdd:PRK11281 161 AQAALyanSQRLQQ--IRNLLKGGKVGG--KALRPSQRVLLQAEQALLNAQNdlQRKSLEGNTQL-----QDLLQKQRDY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1441 TERQRGGAEGELQALRA-----RAEEAEAQKRQAQEEAERLRRQ----VQDESQRKRQ 1489
Cdd:PRK11281 232 LTARIQRLEHQLQLLQEainskRLTLSEKTVQEAQSQDEAARIQanplVAQELEINLQ 289
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1703-1818 |
7.35e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.16 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1703 EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLaskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1782
Cdd:COG0711 30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEII---AEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIE 106
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462619853 1783 lralAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1818
Cdd:COG0711 107 ----QERAKALAELRAEVADLAVAIAEKILGKELDA 138
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1097-1540 |
7.35e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1097 ATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQ 1176
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1177 RELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAI 1256
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1257 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEER 1336
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1337 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQ 1416
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1417 AEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS 1496
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462619853 1497 RVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1540
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1316-1483 |
7.45e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRA---EERERLAEVEAALEKQRQLAEAHAQ----AKAQAEREAKELqqrmqeevvrreeaavda 1388
Cdd:PRK00409 492 EIAKRLGLPENIIEEAKKligEDKEKLNELIASLEELERELEQKAEeaeaLLKEAEKLKEEL------------------ 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1389 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAersrlrIEEEIRVVRL--QLEATERQRGGAEGELQALRARAEEAEAQK 1466
Cdd:PRK00409 554 EEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE------ADEIIKELRQlqKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
170
....*....|....*..
gi 2462619853 1467 RQAQEEAERLrrQVQDE 1483
Cdd:PRK00409 628 KKQKEKQEEL--KVGDE 642
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1655-1795 |
7.70e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 41.51 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1655 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEA-- 1732
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619853 1733 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1795
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1330-1533 |
7.81e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1330 QQRAEERERLAEVEAALEKQRQLAEAHAQAK---AQAEREAKELQQRMQEEVVRREE------------AAVDAQQQKRS 1394
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEekelvekikeleKELEKAKKALE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1395 IQEELQQLRqsseAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAE 1474
Cdd:COG1340 158 KNEKLKELR----AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA-------DELRKEADELHKEIVEAQEKAD 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 1475 RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRalqalEELRLQAEEAERRLRQAE 1533
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----EELEEKAEEIFEKLKKGE 280
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1761-1908 |
7.84e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1761 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAigEATRLKTE 1828
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1829 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALK 1908
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1316-1417 |
7.90e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1316 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAKELQQrmqeevvRREEAAVDAQQQKRSI 1395
Cdd:PRK11448 152 LTLKQQLELQAREKAQSQALAEAQQQELVALEG---LAAELEEKQQELEAQLEQLQE-------KAAETSQERKQKRKEI 221
|
90 100
....*....|....*....|....*.
gi 2462619853 1396 QEELQQLRQSSEAE----IQAKARQA 1417
Cdd:PRK11448 222 TDQAAKRLELSEEEtrilIDQQLRKA 247
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2297-2375 |
8.05e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 42.01 E-value: 8.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619853 2297 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAEETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2375
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1505-1559 |
8.19e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462619853 1505 AREKQRALQaleelRLQAEEAERRlRQAEVERARQVQVALETAQRS-AEAELQSKR 1559
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1664-1831 |
8.45e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1664 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtqkRQELEAELAKVRAEmev 1743
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKE--- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1744 llaskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1823
Cdd:PRK00409 582 -----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNK-ANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL 655
|
....*...
gi 2462619853 1824 RLKTEAEI 1831
Cdd:PRK00409 656 SIPDDKEA 663
|
|
| PRK01294 |
PRK01294 |
lipase secretion chaperone; |
1370-1543 |
8.55e-03 |
|
lipase secretion chaperone;
Pssm-ID: 234937 [Multi-domain] Cd Length: 336 Bit Score: 41.97 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1370 LQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaersrlrieeeirvvrLQLEATERQRGGAE 1449
Cdd:PRK01294 187 YQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQAL----------------LQQLAQLQASGASP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1450 GELQALRARAEEAEAqkrqaqeeAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1529
Cdd:PRK01294 251 QELRLMRAQLVGPEA--------AQRLEQLDQQRAAWQQRYDDYLAQRAQILNAAGLSPQDRQAQIAQLRQQRFSPQEAL 322
|
170
....*....|....
gi 2462619853 1530 RQAEVERARQVQVA 1543
Cdd:PRK01294 323 RLAALERIHDAGQT 336
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2264-2446 |
8.57e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2264 AQEAARLRQLAEED--LAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETqgf 2341
Cdd:COG1579 3 PEDLRALLDLQELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2342 qrtleaERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTElatqekvtlvQTLEIQRQQSDHD 2421
Cdd:COG1579 80 ------EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEK 143
|
170 180
....*....|....*....|....*
gi 2462619853 2422 AERLREAIAELEREKEKLQQEAKLL 2446
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREEL 168
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1408-1575 |
8.70e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1408 AEIQAKARQAEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1487
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA-AAATPAAPAAAARRAARAAAAARQAEQPAAEAAAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1488 RQAEVELASRVKAEAEAAREKQRALQALEelRLQAEEAERRLRQAEVERARQVQVALE---TAQRSAEAELQSKRASFAE 1564
Cdd:PRK12678 101 KAEAAPAARAAAAAAAEAASAPEAAQARE--RRERGEAARRGAARKAGEGGEQPATEAradAAERTEEEERDERRRRGDR 178
|
170
....*....|.
gi 2462619853 1565 KTAQLERSLQE 1575
Cdd:PRK12678 179 EDRQAEAERGE 189
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1972-2475 |
9.05e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1972 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQS 2051
Cdd:COG3899 738 DPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2052 VLDQLRGEAEAARRAAEEAEEARVQAER-EAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAE 2130
Cdd:COG3899 818 ALAERLGDRRLEARALFNLGFILHWLGPlREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLL 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2131 QAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSV 2210
Cdd:COG3899 898 AAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2211 RVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2290
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2291 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMS 2370
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2371 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKS 2450
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*
gi 2462619853 2451 EEMQTVQQEQLLQETQALQQSFLSE 2475
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRL 1242
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1424-1541 |
9.09e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1424 RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQR-KRQAEVELASRVK 1499
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLeqkRQEAEEEKERlEESAEMEAEEKEQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462619853 1500 AEAEaAREKQRALQALEELRLQAEEAERRLrQAEVERARQVQ 1541
Cdd:pfam20492 81 LEAE-LAEAQEEIARLEEEVERKEEEARRL-QEELEEAREEE 120
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1685-2031 |
9.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1685 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQ 1764
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1765 RLEAEAgRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1844
Cdd:COG4372 96 LAQAQE-ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1845 RLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRR--QVEEEILALKASFEKAAAGKAELE 1922
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEakLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1923 LELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2002
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
330 340
....*....|....*....|....*....
gi 2462619853 2003 ERAEQESARQLQLAQEAAQKRLQAEEKAH 2031
Cdd:COG4372 335 LLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1322-1509 |
9.36e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.29 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1322 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER----------EAKELQQRMQEEVVRRE-----EAAV 1386
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegeiEAKEADHKGETEAEEVEhegetEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1387 DAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1463
Cdd:TIGR00927 726 TEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462619853 1464 AQKRQAQEEAERlRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1509
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2280-2480 |
9.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2280 QQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaeETQGFQRTLEAERQRQLEMSAEA 2359
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2360 ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvqtleiqrqqsdhdaERLREAIAELEREKEKL 2439
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL-----------------QDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462619853 2440 QQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLL 2480
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2310-2444 |
9.46e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 2310 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSR------AQARAEEDAQRF 2383
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462619853 2384 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLQQEAK 2444
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1658-1918 |
9.47e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1658 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQreaaaatQKRQELEAELAKV 1737
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK-------EERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1738 RAEMEVLLASKARAEEESRSTSEKSKqRLEAEAGRF----------RELAEEAARLRALAEEAKRQRQLAEE-DAARQRA 1806
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKLRK-EIERLEWRQqtevlspeeeKELVEKIKELEKELEKAKKALEKNEKlKELRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619853 1807 EAERVLAEKL-----AAIGEATRLKTEAeIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDS 1881
Cdd:COG1340 170 KELRKEAEEIhkkikELAEEAQELHEEM-IELYKEA---DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462619853 1882 ElerqKGLVEDTLRQRRQVEEEILALKAS--FEKAAAGK 1918
Cdd:COG1340 246 L----KKLRKKQRALKREKEKEELEEKAEeiFEKLKKGE 280
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4258-4288 |
9.83e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.83e-03
10 20 30
....*....|....*....|....*....|.
gi 2462619853 4258 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4288
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| |
