NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578837834|ref|XP_006724533|]
View 

dystrophin isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3125-3286 2.46e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


:

Pssm-ID: 320004  Cd Length: 162  Bit Score: 357.03  E-value: 2.46e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3125 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3204
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3205 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3284
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837834 3285 MR 3286
Cdd:cd16246   161 MR 162
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
136-246 6.76e-69

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: 227.50  E-value: 6.76e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834  216 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 246
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
11-121 6.33e-67

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: 222.11  E-value: 6.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   11 YEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3311-3359 6.47e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


:

Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 6.47e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837834 3311 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3359
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
341-558 1.01e-26

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: 110.61  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  341 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 420
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  421 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 499
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834  500 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 558
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2105-2320 2.39e-23

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: 100.98  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2105 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2183
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2184 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2263
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2264 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2320
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2690-2933 1.62e-20

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: 92.89  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2690 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2769
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2770 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2849
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2850 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2929
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837834 2930 DETL 2933
Cdd:cd00176   210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2472-2688 2.93e-20

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: 92.12  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2472 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2551
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2552 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2631
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2632 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2688
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1049-1263 3.89e-16

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: 80.18  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1049 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1128
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1129 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1208
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837834 1209 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1263
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
235kDa-fam super family cl31124
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
763-1938 9.30e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


The actual alignment was detected with superfamily member TIGR01612:

Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 9.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   763 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 834
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   835 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 890
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   891 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 962
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   963 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1042
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1043 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1122
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1123 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1202
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1203 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1274
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1275 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1353
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1354 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1432
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1433 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1511
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1512 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1590
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1591 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1670
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1671 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1750
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1751 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1823
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1824 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1898
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837834  1899 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1938
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2934-3040 1.57e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


:

Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 63.49  E-value: 1.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2934 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3013
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837834  3014 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3040
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3059-3088 8.33e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 8.33e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837834 3059 GPWERAISPNKVPYYINHETQTTCWDHPKM 3088
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1878-2102 2.46e-05

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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 48.21  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1878 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1950
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1951 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2028
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837834 2029 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2102
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
560-827 5.17e-03

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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  560 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 639
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  640 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 719
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  720 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 799
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837834  800 SIKQASEQLNSRWIEFCQLLSERLNWLE 827
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3125-3286 2.46e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 357.03  E-value: 2.46e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3125 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3204
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3205 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3284
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837834 3285 MR 3286
Cdd:cd16246   161 MR 162
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
136-246 6.76e-69

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: 227.50  E-value: 6.76e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834  216 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 246
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
11-121 6.33e-67

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: 222.11  E-value: 6.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   11 YEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3089-3207 1.21e-56

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 193.14  E-value: 1.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  3089 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 3166
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578837834  3167 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 3207
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
12-232 5.63e-34

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 141.62  E-value: 5.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNV 89
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   90 DLVNIGSTDIVDGNHKLTLGLIWNIILhwqvKNVMKNIMAGLQQTNSEKILLsWVRQSTRNY-PQVNVINFTTSWSDGLA 168
Cdd:COG5069    85 KLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLL-WCDEDTGGYkPEVDTFDFFRSWRDGLA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578837834  169 LNALIHSHRPDLFDWNSVVCQQSATQ-RLEHAFNIARYQLGIEKLLDPEDV-DTTYPDKKSILMYI 232
Cdd:COG5069   160 FSALIHDSRPDTLDPNVLDLQKKNKAlNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3311-3359 6.47e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 6.47e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837834 3311 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3359
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
341-558 1.01e-26

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: 110.61  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  341 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 420
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  421 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 499
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834  500 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 558
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2105-2320 2.39e-23

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: 100.98  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2105 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2183
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2184 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2263
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2264 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2320
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
19-117 3.22e-21

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: 90.84  E-value: 3.22e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834     19 KTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK---GSTRVHALNNVNKALRVLQNNNVDLVNIG 95
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 578837834     96 STDIVDGNhKLTLGLIWNIILH 117
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
138-235 3.80e-21

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: 90.84  E-value: 3.80e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    138 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQ---QSATQRLEHAFNIARYQLGIEKLLD 214
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 578837834    215 PEDVDTTYPDKKSILMYITSL 235
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2690-2933 1.62e-20

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: 92.89  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2690 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2769
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2770 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2849
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2850 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2929
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837834 2930 DETL 2933
Cdd:cd00176   210 EEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
136-240 2.49e-20

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: 88.88  E-value: 2.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   136 SEKILLSWVRQSTRNY-PQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQS-ATQRLEHAFNIARYQLGIEK-L 212
Cdd:pfam00307    3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFdKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|....*...
gi 578837834   213 LDPEDVDTtyPDKKSILMYITSLFQVLP 240
Cdd:pfam00307   83 IEPEDLVE--GDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2472-2688 2.93e-20

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: 92.12  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2472 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2551
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2552 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2631
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2632 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2688
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
15-119 4.55e-20

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: 88.11  E-value: 4.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    15 DVQKKTFTKWVNAQFSK-FGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK-GSTRVHALNNVNKALRVLQNN-NVDL 91
Cdd:pfam00307    1 LELEKELLRWINSHLAEyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 578837834    92 VNIGSTDIVDGNHKLTLGLIWNIILHWQ 119
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3307-3352 9.73e-17

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 76.37  E-value: 9.73e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 578837834  3307 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 3352
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1049-1263 3.89e-16

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: 80.18  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1049 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1128
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1129 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1208
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837834 1209 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1263
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
763-1938 9.30e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 9.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   763 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 834
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   835 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 890
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   891 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 962
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   963 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1042
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1043 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1122
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1123 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1202
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1203 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1274
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1275 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1353
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1354 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1432
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1433 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1511
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1512 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1590
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1591 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1670
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1671 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1750
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1751 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1823
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1824 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1898
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837834  1899 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1938
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3308-3351 2.35e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 2.35e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 578837834   3308 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 3351
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2123-2818 4.36e-14

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: 79.33  E-value: 4.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2123 AEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQtvvRTLNATGEEIiqQSSKTDASILQEKLGSLNLRWQEVCKQLSDR 2202
Cdd:TIGR02168  212 AERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2203 KKRLEEQKNILSEFQRDLNEFVLWLEEADNI-----ASIPLEPGKEQQLKEKLEQVKLLVEEL-PLRQGILKQLNEtggp 2276
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQleeleAQLEELESKLDELAEELAELEEKLEELkEELESLEAELEE---- 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2277 vlvsapiSPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2356
Cdd:TIGR02168  363 -------LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2357 PNQEGPFDVKETEIA-VQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLApGLTTI 2434
Cdd:TIGR02168  436 KELQAELEELEEELEeLQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKN 514
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2435 GASPTQTVTLVTQPVVTK---ETAISKLEMPSSLMLEVPALADFNRA-----WTELTDWLSLLDQVIKSQRVMVGDLEDI 2506
Cdd:TIGR02168  515 QSGLSGILGVLSELISVDegyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2507 NEmIIKQKATMQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD--------------------- 2552
Cdd:TIGR02168  595 KN-IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssi 672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2553 -----RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLA 2627
Cdd:TIGR02168  673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2628 KDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINA---SWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 2704
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2705 LTEAETTANVLQDatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNF 2784
Cdd:TIGR02168  833 IAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES 908
                          730       740       750
                   ....*....|....*....|....*....|....
gi 578837834  2785 KWSELRKKSLNIRSHLEASSDQWKRLHLSLQELL 2818
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
727-933 1.38e-12

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: 69.78  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  727 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 806
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  807 QLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSePTAIKSQLKICKDEVNRLSDLQPQ 886
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578837834  887 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFKQVFSDVQAREKELQ 933
Cdd:cd00176   162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1048-1152 5.64e-12

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 64.65  E-value: 5.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1048 NKLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEaEPEFASRL 1127
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 578837834  1128 ETELKELNTQWDHMCQQVYARKEAL 1152
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2934-3040 1.57e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 63.49  E-value: 1.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2934 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3013
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837834  3014 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3040
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
449-556 2.31e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 63.11  E-value: 2.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   449 LMDLQNQKLKELNDWLTKTEErtrKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVdESSGDHATAA 528
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 578837834   529 LEEQLKVLGDRWANICRWTEDRWVLLQD 556
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2107-2207 4.66e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.96  E-value: 4.66e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2107 RRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQEKL 2185
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837834   2186 GSLNLRWQEVCKQLSDRKKRLE 2207
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2935-3045 1.56e-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: 63.62  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2935 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 3014
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834 3015 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 3045
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
SPEC smart00150
Spectrin repeats;
343-445 2.71e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 2.71e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    343 RYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQE 422
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI---EEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 578837834    423 QMNLLNSRWECLRVASMEKQSNL 445
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
2475-2576 3.14e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 3.14e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2475 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2554
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837834   2555 ERIQNQWDEVQEHLQNRRQQLN 2576
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2104-2208 3.33e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 59.64  E-value: 3.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2104 EKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEH--AKYKWYlKELQDGIGQRQTVVRTLNATGEEIIQqSSKTDASIL 2181
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837834  2182 QEKLGSLNLRWQEVCKQLSDRKKRLEE 2208
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2570-2686 2.88e-09

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 56.94  E-value: 2.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2570 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 2649
Cdd:pfam00435    1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 578837834  2650 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 2686
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
PTZ00121 PTZ00121
MAEBL; Provisional
1357-1964 4.88e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1357 EAVRRQKLLEQSIQSAQETEKsLHLIQESLTFIDKQLAAYI----ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHN 1431
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFArrqaAIKAEEARKADELKKAEEKKKADEAkKAEEKKKAD 1305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1432 QGKEAAQRVlSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM-HLPALETKSVEQEVVQSQLNhcvnlyK 1510
Cdd:PTZ00121 1306 EAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKEEAK------K 1378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1511 SLSEVKSEVEMVIKTGRqiVQKKQTENPKELDE--RVTALKLHYNELGAKvTERKQQLEKCLKLSRKMRKEMNVLTEWLA 1588
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADE--AKKKAEEDKKKADElkKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1589 ATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgEALKTVLGKKETLVEDKlsllnsnwiAVTSRAE 1668
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKK---------AEEAKKA 1524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1669 EWLNLLLEYQKHMETfdQNVDHITKwiiqADTLLDESEKKKPQQKEDVLKRLKAElnDIRPKVDSTRDQAANLMANRGDH 1748
Cdd:PTZ00121 1525 DEAKKAEEAKKADEA--KKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEE 1596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1749 CRKLVEPQISELNHRF-AAISHRIKTGKasipLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDMNEDNEGTVKE 1826
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAkKAEEAKIKAEE----LKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEE 1672
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1827 LLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEP 1906
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834 1907 RDER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFA 1964
Cdd:PTZ00121 1753 EEEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3059-3088 8.33e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 8.33e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837834 3059 GPWERAISPNKVPYYINHETQTTCWDHPKM 3088
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
2692-2801 1.62e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 54.64  E-value: 1.62e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2692 QQFPLDLEKFLAWLTEAETTAnvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 2771
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 578837834   2772 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 2801
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1877-1979 3.13e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1877 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 1954
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 578837834  1955 RWREIESKFAQFRRLNFAQIHTVRE 1979
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
3056-3088 3.16e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 51.83  E-value: 3.16e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 578837834   3056 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 3088
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
SPEC smart00150
Spectrin repeats;
2937-3038 3.78e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 3.78e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2937 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 3016
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 578837834   3017 LEDLNTRWKLLQVAVEDRVRQL 3038
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
3060-3086 9.42e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 50.20  E-value: 9.42e-08
                           10        20
                   ....*....|....*....|....*..
gi 578837834  3060 PWERAISPNKVPYYINHETQTTCWDHP 3086
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SPEC smart00150
Spectrin repeats;
1060-1153 3.33e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.09  E-value: 3.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   1060 LKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLETELKELNTQWD 1139
Cdd:smart00150   10 LEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEELNERWE 87
                            90
                    ....*....|....
gi 578837834   1140 HMCQQVYARKEALK 1153
Cdd:smart00150   88 ELKELAEERRQKLE 101
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1697-1971 8.83e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.68  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1697 QADTLLDESEKKKPQQKE--DVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVE--PQISELNHRFAAISHRIK 1772
Cdd:COG1340    16 KIEELREEIEELKEKRDElnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKElkEERDELNEKLNELREELD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1773 TGKASIPLKELEQFNSD-IQKLLEPLEAEIQqgvnlkeedfNKDMNEDNEgtvKELLQRGDNLQQRITDERKREEIKIKQ 1851
Cdd:COG1340    96 ELRKELAELNKAGGSIDkLRKEIERLEWRQQ----------TEVLSPEEE---KELVEKIKELEKELEKAKKALEKNEKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1852 QLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER--KIKEIDRELQKKKEELNAV 1929
Cdd:COG1340   163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqeKADELHEEIIELQKELREL 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578837834 1930 RRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNF 1971
Cdd:COG1340   243 RKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTT 284
SPEC smart00150
Spectrin repeats;
727-827 1.01e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 1.01e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    727 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 806
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837834    807 QLNSRWIEFCQLLSERLNWLE 827
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2477-2781 1.44e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2477 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 2549
Cdd:COG1196   232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2550 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 2624
Cdd:COG1196   309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2625 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 2704
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2705 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 2781
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2193-2628 1.91e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2193 QEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASI------------PLEPGKEQQLKEKLEQVKLLVEE- 2259
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKkeelerlkkrltGLTPEKLEKELEELEKAKEEIEEe 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2260 ---LPLRQGILKQ--------LNETGG-----PVlVSAPISPEEQDKLENKLKqtnlqwikvsralpEKQGEIEAQIKDL 2323
Cdd:PRK03918  407 iskITARIGELKKeikelkkaIEELKKakgkcPV-CGRELTEEHRKELLEEYT--------------AELKRIEKELKEI 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2324 GQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ----PNQEGPFDVKETEiavqAKQPDVEEILSKGQHLYKEKPATQPV 2399
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKE 547
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2400 KRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVtlvtqpvvtkETAISKLEmpsslmlevpalaDFNRAW 2479
Cdd:PRK03918  548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----------EERLKELE-------------PFYNEY 604
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2480 TELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKAtmqDLEQRRPQLEELITA--------AQNLKNKTSNQEARtiIT 2551
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEELRKELEELEKKyseeeyeeLREEYLELSRELAG--LR 679
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2552 DRIERIQNQWDEVQEHLQNRRQQLNEMLKdstqwleAKEEAEqVLGQARAKLEswkegpytvdAIQKKITETKQLAK 2628
Cdd:PRK03918  680 AELEELEKRREEIKKTLEKLKEELEEREK-------AKKELE-KLEKALERVE----------ELREKVKKYKALLK 738
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1878-2102 2.46e-05

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: 48.21  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1878 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1950
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1951 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2028
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837834 2029 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2102
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2689-2791 5.39e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.00  E-value: 5.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2689 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 2768
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 578837834  2769 SDDAVLLQRRLDNMNFKWSELRK 2791
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2486-2625 9.29e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2486 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 2564
Cdd:PRK00409  497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578837834 2565 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQARaklESWKEGPYTVDAiqKKITETKQ 2625
Cdd:PRK00409  557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR---QLQKGGYASVKA--HELIEARK 614
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2160-2356 2.15e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2160 RTLNATGEEIIQQSSKTDASILQEKLGSLNlrwqevcKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIple 2239
Cdd:COG3206   152 AVANALAEAYLEQNLELRREEARKALEFLE-------EQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL--- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2240 pgkeQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDkLENKLKQTNLQWIKVS----------RAL 2309
Cdd:COG3206   222 ----SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSarytpnhpdvIAL 296
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578837834 2310 PEKQGEIEAQIKDlgQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2356
Cdd:COG3206   297 RAQIAALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEA 341
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1125-1387 4.03e-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: 43.12  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1125 SRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDfeyktpDELQKAVEEMKRAK 1204
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE------ERLEEAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1205 EEAQQKEAKVKLLTESVNSVIAQappvaQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNE 1284
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1285 VEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDG-----GVMDEL-------------------- 1339
Cdd:TIGR02168  857 LAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEELSEElreleSKRSELrreleelreklaqlelrleg 933
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578837834  1340 ----INEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEtekSLHLIQESLT 1387
Cdd:TIGR02168  934 levrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIK 982
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
560-827 5.17e-03

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: 41.28  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  560 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 639
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  640 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 719
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  720 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 799
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837834  800 SIKQASEQLNSRWIEFCQLLSERLNWLE 827
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3125-3286 2.46e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 357.03  E-value: 2.46e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3125 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3204
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3205 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3284
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837834 3285 MR 3286
Cdd:cd16246   161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
3125-3286 1.12e-103

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 329.20  E-value: 1.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3125 SLSAACDALDQHNLK-QNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGI 3203
Cdd:cd16242     1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3204 ISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLD 3283
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160

                  ...
gi 578837834 3284 WMR 3286
Cdd:cd16242   161 WLK 163
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
3126-3286 7.85e-84

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 272.54  E-value: 7.85e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3126 LSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 3205
Cdd:cd16247     2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3206 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 3285
Cdd:cd16247    82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161

                  .
gi 578837834 3286 R 3286
Cdd:cd16247   162 R 162
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
3125-3285 4.97e-80

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 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 only two spectrin repeats (SRs) and a WW domain.


Pssm-ID: 320006  Cd Length: 162  Bit Score: 261.65  E-value: 4.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3125 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3204
Cdd:cd16248     1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3205 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3284
Cdd:cd16248    81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160

                  .
gi 578837834 3285 M 3285
Cdd:cd16248   161 M 161
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
136-246 6.76e-69

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: 227.50  E-value: 6.76e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834  216 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 246
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
3126-3285 9.72e-68

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family 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. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 226.38  E-value: 9.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3126 LSAACDALDQHNLKQ-NDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3204
Cdd:cd15901     2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3205 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3284
Cdd:cd15901    82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161

                  .
gi 578837834 3285 M 3285
Cdd:cd15901   162 L 162
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
11-121 6.33e-67

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: 222.11  E-value: 6.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   11 YEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
15-121 1.82e-64

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: 214.55  E-value: 1.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   15 DVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNI 94
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 578837834   95 GSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21186    81 SSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
136-240 2.17e-59

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: 199.96  E-value: 2.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21187     1 LEKTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLV-KDSPESRLEHAFTVAHEHLGIEKLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 578837834  216 EDVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21187    80 EDVNVEQPDKKSILMYVTSLFQVLP 104
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3089-3207 1.21e-56

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 193.14  E-value: 1.21e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  3089 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 3166
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578837834  3167 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 3207
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
15-121 1.19e-55

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: 189.45  E-value: 1.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   15 DVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNI 94
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 578837834   95 GSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21232    81 GGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
136-240 1.38e-51

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: 177.84  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVV-KMSPVERLEHAFSKAKNHLGIEKLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 578837834  216 EDVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21234    80 EDVAVQLPDKKSIIMYLTSLFEVLP 104
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3211-3302 1.83e-49

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462669  Cd Length: 90  Bit Score: 171.33  E-value: 1.83e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  3211 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 3290
Cdd:pfam09069    1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78
                           90
                   ....*....|..
gi 578837834  3291 SMVWLPVLHRVA 3302
Cdd:pfam09069   79 SLVWLPVLHRLA 90
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
135-240 9.38e-43

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: 152.55  E-value: 9.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  135 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLD 214
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVR-NQSNRENLENAFNVAEKEFGVTRLLD 79
                          90       100
                  ....*....|....*....|....*.
gi 578837834  215 PEDVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVSSLYDVFP 105
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
16-119 1.23e-41

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: 149.47  E-value: 1.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   16 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIG 95
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARR-RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNIR 81
                          90       100
                  ....*....|....*....|....
gi 578837834   96 STDIVDGNHKLTLGLIWNIILHWQ 119
Cdd:cd21188    82 AEDIVDGNPKLTLGLIWTIILHFQ 105
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
12-116 6.65e-41

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: 147.90  E-value: 6.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21246    12 EREAVQKKTFTKWVNSHLARVG-CRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
                          90       100
                  ....*....|....*....|....*.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIIL 116
Cdd:cd21246    91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
140-236 1.00e-37

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: 138.31  E-value: 1.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 219
Cdd:cd21194     7 LLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLD-PNDHLGNLNNAFDVAEQELGIAKLLDAEDVD 85
                          90
                  ....*....|....*..
gi 578837834  220 TTYPDKKSILMYITSLF 236
Cdd:cd21194    86 VARPDEKSIMTYVASYY 102
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
140-236 1.59e-37

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: 137.53  E-value: 1.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 219
Cdd:cd21248     7 LLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLS-KSNALYNLQNAFNVAEQKLGLTKLLDPEDVN 85
                          90
                  ....*....|....*..
gi 578837834  220 TTYPDKKSILMYITSLF 236
Cdd:cd21248    86 VEQPDEKSIITYVVTYY 102
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
12-116 4.07e-37

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: 137.04  E-value: 4.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNnVD 90
Cdd:cd21193    12 ERINIQKKTFTKWINSFLEKAN-LEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFLKTK-VR 89
                          90       100
                  ....*....|....*....|....*.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIIL 116
Cdd:cd21193    90 LENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
132-237 7.28e-36

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: 133.21  E-value: 7.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  132 QQTNSEK-ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIE 210
Cdd:cd21319     1 RETRSAKdALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLK-KSNARHNLEHAFNVAERQLGIT 79
                          90       100
                  ....*....|....*....|....*..
gi 578837834  211 KLLDPEDVDTTYPDKKSILMYITSLFQ 237
Cdd:cd21319    80 KLLDPEDVFTENPDEKSIITYVVAFYH 106
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
12-121 2.25e-35

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: 131.73  E-value: 2.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGK-QHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGST--RVHALNNVNKALRVLQNNN 88
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPpMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837834   89 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
12-116 6.60e-35

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: 131.69  E-value: 6.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21318    34 EREAVQKKTFTKWVNSHLARVP-CRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
                          90       100
                  ....*....|....*....|....*.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIIL 116
Cdd:cd21318   113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
12-116 1.10e-34

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: 130.56  E-value: 1.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21317    27 EREAVQKKTFTKWVNSHLARVTCR-IGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKVH 105
                          90       100
                  ....*....|....*....|....*.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIIL 116
Cdd:cd21317   106 LENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
12-121 1.13e-34

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: 129.95  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQH-IENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSvVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
12-123 1.85e-34

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: 129.72  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFgKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDL 91
Cdd:cd21236    13 ERDKVQKKTFTKWINQHLMKV-RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKL 91
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837834   92 VNIGSTDIVDGNHKLTLGLIWNIILHWQVKNV 123
Cdd:cd21236    92 VNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
12-232 5.63e-34

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 141.62  E-value: 5.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNV 89
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   90 DLVNIGSTDIVDGNHKLTLGLIWNIILhwqvKNVMKNIMAGLQQTNSEKILLsWVRQSTRNY-PQVNVINFTTSWSDGLA 168
Cdd:COG5069    85 KLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLL-WCDEDTGGYkPEVDTFDFFRSWRDGLA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578837834  169 LNALIHSHRPDLFDWNSVVCQQSATQ-RLEHAFNIARYQLGIEKLLDPEDV-DTTYPDKKSILMYI 232
Cdd:COG5069   160 FSALIHDSRPDTLDPNVLDLQKKNKAlNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
12-126 6.50e-33

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: 125.14  E-value: 6.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKfGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDL 91
Cdd:cd21235     2 ERDRVQKKTFTKWVNKHLIK-AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578837834   92 VNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKN 126
Cdd:cd21235    81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
12-121 1.12e-32

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: 124.22  E-value: 1.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQH-IENLFSDLQDGRRLLDLLEGLTGQKLPKEKG--STRVHALNNVNKALRVLQNNN 88
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIvINDLFVDIKDGTALLRLLEVLSGQKLPIESGrvLQRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837834   89 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
14-116 3.50e-32

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: 122.50  E-value: 3.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   14 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNVDLV 92
Cdd:cd21214     3 EKQQRKTFTAWCNSHLRKAGTQ-IENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLV 81
                          90       100
                  ....*....|....*....|....
gi 578837834   93 NIGSTDIVDGNHKLTLGLIWNIIL 116
Cdd:cd21214    82 SIGAEEIVDGNLKMTLGMIWTIIL 105
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
134-240 4.50e-31

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: 119.32  E-value: 4.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  134 TNSEKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQrLEHAFNIARyQLGIEKLL 213
Cdd:cd21239     1 SAKERLLL-WSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLAN-LEHAFYVAE-KLGVTRLL 77
                          90       100
                  ....*....|....*....|....*..
gi 578837834  214 DPEDVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21239    78 DPEDVDVSSPDEKSVITYVSSLYDVFP 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
14-116 2.31e-30

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: 117.12  E-value: 2.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   14 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDL 91
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRGLS-ITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKL 80
                          90       100
                  ....*....|....*....|....*
gi 578837834   92 VNIGSTDIVDGNHKLTLGLIWNIIL 116
Cdd:cd21215    81 TNIGAEDIVDGNLKLILGLLWTLIL 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
133-236 2.43e-30

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: 117.27  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  133 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 212
Cdd:cd21249     2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLR-PDRPLYNLANAFLVAEQELGISQL 80
                          90       100
                  ....*....|....*....|....
gi 578837834  213 LDPEDVDTTYPDKKSILMYItSLF 236
Cdd:cd21249    81 LDPEDVAVPHPDERSIMTYV-SLY 103
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
12-123 2.50e-30

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: 117.83  E-value: 2.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFgKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDL 91
Cdd:cd21237     2 ERDRVQKKTFTKWVNKHLMKV-RKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837834   92 VNIGSTDIVDGNHKLTLGLIWNIILHWQVKNV 123
Cdd:cd21237    81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
132-237 3.42e-30

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: 117.47  E-value: 3.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  132 QQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEK 211
Cdd:cd21321     2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLK-KSNAHYNLQNAFNVAEKELGLTK 80
                          90       100
                  ....*....|....*....|....*.
gi 578837834  212 LLDPEDVDTTYPDKKSILMYITSLFQ 237
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYH 106
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
132-237 3.57e-30

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: 117.85  E-value: 3.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  132 QQTNSEK-ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIE 210
Cdd:cd21322    13 RETRSAKdALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLT-KSNATYNLQQAFNTAEQHLGLT 91
                          90       100
                  ....*....|....*....|....*..
gi 578837834  211 KLLDPEDVDTTYPDKKSILMYITSLFQ 237
Cdd:cd21322    92 KLLDPEDVNMEAPDEKSIITYVVSFYH 118
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3311-3359 6.47e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 6.47e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837834 3311 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3359
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
133-240 7.35e-30

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: 115.88  E-value: 7.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  133 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 212
Cdd:cd21243     3 KGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLK-RRSNRENLETAFTVAEKELGIPRL 81
                          90       100
                  ....*....|....*....|....*...
gi 578837834  213 LDPEDVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21243    82 LDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
12-121 1.73e-29

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: 114.98  E-value: 1.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQ-HIENLFSDLQDGRRLLDLLEGLTGQKLPKE--KGSTRVHALNNVNKALRVLQNNN 88
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837834   89 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 121
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 113
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
12-116 1.67e-28

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: 113.99  E-value: 1.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21316    49 EREAVQKKTFTKWVNSHLARVSCR-ITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
                          90       100
                  ....*....|....*....|....*.
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIIL 116
Cdd:cd21316   128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
15-120 2.84e-28

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: 111.23  E-value: 2.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   15 DVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDLV 92
Cdd:cd21227     3 EIQKNTFTNWVNEQLKPTGMS-VEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLV 81
                          90       100
                  ....*....|....*....|....*...
gi 578837834   93 NIGSTDIVDGNHKLTLGLIWNIILHWQV 120
Cdd:cd21227    82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
134-240 8.34e-28

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: 110.11  E-value: 8.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  134 TNSEKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLL 213
Cdd:cd21238     2 TAKEKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLL 79
                          90       100
                  ....*....|....*....|....*..
gi 578837834  214 DPEDVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21238    80 DPEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
132-238 2.44e-27

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: 108.99  E-value: 2.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  132 QQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEK 211
Cdd:cd21216     7 EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLR-KDDPRENLNLAFDVAEKHLDIPK 85
                          90       100
                  ....*....|....*....|....*...
gi 578837834  212 LLDPED-VDTTYPDKKSILMYITSLFQV 238
Cdd:cd21216    86 MLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
135-237 3.47e-27

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: 108.26  E-value: 3.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  135 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLD 214
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLK-KSNAHYNLQNAFNLAEQHLGLTKLLD 80
                          90       100
                  ....*....|....*....|...
gi 578837834  215 PEDVDTTYPDKKSILMYITSLFQ 237
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTYYH 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
341-558 1.01e-26

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: 110.61  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  341 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 420
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  421 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 499
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834  500 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 558
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
137-240 1.14e-25

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: 103.97  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  137 EKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARyQLGIEKLLDPE 216
Cdd:cd21240     7 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQ-IQSNRENLEQAFEVAE-RLGVTRLLDAE 83
                          90       100
                  ....*....|....*....|....
gi 578837834  217 DVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21240    84 DVDVPSPDEKSVITYVSSIYDAFP 107
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
133-240 1.66e-25

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: 103.27  E-value: 1.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  133 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 212
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVK-NRSPRDNLELAFRIAEQHLNIPRL 79
                          90       100
                  ....*....|....*....|....*...
gi 578837834  213 LDPEDVDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21192    80 LEVEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
16-120 1.88e-25

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: 104.07  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   16 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNN-NVDLV 92
Cdd:cd21311    15 IQQNTFTRWANEHLKTANK-HIADLETDLSDGLRLIALVEVLSGKKFPKfnKRPTFRSQKLENVSVALKFLEEDeGIKIV 93
                          90       100
                  ....*....|....*....|....*...
gi 578837834   93 NIGSTDIVDGNHKLTLGLIWNIILHWQV 120
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
136-236 2.34e-25

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: 102.93  E-value: 2.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDwNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFK-QAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79
                          90       100
                  ....*....|....*....|.
gi 578837834  216 EDVDTTYPDKKSILMYiTSLF 236
Cdd:cd21226    80 EDVMTGNPDERSIVLY-TSLF 99
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
138-239 1.29e-24

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: 100.88  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  138 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQRLEH---AFNIARYQLGIEKLLD 214
Cdd:cd21253     4 KALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSL----SKENVYENnklAFTVAEKELGIPALLD 79
                          90       100
                  ....*....|....*....|....*.
gi 578837834  215 PED-VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21253    80 AEDmVALKVPDKLSILTYVSQYYNYF 105
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
140-236 5.24e-24

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: 99.52  E-value: 5.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDV- 218
Cdd:cd21291    15 LLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLD-KKDHRGNMQLAFDIASKEIGIPQLLDVEDVc 93
                          90
                  ....*....|....*...
gi 578837834  219 DTTYPDKKSILMYITSLF 236
Cdd:cd21291    94 DVAKPDERSIMTYVAYYF 111
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2105-2320 2.39e-23

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: 100.98  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2105 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2183
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2184 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2263
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2264 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2320
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
12-120 3.08e-23

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: 97.52  E-value: 3.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKFGKQ-HIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN-N 88
Cdd:cd21247    16 QRMTMQKKTFTKWMNNVFSKNGAKiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTKvP 95
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837834   89 VDLvnIGSTDIVDGNHKLTLGLIWNIILHWQV 120
Cdd:cd21247    96 VKL--IGPENIVDGDRTLILGLIWIIILRFQI 125
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
140-239 9.22e-23

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: 95.43  E-value: 9.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSA--TQRlehAFNIARYQLGIEKLLDPED 217
Cdd:cd22198     5 LLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAenNQL---AFDVAEQELGIPPVMTGQE 81
                          90       100
                  ....*....|....*....|...
gi 578837834  218 -VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd22198    82 mASLAVPDKLSMVSYLSQFYEAF 104
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
16-118 9.71e-23

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: 95.63  E-value: 9.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   16 VQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVDLV 92
Cdd:cd21183     4 IQANTFTRWCNEHLKERGMQ-IHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 578837834   93 NIGSTDIVDGNHKLTLGLIWNIILHW 118
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLILHY 108
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
135-235 4.32e-22

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: 93.64  E-value: 4.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  135 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARyQLGIEKLLD 214
Cdd:cd21198     1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSS-LSPHDIKENCKLAFDAAA-KLGIPRLLD 78
                          90       100
                  ....*....|....*....|..
gi 578837834  215 PED-VDTTYPDKKSILMYITSL 235
Cdd:cd21198    79 PADmVLLSVPDKLSVMTYLHQI 100
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
133-237 4.86e-22

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: 93.75  E-value: 4.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  133 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 212
Cdd:cd21244     3 KMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLK-GRSNRENLEEAFRIAEQELKIPRL 81
                          90       100
                  ....*....|....*....|....*
gi 578837834  213 LDPEDVDTTYPDKKSILMYITSLFQ 237
Cdd:cd21244    82 LEPEDVDVVNPDEKSIMTYVAQFLQ 106
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
3125-3285 2.70e-21

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 93.51  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3125 SLSAACDALDQHNLKQND-----QPMDILQIINcltTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSF 3199
Cdd:cd16245     1 PLKLIMGVFDRHQLSNSEnnlclPPDELEAVLH---DIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3200 KTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAA 3279
Cdd:cd16245    78 KVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEY 157

                  ....*.
gi 578837834 3280 LFLDWM 3285
Cdd:cd16245   158 QFIGWW 163
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
19-117 3.22e-21

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: 90.84  E-value: 3.22e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834     19 KTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK---GSTRVHALNNVNKALRVLQNNNVDLVNIG 95
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 578837834     96 STDIVDGNhKLTLGLIWNIILH 117
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
138-235 3.80e-21

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: 90.84  E-value: 3.80e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    138 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQ---QSATQRLEHAFNIARYQLGIEKLLD 214
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 578837834    215 PEDVDTTYPDKKSILMYITSL 235
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
139-239 9.88e-21

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: 89.71  E-value: 9.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  139 ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQR---LEHAFNIARYQLGIEKLLDP 215
Cdd:cd21200     5 MLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSL----DPKNRrknFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*.
gi 578837834  216 ED--VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21200    81 EDmvRMGNRPDWKCVFTYVQSLYRHL 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2690-2933 1.62e-20

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: 92.89  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2690 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2769
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2770 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2849
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2850 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2929
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837834 2930 DETL 2933
Cdd:cd00176   210 EEAL 213
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
16-118 1.94e-20

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: 89.08  E-value: 1.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   16 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVDLV 92
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVNK-RIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 578837834   93 NIGSTDIVDGNHKLTLGLIWNIILHW 118
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTLILHY 108
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
138-236 2.03e-20

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: 88.75  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  138 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQRLEH---AFNIARYQLGIEKLLD 214
Cdd:cd21197     3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSL----KKDNWLENnrlAFRVAETSLGIPALLD 78
                          90       100
                  ....*....|....*....|...
gi 578837834  215 PED-VDTTYPDKKSILMYITSLF 236
Cdd:cd21197    79 AEDmVTMHVPDRLSIITYVSQYY 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
136-240 2.49e-20

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: 88.88  E-value: 2.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   136 SEKILLSWVRQSTRNY-PQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQS-ATQRLEHAFNIARYQLGIEK-L 212
Cdd:pfam00307    3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFdKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|....*...
gi 578837834   213 LDPEDVDTtyPDKKSILMYITSLFQVLP 240
Cdd:pfam00307   83 IEPEDLVE--GDNKSVLTYLASLFRRFQ 108
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
131-239 2.89e-20

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: 89.37  E-value: 2.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  131 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQrLEHAFNIARYQLGIE 210
Cdd:cd21290     9 VEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTN-LNNAFEVAEKYLDIP 87
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837834  211 KLLDPED-VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21290    88 KMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2472-2688 2.93e-20

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: 92.12  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2472 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2551
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2552 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2631
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2632 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2688
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
15-119 4.55e-20

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: 88.11  E-value: 4.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    15 DVQKKTFTKWVNAQFSK-FGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK-GSTRVHALNNVNKALRVLQNN-NVDL 91
Cdd:pfam00307    1 LELEKELLRWINSHLAEyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 578837834    92 VNIGSTDIVDGNHKLTLGLIWNIILHWQ 119
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
138-240 1.24e-19

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: 86.77  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  138 KILLSWVRQSTRNYpQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPED 217
Cdd:cd21245     6 KALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQAL-EKSPRENLEDAFRIAQESLGIPPLLEPED 83
                          90       100
                  ....*....|....*....|...
gi 578837834  218 VDTTYPDKKSILMYITSLFQVLP 240
Cdd:cd21245    84 VMVDSPDEQSIMTYVAQFLEHFP 106
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
131-239 2.12e-19

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: 86.70  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  131 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWnSVVCQQSATQRLEHAFNIARYQLGIE 210
Cdd:cd21289     6 VEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDY-AKLRKDDPIGNLNTAFEVAEKYLDIP 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837834  211 KLLDPED-VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21289    85 KMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
131-239 4.25e-19

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: 85.91  E-value: 4.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  131 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQrLEHAFNIARYQLGIE 210
Cdd:cd21287     6 VEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTN-LNTAFDVAEKYLDIP 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837834  211 KLLDPED-VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21287    85 KMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
140-239 4.92e-19

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: 85.09  E-value: 4.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 219
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLN-EDDAVENNQLAFDVAEREFGIPPVTTGKEMA 87
                          90       100
                  ....*....|....*....|.
gi 578837834  220 TT-YPDKKSILMYITSLFQVL 239
Cdd:cd21195    88 SAqEPDKLSMVMYLSKFYELF 108
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
136-234 6.48e-19

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: 84.60  E-value: 6.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21184     2 GKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITP 78
                          90
                  ....*....|....*....
gi 578837834  216 EDVDTTYPDKKSILMYITS 234
Cdd:cd21184    79 EDMVSPNVDELSVMTYLSY 97
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
3144-3285 9.93e-19

EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins 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, dystrobrevins contain one or two syntrophin binding sites (SBSs).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 86.14  E-value: 9.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3144 PMDILQIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLF 3219
Cdd:cd16244    22 ELSVSRLETLLSSIYyqlnKRLPTTHQ--IDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTLCAGKLVDKLRYIF 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578837834 3220 KQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCFQfANNKPEIEAalFLDWM 3285
Cdd:cd16244   100 SQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFP-GQSKVTVND--FLDVM 160
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
140-239 1.10e-18

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: 84.23  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 219
Cdd:cd21251    10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLD-EQDVEKNNQLAFDIAEKEFGISPIMTGKEMA 88
                          90       100
                  ....*....|....*....|.
gi 578837834  220 TT-YPDKKSILMYITSLFQVL 239
Cdd:cd21251    89 SVgEPDKLSMVMYLTQFYEMF 109
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
137-242 1.39e-18

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: 83.89  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  137 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPE 216
Cdd:cd21259     3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQ-LSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81
                          90       100
                  ....*....|....*....|....*..
gi 578837834  217 D-VDTTYPDKKSILMYITSLFQVLPQQ 242
Cdd:cd21259    82 DmVRMREPDWKCVYTYIQEFYRCLVQK 108
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
135-238 4.04e-18

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: 82.21  E-value: 4.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  135 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARyQLGIEKLLD 214
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKS-LNPHDIKENNKKAYDGFA-SLGISRLLE 78
                          90       100
                  ....*....|....*....|....*
gi 578837834  215 PED-VDTTYPDKKSILMYitsLFQV 238
Cdd:cd21254    79 PSDmVLLAVPDKLTVMTY---LYQI 100
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
140-236 4.35e-18

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: 82.22  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPED-V 218
Cdd:cd21252     5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDS-LSKDNVYENNRLAFEVAERELGIPALLDPEDmV 83
                          90
                  ....*....|....*...
gi 578837834  219 DTTYPDKKSILMYITSLF 236
Cdd:cd21252    84 SMKVPDCLSIMTYVSQYY 101
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
136-242 7.11e-18

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: 82.05  E-value: 7.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqQSATQR--LEHAFNIARYQLGIEKLL 213
Cdd:cd21260     2 VKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL---DPANRRhnFTLAFSTAEKHADCAPLL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837834  214 DPED-VDTTYPDKKSILMYITSLFQVLPQQ 242
Cdd:cd21260    79 EVEDmVRMSVPDSKCVYTYIQELYRSLVQK 108
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
131-239 8.85e-18

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: 82.04  E-value: 8.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  131 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWnSVVCQQSATQRLEHAFNIARYQLGIE 210
Cdd:cd21288     6 VEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDY-SKLNKDDPIGNINLAMEIAEKHLDIP 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837834  211 KLLDPED-VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21288    85 KMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
17-117 9.48e-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: 81.09  E-value: 9.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   17 QKKTFTKWVNAQFSKFG-KQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDLVN 93
Cdd:cd21212     1 EIEIYTDWANHYLEKGGhKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGihSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                          90       100
                  ....*....|....*....|....
gi 578837834   94 IGSTDIVDGNHKLTLGLIWNIILH 117
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRY 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
137-239 8.28e-17

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: 78.94  E-value: 8.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  137 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPE 216
Cdd:cd21258     3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQ-LSPQNRRQNFEVAFSAAEMLADCVPLVEVE 81
                          90       100
                  ....*....|....*....|....*
gi 578837834  217 D--VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21258    82 DmmIMGKKPDSKCVFTYVQSLYNHL 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
16-120 9.34e-17

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: 79.30  E-value: 9.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   16 VQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPKE---KGSTRVHALNNVNKALRVLQNNNVDLV 92
Cdd:cd21310    16 IQQNTFTRWCNEHLKCVQKR-LNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
                          90       100
                  ....*....|....*....|....*...
gi 578837834   93 NIGSTDIVDGNHKLTLGLIWNIILHWQV 120
Cdd:cd21310    95 SIDSKAIVDGNLKLILGLIWTLILHYSI 122
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3307-3352 9.73e-17

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 76.37  E-value: 9.73e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 578837834  3307 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 3352
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
140-238 3.11e-16

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: 77.23  E-value: 3.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 219
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDS-LNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMA 87
                          90       100
                  ....*....|....*....|
gi 578837834  220 TTY-PDKKSILMYITSLFQV 238
Cdd:cd21250    88 SAEePDKLSMVMYLSKFYEL 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
140-235 3.66e-16

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: 76.75  E-value: 3.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNiARYQLGIEKLLDPED-V 218
Cdd:cd21255     6 LLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLD-PLDIKENNKKAFE-AFASLGVPRLLEPADmV 83
                          90
                  ....*....|....*..
gi 578837834  219 DTTYPDKKSILMYITSL 235
Cdd:cd21255    84 LLPIPDKLIVMTYLCQL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1049-1263 3.89e-16

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: 80.18  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1049 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1128
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1129 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1208
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837834 1209 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1263
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
137-239 4.20e-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: 76.54  E-value: 4.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  137 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQR---LEHAFNIARYQLGIEKLL 213
Cdd:cd21261     3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSL----SPSNRkhnFELAFSMAEKLANCDRLI 78
                          90       100
                  ....*....|....*....|....*...
gi 578837834  214 DPED--VDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21261    79 EVEDmmVMGRKPDPMCVFTYVQSLYNHL 106
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
14-120 1.69e-15

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: 75.89  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   14 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21308    18 KKIQQNTFTRWCNEHLKCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIK 96
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIILHWQV 120
Cdd:cd21308    97 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
14-120 3.27e-15

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: 75.12  E-value: 3.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   14 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVD 90
Cdd:cd21309    15 KKIQQNTFTRWCNEHLKCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIK 93
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837834   91 LVNIGSTDIVDGNHKLTLGLIWNIILHWQV 120
Cdd:cd21309    94 LVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
14-112 6.19e-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: 73.33  E-value: 6.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   14 EDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKE---KGSTRVHALNNVNKALRVLQNN-NV 89
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
                          90       100
                  ....*....|....*....|...
gi 578837834   90 DLVNIGSTDIVDGNHKLTLGLIW 112
Cdd:cd21225    82 RVQGIGAEDFVDNNKKLILGLLW 104
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
140-237 6.50e-15

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: 73.55  E-value: 6.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSAtQRLEHAFNIARYQlGIEKLLDPED-V 218
Cdd:cd21199    13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKR-RNFTLAFKAAESV-GIPTTLTIDEmV 90
                          90
                  ....*....|....*....
gi 578837834  219 DTTYPDKKSILMYITSLFQ 237
Cdd:cd21199    91 SMERPDWQSVMSYVTAIYK 109
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
18-116 6.92e-15

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: 73.14  E-value: 6.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   18 KKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKE--KGSTRVHALNNVNKALRVLQNNNV-DLVNI 94
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
                          90       100
                  ....*....|....*....|...
gi 578837834   95 GSTDIV-DGNHKLTLGLIWNIIL 116
Cdd:cd00014    81 EPEDLYeKGNLKKVLGTLWALAL 103
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
763-1938 9.30e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 9.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   763 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 834
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   835 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 890
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   891 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 962
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   963 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1042
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1043 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1122
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1123 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1202
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1203 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1274
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1275 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1353
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1354 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1432
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1433 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1511
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1512 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1590
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1591 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1670
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1671 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1750
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1751 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1823
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1824 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1898
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837834  1899 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1938
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3308-3351 2.35e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 2.35e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 578837834   3308 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 3351
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
454-660 3.47e-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: 74.40  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  454 NQKLKELNDWLTKTEErtrKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESsGDHATAALEEQL 533
Cdd:cd00176     6 LRDADELEAWLSEKEE---LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  534 KVLGDRWANICRWTEDRWVLLQDiLLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKK 613
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEE-ALDLQQFFRDADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578837834  614 KQSMGKLYSLKQDLLStLKNKSVTQKTEAWLDNFARCWDNLVQKLEK 660
Cdd:cd00176   159 EPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEE 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2123-2818 4.36e-14

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: 79.33  E-value: 4.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2123 AEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQtvvRTLNATGEEIiqQSSKTDASILQEKLGSLNLRWQEVCKQLSDR 2202
Cdd:TIGR02168  212 AERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2203 KKRLEEQKNILSEFQRDLNEFVLWLEEADNI-----ASIPLEPGKEQQLKEKLEQVKLLVEEL-PLRQGILKQLNEtggp 2276
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQleeleAQLEELESKLDELAEELAELEEKLEELkEELESLEAELEE---- 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2277 vlvsapiSPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2356
Cdd:TIGR02168  363 -------LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2357 PNQEGPFDVKETEIA-VQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLApGLTTI 2434
Cdd:TIGR02168  436 KELQAELEELEEELEeLQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKN 514
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2435 GASPTQTVTLVTQPVVTK---ETAISKLEMPSSLMLEVPALADFNRA-----WTELTDWLSLLDQVIKSQRVMVGDLEDI 2506
Cdd:TIGR02168  515 QSGLSGILGVLSELISVDegyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2507 NEmIIKQKATMQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD--------------------- 2552
Cdd:TIGR02168  595 KN-IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssi 672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2553 -----RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLA 2627
Cdd:TIGR02168  673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2628 KDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINA---SWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 2704
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2705 LTEAETTANVLQDatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNF 2784
Cdd:TIGR02168  833 IAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES 908
                          730       740       750
                   ....*....|....*....|....*....|....
gi 578837834  2785 KWSELRKKSLNIRSHLEASSDQWKRLHLSLQELL 2818
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1126-1936 1.38e-13

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: 77.79  E-value: 1.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1126 RLETELKELNTQWDHMCQQVYARKE--ALKGGLEktvSLQKDLSEMHewMTQAEEEYLERDFEYKtpdelqKAVEEMKRA 1203
Cdd:TIGR02168  190 RLEDILNELERQLKSLERQAEKAERykELKAELR---ELELALLVLR--LEELREELEELQEELK------EAEEELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1204 KEEAQQKEAKVKLLTESVNSV-----IAQAppvAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKA 1278
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELeeeieELQK---ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1279 NKWLNEVEFKLkttenipggaEEISEVLDSLENLMRHSEDnpnqirilaqtltdggvmdelINEELETFNSRWRELHEEA 1358
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEA---------------------ELEELESRLEELEEQLETL 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1359 VRRQKLLEQSIQSAQETeksLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQK--IQSDLTSHEISLEEMKKHNQGKEA 1436
Cdd:TIGR02168  385 RSKVAQLELQIASLNNE---IERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEE 461
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1437 AQRVLS-QIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEvkmhlpalETKSVEQEvvQSQLNHCVNLYKSLSEV 1515
Cdd:TIGR02168  462 ALEELReELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE--------GVKALLKN--QSGLSGILGVLSELISV 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1516 KSEVEMVIktgrqivqkkqtenpkelderVTALKLHyneLGAKVTERKQQLEKC---LKLSRKMRKEMNVLTEW----LA 1588
Cdd:TIGR02168  532 DEGYEAAI---------------------EAALGGR---LQAVVVENLNAAKKAiafLKQNELGRVTFLPLDSIkgteIQ 587
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1589 ATDMELTKRsaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEAL--KTVLGKKETLVEDKLSLLNSNWIaVTSR 1666
Cdd:TIGR02168  588 GNDREILKN--IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALelAKKLRPGYRIVTLDGDLVRPGGV-ITGG 664
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1667 AEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKpQQKEDVLKRLKAELNDIRPKVDSTRDQAANL----- 1741
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLeaeve 743
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1742 ----MANRGDHCRKLVEPQISELNHRFAAISHRIKTGKAsiplkELEQFNSDIQKLLEPLEAEIQQGVNLKEEdfnkdmn 1817
Cdd:TIGR02168  744 qleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-----EIEELEAQIEQLKEELKALREALDELRAE------- 811
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1818 ednegtVKELLQRGDNLQQRITDERKReeIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY---KRQADDLLKCLD 1894
Cdd:TIGR02168  812 ------LTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALLNERA 883
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578837834  1895 DIEKKLASLPEPRD---------ERKIKEIDRELQKKKEELNAVRRQAEGL 1936
Cdd:TIGR02168  884 SLEEALALLRSELEelseelrelESKRSELRRELEELREKLAQLELRLEGL 934
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2584-2803 2.32e-13

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: 72.09  E-value: 2.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2584 QWLEAKEEAEQVLGQARAKLESWkEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSaDDTRKVHMIT 2663
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2664 ENINASWRSIHKRVSEREAALEETHRLLQQFpLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQG 2743
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-------SEDLGKDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2744 EIEAHTDVYHNLDENSQKiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEAS 2803
Cdd:cd00176   154 ELEAHEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
140-237 4.05e-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: 68.13  E-value: 4.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSAtQRLEHAFNIARyQLGIEKLLDPED-V 218
Cdd:cd21257    13 LLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKK-RNLLLAFQAAE-SVGIKPSLELSEmM 90
                          90
                  ....*....|....*....
gi 578837834  219 DTTYPDKKSILMYITSLFQ 237
Cdd:cd21257    91 YTDRPDWQSVMQYVAQIYK 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
727-933 1.38e-12

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: 69.78  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  727 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 806
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  807 QLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSePTAIKSQLKICKDEVNRLSDLQPQ 886
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578837834  887 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFKQVFSDVQAREKELQ 933
Cdd:cd00176   162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2011-2208 4.46e-12

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: 68.24  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2011 LLEVEQLLNAPDLcAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHsKKTAALQSATPVERVKLQEALSQLDFQWEKVNK 2090
Cdd:cd00176    16 LSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALN-ELGEQLIEEGHPDAEEIQERLEELNQRWEELRE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2091 MYKDRQGRFDRSVEKWRRFHyDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEI 2169
Cdd:cd00176    94 LAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLkKHKELEEELEAHEPRLKSLNELAEEL 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578837834 2170 IQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEE 2208
Cdd:cd00176   173 LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
136-233 4.89e-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: 65.10  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVvcqqSATQRLEH---AFNIARYQLGIEK 211
Cdd:cd21229     4 PKKLMLAWLQAVL---PELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKL----DPSNSLENcrrAMDLAKREFNIPM 76
                          90       100
                  ....*....|....*....|..
gi 578837834  212 LLDPEDVDTTYPDKKSILMYIT 233
Cdd:cd21229    77 VLSPEDLSSPHLDELSGMTYLS 98
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1048-1152 5.64e-12

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 64.65  E-value: 5.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1048 NKLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEaEPEFASRL 1127
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 578837834  1128 ETELKELNTQWDHMCQQVYARKEAL 1152
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
140-237 8.42e-12

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: 64.71  E-value: 8.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARyQLGIEKLLDPED-V 218
Cdd:cd21256    19 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELN-SQDKRRNFTLAFQAAE-SVGIKSTLDINEmV 96
                          90
                  ....*....|....*....
gi 578837834  219 DTTYPDKKSILMYITSLFQ 237
Cdd:cd21256    97 RTERPDWQSVMTYVTAIYK 115
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
12-117 9.56e-12

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: 64.23  E-value: 9.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREdvqKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGL-----TGQKLPKEKGSTRVHALNNVNKALRVLQN 86
Cdd:cd21219     3 SRE---ERAFRMWLN---SLGLDPLINNLYEDLRDGLVLLQVLDKIqpgcvNWKKVNKPKPLNKFKKVENCNYAVDLAKK 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834   87 NNVDLVNIGSTDIVDGNHKLTLGLIWNIILH 117
Cdd:cd21219    77 LGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2806-3042 1.07e-11

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: 67.09  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2806 QWKRLHLSLQELLVWLQLKDDELSRQAPiGGDFPAVQKQNDVHRAFKRELKTKEPVImstletvriflteqplEGLEKLY 2885
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERV----------------EALNELG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2886 QEPRELPPEERAQnvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEAtDELDLKLRQAEVIKGSWQPVGD 2965
Cdd:cd00176    64 EQLIEEGHPDAEE-----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837834 2966 LliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL-STLEDLNTRWKLLQVAVEDRVRQLHEAH 3042
Cdd:cd00176   138 L--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIeEKLEELNERWEELLELAEERQKKLEEAL 213
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
3154-3286 1.25e-11

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains 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. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 320001  Cd Length: 163  Bit Score: 65.49  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3154 LTTIYDRLEQEHNNLVNVPLCvDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFK----QVASSTGFC 3229
Cdd:cd16243    31 LERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFQlyesGQGGSSGSI 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 3230 DQRRLGLLLHDSIQIPRQLGEVASFGgsNIEPSVRSCFQFANNkPEIEAALFLDWMR 3286
Cdd:cd16243   110 TRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2934-3040 1.57e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 63.49  E-value: 1.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2934 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3013
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837834  3014 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3040
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
449-556 2.31e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 63.11  E-value: 2.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   449 LMDLQNQKLKELNDWLTKTEErtrKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVdESSGDHATAA 528
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 578837834   529 LEEQLKVLGDRWANICRWTEDRWVLLQD 556
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
943-1152 3.01e-11

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: 65.93  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  943 RYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLgELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEiSRKYQSEF 1022
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLK-KHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1023 EEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQtLKKWMAEVDVFLKEEWPaLGDSEILKKQLKQCRLLVSDIQTIQ 1102
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578837834 1103 PSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEAL 1152
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
340-447 3.28e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 62.72  E-value: 3.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   340 NLDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKlseDEETE 419
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 578837834   420 VQEQMNLLNSRWECLRVASMEKQSNLHR 447
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2107-2207 4.66e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.96  E-value: 4.66e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2107 RRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQEKL 2185
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837834   2186 GSLNLRWQEVCKQLSDRKKRLE 2207
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
140-233 6.05e-11

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: 61.63  E-value: 6.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF----DWNSVVCQQSATQrlehAFNIARYQLGIEKLLDP 215
Cdd:cd21230     6 LLGWIQNKI---PQLPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDALENATE----AMQLAEDWLGVPQLITP 78
                          90
                  ....*....|....*...
gi 578837834  216 EDVDTTYPDKKSILMYIT 233
Cdd:cd21230    79 EEIINPNVDEMSVMTYLS 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1162-1369 6.29e-11

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: 64.77  E-value: 6.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1162 LQKDLSEMHEWMTQAEEEYLERDFEyKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEaLKKELE 1241
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1242 TLTTNYQWLCTRLNGKCKTLEEVWAcWHELLSYLEKANKWLNEVEFKLKTTEnIPGGAEEISEVLDSLENLMRH---SED 1318
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEEleaHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578837834 1319 NPNQIRILAQTLTDGGV--MDELINEELETFNSRWRELHEEAVRRQKLLEQSI 1369
Cdd:cd00176   161 RLKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
137-235 7.43e-11

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: 61.59  E-value: 7.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  137 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDW--NSVVCQQSATQRLEHAFNIAR-YQLGIEKLL 213
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinKKPKSPFKKRENINLFLNACKkLGLPELDLF 80
                          90       100
                  ....*....|....*....|..
gi 578837834  214 DPEDVDTTyPDKKSILMYITSL 235
Cdd:cd00014    81 EPEDLYEK-GNLKKVLGTLWAL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2935-3045 1.56e-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: 63.62  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2935 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 3014
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834 3015 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 3045
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
36-115 1.65e-10

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: 60.68  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   36 HIENLFSDLQDGRRLLDLLEGLTGQKLPKEKgsTRVHALN------NVNKALRVLQNNNV----DLVNIGSTDIVDGNHK 105
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSK--LRVPAISrlqklhNVEVALKALKEAGVlrggDGGGITAKDIVDGHRE 102
                          90
                  ....*....|
gi 578837834  106 LTLGLIWNII 115
Cdd:cd21223   103 KTLALLWRII 112
SPEC smart00150
Spectrin repeats;
343-445 2.71e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 2.71e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    343 RYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQE 422
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI---EEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 578837834    423 QMNLLNSRWECLRVASMEKQSNL 445
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
2475-2576 3.14e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 3.14e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2475 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2554
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837834   2555 ERIQNQWDEVQEHLQNRRQQLN 2576
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
12-112 3.19e-10

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: 60.13  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREdvqKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTG--------QKLPKEKGSTRVHALNNVNKALRV 83
Cdd:cd21300     6 ERE---ARVFTLWLN---SLDVEPAVNDLFEDLRDGLILLQAYDKVIPgsvnwkkvNKAPASAEISRFKAVENTNYAVEL 79
                          90       100
                  ....*....|....*....|....*....
gi 578837834   84 LQNNNVDLVNIGSTDIVDGNHKLTLGLIW 112
Cdd:cd21300    80 GKQLGFSLVGIQGADITDGSRTLTLALVW 108
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2104-2208 3.33e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 59.64  E-value: 3.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2104 EKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEH--AKYKWYlKELQDGIGQRQTVVRTLNATGEEIIQqSSKTDASIL 2181
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837834  2182 QEKLGSLNLRWQEVCKQLSDRKKRLEE 2208
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
17-111 3.78e-10

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: 59.62  E-value: 3.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   17 QKKTFTKWVNAQFSKF-GKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHAL--NNVNKALRVLQNNNVDLVN 93
Cdd:cd21213     1 QLQAYVAWVNSQLKKRpGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAErkENVEKVLQFMASKRIRMHQ 80
                          90
                  ....*....|....*...
gi 578837834   94 IGSTDIVDGNHKLTLGLI 111
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLI 98
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
3160-3285 7.36e-10

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin 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, beta-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 60.42  E-value: 7.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3160 RLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLH 3239
Cdd:cd16250    42 RLPSTHQ--ISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLR 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 578837834 3240 DSIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDWM 3285
Cdd:cd16250   120 EVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQKKIMLNMFLDTM 160
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
3154-3267 8.77e-10

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin 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, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320007  Cd Length: 161  Bit Score: 60.30  E-value: 8.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 3154 LTTIYDRLEQE--HNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQ 3231
Cdd:cd16249    32 LSTIFYQLNKRmpTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNGVMVY 111
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 578837834 3232 RRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCF 3267
Cdd:cd16249   112 GRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCF 145
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
12-112 1.11e-09

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: 58.79  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQ--------KLPKEKGSTrVHALNNVNKALRV 83
Cdd:cd21298     2 IEETREEKTYRNWMN---SLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGvvdwsrvnKPFKKLGAN-MKKIENCNYAVEL 77
                          90       100
                  ....*....|....*....|....*....
gi 578837834   84 LQNNNVDLVNIGSTDIVDGNHKLTLGLIW 112
Cdd:cd21298    78 GKKLKFSLVGIGGKDIYDGNRTLTLALVW 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1780-1968 1.19e-09

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: 61.31  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1780 LKELEQFNSDIQKLLEPLEAEIQQgvnLKEEDFNKDMNEdNEGTVKELLQRGDNLQQRitDERKREEIKIKQQLLQTKHN 1859
Cdd:cd00176    16 LSEKEELLSSTDYGDDLESVEALL---KKHEALEAELAA-HEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1860 ALKDLrSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQ 1932
Cdd:cd00176    90 ELREL-AEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLesveellKKHKELEEELEAHEPRLKSLNEL 168
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578837834 1933 AEGLSEDG---AAMAVEPTQIQLSKRWREIESKFAQFRR 1968
Cdd:cd00176   169 AEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQK 207
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
140-218 1.59e-09

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: 57.75  E-value: 1.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834  140 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDwNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDV 218
Cdd:cd21196     8 LLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLE-PSELQGLGALEATAWALKVAENELGITPVVSAQAV 85
SPEC smart00150
Spectrin repeats;
454-555 1.69e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 57.72  E-value: 1.69e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    454 NQKLKELNDWLTKTEertRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDEsSGDHATAALEEQL 533
Cdd:smart00150    4 LRDADELEAWLEEKE---QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837834    534 KVLGDRWANICRWTEDRWVLLQ 555
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2570-2686 2.88e-09

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 56.94  E-value: 2.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2570 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 2649
Cdd:pfam00435    1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 578837834  2650 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 2686
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2213-2318 4.47e-09

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 56.56  E-value: 4.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2213 LSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLE 2292
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE---GHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 578837834  2293 NKLKQTNLQWIKVSRALPEKQGEIEA 2318
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1268-1474 4.79e-09

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: 59.38  E-value: 4.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1268 WHELLSYLEKANKWLNEVEFKLKTTENI--PGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMD-ELINEEL 1344
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGddLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1345 ETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQK-IQSDLTSHEIS 1423
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKeLEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578837834 1424 LEEMKKhnQGKE-AAQRVLSQIDVAQKKLQDVSMKFRLFQKPA-NFEQRLQES 1474
Cdd:cd00176   162 LKSLNE--LAEElLEEGHPDADEEIEEKLEELNERWEELLELAeERQKKLEEA 212
PTZ00121 PTZ00121
MAEBL; Provisional
1357-1964 4.88e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1357 EAVRRQKLLEQSIQSAQETEKsLHLIQESLTFIDKQLAAYI----ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHN 1431
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFArrqaAIKAEEARKADELKKAEEKKKADEAkKAEEKKKAD 1305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1432 QGKEAAQRVlSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM-HLPALETKSVEQEVVQSQLNhcvnlyK 1510
Cdd:PTZ00121 1306 EAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKEEAK------K 1378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1511 SLSEVKSEVEMVIKTGRqiVQKKQTENPKELDE--RVTALKLHYNELGAKvTERKQQLEKCLKLSRKMRKEMNVLTEWLA 1588
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADE--AKKKAEEDKKKADElkKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1589 ATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgEALKTVLGKKETLVEDKlsllnsnwiAVTSRAE 1668
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKK---------AEEAKKA 1524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1669 EWLNLLLEYQKHMETfdQNVDHITKwiiqADTLLDESEKKKPQQKEDVLKRLKAElnDIRPKVDSTRDQAANLMANRGDH 1748
Cdd:PTZ00121 1525 DEAKKAEEAKKADEA--KKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEE 1596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1749 CRKLVEPQISELNHRF-AAISHRIKTGKasipLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDMNEDNEGTVKE 1826
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAkKAEEAKIKAEE----LKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEE 1672
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1827 LLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEP 1906
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834 1907 RDER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFA 1964
Cdd:PTZ00121 1753 EEEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1162-1263 5.75e-09

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 56.17  E-value: 5.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1162 LQKDLSEMHEWMTQAEEEYLERDFEyKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIaQAPPVAQEALKKELE 1241
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 578837834  1242 TLTTNYQWLCTRLNGKCKTLEE 1263
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3059-3088 8.33e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 8.33e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837834 3059 GPWERAISPNKVPYYINHETQTTCWDHPKM 3088
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
12-115 8.36e-09

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: 56.55  E-value: 8.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAQFSKfgkQHIENLFSDLQDGRRLLDLLEGL-------TGQKLPKEKGSTRVHALNNVNKALRVL 84
Cdd:cd21331    18 EGETREERTFRNWMNSLGVN---PHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELG 94
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837834   85 QNN-NVDLVNIGSTDIVDGNHKLTLGLIWNII 115
Cdd:cd21331    95 KHPaKFSLVGIGGQDLNDGNPTLTLALVWQLM 126
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1021-1633 1.25e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1021 EFEEIEGRWKKLSS---QLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEI----LKKQLKQCRL 1093
Cdd:PRK03918  201 ELEEVLREINEISSelpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEErieeLKKEIEELEE 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1094 LVSDIQTIQPS------LNSVNEGGQKIKNEAEPEfASRLETELKELNTQWDHMCQQVyARKEALKGGLEKtvsLQKDLS 1167
Cdd:PRK03918  281 KVKELKELKEKaeeyikLSEFYEEYLDELREIEKR-LSRLEEEINGIEERIKELEEKE-ERLEELKKKLKE---LEKRLE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1168 EMHEWMTQAEE--------EYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQappvaqeaLKKE 1239
Cdd:PRK03918  356 ELEERHELYEEakakkeelERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE--------LKKA 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1240 LETLttnyqwlcTRLNGKCKT----LEEvwacwHELLSYLEKANKWLNEVEFKLKTTENIpggAEEISEVLDSLENLMRH 1315
Cdd:PRK03918  428 IEEL--------KKAKGKCPVcgreLTE-----EHRKELLEEYTAELKRIEKELKEIEEK---ERKLRKELRELEKVLKK 491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1316 SEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVR---RQKLLEQSIQSAQETEKSLHLIQESLTFIDKQ 1392
Cdd:PRK03918  492 ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1393 LAAYIadkvdaAQMPQEAQKIQSDLTSHEISLEEM-KKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFrlfqkpanfeQRL 1471
Cdd:PRK03918  572 LAELL------KELEELGFESVEELEERLKELEPFyNEYLELKDAEKELEREEKELKKLEEELDKAF----------EEL 635
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1472 QESKMILDEVKMHLPALETKSVEQEvvqsqlnhcvnlYKSLSEVKSEVEMVIKTGRqivqkkqtENPKELDERVTALKLH 1551
Cdd:PRK03918  636 AETEKRLEELRKELEELEKKYSEEE------------YEELREEYLELSRELAGLR--------AELEELEKRREEIKKT 695
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1552 YNELGAKVTERKQQLEKcLKLSRKMRKEMNVLTEWLAATDMELTKR--SAVEGMPSNLDSEVAWGKATQKEI--EKQKVH 1627
Cdd:PRK03918  696 LEKLKEELEEREKAKKE-LEKLEKALERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVkaEENKVK 774

                  ....*.
gi 578837834 1628 LKSITE 1633
Cdd:PRK03918  775 LFVVYQ 780
SPEC smart00150
Spectrin repeats;
2692-2801 1.62e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 54.64  E-value: 1.62e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2692 QQFPLDLEKFLAWLTEAETTAnvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 2771
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 578837834   2772 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 2801
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1877-1979 3.13e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 3.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1877 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 1954
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 578837834  1955 RWREIESKFAQFRRLNFAQIHTVRE 1979
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
3056-3088 3.16e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 51.83  E-value: 3.16e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 578837834   3056 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 3088
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1350-1980 3.35e-08

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: 60.07  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1350 RWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKK 1429
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1430 HNQGKEAA-----QRVLSQIDVAQKKLQDVSMKFRLFQKP-ANFEQRLQESKMILDEVKMHLPALETK--SVEQEVVQSQ 1501
Cdd:TIGR02168  313 NLERQLEEleaqlEELESKLDELAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1502 L------NHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRK 1575
Cdd:TIGR02168  393 LqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1576 MRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGE----ALKTVLGKK------ 1645
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaAIEAALGGRlqavvv 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1646 ----------ETLVEDKL-------------SLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLL 1702
Cdd:TIGR02168  553 enlnaakkaiAFLKQNELgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLD 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1703 DESEKKKPQQKEDVLKRLKAELndIRPKVDST--RDQAANLMANRG---DHCRKLVEPQISELNhrfaaishriktgKAS 1777
Cdd:TIGR02168  633 NALELAKKLRPGYRIVTLDGDL--VRPGGVITggSAKTNSSILERRreiEELEEKIEELEEKIA-------------ELE 697
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1778 IPLKELEQFNSDIQKLLEPLEA---EIQQGVNLKEEDFnkdmnEDNEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQL 1853
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKeleELSRQISALRKDL-----ARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEE 772
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1854 LQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEELNAVRRQA 1933
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERLESLERRIAATERRLEDLEEQI 847
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 578837834  1934 EGLSEDGAAMA--VEPTQIQLSKRWREIESKFAQFRRLNfAQIHTVREE 1980
Cdd:TIGR02168  848 EELSEDIESLAaeIEELEELIEELESELEALLNERASLE-EALALLRSE 895
SPEC smart00150
Spectrin repeats;
2937-3038 3.78e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 3.78e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2937 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 3016
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 578837834   3017 LEDLNTRWKLLQVAVEDRVRQL 3038
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
18-115 6.00e-08

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: 53.73  E-value: 6.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   18 KKTFTKWVNAQFSK--FGKQHI------ENLFSDLQDGRRLLDLLE----GLTG-QKLPKEKGSTRVHALNNVNKALRVL 84
Cdd:cd21217     3 KEAFVEHINSLLADdpDLKHLLpidpdgDDLFEALRDGVLLCKLINkivpGTIDeRKLNKKKPKNIFEATENLNLALNAA 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837834   85 QNNNVDLVNIGSTDIVDGNHKLTLGLIWNII 115
Cdd:cd21217    83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
3060-3086 9.42e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 50.20  E-value: 9.42e-08
                           10        20
                   ....*....|....*....|....*..
gi 578837834  3060 PWERAISPNKVPYYINHETQTTCWDHP 3086
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1147-1979 1.24e-07

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: 58.06  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1147 ARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQK-EAKVKLLTESVNSVI 1225
Cdd:pfam02463  170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKlNEERIDLLQELLRDE 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1226 AQAPPVAQEALKKELETLTTNYQWLctRLNGKCKTLEEVWACWHELLsyLEKANKWLNEVEFKLKTTENIPGGAEEISEV 1305
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKEN--KEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1306 LDSLENLMRHSEDNPNQIRILAQTLTdggvmdelINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQ-ETEKSLHLIQE 1384
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKELEIKR--------EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlSSAAKLKEEEL 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1385 SLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKP 1464
Cdd:pfam02463  398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1465 ANFEQRLQESKMILDEVKMHLPALETKSVE---------QEVVQSQLNHCVNLYKSLSEVK--------------SEVEM 1521
Cdd:pfam02463  478 QLVKLQEQLELLLSRQKLEERSQKESKARSglkvllaliKDGVGGRIISAHGRLGDLGVAVenykvaistaviveVSATA 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1522 VIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVE 1601
Cdd:pfam02463  558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1602 GMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgealktvLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHM 1681
Cdd:pfam02463  638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLS--------ELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1682 ETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAA------NLMANRGDHCRKLVEP 1755
Cdd:pfam02463  710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSelslkeKELAEEREKTEKLKVE 789
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1756 QISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQ-------GVNLKEEDFNKDMNEDNEGTVKELL 1828
Cdd:pfam02463  790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEElalelkeEQKLEKLAEEELERLEEEITKEELL 869
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1829 QRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKklaSLPEPRD 1908
Cdd:pfam02463  870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE---LLLEEAD 946
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578837834  1909 ERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVRE 1979
Cdd:pfam02463  947 EKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1679-1776 1.26e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 52.32  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1679 KHMETFDQNVDHITKWIIQADTLLDESEKKK----PQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANrGDHCRKLVE 1754
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKdlesVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
                           90       100
                   ....*....|....*....|..
gi 578837834  1755 PQISELNHRFAAISHRIKTGKA 1776
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQ 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1571-1676 1.78e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 51.94  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1571 KLSRKMRKEMNVLTEWLAATDMELTKRSaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVE 1650
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 578837834  1651 DKLSLLNSNWIAVTSRAEEWLNLLLE 1676
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
922-1566 2.00e-07

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: 57.37  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   922 FSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSI--PQLSVTDYEIMEQRLgELQALQSSLQEQQSGLYYL 999
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEEltAELQELEEKLEELRL-EVSELEEEIEELQKELYAL 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1000 STTVKEMSKKApseisRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALG 1079
Cdd:TIGR02168  294 ANEISRLEQQK-----QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1080 DSEILKKQL---------------KQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDhmcqq 1144
Cdd:TIGR02168  369 ELESRLEELeeqletlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE----- 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1145 vyARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKL-------- 1216
Cdd:TIGR02168  444 --ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsglsgi 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1217 ---------------------LTESVNSVI---AQAPPVAQEALKKELETLTTNY---QWLCTRLNGK----CKTLEEVW 1265
Cdd:TIGR02168  522 lgvlselisvdegyeaaieaaLGGRLQAVVvenLNAAKKAIAFLKQNELGRVTFLpldSIKGTEIQGNdreiLKNIEGFL 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1266 ACWHELLSYLEKANKWLN----------------EVEFKLKTTENI---------------PGGAEEISEVLD---SLEN 1311
Cdd:TIGR02168  602 GVAKDLVKFDPKLRKALSyllggvlvvddldnalELAKKLRPGYRIvtldgdlvrpggvitGGSAKTNSSILErrrEIEE 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1312 LMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDK 1391
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1392 QLAAYIADKVDAAQMPQEA-QKIQSDLTSHEISLEEMKKHNQGKEAAQRVLS--QIDVAQKKLQDVSMKFRLFQKPANFE 1468
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALDELRAELTllNEEAANLRERLESLERRIAATERRLE 841
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1469 QRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSE----VKSEVEMVIKTGRQIVQKKQ--TENPKELD 1542
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELSEELRELESKRSelRRELEELR 921
                          730       740
                   ....*....|....*....|....
gi 578837834  1543 ERVTALKLHYNELGAKVTERKQQL 1566
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDNLQERL 945
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
136-237 2.48e-07

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: 51.92  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  136 SEKILLSWVrqstrNY-------PQVNVINFTTSWSDGLALNALIHSHRP---DLFDWNSVVCQQSATQRLEHAFNIARy 205
Cdd:cd21218    11 PEEILLRWV-----NYhlkkagpTKKRVTNFSSDLKDGEVYALLLHSLAPelcDKELVLEVLSEEDLEKRAEKVLQAAE- 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837834  206 QLGIEKLLDPEDVDTtyPDKKSILMYITSLFQ 237
Cdd:cd21218    85 KLGCKYFLTPEDIVS--GNPRLNLAFVATLFN 114
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
132-235 2.49e-07

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: 52.00  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  132 QQTNSEKiLLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVVCQQsATQRLEHAFNIARYQLGIE 210
Cdd:cd21314     9 KQTPKQR-LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQ-PVQNAREAMQQADDWLGVP 83
                          90       100
                  ....*....|....*....|....*
gi 578837834  211 KLLDPEDVDTTYPDKKSILMYITSL 235
Cdd:cd21314    84 QVIAPEEIVDPNVDEHSVMTYLSQF 108
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
751-1496 2.71e-07

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: 56.99  E-value: 2.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   751 RKEGNFSDLKEKVNAIER--EKAEKFRKLQDASRSAQ---------ALVEQM----VNEGVNADSIKQASEQLNSRWIEF 815
Cdd:TIGR02168  190 RLEDILNELERQLKSLERqaEKAERYKELKAELRELElallvlrleELREELeelqEELKEAEEELEELTAELQELEEKL 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   816 CQL------LSERLNwlEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVN-RLSDLQPQIE 888
Cdd:TIGR02168  270 EELrlevseLEEEIE--ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   889 RLKIQSIALKEKGQGpmfLDADFVAFTNHFKQVF-------SDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETK 961
Cdd:TIGR02168  348 ELKEELESLEAELEE---LEAELEELESRLEELEeqletlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   962 LSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEIsRKYQSEFEEIEGRWKKLSSQLVEH-- 1039
Cdd:TIGR02168  425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLeg 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1040 -CQKLEEQMNKLRKIQNHIQTL-------KKWMAEVDVFLKE---------EWPALGDSEILKKQLKQcRLLVSDIQTIQ 1102
Cdd:TIGR02168  504 fSEGVKALLKNQSGLSGILGVLselisvdEGYEAAIEAALGGrlqavvvenLNAAKKAIAFLKQNELG-RVTFLPLDSIK 582
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1103 PSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVY--------ARKEALKGGLEKTVSLQKDLSEMHEWMT 1174
Cdd:TIGR02168  583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvddldnaLELAKKLRPGYRIVTLDGDLVRPGGVIT 662
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1175 QAEEEY----LERDFEYKtpdELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQE------ALKKELETLT 1244
Cdd:TIGR02168  663 GGSAKTnssiLERRREIE---ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqisALRKDLARLE 739
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1245 TNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEfklkttenipggaEEISEVLDSLENLMRHSEDNPNQIR 1324
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------------AEIEELEAQIEQLKEELKALREALD 806
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1325 ILAQTLTDggvMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAA 1404
Cdd:TIGR02168  807 ELRAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1405 QMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAaqrvlsQIDVAQKKLQDVSMKF-RLFQKPANFEQRLQES-KMILDEVK 1482
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRR------ELEELREKLAQLELRLeGLEVRIDNLQERLSEEySLTLEEAE 957
                          810
                   ....*....|....
gi 578837834  1483 MHLPALETKSVEQE 1496
Cdd:TIGR02168  958 ALENKIEDDEEEAR 971
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1467-1676 3.45e-07

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: 53.99  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1467 FEQRLQESKMILDEVKMHLPALETKSVEQEVvQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPkELDERVT 1546
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1547 ALKLHYNELGAKVTERKQQLEKCLKLSRKMRkEMNVLTEWLAATDMELTKRSAVEGMPSnLDSEVAWGKATQKEIEKQKV 1626
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578837834 1627 HLKSITEVGEALKTVLGKKETL-VEDKLSLLNSNWIAVTSRAEEWLNLLLE 1676
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEE 211
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
3313-3359 3.87e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 48.97  E-value: 3.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578837834 3313 CNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRvaKGHKMHYPMVEY 3359
Cdd:cd02249     3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2065-2906 3.95e-07

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: 56.61  E-value: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2065 SATPVERVKLQEALSQLDFQWEKVNKMYKDrqgrFDRSVEKWRRFHYDIKIFNQWL----TEAEQFLRKTQIPENWEHAK 2140
Cdd:TIGR02169  149 SMSPVERRKIIDEIAGVAEFDRKKEKALEE----LEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYE 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2141 YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDAsiLQEKLGSLNLRWQEVCKQLSDR--------KKRLEEQKNI 2212
Cdd:TIGR02169  225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE--LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAE 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2213 LSEFQRDLNEFVLWLEEADNiasiplepgKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLE 2292
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEE---------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE---LKEELEDLR 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2293 NKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAV 2372
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2373 QAKQPDVEEI---LSK-GQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQP 2448
Cdd:TIGR02169  451 KKQEWKLEQLaadLSKyEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2449 VVTKETAISKLEMPSSLMLEVPALADFNRA-------------------WTELTDWLSLLDqvIKSQRVMVGDLEDINEM 2509
Cdd:TIGR02169  531 GSVGERYATAIEVAAGNRLNNVVVEDDAVAkeaiellkrrkagratflpLNKMRDERRDLS--ILSEDGVIGFAVDLVEF 608
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2510 ----------IIKQKATMQDLEQRRPQLEE--LITAAQNL------------------KNKTSNQEARTIITDRIERIQN 2559
Cdd:TIGR02169  609 dpkyepafkyVFGDTLVVEDIEAARRLMGKyrMVTLEGELfeksgamtggsraprggiLFSRSEPAELQRLRERLEGLKR 688
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2560 QWDEVQE---HLQNRRQQLNEMLKDSTQWLEAKE-EAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLR---Q 2632
Cdd:TIGR02169  689 ELSSLQSelrRIENRLDELSQELSDASRKIGEIEkEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariE 768
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2633 WQTNVDVANDLALKLLRDysaddtRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAwltEAEtta 2712
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEA------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--LTLEKEYL---EKE--- 834
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2713 nvLQDATRKERLLEDSKgvKELMKQWQDLQGEIEAHTDVYhnldENSQKILRSLEGSddAVLLQRRLDNMNFKWSELRKK 2792
Cdd:TIGR02169  835 --IQELQEQRIDLKEQI--KSIEKEIENLNGKKEELEEEL----EELEAALRDLESR--LGDLKKERDELEAQLRELERK 904
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2793 SLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTL----ET 2868
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIqeyeEV 984
                          890       900       910
                   ....*....|....*....|....*....|....*...
gi 578837834  2869 VRIFLTEQplEGLEKLYQEPRELppEERAQNVTRLLRK 2906
Cdd:TIGR02169  985 LKRLDELK--EKRAKLEEERKAI--LERIEEYEKKKRE 1018
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
17-117 4.59e-07

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: 50.96  E-value: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   17 QKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQ------------KLPKEKgstrvhaLNNVNKALRVL 84
Cdd:cd21299     5 EERCFRLWIN---SLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGsvnwkhankppiKMPFKK-------VENCNQVVKIG 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837834   85 QNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILH 117
Cdd:cd21299    75 KQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2366-2579 4.92e-07

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: 53.22  E-value: 4.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2366 KETEIAVQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKqpdlapglttigasptqtvtl 2444
Cdd:cd00176    43 EALEAELAAHEERVEALNELGEQLIEEGHpDAEEIQERLEELNQRWEELRELAEERRQR--------------------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2445 vtqpvvtketaisklempsslMLEVPALADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRR 2524
Cdd:cd00176   102 ---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837834 2525 PQLEELITAAQNLKNKtSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEML 2579
Cdd:cd00176   160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
18-117 5.90e-07

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: 51.05  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   18 KKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLP----KEKGSTRVHALNNVNKALRVLQNNNVDLVN 93
Cdd:cd21222    18 KELLLQFVNKHLAKLNIE-VTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMEDAGISTPK 96
                          90       100
                  ....*....|....*....|....
gi 578837834   94 IGSTDIVDGNHKLTLGLIWNIILH 117
Cdd:cd21222    97 IRPEDIVNGDLKSILRVLYSLFSK 120
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1360-1938 6.35e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1360 RRQKLLEQSIQSAQETEKSLH-----LIQEsLTFIDKQLAAYIADKVDAAQMPQEAQKIqsdLTSHEISLEEmkkhnqgk 1434
Cdd:PRK02224  185 QRGSLDQLKAQIEEKEEKDLHerlngLESE-LAELDEEIERYEEQREQARETRDEADEV---LEEHEERREE-------- 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1435 eaaqrvlsqIDVAQKKLQDVSMKFR-LFQKPANFEQRLQESKMILDEVKMHLPAL----ETKSVEQEVVQSQLNhcvnly 1509
Cdd:PRK02224  253 ---------LETLEAEIEDLRETIAeTEREREELAEEVRDLRERLEELEEERDDLlaeaGLDDADAEAVEARRE------ 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1510 kSLSEVKSEVEMVIKTGRQIVQKKQ------TENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVL 1583
Cdd:PRK02224  318 -ELEDRDEELRDRLEECRVAAQAHNeeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1584 TEWLAATDMEL----TKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVG---------------EALKTVLGK 1644
Cdd:PRK02224  397 RERFGDAPVDLgnaeDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvegsphvETIEEDRER 476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1645 KETLvEDKLSLLNSNWIAVTSRAEEwLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDEsekkkpqqKEDVLKRLKAEL 1724
Cdd:PRK02224  477 VEEL-EAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEE--------KRERAEELRERA 546
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1725 NDIRPKVDSTRDQAANLMaNRGDHCRKlvepQISELNHRFAAISHRIKTgkasipLKELEqfnsDIQKLLEPLEAEIQQg 1804
Cdd:PRK02224  547 AELEAEAEEKREAAAEAE-EEAEEARE----EVAELNSKLAELKERIES------LERIR----TLLAAIADAEDEIER- 610
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1805 VNLKEEDFNkDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKaleishqwyqykr 1884
Cdd:PRK02224  611 LREKREALA-ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREER------------- 676
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578837834 1885 qaDDLLKCLDDIEKKLASLPEPRDERKikeidrELQKKKEELNAVRRQAEGLSE 1938
Cdd:PRK02224  677 --DDLQAEIGAVENELEELEELRERRE------ALENRVEALEALYDEAEELES 722
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
132-235 6.49e-07

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: 50.57  E-value: 6.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  132 QQTNSEKiLLSWVRQstrNYPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVVCQQSATQRLEhAFNIARYQLGIE 210
Cdd:cd21312    10 KQTPKQR-LLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNARE-AMQQADDWLGIP 84
                          90       100
                  ....*....|....*....|....*
gi 578837834  211 KLLDPEDVDTTYPDKKSILMYITSL 235
Cdd:cd21312    85 QVITPEEIVDPNVDEHSVMTYLSQF 109
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2286-3020 8.02e-07

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: 55.45  E-value: 8.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2286 EEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ--PNQEGPF 2363
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2364 DVKETEIAVQAKQPD--------VEEILSKGQHLYKEKPATQPVKR-KLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTI 2434
Cdd:TIGR02168  319 EELEAQLEELESKLDelaeelaeLEEKLEELKEELESLEAELEELEaELEELESRLEELEEQLETLRSKVAQLELQIASL 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2435 GASPTQTVTLVTQPVVTKETAISKLEmpssLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQK 2514
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIE----ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2515 ATMQDLEQRRPQLEELITAAQNLKNKTS-----------NQEARTIITDRIE---RIQNQWD-EVQEHLQNRRQQLneML 2579
Cdd:TIGR02168  475 QALDAAERELAQLQARLDSLERLQENLEgfsegvkallkNQSGLSGILGVLSeliSVDEGYEaAIEAALGGRLQAV--VV 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2580 KDSTQWLEAKEEAEQ---------VLGQARA------KLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDL- 2643
Cdd:TIGR02168  553 ENLNAAKKAIAFLKQnelgrvtflPLDSIKGteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLd 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2644 -ALKLLRDYSAdDTRKVHMITENINASWRSIHKRVS------EREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQ 2716
Cdd:TIGR02168  633 nALELAKKLRP-GYRIVTLDGDLVRPGGVITGGSAKtnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2717 DATRK--ERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGsddavlLQRRLDNMNFKWSELRKKSL 2794
Cdd:TIGR02168  712 EELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE------LEERLEEAEEELAEAEAEIE 785
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2795 NIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQApiggdFPAVQKQNDVHRAfKRELKTKEPVIMSTLETVrIFLT 2874
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR-----ERLESLERRIAAT-ERRLEDLEEQIEELSEDI-ESLA 858
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2875 EQplegLEKLYQEPRELPPE-ERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQA 2953
Cdd:TIGR02168  859 AE----IEELEELIEELESElEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837834  2954 EV-IKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKEnvsHVNDLARQLTTLGiqlsPYNLSTLEDL 3020
Cdd:TIGR02168  935 EVrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELG----PVNLAAIEEY 995
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
655-1264 2.93e-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: 53.43  E-value: 2.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   655 VQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSw 734
Cdd:TIGR00618  221 KQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI- 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   735 itrsEAVLQSPefaiFRKEGNFSDLKEKvnaiEREKAEKFRKLQDASRSAQALVEQMVNEGV---NADSIKQASEQLNSR 811
Cdd:TIGR00618  300 ----KAVTQIE----QQAQRIHTELQSK----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSI 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   812 WIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVnrlsdlQPQIERLK 891
Cdd:TIGR00618  368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ------ELQQRYAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   892 IQSIALKEKGQGPMFLDAdfvaftnHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSvtD 971
Cdd:TIGR00618  442 LCAAAITCTAQCEKLEKI-------HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI--H 512
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   972 YEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEisRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLR 1051
Cdd:TIGR00618  513 PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE--RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1052 KIQNHIQTLKKWMAEVDVFLKEEW--------PALGDSEI-LKKQLKQCRL-------------LVSDIQTIQPSLNSVN 1109
Cdd:TIGR00618  591 NITVRLQDLTEKLSEAEDMLACEQhallrklqPEQDLQDVrLHLQQCSQELalkltalhalqltLTQERVREHALSIRVL 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1110 EGGQKIKNEAEPEFASR---------------------LETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSE 1168
Cdd:TIGR00618  671 PKELLASRQLALQKMQSekeqltywkemlaqcqtllreLETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1169 MHEWMTQAEEEYLERDFE-----YKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESvnsvIAQAPPVAQEALKKELETL 1243
Cdd:TIGR00618  751 QARTVLKARTEAHFNNNEevtaaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE----IGQEIPSDEDILNLQCETL 826
                          650       660
                   ....*....|....*....|.
gi 578837834  1244 TTNYQWLCTRLNGKCKTLEEV 1264
Cdd:TIGR00618  827 VQEEEQFLSRLEEKSATLGEI 847
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
141-236 3.15e-06

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: 48.07  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  141 LSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSaTQRLEHAFNIARyQLGIEKLLDPEDVDT 220
Cdd:cd21185     7 LRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEES-ENNIQRGLEAGK-SLGVEPVLTAEEMAD 81
                          90
                  ....*....|....*.
gi 578837834  221 TYPDKKSILMYITSLF 236
Cdd:cd21185    82 PEVEHLGIMAYAAQLQ 97
SPEC smart00150
Spectrin repeats;
1060-1153 3.33e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.09  E-value: 3.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   1060 LKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLETELKELNTQWD 1139
Cdd:smart00150   10 LEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEELNERWE 87
                            90
                    ....*....|....
gi 578837834   1140 HMCQQVYARKEALK 1153
Cdd:smart00150   88 ELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1615-1772 3.38e-06

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: 50.91  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1615 KATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQnVDHITKW 1694
Cdd:cd00176    43 EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQW 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1695 IIQADTLLDESEK-KKPQQKEDVLKRLKA---ELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHR 1770
Cdd:cd00176   122 LEEKEAALASEDLgKDLESVEELLKKHKEleeELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLEL 201

                  ..
gi 578837834 1771 IK 1772
Cdd:cd00176   202 AE 203
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
3313-3356 5.67e-06

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 45.80  E-value: 5.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578837834 3313 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPM 3356
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1697-1971 8.83e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.68  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1697 QADTLLDESEKKKPQQKE--DVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVE--PQISELNHRFAAISHRIK 1772
Cdd:COG1340    16 KIEELREEIEELKEKRDElnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKElkEERDELNEKLNELREELD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1773 TGKASIPLKELEQFNSD-IQKLLEPLEAEIQqgvnlkeedfNKDMNEDNEgtvKELLQRGDNLQQRITDERKREEIKIKQ 1851
Cdd:COG1340    96 ELRKELAELNKAGGSIDkLRKEIERLEWRQQ----------TEVLSPEEE---KELVEKIKELEKELEKAKKALEKNEKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1852 QLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER--KIKEIDRELQKKKEELNAV 1929
Cdd:COG1340   163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqeKADELHEEIIELQKELREL 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578837834 1930 RRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNF 1971
Cdd:COG1340   243 RKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTT 284
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
140-239 9.19e-06

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: 48.07  E-value: 9.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTRNYpQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHA-------------------- 199
Cdd:cd21224     5 LLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDeaedfwvaefspstgdsgls 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578837834  200 ----------FNIAR---YQLG-IEKLLDPEDVDTTYPDKKSILMYITSLFQVL 239
Cdd:cd21224    84 sellanekrnFKLVQqavAELGgVPALLRASDMSNTIPDEKVVILFLSYLCARL 137
SPEC smart00150
Spectrin repeats;
727-827 1.01e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 1.01e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    727 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 806
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837834    807 QLNSRWIEFCQLLSERLNWLE 827
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1420-2066 1.25e-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: 51.66  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1420 HEISLEEMKKHNQ--GKEAAQRVLS----QIDVAQKKLQDVS-----MKFRLFQKPANFEQRLQESKMILDEVkMHLPAL 1488
Cdd:pfam15921   57 YEVELDSPRKIIAypGKEHIERVLEeyshQVKDLQRRLNESNelhekQKFYLRQSVIDLQTKLQEMQMERDAM-ADIRRR 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1489 ETKSveQEVVQSQLNHCVNLYKSLSEVKSEveMVIKTGRQIVQKKQTENPKE--LDERVTALKLHYNELGAKVTERKQql 1566
Cdd:pfam15921  136 ESQS--QEDLRNQLQNTVHELEAAKCLKED--MLEDSNTQIEQLRKMMLSHEgvLQEIRSILVDFEEASGKKIYEHDS-- 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1567 ekclkLSRKMRKEMNvltewlaatdmeltkrSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSitEVGEALKTVLGKKE 1646
Cdd:pfam15921  210 -----MSTMHFRSLG----------------SAISKILRELDTEISYLKGRIFPVEDQLEALKS--ESQNKIELLLQQHQ 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1647 TLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETF-----DQN------VDHITKWIIQADTLLDESEKKKPQQKED 1715
Cdd:pfam15921  267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIqeqarNQNsmymrqLSDLESTVSQLRSELREAKRMYEDKIEE 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1716 VLKRL---KAELNDIRpkvdSTRDQAANLMANRGDHCRKLvepqISELNHRFAAISHRIKTGKA--------SIPL---- 1780
Cdd:pfam15921  347 LEKQLvlaNSELTEAR----TERDQFSQESGNLDDQLQKL----LADLHKREKELSLEKEQNKRlwdrdtgnSITIdhlr 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1781 KELEQFNSDIQK---LLEPLEAEIqQGVNLKEEDFNKDMNEDNEgTVKELLQRGDNLQQRItdERKREEIKIKQQLLQTK 1857
Cdd:pfam15921  419 RELDDRNMEVQRleaLLKAMKSEC-QGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEML--RKVVEELTAKKMTLESS 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1858 HNALKDLRS--QRRKKALEISHQWYQYKRQADDL-LKCLDDIEKKLASLPEPRDErkIKEIDRELQKKKEELNAVRRQAE 1934
Cdd:pfam15921  495 ERTVSDLTAslQEKERAIEATNAEITKLRSRVDLkLQELQHLKNEGDHLRNVQTE--CEALKLQMAEKDKVIEILRQQIE 572
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1935 GLSE-------DGAAMAVEPTQIQLSKRWREIESKfaQFRRLNFAQIHTVREetMMVMTEDMPLEISYVPSTYLTEITHV 2007
Cdd:pfam15921  573 NMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQ--EFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAV 648
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834  2008 SQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNikdSLQQSSGRIDIIHSKKTAALQSA 2066
Cdd:pfam15921  649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR---NFRNKSEEMETTTNKLKMQLKSA 704
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2477-2781 1.44e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2477 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 2549
Cdd:COG1196   232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2550 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 2624
Cdd:COG1196   309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2625 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 2704
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2705 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 2781
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2489-3021 1.69e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2489 LDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRrpqLEELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEH 2567
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAE 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2568 LQNRRQQLNEMLKDSTQWLEA-KEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALK 2646
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2647 LLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAWLTEAETTANVLQDATRKERLLE 2726
Cdd:COG1196   440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2727 DSKGVKELMKQWQDLQGEIEAHTDVYhnLDENSQKILRSLEGSDDAV---LLQRRLDNMNFKwselrkkSLNIRSHLEAS 2803
Cdd:COG1196   518 GLRGLAGAVAVLIGVEAAYEAALEAA--LAAALQNIVVEDDEVAAAAieyLKAAKAGRATFL-------PLDKIRARAAL 588
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2804 SDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEpvimsTLETVRIFLTEQPLEGLEK 2883
Cdd:COG1196   589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG-----RLREVTLEGEGGSAGGSLT 663
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2884 LYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIkgswqpV 2963
Cdd:COG1196   664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------L 737
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578837834 2964 GDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGiqlsPYNLSTLEDLN 3021
Cdd:COG1196   738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG----PVNLLAIEEYE 791
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2193-2628 1.91e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2193 QEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASI------------PLEPGKEQQLKEKLEQVKLLVEE- 2259
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKkeelerlkkrltGLTPEKLEKELEELEKAKEEIEEe 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2260 ---LPLRQGILKQ--------LNETGG-----PVlVSAPISPEEQDKLENKLKqtnlqwikvsralpEKQGEIEAQIKDL 2323
Cdd:PRK03918  407 iskITARIGELKKeikelkkaIEELKKakgkcPV-CGRELTEEHRKELLEEYT--------------AELKRIEKELKEI 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2324 GQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ----PNQEGPFDVKETEiavqAKQPDVEEILSKGQHLYKEKPATQPV 2399
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKE 547
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2400 KRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVtlvtqpvvtkETAISKLEmpsslmlevpalaDFNRAW 2479
Cdd:PRK03918  548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----------EERLKELE-------------PFYNEY 604
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2480 TELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKAtmqDLEQRRPQLEELITA--------AQNLKNKTSNQEARtiIT 2551
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEELRKELEELEKKyseeeyeeLREEYLELSRELAG--LR 679
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834 2552 DRIERIQNQWDEVQEHLQNRRQQLNEMLKdstqwleAKEEAEqVLGQARAKLEswkegpytvdAIQKKITETKQLAK 2628
Cdd:PRK03918  680 AELEELEKRREEIKKTLEKLKEELEEREK-------AKKELE-KLEKALERVE----------ELREKVKKYKALLK 738
SPEC smart00150
Spectrin repeats;
1880-1962 1.96e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 1.96e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   1880 YQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDG--AAMAVEPTQI 1950
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLesveallKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90
                    ....*....|..
gi 578837834   1951 QLSKRWREIESK 1962
Cdd:smart00150   81 ELNERWEELKEL 92
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1878-2102 2.46e-05

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: 48.21  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1878 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1950
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1951 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2028
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837834 2029 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2102
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
2215-2317 2.58e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 2.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2215 EFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLENK 2294
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 578837834   2295 LKQTNLQWIKVSRALPEKQGEIE 2317
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1618-1926 2.87e-05

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: 50.02  E-value: 2.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1618 QKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKwiiQ 1697
Cdd:TIGR04523  213 NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK---Q 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1698 ADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANlmanrgdhcrklVEPQISELNHRFAAISHRiktgkas 1777
Cdd:TIGR04523  290 LNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQ------------NNKIISQLNEQISQLKKE------- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1778 ipLKELEQFNSDIQKLLEPLEAEIQQgvNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQriTDERKREEIKIKQQLLQTK 1857
Cdd:TIGR04523  351 --LTNSESENSEKQRELEEKQNEIEK--LKKENQSYKQEIKNLESQINDLESKIQNQEK--LNQQKDEQIKKLQQEKELL 424
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578837834  1858 HNALKDLRSQRRKKALEIS---HQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEEL 1926
Cdd:TIGR04523  425 EKEIERLKETIIKNNSEIKdltNQDSVKELIIKNLDNTRESLETQLKVL-----SRSINKIKQNLEQKQKEL 491
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
922-1868 3.81e-05

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: 50.05  E-value: 3.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   922 FSDVQAREKELQTIFDTLPPMRYQETMSAIRtwvQQSETKLSIPQLSVTDYEIMEQRLGELQAlqsslqeqqsglyylST 1001
Cdd:TIGR00606  165 LSEGKALKQKFDEIFSATRYIKALETLRQVR---QTQGQKVQEHQMELKYLKQYKEKACEIRD---------------QI 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1002 TVKEMSKKAPSEISRKYQSEFEEIEGRWKKLssqlvehcqklEEQMNKLRKIQNHIQTLKKWMAEVdvflkeewpalgds 1081
Cdd:TIGR00606  227 TSKEAQLESSREIVKSYENELDPLKNRLKEI-----------EHNLSKIMKLDNEIKALKSRKKQM-------------- 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1082 EILKKQLKQCRllVSDIQTIQPSLNSVNEGGQKIKNEAEPEFAsRLETELKELNTQWDHMCQQ-----VYARKEALKGGL 1156
Cdd:TIGR00606  282 EKDNSELELKM--EKVFQGTDEQLNDLYHNHQRTVREKERELV-DCQRELEKLNKERRLLNQEktellVEQGRLQLQADR 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1157 EKTVSLQKDlSEMHEWMTQAEEEYLERDfeyktPDeLQKAVEEMKRAKEEAQQKEAKV--KLLTEsvnsvIAQAPPVAQE 1234
Cdd:TIGR00606  359 HQEHIRARD-SLIQSLATRLELDGFERG-----PF-SERQIKNFHTLVIERQEDEAKTaaQLCAD-----LQSKERLKQE 426
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1235 ALKKeletlttnyqwLCTRLNGKCKTLEevwacwhellSYLEKANKWLNEVEFKLKTTENIPGGAEEISEvldsLENLMR 1314
Cdd:TIGR00606  427 QADE-----------IRDEKKGLGRTIE----------LKKEILEKKQEELKFVIKELQQLEGSSDRILE----LDQELR 481
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1315 HSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRwRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLA 1394
Cdd:TIGR00606  482 KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKL-RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1395 AYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKL--QDVSMKFRLFQ--KPANFEQR 1470
Cdd:TIGR00606  561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKeeQLSSYEDKLFDvcGSQDEESD 640
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1471 LQESKMILDEVKMHLPALETKS------VEQEVVQSQlnHCVNLYKSLSEVKSEVEMVIK----------TGRQIVQKKQ 1534
Cdd:TIGR00606  641 LERLKEEIEKSSKQRAMLAGATavysqfITQLTDENQ--SCCPVCQRVFQTEAELQEFISdlqsklrlapDKLKSTESEL 718
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1535 TENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEW---------------LAATDMELTKR-- 1597
Cdd:TIGR00606  719 KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQetllgtimpeeesakVCLTDVTIMERfq 798
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1598 -------SAVEGMPSNLDSEVAWGKATQ--KEIEKQKVHLKSITEVGEALKTVL---GKKETLVEDKLSLLNSNWIAVTS 1665
Cdd:TIGR00606  799 melkdveRKIAQQAAKLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIELNRKLIqdqQEQIQHLKSKTNELKSEKLQIGT 878
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1666 RAEEwlnlLLEYQKHMETFDQNVDHITKWIIQA--DTLLDESEKKKPQQKEDVL--------KRLKAELNDIRPKVDSTR 1735
Cdd:TIGR00606  879 NLQR----RQQFEEQLVELSTEVQSLIREIKDAkeQDSPLETFLEKDQQEKEELissketsnKKAQDKVNDIKEKVKNIH 954
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1736 DQAANLMANRGDHCRKLVEPQISELNHRFAAISHRiktgkasipLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKD 1815
Cdd:TIGR00606  955 GYMKDIENKIQDGKDDYLKQKETELNTVNAQLEEC---------EKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK 1025
                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578837834  1816 MNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQR 1868
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQK 1078
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1191-1934 4.30e-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: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1191 DELQKAVEEMKRAKEEAQQKEAKVKLLTEsvnsviaqappVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHE 1270
Cdd:TIGR02169  194 DEKRQQLERLRREREKAERYQALLKEKRE-----------YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1271 LLSYLEKANKWLNEVEFKLK--TTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGgvmDELINEELETFN 1348
Cdd:TIGR02169  263 LEKRLEEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL---EAEIDKLLAEIE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1349 SRWRELHEEAVRRQKLLEQSIQSAQETEKSLhliqesltfidkqlaayiadkvdaaqmpqeaQKIQSDLTSHEISLEEMK 1428
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEELEDLR-------------------------------AELEEVDKEFAETRDELK 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1429 KHNQGKEAAQRVLSQIDVAQKKLQDvsmkfrlfqkpanfeqRLQESKMILDEVKMHLPALETKsveqevvqsqlnhcvnl 1508
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQE----------------ELQRLSEELADLNAAIAGIEAK----------------- 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1509 yksLSEVKSEVEMVIKTGRQIVQKKQT--ENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMnvlTEW 1586
Cdd:TIGR02169  436 ---INELEEEKEDKALEIKKQEWKLEQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV---RGG 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1587 LAATDMELTKRSAVEGMPSNLDSevaWGKATQKEIEkqkvhlksiTEVGEALKTVLGKKETLVEDKLSLLNS-------- 1658
Cdd:TIGR02169  510 RAVEEVLKASIQGVHGTVAQLGS---VGERYATAIE---------VAAGNRLNNVVVEDDAVAKEAIELLKRrkagratf 577
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1659 ---NWIAVTSRAEEWLNL--LLEYQKHMETFDQNVDHITKWIIQaDTLLDES---------------------------- 1705
Cdd:TIGR02169  578 lplNKMRDERRDLSILSEdgVIGFAVDLVEFDPKYEPAFKYVFG-DTLVVEDieaarrlmgkyrmvtlegelfeksgamt 656
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1706 ---------------EKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQ--ISELNHRFAAIS 1768
Cdd:TIGR02169  657 ggsraprggilfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeIEQLEQEEEKLK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1769 HRIKTGKASIplKELEQFNSDIQKLLEPLEAEIQQ------GVNLKEEDFNKDMN-----------EDNEGTVKELLQRG 1831
Cdd:TIGR02169  737 ERLEELEEDL--SSLEQEIENVKSELKELEARIEEleedlhKLEEALNDLEARLShsripeiqaelSKLEEEVSRIEARL 814
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1832 DNLQQRITDERKREEI-KIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER 1910
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYlEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
                          810       820
                   ....*....|....*....|....
gi 578837834  1911 KIKEidRELQKKKEELNAVRRQAE 1934
Cdd:TIGR02169  895 EAQL--RELERKIEELEAQIEKKR 916
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
130-235 4.35e-05

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: 45.47  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  130 GLQQTNSEKiLLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVVCQQSATQRLEhAFNIARYQLG 208
Cdd:cd21313     4 AKKQTPKQR-LLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNARE-AMQQADDWLG 78
                          90       100
                  ....*....|....*....|....*..
gi 578837834  209 IEKLLDPEDVDTTYPDKKSILMYITSL 235
Cdd:cd21313    79 VPQVITPEEIIHPDVDEHSVMTYLSQF 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2475-2577 5.13e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.00  E-value: 5.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2475 FNRAWTELTDWLSLLDQVIKSQRvMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2554
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 578837834  2555 ERIQNQWDEVQEHLQNRRQQLNE 2577
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2689-2791 5.39e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 45.00  E-value: 5.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2689 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 2768
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 578837834  2769 SDDAVLLQRRLDNMNFKWSELRK 2791
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
19-114 6.31e-05

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: 44.64  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   19 KTFTKWVNAQFSKFG-KQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHA--LNNVNKALRVLQNNNVDLVNIG 95
Cdd:cd21286     3 KIYTDWANHYLAKSGhKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARGVNVQGLS 82
                          90
                  ....*....|....*....
gi 578837834   96 STDIVDGNHKLTLGLIWNI 114
Cdd:cd21286    83 AEEIRNGNLKAILGLFFSL 101
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
12-115 6.93e-05

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: 45.37  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTG-------QKLPKEKGSTRVHALNNVNKALRVL 84
Cdd:cd21330     9 EGETREERTFRNWMN---SLGVNPRVNHLYSDLSDALVIFQLYEKIKVpvdwnrvNKPPYPKLGENMKKLENCNYAVELG 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837834   85 QNN-NVDLVNIGSTDIVDGNHKLTLGLIWNII 115
Cdd:cd21330    86 KNKaKFSLVGIAGQDLNEGNRTLTLALIWQLM 117
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1665-2427 7.19e-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: 48.91  E-value: 7.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1665 SRAEEWLNLLLEYQKHMETFDQNVDHITKwiiQADTLLDESEKKKPQQkeDVLKRL-KAELNDIRPKVDSTRDQAANLMA 1743
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQ--ALLKEKrEYEGYELLKEKEALERQKEAIER 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1744 NRGDHCRKL--VEPQISELNHRFAAISHRIKTGKASI-PLKELEQFNsdIQKLLEPLEAEIQQGVnlKEEDFNKDMNEDN 1820
Cdd:TIGR02169  245 QLASLEEELekLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLR--VKEKIGELEAEIASLE--RSIAEKERELEDA 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1821 EGTVKELLQRGDNLQQRITD--------------------ERKREEIKIKQQL--LQTKHNALKDLRSQRRKKALEISHQ 1878
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEElereieeerkrrdklteeyaELKEELEDLRAELeeVDKEFAETRDELKDYREKLEKLKRE 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1879 WYQYKRQADDLLKCLDDIEKKLASLPE--PRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQ----- 1951
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeeydr 480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1952 ----LSKRWREIESKFAQFRRLNFAQIHTVREEtmMVMTEDMPLEISYVPStyLTEITHVSQALLEVEQLLNAPDLCAKD 2027
Cdd:TIGR02169  481 vekeLSKLQRELAEAEAQARASEERVRGGRAVE--EVLKASIQGVHGTVAQ--LGSVGERYATAIEVAAGNRLNNVVVED 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2028 FEDLFKQEESLKNIKdslqqsSGRIDIIHSKKTAALQSatPVERVKLQEALsqlDFQWEKVnkmykdrqgRFDRSVEKWR 2107
Cdd:TIGR02169  557 DAVAKEAIELLKRRK------AGRATFLPLNKMRDERR--DLSILSEDGVI---GFAVDLV---------EFDPKYEPAF 616
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2108 RFhydikifnqwlteaeqFLRKTQIPENWEHAKY---KWYLKELQDGIGQRQTVVrtlnaTGEEIIQQSSKTDASILQEK 2184
Cdd:TIGR02169  617 KY----------------VFGDTLVVEDIEAARRlmgKYRMVTLEGELFEKSGAM-----TGGSRAPRGGILFSRSEPAE 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2185 LGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEpgKEQQLKEKLEQVKLLVEELplrq 2264
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--EEEKLKERLEELEEDLSSL---- 749
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2265 gilkqlnetggpvlvsapispeEQDKLENKLKQTNLQwikvsralpekqGEIEAQIKDLGQLEKKLEDLEEQLNHLLlwL 2344
Cdd:TIGR02169  750 ----------------------EQEIENVKSELKELE------------ARIEELEEDLHKLEEALNDLEARLSHSR--I 793
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2345 SPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQ----PVKRKLEDLSSEWKAVNRLLQEL 2420
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqikSIEKEIENLNGKKEELEEELEEL 873

                   ....*..
gi 578837834  2421 RAKQPDL 2427
Cdd:TIGR02169  874 EAALRDL 880
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1692-2578 7.35e-05

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: 48.89  E-value: 7.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1692 TKWIIQADTL----LDESEKKKPQQKE-DVLKRLKAELNDIRPKVDSTRDQAANlmanrGDHCRKLVEPQISELNHRFAA 1766
Cdd:TIGR00606  182 TRYIKALETLrqvrQTQGQKVQEHQMElKYLKQYKEKACEIRDQITSKEAQLES-----SREIVKSYENELDPLKNRLKE 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1767 ISH-RIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNkDMNEDNEGTVKELLQRgdnlqqRITDERKRE 1845
Cdd:TIGR00606  257 IEHnLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN-DLYHNHQRTVREKERE------LVDCQRELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1846 EIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY--KRQADDLLKCLDDIE---------KKLASLPEPRDERKIKE 1914
Cdd:TIGR00606  330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARdsLIQSLATRLELDGFErgpfserqiKNFHTLVIERQEDEAKT 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1915 IDRELQKKKEELNAVRRQAEGLSED--GAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDmplE 1992
Cdd:TIGR00606  410 AAQLCADLQSKERLKQEQADEIRDEkkGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER---E 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1993 ISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDfedlfKQEESLKNIKDSLQQssgrIDIIHSKKTAALQSATPVERV 2072
Cdd:TIGR00606  487 LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD-----QEMEQLNHHTTTRTQ----MEMLTKDKMDKDEQIRKIKSR 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2073 KLQEALSQL-DFQWEKVnkmykdrqgrfdrsVEKWrrFHYDIKIFNQwlteAEQFLRKTQIPENWEHAKYKWYLKELQDG 2151
Cdd:TIGR00606  558 HSDELTSLLgYFPNKKQ--------------LEDW--LHSKSKEINQ----TRDRLAKLNKELASLEQNKNHINNELESK 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2152 IGQrqtvvrtLNATGEEIIQQSSKTDasiLQEKLGSLNLRWQEVCKQLSdrkkRLEEQKNILSEFQRDLNEfvlwleeaD 2231
Cdd:TIGR00606  618 EEQ-------LSSYEDKLFDVCGSQD---EESDLERLKEEIEKSSKQRA----MLAGATAVYSQFITQLTD--------E 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2232 NIASIPL-----EPGKE-QQLKEKLEQVKLLV-EELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIK 2304
Cdd:TIGR00606  676 NQSCCPVcqrvfQTEAElQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2305 VSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLL----LWLSPIRNQLEIYNQPNQ----EGPFDVKETEIAVQAKQ 2376
Cdd:TIGR00606  756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKlqgsDLDRTVQQVNQEKQEKQ 835
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2377 PDVEEILSKGQHLYK----EKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIgASPTQTVTLVTQPVVTK 2452
Cdd:TIGR00606  836 HELDTVVSKIELNRKliqdQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPL 914
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2453 ETAISKLEMPSSLMLEVPALADfNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQK--------ATMQDLEQRR 2524
Cdd:TIGR00606  915 ETFLEKDQQEKEELISSKETSN-KKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKetelntvnAQLEECEKHQ 993
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578837834  2525 PQLEELITAAQNLKNKTSNQEarTIITDRIER--IQNQWDEVQEHLQNRRQQLNEM 2578
Cdd:TIGR00606  994 EKINEDMRLMRQDIDTQKIQE--RWLQDNLTLrkRENELKEVEEELKQHLKEMGQM 1047
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
145-218 7.83e-05

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 43.83  E-value: 7.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   145 RQSTRNYPQVNviNFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQR-----LEHAFNIARYQLGIEKL-LDPEDV 218
Cdd:pfam11971    4 QRSLPLSPPVE--DLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLAdslynIQLLQEFCQRHLGNRCChLTLEDL 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1704-2352 8.45e-05

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: 48.90  E-value: 8.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1704 ESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMAnrgdhcrkLVEPQISELNHRFAAISHRIKTGKASipLKEL 1783
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA--------ELEEKLEELKEELESLEAELEELEAE--LEEL 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1784 EQFNSDIQKLLEPLEAEiqqgVNLKEEDFNKDMNEdnegtvkelLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKD 1863
Cdd:TIGR02168  371 ESRLEELEEQLETLRSK----VAQLELQIASLNNE---------IERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1864 LRSQRRKKaleishqwyqyKRQADDLLKCLDDIEKKLASLPEPRDE-----RKIKEIDRELQKKKEELNAVRRQAEGLSE 1938
Cdd:TIGR02168  438 LQAELEEL-----------EEELEELQEELERLEEALEELREELEEaeqalDAAERELAQLQARLDSLERLQENLEGFSE 506
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1939 DGAAMAVEPTQI-----QLSKRWrEIESKFAqfrrlnfAQIHTVREETM-MVMTEDMpleisyvpSTYLTEITHVSQALL 2012
Cdd:TIGR02168  507 GVKALLKNQSGLsgilgVLSELI-SVDEGYE-------AAIEAALGGRLqAVVVENL--------NAAKKAIAFLKQNEL 570
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2013 EVEQLLNAPDLcaKDFEDLFKQEESLKNIKDSLQQSSGRIDI---IHSKKTAALQSATPVERvkLQEAL---SQLDFQW- 2085
Cdd:TIGR02168  571 GRVTFLPLDSI--KGTEIQGNDREILKNIEGFLGVAKDLVKFdpkLRKALSYLLGGVLVVDD--LDNALelaKKLRPGYr 646
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2086 ------EKVNKMY-------KDRQGRFDRSVEkwrrfhydIKIFNQWLTEAEQFLRKTQIPenwehakykwyLKELQDGI 2152
Cdd:TIGR02168  647 ivtldgDLVRPGGvitggsaKTNSSILERRRE--------IEELEEKIEELEEKIAELEKA-----------LAELRKEL 707
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2153 GQRQTVVRTLNATGEEIIQQSSKtdasiLQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEA-D 2231
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISA-----LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeA 782
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2232 NIASIplepgkEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPE 2311
Cdd:TIGR02168  783 EIEEL------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 578837834  2312 KQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLE 2352
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1114-1882 8.70e-05

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: 48.81  E-value: 8.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1114 KIKNEAEPEfASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDfeyktpdEL 1193
Cdd:TIGR00618  187 AKKKSLHGK-AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL-------KK 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1194 QKAVEEMKRAKEEAQQKEAKVKLLTESVNsviaQAPPVAQEALKKEletlttnyqwlctrlngkcktleevwacwhells 1273
Cdd:TIGR00618  259 QQLLKQLRARIEELRAQEAVLEETQERIN----RARKAAPLAAHIK---------------------------------- 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1274 YLEKANKWLNEVEFKLKTTENipggaeEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggvmdelineelETFNSRWRE 1353
Cdd:TIGR00618  301 AVTQIEQQAQRIHTELQSKMR------SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ------------EIHIRDAHE 362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1354 lhEEAVRRqkllEQSIQSAQETEKSLHLIQESLTFIDK-QLAAYIADKVDAAQMPQEAQKI-QSDLTSHEISLEEMKKHN 1431
Cdd:TIGR00618  363 --VATSIR----EISCQQHTLTQHIHTLQQQKTTLTQKlQSLCKELDILQREQATIDTRTSaFRDLQGQLAHAKKQQELQ 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1432 QGKEAAQRVLSQiDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKmhlpalETKSVEQEVVQSQLNHCVNLYKS 1511
Cdd:TIGR00618  437 QRYAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET------RKKAVVLARLLELQEEPCPLCGS 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1512 LSEVKSEVEMVIKTG------RQIVQ--KKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVL 1583
Cdd:TIGR00618  510 CIHPNPARQDIDNPGpltrrmQRGEQtyAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1584 TEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVL-GKKETLVEDKLSllnSNWIA 1662
Cdd:TIGR00618  590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhALQLTLTQERVR---EHALS 666
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1663 VTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEK------KKPQQKEDVLKRLKAELNdirpkvdsTRD 1736
Cdd:TIGR00618  667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEThieeydREFNEIENASSSLGSDLA--------ARE 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1737 QAANLMANRGDHCRKLV-EPQISELNHRFAAISHRIKTGkasiplKELEQFNSDIQKLLEPLEAEIQQGVNLKEE--DFN 1813
Cdd:TIGR00618  739 DALNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTG------AELSHLAAEIQFFNRLREEDTHLLKTLEAEigQEI 812
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1814 KDMNEDNEGTVKELLQRGDNLQQRItDERKREEIKIKQQLLQTKHNA-LKDLRSQRRKKALEISHQWYQY 1882
Cdd:TIGR00618  813 PSDEDILNLQCETLVQEEEQFLSRL-EEKSATLGEITHQLLKYEECSkQLAQLTQEQAKIIQLSDKLNGI 881
SPEC smart00150
Spectrin repeats;
1269-1366 9.05e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 9.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   1269 HELLSYLEKANKWLNEVEFKLKTTE--NIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMD-ELINEELE 1345
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDlgKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDaEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837834   1346 TFNSRWRELHEEAVRRQKLLE 1366
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1824-2605 1.00e-04

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: 48.51  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1824 VKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLAS 1902
Cdd:TIGR02168  234 LEELREELEELQEELKEaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1903 LPEPRD--ERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAM-----AVEPTQIQLSKRWREIESKFAQFRR------- 1968
Cdd:TIGR02168  314 LERQLEelEAQLEELESKLDELAEELAELEEKLEELKEELESLeaeleELEAELEELESRLEELEEQLETLRSkvaqlel 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1969 -LNFAQIHTVREETMMVMTEDMpleisyvpstylTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQ 2047
Cdd:TIGR02168  394 qIASLNNEIERLEARLERLEDR------------RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2048 SSGRIDIIHSKKTAALQSAtpveRVKLQEALSQLDfqwekvnkMYKDRQGRFdrsvekwRRFHYDIKifnQWLTEAEQF- 2126
Cdd:TIGR02168  462 ALEELREELEEAEQALDAA----ERELAQLQARLD--------SLERLQENL-------EGFSEGVK---ALLKNQSGLs 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2127 ------LRKTQIPENWEHAKykwyLKELQDGIGQrqTVVRTLNATGEEI--IQQSSKTDASILQEKLgslnLRWQEVCKQ 2198
Cdd:TIGR02168  520 gilgvlSELISVDEGYEAAI----EAALGGRLQA--VVVENLNAAKKAIafLKQNELGRVTFLPLDS----IKGTEIQGN 589
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2199 LSDRKKRLEEQKNILSEFQRDLNEFVLWLEE-------ADNIASiplepgKEQQLKEKLEQVKLLVE--ELPLRQGILkq 2269
Cdd:TIGR02168  590 DREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDN------ALELAKKLRPGYRIVTLdgDLVRPGGVI-- 661
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2270 lneTGGPVlvsapispeeqdklenklkQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRN 2349
Cdd:TIGR02168  662 ---TGGSA-------------------KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2350 QLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQpvkRKLEDLSSEWKAVNRLLQELRAKQPDLAP 2429
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE---ERLEEAEEELAEAEAEIEELEAQIEQLKE 796
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2430 GLTTIgasptqtvtlvtqpvvtkETAISKLEMpsslmlevpALADFNRAWTELTDwlslldqviksqrvmvgDLEDINEM 2509
Cdd:TIGR02168  797 ELKAL------------------REALDELRA---------ELTLLNEEAANLRE-----------------RLESLERR 832
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2510 IIKQKATMQDLEQRRPQLEELITAAQnlKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAK 2589
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          810
                   ....*....|....*.
gi 578837834  2590 EEAEQVLGQARAKLES 2605
Cdd:TIGR02168  911 SELRRELEELREKLAQ 926
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1832-2632 1.30e-04

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: 48.13  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1832 DNLQqRITDERKreEIKIKQQLLQT---KHNALKDLRSQRRKKALEIshqwyqYKRQADDLLKCLDDIEKKLASLpeprd 1908
Cdd:TIGR02168  186 ENLD-RLEDILN--ELERQLKSLERqaeKAERYKELKAELRELELAL------LVLRLEELREELEELQEELKEA----- 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1909 ERKIKEIDRELQKKKEELNAVRRQaeglsedgaamaveptQIQLSKRWREIESKFAQFRrlnfAQIHTVREETMMVMTED 1988
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLE----------------VSELEEEIEELQKELYALA----NEISRLEQQKQILRERL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1989 MPLEISYVpstylteithvsQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQssgRIDIIHSKKTAALQSATP 2068
Cdd:TIGR02168  312 ANLERQLE------------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEE 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2069 VERV--KLQEALSQLDFQWEKVNK---MYKDRQGRFDRSVEKWRrfhydikifnqwlTEAEQFLRKTQIPEnwehakykw 2143
Cdd:TIGR02168  377 LEEQleTLRSKVAQLELQIASLNNeieRLEARLERLEDRRERLQ-------------QEIEELLKKLEEAE--------- 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2144 yLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEvcKQLSDRKKRLEEQKNILSEFQRDLNEF 2223
Cdd:TIGR02168  435 -LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL--AQLQARLDSLERLQENLEGFSEGVKAL 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2224 VLWLEEADNIA-----SIPLEPGKEQQLKEKLEQV--KLLVEEL-PLRQGILKQLNETGGPVLVSAPISPEEQDKLENKl 2295
Cdd:TIGR02168  512 LKNQSGLSGILgvlseLISVDEGYEAAIEAALGGRlqAVVVENLnAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGND- 590
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2296 kqtnlqwikvsRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIA---- 2371
Cdd:TIGR02168  591 -----------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpgg 659
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2372 VQAKQPDVEE--ILSKGQHLykeKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPV 2449
Cdd:TIGR02168  660 VITGGSAKTNssILERRREI---EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2450 VTKETAISKLEMPSSLMLEvpaLADFNRAWTELTDWLSLLDQVIKSQRVMVGDLE-DINEMIIKQKATMQDLEQRRPQLE 2528
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKE---LTELEAEIEELEERLEEAEEELAEAEAEIEELEaQIEQLKEELKALREALDELRAELT 813
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2529 ELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEHLQ-------NRRQQLNEMLKDSTQWLEAKEEAEQVLGQAR 2600
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAaTERRLEDLEEQIEELSEDIEslaaeieELEELIEELESELEALLNERASLEEALALLR 893
                          810       820       830
                   ....*....|....*....|....*....|..
gi 578837834  2601 AKLESWKEgpyTVDAIQKKITETKQLAKDLRQ 2632
Cdd:TIGR02168  894 SELEELSE---ELRELESKRSELRRELEELRE 922
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
835-1047 1.31e-04

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: 46.28  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  835 FYNQLQQLEQMTTTAENWLKiQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGpmflDADFV-- 912
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP----DAEEIqe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  913 ---AFTNHFKQVFSDVQAREKELQtifDTLPPMRYQETMSAIRTWVQQSETKLSiPQLSVTDYEIMEQRLGELQALQSSL 989
Cdd:cd00176    80 rleELNQRWEELRELAEERRQRLE---EALDLQQFFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578837834  990 QEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQM 1047
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PRK01156 PRK01156
chromosome segregation protein; Provisional
1282-1850 1.64e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.59  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1282 LNEVEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVM-DELINE---ELETFNSRWRELHEE 1357
Cdd:PRK01156  185 IDYLEEKLKSSNL---ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNlKSALNElssLEDMKNRYESEIKTA 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1358 AVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEIS---LEEMKKHNQGK 1434
Cdd:PRK01156  262 ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIikkLSVLQKDYNDY 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1435 EAAQRVLSQIDVAQKKLQDVSMKFRLFQKpaNFEQ----RLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHcvnLYK 1510
Cdd:PRK01156  342 IKKKSRYDDLNNQILELEGYEMDYNSYLK--SIESlkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE---INV 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1511 SLSEVKSEVEMVIKTGRQIVQKKQ--TENPKEL--------------DERVTALKLHYNELGAKVTERKQQLEKCLKLSR 1574
Cdd:PRK01156  417 KLQDISSKVSSLNQRIRALRENLDelSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1575 KMRKEMNVLTEWLAATDMEltkrsavegmpsNLDSEVAWGKATQKEIEKQKVHLKSITEvgealktvlgkKETLVEDKLS 1654
Cdd:PRK01156  497 EKIVDLKKRKEYLESEEIN------------KSINEYNKIESARADLEDIKIKINELKD-----------KHDKYEEIKN 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1655 LLNSNWIA-VTSRAEEWLNLLLEYQK-HMETFDQNVDHITKWIIQADTLLDESEKKKPQQK---EDVLKRLKAELNDIRP 1729
Cdd:PRK01156  554 RYKSLKLEdLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyiDKSIREIENEANNLNN 633
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1730 KVDSTRDQAANLMANRGdhcrklvepQISELNHRFAAISHRIKTgkasipLKELEQFNSDIQKLLEPLEAEIQqgvnlke 1809
Cdd:PRK01156  634 KYNEIQENKILIEKLRG---------KIDNYKKQIAEIDSIIPD------LKEITSRINDIEDNLKKSRKALD------- 691
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 578837834 1810 eDFNKDMNEdNEGTVKELLQRGDNLQQRITDERKREEIKIK 1850
Cdd:PRK01156  692 -DAKANRAR-LESTIEILRTRINELSDRINDINETLESMKK 730
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1340-2360 1.71e-04

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: 47.74  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1340 INEELETfnsRWRELHEEAVRRQKLLEQSiqsAQETEKSLHLIQESLTFIDKQLAAYiadKVDAAQMPQEAQKIQSDLTS 1419
Cdd:TIGR02168  194 ILNELER---QLKSLERQAEKAERYKELK---AELRELELALLVLRLEELREELEEL---QEELKEAEEELEELTAELQE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1420 HEISLEEMKKHNQGKEaaqrvlSQIDVAQKKLQDVSMKFrlfqkpanfeQRLQESKMILDEVKMHLPA-LETKSVEQEVV 1498
Cdd:TIGR02168  265 LEEKLEELRLEVSELE------EEIEELQKELYALANEI----------SRLEQQKQILRERLANLERqLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1499 QSQLNHcvnLYKSLSEVKSEVEMViktgrqivqkkqTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRK 1578
Cdd:TIGR02168  329 ESKLDE---LAEELAELEEKLEEL------------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1579 EMNVLTEWLAATDMELTkrsAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKsITEVGEALKTVLGKKETLVEDKLSL--- 1655
Cdd:TIGR02168  394 QIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAE-LEELEEELEELQEELERLEEALEELree 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1656 LNSNWIAVTSRAEEW------LNLLLEYQKHMETFDQNVDHITKWIIQADTLLD------ESEKKKPQQKEDVLKrlkAE 1723
Cdd:TIGR02168  470 LEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAALG---GR 546
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1724 LNDIRPKVDSTRDQAANLMA-NRGDHCRKLVEPQIS----ELNHRFAAISHRIKTGkasiPLKELEQFNSDIQKLLEPLE 1798
Cdd:TIGR02168  547 LQAVVVENLNAAKKAIAFLKqNELGRVTFLPLDSIKgteiQGNDREILKNIEGFLG----VAKDLVKFDPKLRKALSYLL 622
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1799 AEIqqgvnlkeedfnkdmnednegTVKELLQRGDNLQQRItdeRKREEIKIKQQLLQTKHNALKDLRSQRRKKALEishq 1878
Cdd:TIGR02168  623 GGV---------------------LVVDDLDNALELAKKL---RPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE---- 674
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1879 wyqYKRQADDLlkclddiekklaslpeprdERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAamaveptqiQLSKRWRE 1958
Cdd:TIGR02168  675 ---RRREIEEL-------------------EEKIEELEEKIAELEKALAELRKELEELEEELE---------QLRKELEE 723
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1959 IESKFAQFR-RLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNapdlcakdfedlfKQEES 2037
Cdd:TIGR02168  724 LSRQISALRkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-------------ELEAQ 790
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2038 LKNIKDSLQQSSGRIDIIHSKKTAalqsatpvervkLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFN 2117
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTL------------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2118 QWLTEAEQFLRKTQIP-ENW--EHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtdasiLQEKLGSLNLRWQE 2194
Cdd:TIGR02168  859 AEIEELEELIEELESElEALlnERASLEEALALLRSELEELSEELRELESKRSELRRELEE-----LREKLAQLELRLEG 933
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2195 VckqlsdrKKRLEEQKNILSEFQRDLNEFVLWLEEADniasiplePGKEQQLKEKLEQVKLLVEELplrqgilkqlnetg 2274
Cdd:TIGR02168  934 L-------EVRIDNLQERLSEEYSLTLEEAEALENKI--------EDDEEEARRRLKRLENKIKEL-------------- 984
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2275 GPVlvsapispeeqdklenklkqtNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNhlllwlSPIRNQ-LEI 2353
Cdd:TIGR02168  985 GPV---------------------NLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID------REARERfKDT 1037

                   ....*..
gi 578837834  2354 YNQPNQE 2360
Cdd:TIGR02168 1038 FDQVNEN 1044
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
140-233 1.74e-04

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: 44.00  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  140 LLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHR----PDLFDWNSvvcqQSATQRLEHAFNIARYQLGIEKLLDP 215
Cdd:cd21315    21 LLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALApglcPDWEDWDP----KDAVKNAKEAMDLAEDWLDVPQLIKP 93
                          90
                  ....*....|....*...
gi 578837834  216 EDVDTTYPDKKSILMYIT 233
Cdd:cd21315    94 EEMVNPKVDELSMMTYLS 111
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2197-2632 1.75e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2197 KQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASiplepgKEQQLKEKLEQVKLLVEELPLRQgilkqlnetggp 2276
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA------ELEELREELEKLEKLLQLLPLYQ------------ 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2277 vlvsapispeEQDKLENKLKQTNLQWikvsRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSP-IRNQLEIYN 2355
Cdd:COG4717   133 ----------ELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2356 QPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPvKRKLEDLSSEWKAVNRLLqELRAKQPDLAPGLTTIG 2435
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2436 ASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADF-NRAWTEL------------TDWLSLLDQVIKSQRVM--- 2499
Cdd:COG4717   277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeEEELEELlaalglppdlspEELLELLDRIEELQELLrea 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2500 ------------------------VGDLEDINEmIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIE 2555
Cdd:COG4717   357 eeleeelqleeleqeiaallaeagVEDEEELRA-ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2556 RIQNQWDEVQEHLQNRRQQLNE------MLKDSTQWLEAKEEAEQVLGQARAKLESWKegpyTVDAIQKKITETKQLAKD 2629
Cdd:COG4717   436 ELEEELEELEEELEELREELAEleaeleQLEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYRE 511

                  ...
gi 578837834 2630 LRQ 2632
Cdd:COG4717   512 ERL 514
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
12-124 2.42e-04

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: 43.44  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   12 EREDVQKKTFTKWVNAqfskFG-KQHIENLFSDLQDGRRLLDLLEGLT-------GQKLPKEKGSTRVHALNNVNKALRV 83
Cdd:cd21329     2 EGESSEERTFRNWMNS----LGvNPYVNHLYSDLCDALVIFQLYEMTRvpvdwghVNKPPYPALGGNMKKIENCNYAVEL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 578837834   84 LQNN-NVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVkNVM 124
Cdd:cd21329    78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL-NVL 118
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
830-933 2.50e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.08  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   830 NNIIAFYNQLQQLEQMTTTAENWLKIQPTtPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIAL-KEKGQGPMFLD 908
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*
gi 578837834   909 ADFVAFTNHFKQVFSDVQAREKELQ 933
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLE 104
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
69-115 2.65e-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: 43.59  E-value: 2.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837834   69 TRVHALNNvnkaLRVLQNNNV----------DLVNIGSTDIVDGNHKLTLGLIWNII 115
Cdd:cd21294    70 RKNKPLNN----FQMIENNNIvinsakaigcSVVNIGAGDIIEGREHLILGLIWQII 122
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
5-115 2.89e-04

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: 43.88  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834    5 EEVEDCYEREdvQKKTFTKWVNAQFSKFGK-QHI-------ENLFSDLQDGR---RLLDLLEGLT-GQKLPKEKGSTRVH 72
Cdd:cd21323    15 EGTQHSYSEE--EKVAFVNWINKALEGDPDcKHVvpmnptdESLFKSLADGIllcKMINLSQPDTiDERAINKKKLTPFT 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578837834   73 ALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNII 115
Cdd:cd21323    93 ISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
SPEC smart00150
Spectrin repeats;
1496-1567 3.24e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.70  E-value: 3.24e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578837834   1496 EVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKkQTENPKELDERVTALKLHYNELGAKVTERKQQLE 1567
Cdd:smart00150   31 ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
976-1748 3.75e-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: 46.50  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   976 EQRLGELQALQSSLQEQQSGLYYLSTT-----VKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKL 1050
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVlkenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1051 RKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETE 1130
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1131 LKELNTQWDHMCQQVYARKEALKGGLEKTVSLQK--DLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQ 1208
Cdd:pfam02463  404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEEsiELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1209 QKEAK----VKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNE 1284
Cdd:pfam02463  484 EQLELllsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1285 VEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQtlTDGGVMDELINEELETFNSRWRELHEEAVRRQKL 1364
Cdd:pfam02463  564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ--LDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1365 LEQSIQSaQETEKSLHLIQESLTFIDKQLAayIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEaaqrvLSQI 1444
Cdd:pfam02463  642 KAKESGL-RKGVSLEEGLAEKSEVKASLSE--LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK-----EELK 713
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1445 DVAQKKLQDVSMKFRLFQKPANFEQRLQESKmiLDEVKMHLPALETKSVEQEVVQSQLnhcvnlyksLSEVKSEVEMVIK 1524
Cdd:pfam02463  714 KLKLEAEELLADRVQEAQDKINEELKLLKQK--IDEEEEEEEKSRLKKEEKEEEKSEL---------SLKEKELAEEREK 782
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1525 TGRQIVQKKQTENPKELDERVTALKlhynelgAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAvegmp 1604
Cdd:pfam02463  783 TEKLKVEEEKEEKLKAQEEELRALE-------EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK----- 850
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1605 SNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETF 1684
Cdd:pfam02463  851 LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEIL 930
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837834  1685 DQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDH 1748
Cdd:pfam02463  931 LKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
3313-3359 4.03e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 40.52  E-value: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578837834 3313 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRvakgHKMHYPMVEY 3359
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
23-114 4.21e-04

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: 42.67  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   23 KWVNAQFSKFGKQH--IENLFSDLQDGRRLLDLLEGLTGQKLPKEKGStrvHALNNVNKALR---VLQnnNVDLVN---- 93
Cdd:cd21218    17 RWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPELCDKELVL---EVLSEEDLEKRaekVLQ--AAEKLGckyf 91
                          90       100
                  ....*....|....*....|.
gi 578837834   94 IGSTDIVDGNHKLTLGLIWNI 114
Cdd:cd21218    92 LTPEDIVSGNPRLNLAFVATL 112
SPEC smart00150
Spectrin repeats;
2573-2685 5.33e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 5.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2573 QQLNEMLKDSTQWLEAKEeaeqvlgqaraKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDyS 2652
Cdd:smart00150    1 QQFLRDADELEAWLEEKE-----------QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-G 68
                            90       100       110
                    ....*....|....*....|....*....|...
gi 578837834   2653 ADDTRKVHMITENINASWRSIHKRVSEREAALE 2685
Cdd:smart00150   69 HPDAEEIEERLEELNERWEELKELAEERRQKLE 101
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
3313-3358 6.45e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 40.27  E-value: 6.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578837834 3313 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVE 3358
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
SPEC smart00150
Spectrin repeats;
1162-1262 6.53e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.55  E-value: 6.53e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   1162 LQKDLSEMHEWMTQAEEeYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEaLKKELE 1241
Cdd:smart00150    3 FLRDADELEAWLEEKEQ-LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837834   1242 TLTTNYQWLCTRLNGKCKTLE 1262
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
929-1473 7.11e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  929 EKELQTIFDTLPPMRyqETMSAIRTWVQQ-SETKLSIPQLSVTdyeiMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMS 1007
Cdd:PRK03918  206 LREINEISSELPELR--EELEKLEKEVKElEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1008 KKAP---------------SEISRKYQSEFEEIEGRWKKLSSQ---LVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEvdv 1069
Cdd:PRK03918  280 EKVKelkelkekaeeyiklSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEE--- 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1070 fLKEEWPALGDSEILKKQLKQCRLLVSDIqtiqpSLNSVNEGGQKIKNEAEpefasRLETELKELNTQWDHMCQQVYARK 1149
Cdd:PRK03918  357 -LEERHELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKE-----EIEEEISKITARIGELKKEIKELK 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1150 EA---LKGGLEKTVSLQKDLSEMH--EWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSV 1224
Cdd:PRK03918  426 KAieeLKKAKGKCPVCGRELTEEHrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQL 505
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1225 IAqappvAQEALKK----ELETLTTNYQWLCTRLN---GKCKTLEEVwacwhelLSYLEKANKWLNEVEFKLKTTEnipg 1297
Cdd:PRK03918  506 KE-----LEEKLKKynleELEKKAEEYEKLKEKLIklkGEIKSLKKE-------LEKLEELKKKLAELEKKLDELE---- 569
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1298 gaEEISEVLDSLENLMRHSEDNpnqirilaqtltdggvmDELINEELETFNSRWREL---HEEAVRRQKLLEQSIQSAQE 1374
Cdd:PRK03918  570 --EELAELLKELEELGFESVEE-----------------LEERLKELEPFYNEYLELkdaEKELEREEKELKKLEEELDK 630
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1375 TEKSLHLIQESLTFIDKQLAA--YIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHnqgKEAAQRVLSQIDVAQKKLQ 1452
Cdd:PRK03918  631 AFEELAETEKRLEELRKELEEleKKYSEEEYEELREEYLELSRELAGLRAELEELEKR---REEIKKTLEKLKEELEERE 707
                         570       580
                  ....*....|....*....|.
gi 578837834 1453 DVSMKFRLFQKPANFEQRLQE 1473
Cdd:PRK03918  708 KAKKELEKLEKALERVEELRE 728
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
1668-1934 9.02e-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: 45.33  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1668 EEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDEsekkKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGD 1747
Cdd:COG5185   232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE----KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1748 hcrKLVEPQISELNHRFAAISHRIK-----TGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKE-EDFNKDMNEDN- 1820
Cdd:COG5185   308 ---KKATESLEEQLAAAEAEQELEEskretETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSEELDSFKd 384
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1821 --EGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQtkhnaLKDLRSQRRKKALEIShqwyQYKRQADDLLKCLDDIEK 1898
Cdd:COG5185   385 tiESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ-----IEELQRQIEQATSSNE----EVSKLLNELISELNKVMR 455
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578837834 1899 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAE 1934
Cdd:COG5185   456 EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIE 491
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2486-2625 9.29e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2486 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 2564
Cdd:PRK00409  497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578837834 2565 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQARaklESWKEGPYTVDAiqKKITETKQ 2625
Cdd:PRK00409  557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR---QLQKGGYASVKA--HELIEARK 614
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
905-1814 1.32e-03

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: 45.04  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   905 MFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPpmRYQETMSAIRTWVQQSETKLSIPQLSVTDYEI----MEQRLG 980
Cdd:TIGR00606  178 IFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLK--QYKEKACEIRDQITSKEAQLESSREIVKSYENeldpLKNRLK 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   981 ELQALQSSLQEQQSGLYYLSTTVKEMsKKAPSEISRK----YQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNH 1056
Cdd:TIGR00606  256 EIEHNLSKIMKLDNEIKALKSRKKQM-EKDNSELELKmekvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1057 IQTLKKWMAEvdvFLKEEWPALGDSEILKKQLKQCRLLVSDIQTiQPSLNSVNEGG---QKIKN---------EAEPEFA 1124
Cdd:TIGR00606  335 RRLLNQEKTE---LLVEQGRLQLQADRHQEHIRARDSLIQSLAT-RLELDGFERGPfseRQIKNfhtlvierqEDEAKTA 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1125 SRLETELKELNTQWDHMCQQVYARKEALKGGLE-KTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRA 1203
Cdd:TIGR00606  411 AQLCADLQSKERLKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1204 KEEA--QQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTR--LNGKCKTLEEVWACWHELLSYL---- 1275
Cdd:TIGR00606  491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKdkMDKDEQIRKIKSRHSDELTSLLgyfp 570
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1276 --EKANKWLNEVEFKLKTTEnipggaeeisEVLDSLENLMRHSEDNPNQIRILAQTLT------DGGVMDELINEELETF 1347
Cdd:TIGR00606  571 nkKQLEDWLHSKSKEINQTR----------DRLAKLNKELASLEQNKNHINNELESKEeqlssyEDKLFDVCGSQDEESD 640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1348 NSRWRELHEEAVRRQKLL-------EQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQM-PQEAQKIQSDLTS 1419
Cdd:TIGR00606  641 LERLKEEIEKSSKQRAMLagatavySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLaPDKLKSTESELKK 720
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1420 HEISLEEMKKHNQGKEAA-QRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKM--------------ILDEVKMH 1484
Cdd:TIGR00606  721 KEKRRDEMLGLAPGRQSIiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpeeesakvcltdvtIMERFQME 800
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1485 LPALEtKSVEQEVVQSQlnhCVNLYKSLSEVKSEVEMVIKTGRQIVQK---------KQTENPKELDERVTALKLHYNEL 1555
Cdd:TIGR00606  801 LKDVE-RKIAQQAAKLQ---GSDLDRTVQQVNQEKQEKQHELDTVVSKielnrkliqDQQEQIQHLKSKTNELKSEKLQI 876
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1556 GAKVTERKQQLEKCLKLSRKMRKemnVLTEWLAATDMELTKRSAVEGMPSNlDSEVAWGKATQKEIEKQKVHL--KSITE 1633
Cdd:TIGR00606  877 GTNLQRRQQFEEQLVELSTEVQS---LIREIKDAKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDikEKVKN 952
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1634 VGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVD--HITKWIIQAD-TLLDESEKKKP 1710
Cdd:TIGR00606  953 IHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqKIQERWLQDNlTLRKRENELKE 1032
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1711 ----------QQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCR--KLVEPQISELNHRFAAISHRiktgKASI 1778
Cdd:TIGR00606 1033 veeelkqhlkEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKeiKHFKKELREPQFRDAEEKYR----EMMI 1108
                          970       980       990
                   ....*....|....*....|....*....|....*.
gi 578837834  1779 PLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNK 1814
Cdd:TIGR00606 1109 VMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2292-3047 1.33e-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: 45.05  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2292 ENKLKQTNLQWIKVSRALpekqGEIEAQIKDLG-QLEK--KLEDLEEQLNHLLLWLSPIR-----NQLEIYNQPNQEGPF 2363
Cdd:TIGR02168  178 ERKLERTRENLDRLEDIL----NELERQLKSLErQAEKaeRYKELKAELRELELALLVLRleelrEELEELQEELKEAEE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2364 DVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQpvkRKLEDLSSEWKAVNRLLQELRAKQPDLapglttigasptqtvt 2443
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQ---KELYALANEISRLEQQKQILRERLANL---------------- 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2444 lvtqpvvtkETAISKLEMpsslmlevpALADFNRAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQR 2523
Cdd:TIGR02168  315 ---------ERQLEELEA---------QLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELESR 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2524 RPQLEELITAAQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLK--DSTQWLEAK---EEAEQVLGQ 2598
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIAS--LNNEIERLEARLERLEDRRERLQQEIEELLKklEEAELKELQaelEELEEELEE 451
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2599 ARAKLESWKEGPYTVDA-IQKKITETKQLAKDLRQWQTNVDVANDLaLKLLRDYSADdtrkvhmITENINASWR--SIHK 2675
Cdd:TIGR02168  452 LQEELERLEEALEELREeLEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEG-------VKALLKNQSGlsGILG 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2676 RVSER-------EAALE---------------ETHRLLQQF------------PLDL-----------------EKFLAW 2704
Cdd:TIGR02168  524 VLSELisvdegyEAAIEaalggrlqavvvenlNAAKKAIAFlkqnelgrvtflPLDSikgteiqgndreilkniEGFLGV 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2705 LTEAETT-----------------ANVLQDATRKERLL-------------------------EDSKGVKELMKQWQDLQ 2742
Cdd:TIGR02168  604 AKDLVKFdpklrkalsyllggvlvVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggsaKTNSSILERRREIEELE 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2743 GEIEAHTDVYHNLDENSQKILRSL-EGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWL 2821
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2822 QLKDDELsrqapiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLEtvRIFLTEQPLEGLEKLYQEPRE-----LPPEER 2896
Cdd:TIGR02168  764 EELEERL-------------EEAEEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEeaanlRERLES 828
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2897 AQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLE 2976
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2977 KVKALRGEIAPLKEnvsHVNDLARQLTTLGIQLspynLSTLEDLNTRWKL-LQVAV-------------EDRVRQLHEAH 3042
Cdd:TIGR02168  909 KRSELRRELEELRE---KLAQLELRLEGLEVRI----DNLQERLSEEYSLtLEEAEalenkieddeeeaRRRLKRLENKI 981

                   ....*
gi 578837834  3043 RDFGP 3047
Cdd:TIGR02168  982 KELGP 986
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2552-2767 2.11e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2552 DRIERIQNQWD---EVQEHLQNRRQQ---LNEMLKDSTQWLEAKEEAEQvLGQARAKLESWKEGpYTVDAIQKKIT---- 2621
Cdd:COG4913   225 EAADALVEHFDdleRAHEALEDAREQielLEPIRELAERYAAARERLAE-LEYLRAALRLWFAQ-RRLELLEAELEelra 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2622 ETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENInASWRSIHKRVSEREAALEE-THRLLQQFPLDLEK 2700
Cdd:COG4913   303 ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI-ERLERELEERERRRARLEAlLAALGLPLPASAEE 381
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834 2701 FLAWLTEAETTANVLQDATRK--ERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLE 2767
Cdd:COG4913   382 FAALRAEAAALLEALEEELEAleEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2160-2356 2.15e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2160 RTLNATGEEIIQQSSKTDASILQEKLGSLNlrwqevcKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIple 2239
Cdd:COG3206   152 AVANALAEAYLEQNLELRREEARKALEFLE-------EQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL--- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2240 pgkeQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDkLENKLKQTNLQWIKVS----------RAL 2309
Cdd:COG3206   222 ----SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSarytpnhpdvIAL 296
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578837834 2310 PEKQGEIEAQIKDlgQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2356
Cdd:COG3206   297 RAQIAALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEA 341
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2520-3045 2.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2520 LEQRRPQLEELITAAQNLKNKTSNQEAR-TIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQ 2598
Cdd:PRK03918  174 IKRRIERLEKFIKRTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2599 ARAKLESWKEgpytvdaIQKKITETKQLAKDLRQwqtnvdvaNDLALKLLRDYsADDTRKVHMITENINASWRSIHKRVS 2678
Cdd:PRK03918  254 KRKLEEKIRE-------LEERIEELKKEIEELEE--------KVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLS 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2679 EREAALEETHRLLQqfplDLEKflawlteaettanvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDEN 2758
Cdd:PRK03918  318 RLEEEINGIEERIK----ELEE-------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2759 SQkiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELlvwlqlkdDELSRQAPIGGDF 2838
Cdd:PRK03918  375 ER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--------KKAKGKCPVCGRE 444
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2839 PAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEqpLEGLEKLYQEPRELPPEERaqnvtrlLRKQAEEVNTEWEKL 2918
Cdd:PRK03918  445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE--LRELEKVLKKESELIKLKE-------LAEQLKELEEKLKKY 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 2919 NLhsadwqrkidETLERLRELQEATDELDLKLRQAevikgswqpvgdllIDSLQDHLEKVKALRGEIAPLKENvshVNDL 2998
Cdd:PRK03918  516 NL----------EELEKKAEEYEKLKEKLIKLKGE--------------IKSLKKELEKLEELKKKLAELEKK---LDEL 568
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 578837834 2999 ARQLTTLGIQLSPYNLSTLEDLntrwkllqvavEDRVRQLHEAHRDF 3045
Cdd:PRK03918  569 EEELAELLKELEELGFESVEEL-----------EERLKELEPFYNEY 604
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
718-1396 2.64e-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: 43.94  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   718 SEIRKRLDVDITELHSWITRSEAVLQSPEfaifrkegnfSDLKEKVNAIEREKaEKFRKLQDASRSAQALVEQMVNEgvN 797
Cdd:pfam05483   77 SRLYSKLYKEAEKIKKWKVSIEAELKQKE----------NKLQENRKIIEAQR-KAIQELQFENEKVSLKLEEEIQE--N 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   798 ADSIKQ--ASEQLNSRWIEFCQLLSERLNWLEYQNN-----IIAFYNQLQQL----EQMTTTAENW-LKIQPTTPSEPTA 865
Cdd:pfam05483  144 KDLIKEnnATRHLCNLLKETCARSAEKTKKYEYEREetrqvYMDLNNNIEKMilafEELRVQAENArLEMHFKLKEDHEK 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   866 IKSQLKICKDEVNrlsDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQ 945
Cdd:pfam05483  224 IQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   946 ETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSkkapsEISRKYQSEFEEI 1025
Cdd:pfam05483  301 IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-----ELLRTEQQRLEKN 375
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1026 EGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVS----DIQTI 1101
Cdd:pfam05483  376 EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekEIHDL 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1102 QPSLNSVNEGGQKIKNEAEpEFASRLETElKELNTQWDHMCQQV-YARKEALKGGLEKTVSLQKDLSEMHEwmTQAEEEY 1180
Cdd:pfam05483  456 EIQLTAIKTSEEHYLKEVE-DLKTELEKE-KLKNIELTAHCDKLlLENKELTQEASDMTLELKKHQEDIIN--CKKQEER 531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1181 LERDFEYKTPDELQKAvEEMKRAKEEAQQK--EAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNyqwLCTRLNGKC 1258
Cdd:pfam05483  532 MLKQIENLEEKEMNLR-DELESVREEFIQKgdEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN---LKKQIENKN 607
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1259 KTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTE-NIPGGAEEISEVLDSLEnlmrhsednpnqirilaQTLTDGGVMD 1337
Cdd:pfam05483  608 KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQ-----------------KEIEDKKISE 670
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837834  1338 ELINEELEtfnsRWRELHEEAVRRQKLLEQSIQsaqetekslHLIQESLTFIDKQLAAY 1396
Cdd:pfam05483  671 EKLLEEVE----KAKAIADEAVKLQKEIDKRCQ---------HKIAEMVALMEKHKHQY 716
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
17-114 2.66e-03

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: 40.33  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   17 QKKTFTKWVNAQFSKFG-KQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKG--STRVHALNNVNKALRVLQNNNVDLVN 93
Cdd:cd21285    11 DKQIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGINIQG 90
                          90       100
                  ....*....|....*....|.
gi 578837834   94 IGSTDIVDGNHKLTLGLIWNI 114
Cdd:cd21285    91 LSAEEIRNGNLKAILGLFFSL 111
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
3315-3357 2.72e-03

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 38.01  E-value: 2.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578837834 3315 ICKEC--PIIGFRYRSLKHFNYDICQSCffsgrVAKG-HKMHyPMV 3357
Cdd:cd02340     2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1268-1934 3.00e-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: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1268 WHELLSYLEKANKWLNEVEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRI-LAQTLTDGgvmDELINEELET 1346
Cdd:pfam05483   80 YSKLYKEAEKIKKWKVSIEAELKQKEN---KLQENRKIIEAQRKAIQELQFENEKVSLkLEEEIQEN---KDLIKENNAT 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1347 fnSRWRELHEEAVRRQKllEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQ-KIQSDLTSHEISLE 1425
Cdd:pfam05483  154 --RHLCNLLKETCARSA--EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEE 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1426 EMKKHNQGKE-AAQRVLSQIDVAQKKLQDVSmkFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNH 1504
Cdd:pfam05483  230 EYKKEINDKEkQVSLLLIQITEKENKMKDLT--FLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1505 CVNLYKSLSEvksEVEMVIKTGRQIVQKKQTENpKELDERVTALKLHYNELGAKVTerkqQLEKCLKlSRKMRKEMNvlT 1584
Cdd:pfam05483  308 SMSTQKALEE---DLQIATKTICQLTEEKEAQM-EELNKAKAAHSFVVTEFEATTC----SLEELLR-TEQQRLEKN--E 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1585 EWLAATDMELTKRSavegmpSNLDSEVAWGKATQKEIEKqkvhlksitevgeaLKTVLGKKETLVEDKlSLLNSNWIAVT 1664
Cdd:pfam05483  377 DQLKIITMELQKKS------SELEEMTKFKNNKEVELEE--------------LKKILAEDEKLLDEK-KQFEKIAEELK 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1665 SRAEEWLNLLLEYQKHMETFDQNVdhitkwiiqadTLLDESEKKKPQQKEDVLKRLKAElndirpKVDSTRDQAanlman 1744
Cdd:pfam05483  436 GKEQELIFLLQAREKEIHDLEIQL-----------TAIKTSEEHYLKEVEDLKTELEKE------KLKNIELTA------ 492
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1745 rgdHCRKLvepqiselnhrfaAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNkdMNEDNEGTV 1824
Cdd:pfam05483  493 ---HCDKL-------------LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN--LRDELESVR 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1825 KELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLP 1904
Cdd:pfam05483  555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
                          650       660       670
                   ....*....|....*....|....*....|
gi 578837834  1905 EPRDERKIKEIDRELQKKKEELNAVRRQAE 1934
Cdd:pfam05483  635 EIKVNKLELELASAKQKFEEIIDNYQKEIE 664
PTZ00121 PTZ00121
MAEBL; Provisional
1398-1934 3.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1398 ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHNQGK--EAAQRVLSQIDVAQ-------KKLQDVSmKFRLFQKPANF 1467
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVrKAEELRKAEDARkaEAARKAEEERKAEEarkaedaKKAEAVK-KAEEAKKDAEE 1241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1468 EQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQ--KKQTENPKELDE-- 1543
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeaKKKAEEAKKADEak 1321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1544 -RVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIE 1622
Cdd:PTZ00121 1322 kKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1623 KQKVHLKSITEVGEALKTVLGKKETlVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKwiiqADTLL 1702
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK 1476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1703 DESEKKKpqqKEDVLKRlKAElnDIRPKVDSTRDQAANLM----ANRGDHCRKLVEPQISElNHRFAAISHRIKTGKASI 1778
Cdd:PTZ00121 1477 KKAEEAK---KADEAKK-KAE--EAKKKADEAKKAAEAKKkadeAKKAEEAKKADEAKKAE-EAKKADEAKKAEEKKKAD 1549
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1779 PLKELEQFN--SDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQrgDNLQQRITDERKREEIKIKQQLLQT 1856
Cdd:PTZ00121 1550 ELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE--EEKKMKAEEAKKAEEAKIKAEELKK 1627
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1857 KHNALKDLRSQRRKKALEishqwyqyKRQADDLLKCLDDIEKKLASLP--EPRDERKIKEIDRELQKKKEELNAVRRQAE 1934
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEE--------KKKAEELKKAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
SPEC smart00150
Spectrin repeats;
2809-2930 3.84e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.62  E-value: 3.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   2809 RLHLSLQELLVWLQLKDDELSrQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEklyqep 2888
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 578837834   2889 relppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKID 2930
Cdd:smart00150   75 ---------------IEERLEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1125-1387 4.03e-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: 43.12  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1125 SRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDfeyktpDELQKAVEEMKRAK 1204
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE------ERLEEAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1205 EEAQQKEAKVKLLTESVNSVIAQappvaQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNE 1284
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1285 VEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDG-----GVMDEL-------------------- 1339
Cdd:TIGR02168  857 LAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEELSEElreleSKRSELrreleelreklaqlelrleg 933
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578837834  1340 ----INEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEtekSLHLIQESLT 1387
Cdd:TIGR02168  934 levrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIK 982
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
961-1547 4.42e-03

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: 43.03  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   961 KLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTtvkemskkapseisrkyQSEFEEIEGRWKKLSSQLVEHC 1040
Cdd:TIGR00618  207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-----------------KREAQEEQLKKQQLLKQLRARI 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1041 QKLEEQMNKLRKIQNHIQTLKKWMAEVDVflkeewpalgdseilKKQLKQCRllvSDIQTIQPSLnsvneggQKIKNEAE 1120
Cdd:TIGR00618  270 EELRAQEAVLEETQERINRARKAAPLAAH---------------IKAVTQIE---QQAQRIHTEL-------QSKMRSRA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1121 PEFASRLETELKELNTQwdhmcqqvyarkealkgglEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKaVEEM 1200
Cdd:TIGR00618  325 KLLMKRAAHVKQQSSIE-------------------EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH-IHTL 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1201 KRAKEEAQQKEAKVKLLTESVNSVIAQAPP--VAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKA 1278
Cdd:TIGR00618  385 QQQKTTLTQKLQSLCKELDILQREQATIDTrtSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1279 NKWLNEVEFKLKTTENIPGGAEEISEV-------LDSLENLMRHSEDNPNQIRILAQTL-TDGGVMDELINEEL---ETF 1347
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVvlarlleLQEEPCPLCGSCIHPNPARQDIDNPgPLTRRMQRGEQTYAqleTSE 544
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1348 NSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQES------LTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHE 1421
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSkedipnLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1422 ISLEEMKKHNQ-----------GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALET 1490
Cdd:TIGR00618  625 QDLQDVRLHLQqcsqelalkltALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578837834  1491 KSVEQEVVQSQLNHCVN-LYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTA 1547
Cdd:TIGR00618  705 LLRELETHIEEYDREFNeIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1041-1482 4.45e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1041 QKLEEQMNKLRKIQ--------NHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNsvnegg 1112
Cdd:COG4717    49 ERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1113 QKIKNEAEPEFASRLETELKELNTQWDhmcqQVYARKEALKGGLEKTVSLQKDLSEmhewmTQAEEEYLERDFEYKTPDE 1192
Cdd:COG4717   123 KLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELAE-----LQEELEELLEQLSLATEEE 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1193 LQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEAL-KKELETLTTNYQWLCTR-----LNGKCKTLEEVWA 1266
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAaallaLLGLGGSLLSLIL 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1267 CWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENlmrhsednpnqiRILAQTLTDGGVMDELINEELET 1346
Cdd:COG4717   274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE------------EELEELLAALGLPPDLSPEELLE 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834 1347 FNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDkQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEE 1426
Cdd:COG4717   342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE-ELRAALEQAEEYQELKEELEELEEQLEELLGELEE 420
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578837834 1427 ----------MKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVK 1482
Cdd:COG4717   421 llealdeeelEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELR 486
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
440-1141 4.65e-03

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: 43.18  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   440 EKQS-NLHRVLMDLQNqKLKELN---DWLTKTEERTRKMEEEpLGPDLEDLKRQVQQHKVLQEDL------EQEQVRVNS 509
Cdd:pfam15921  102 EKQKfYLRQSVIDLQT-KLQEMQmerDAMADIRRRESQSQED-LRNQLQNTVHELEAAKCLKEDMledsntQIEQLRKMM 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   510 LTH---------MVVVVDESSGD--HATAALEE-QLKVLGDRWANICR-------WTEDRWVLLQDILLKWQrlTEEQCL 570
Cdd:pfam15921  180 LSHegvlqeirsILVDFEEASGKkiYEHDSMSTmHFRSLGSAISKILReldteisYLKGRIFPVEDQLEALK--SESQNK 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   571 FSAWLSEKEDAVNKI---HTTGFKDQNEMLSSLQKLA-VLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEawLDN 646
Cdd:pfam15921  258 IELLLQQHQDRIEQLiseHEVEITGLTEKASSARSQAnSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSE--LRE 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   647 FARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQE-ELPPPPPQKKR--------QITVD 717
Cdd:pfam15921  336 AKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREkELSLEKEQNKRlwdrdtgnSITID 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   718 sEIRKRLDVDITElhswITRSEAVLQSpefaifRKEGNFSDLKEKVNAIE--REKAEKFRKLQDASRSAQALVEQMVNEG 795
Cdd:pfam15921  416 -HLRRELDDRNME----VQRLEALLKA------MKSECQGQMERQMAAIQgkNESLEKVSSLTAQLESTKEMLRKVVEEL 484
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   796 VNADSIKQASEQLNSrwiEFCQLLSERLNWLEYQNNIIAFYN-----QLQQLEQMTTTAENWLKIQpttpSEPTAIKSQL 870
Cdd:pfam15921  485 TAKKMTLESSERTVS---DLTASLQEKERAIEATNAEITKLRsrvdlKLQELQHLKNEGDHLRNVQ----TECEALKLQM 557
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   871 KiCKDEVnrLSDLQPQIERLkIQSIALKEKGQGPMFLDAdfvaftnhfKQVFSDVQAREKELQTIfdtlppmryqetmsa 950
Cdd:pfam15921  558 A-EKDKV--IEILRQQIENM-TQLVGQHGRTAGAMQVEK---------AQLEKEINDRRLELQEF--------------- 609
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   951 iRTWVQQSETKLSIPQLSVTDYEIMEQRL-----GELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSE--ISRKYQSEFE 1023
Cdd:pfam15921  610 -KILKDKKDAKIRELEARVSDLELEKVKLvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYevLKRNFRNKSE 688
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  1024 EIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKwmaevdvflkeewPALGDSEILKKQLKQCRLLVSDIQTIQP 1103
Cdd:pfam15921  689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK-------------VAMGMQKQITAKRGQIDALQSKIQFLEE 755
                          730       740       750
                   ....*....|....*....|....*....|....*...
gi 578837834  1104 SLNSVNEGGQKIKNEaepefASRLETELKELNTQWDHM 1141
Cdd:pfam15921  756 AMTNANKEKHFLKEE-----KNKLSQELSTVATEKNKM 788
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
560-827 5.17e-03

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: 41.28  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  560 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 639
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  640 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 719
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  720 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 799
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837834  800 SIKQASEQLNSRWIEFCQLLSERLNWLE 827
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
727-827 5.95e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 39.22  E-value: 5.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834   727 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEqmvNEGVNADSIKQASE 806
Cdd:pfam00435    9 DADDLESWIEEKEALLSSEDYG--KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 578837834   807 QLNSRWIEFCQLLSERLNWLE 827
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2164-2772 6.57e-03

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: 42.65  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2164 ATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEpgKE 2243
Cdd:TIGR00618  182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK--KQ 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2244 QQLKEKLEQVKLLVEELPlrqgILKQLNETGGPVLVSAPISPEEQdklenKLKQTNLQWIKVSRALPEKQGEIEAQIKDL 2323
Cdd:TIGR00618  260 QLLKQLRARIEELRAQEA----VLEETQERINRARKAAPLAAHIK-----AVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2324 GQLEKKLEDLEEQLNHLLLWLspiRNQLEIYNQPNQEGPFdvkeTEIAVQAKQpDVEEILSKGQHLYKEKPATQPVKRKL 2403
Cdd:TIGR00618  331 AAHVKQQSSIEEQRRLLQTLH---SQEIHIRDAHEVATSI----REISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKEL 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2404 EDLSSEWKAVNRLLQELRAKQPDLAPGLTTIgaSPTQTVTLVTQPVVTKETAISKlempsslmLEVPALADFNRAWTELT 2483
Cdd:TIGR00618  403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQ--ELQQRYAELCAAAITCTAQCEK--------LEKIHLQESAQSLKERE 472
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2484 DWLSLLDQVIKSQrvmvgdlEDINEMIIKQKATMQdlEQRRP---QLEELITAAQNLKNKTSNqeartiiTDRIERIQNQ 2560
Cdd:TIGR00618  473 QQLQTKEQIHLQE-------TRKKAVVLARLLELQ--EEPCPlcgSCIHPNPARQDIDNPGPL-------TRRMQRGEQT 536
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2561 WDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEgpytvdaiqkKITETKQLAKDLRQWQTNVDVA 2640
Cdd:TIGR00618  537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE----------DIPNLQNITVRLQDLTEKLSEA 606
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837834  2641 NDLALKLLRDYSADDTRKVHMitENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATR 2720
Cdd:TIGR00618  607 EDMLACEQHALLRKLQPEQDL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK 684
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578837834  2721 KERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRS----LEGSDDA 2772
Cdd:TIGR00618  685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSlgsdLAAREDA 740
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH