|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-518 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 932.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 1 MLYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFG 80
Cdd:MTH00184 2 SLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 81 NWFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSIL 160
Cdd:MTH00184 82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 161 GSMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 240
Cdd:MTH00184 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 241 HPEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIK 320
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 321 IFSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGK 400
Cdd:MTH00184 322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 401 ITGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVRE 480
Cdd:MTH00184 402 ITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVRE 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 63025108 481 IKFVGWTNDSGHYPSLEWVQASPPAHHTYNELPFVYKI 518
Cdd:MTH00184 482 IKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
11-498 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 916.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 11 TNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWFVPLYIGA 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 91 PDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNFITTIF 170
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 171 NMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILP 250
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 251 GFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIATVVG 330
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 331 GSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCYNEVL 410
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 411 GKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKFVGWTNDS 490
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 63025108 491 GHypSLEW 498
Cdd:cd01663 481 ST--SLEW 486
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-509 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 638.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 8 LYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPvMIGGFGNWFVPLY 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 88 IGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNFIT 167
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 168 TIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 247
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 248 ILPGFGIVSQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIAT 327
Cdd:TIGR02891 240 FLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 328 VVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCYN 407
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 408 EVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDY--HDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKFvg 485
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA-- 476
|
490 500
....*....|....*....|....
gi 63025108 486 wTNDSGHYPSLEWVQASPPAHHTY 509
Cdd:TIGR02891 477 -GANPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-516 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 636.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 4 LTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPvMIGGFGNWF 83
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 84 VPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSM 163
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 164 NFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 243
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 244 VYILILPGFGIVSQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFS 323
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 324 WIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITG 403
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 404 YCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDY--HDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREI 481
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500 510
....*....|....*....|....*....|....*
gi 63025108 482 KFvgwTNDSGHYPSLEWVQASPPAHHTYNELPFVY 516
Cdd:COG0843 484 KA---GGNPWGARTLEWATPSPPPLYNFASIPVVR 515
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-461 |
1.31e-150 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 437.77 E-value: 1.31e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 15 DIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPvMIGGFGNWFVPLYIGAPDMA 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 95 FPRLNNISFWVLPPSLILLLGSAfveQGVGAGWTVYPPLssvqahsgGSVDAAIFSLHLAGISSILGSMNFITTIFNMRA 174
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 175 PGITMdRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGI 254
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 255 VSQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIATVVGGSLR 334
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 335 -TDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCYNEVLGKI 413
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 63025108 414 HFWLMFIGVNITFFPQHFLGLAGLPRRYS----DYHDSFAGWNQISSVGSLI 461
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-518 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 932.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 1 MLYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFG 80
Cdd:MTH00184 2 SLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 81 NWFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSIL 160
Cdd:MTH00184 82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 161 GSMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 240
Cdd:MTH00184 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 241 HPEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIK 320
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 321 IFSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGK 400
Cdd:MTH00184 322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 401 ITGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVRE 480
Cdd:MTH00184 402 ITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVRE 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 63025108 481 IKFVGWTNDSGHYPSLEWVQASPPAHHTYNELPFVYKI 518
Cdd:MTH00184 482 IKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
11-498 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 916.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 11 TNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWFVPLYIGA 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 91 PDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNFITTIF 170
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 171 NMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILP 250
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 251 GFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIATVVG 330
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 331 GSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCYNEVL 410
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 411 GKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKFVGWTNDS 490
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 63025108 491 GHypSLEW 498
Cdd:cd01663 481 ST--SLEW 486
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
4-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 897.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 4 LTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWF 83
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 84 VPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSM 163
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 164 NFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 244 VYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFS 323
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 324 WIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITG 403
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 404 YCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKF 483
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|....
gi 63025108 484 VGWTNDSghyPSLEWVQASPPAHHTYNELPFVYK 517
Cdd:MTH00153 481 LFSLNLS---SSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-520 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 879.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 2 LYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGN 81
Cdd:MTH00182 3 LYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 82 WFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILG 161
Cdd:MTH00182 83 WLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 162 SMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 241
Cdd:MTH00182 163 AINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 242 PEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKI 321
Cdd:MTH00182 243 PEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 322 FSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKI 401
Cdd:MTH00182 323 FSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 402 TGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREI 481
Cdd:MTH00182 403 TGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREE 482
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 63025108 482 KFVGWTNDSG-HYPSLEWVQASPPAHHTYNELPFVYKISN 520
Cdd:MTH00182 483 KFIGWKEGTGeSWASLEWVHSSPPLFHTYNELPFVYKSKL 522
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
2-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 850.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 2 LYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGN 81
Cdd:MTH00167 1 MWINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 82 WFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILG 161
Cdd:MTH00167 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 162 SMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 241
Cdd:MTH00167 161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 242 PEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKI 321
Cdd:MTH00167 241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 322 FSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKI 401
Cdd:MTH00167 321 FSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 402 TGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREI 481
Cdd:MTH00167 401 TGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....
gi 63025108 482 KFVGWTNDSGhypSLEWVQASPPAHHTYNELPFV 515
Cdd:MTH00167 481 KLLPVELTST---NVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
6-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 833.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 6 RWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWFVP 85
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 86 LYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNF 165
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 166 ITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 245
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 246 ILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWI 325
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 326 ATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYC 405
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 406 YNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKFVG 485
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500 510
....*....|....*....|....*....|..
gi 63025108 486 WTNDSGhypSLEWVQASPPAHHTYNELPFVYK 517
Cdd:MTH00223 482 SGHLST---SLEWDNLLPADFHNNSETGALVI 510
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 824.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 2 LYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGN 81
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 82 WFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILG 161
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 162 SMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 241
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 242 PEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKI 321
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 322 FSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKI 401
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 402 TGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREI 481
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....*
gi 63025108 482 KFVGWTNDSGHypsLEWVQASPPAHHTYNELPFVY 516
Cdd:MTH00116 481 KVLQPELTTTN---IEWIHGCPPPYHTFEEPAFVQ 512
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
4-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 795.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 4 LTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWF 83
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 84 VPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSM 163
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 164 NFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 244 VYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFS 323
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 324 WIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITG 403
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 404 YCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYV--REI 481
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVsqRLV 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 63025108 482 KFVGWTNDsghypSLEWVQASPPAHHTYNELPFVYK 517
Cdd:MTH00142 481 MWSSHLST-----SLEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-520 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 746.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 2 LYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGN 81
Cdd:MTH00037 1 MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 82 WFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILG 161
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 162 SMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 241
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 242 PEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKI 321
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 322 FSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKI 401
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 402 TGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREi 481
Cdd:MTH00037 401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQ- 479
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 63025108 482 KFVGWTNDSGHypSLEWVQAS-PPAHHTYNELPFVYKISN 520
Cdd:MTH00037 480 REVISPEFSSS--SLEWQYSSfPPSHHTFDETPSTVILIK 517
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
4-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 733.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 4 LTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWF 83
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 84 VPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSM 163
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 164 NFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 244 VYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFS 323
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 324 WIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITG 403
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 404 YCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYV--REI 481
Cdd:MTH00183 403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAakREV 482
|
490 500 510
....*....|....*....|....*....|....
gi 63025108 482 KFVGWTndsghYPSLEWVQASPPAHHTYNELPFV 515
Cdd:MTH00183 483 LSVELT-----STNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
2-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 721.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 2 LYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGN 81
Cdd:MTH00103 1 MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 82 WFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILG 161
Cdd:MTH00103 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 162 SMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 241
Cdd:MTH00103 161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 242 PEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKI 321
Cdd:MTH00103 241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 322 FSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKI 401
Cdd:MTH00103 321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 402 TGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYV--R 479
Cdd:MTH00103 401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFAskR 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 63025108 480 EIKFVGWTNdsghyPSLEWVQASPPAHHTYNELPFV 515
Cdd:MTH00103 481 EVLTVELTT-----TNLEWLHGCPPPYHTFEEPTYV 511
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 719.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 1 MLYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFG 80
Cdd:MTH00026 1 MTSFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 81 NWFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSIL 160
Cdd:MTH00026 81 NWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 161 GSMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 240
Cdd:MTH00026 161 GAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 241 HPEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIK 320
Cdd:MTH00026 241 HPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 321 IFSWIATVVGG--SLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWF 398
Cdd:MTH00026 321 IFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 399 GKITGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYV 478
Cdd:MTH00026 401 GKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 63025108 479 REIKF----------VGWTNDSGHYPSLEWVQASPPAHHTYNELPFV 515
Cdd:MTH00026 481 REEPFdinimakgplIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYI 527
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
2-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 714.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 2 LYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGN 81
Cdd:MTH00077 1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 82 WFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILG 161
Cdd:MTH00077 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 162 SMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 241
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 242 PEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKI 321
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 322 FSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKI 401
Cdd:MTH00077 321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 402 TGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREI 481
Cdd:MTH00077 401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 63025108 482 KFVGWTNDSghyPSLEWVQASPPAHHTYNELPFVYK 517
Cdd:MTH00077 481 EVLTTELTS---TNIEWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
6-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 700.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 6 RWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWFVP 85
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 86 LYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNF 165
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 166 ITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 245
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 246 ILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWI 325
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 326 ATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYC 405
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 406 YNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKFVG 485
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*..
gi 63025108 486 wtndSGHYP-SLEWVQASPPAHHTYNE 511
Cdd:MTH00007 482 ----SPHMSsSLEWQDTLPLDFHNLPE 504
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
3-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 670.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 3 YLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNW 82
Cdd:MTH00079 3 GLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 83 FVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSvQAHSGGSVDAAIFSLHLAGISSILGS 162
Cdd:MTH00079 83 MLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 163 MNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 242
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 243 EVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIF 322
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 323 SWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKIT 402
Cdd:MTH00079 322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 403 GYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREiK 482
Cdd:MTH00079 402 GIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSY-R 480
|
490 500
....*....|....*....|....*....
gi 63025108 483 FVGWTNDSGHYPslEWVQASPPAHHTYNE 511
Cdd:MTH00079 481 LVLHDNYINSSP--EYSLSSYVFGHSYQS 507
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
13-477 |
0e+00 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 639.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 13 HKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFGNWFVPLyIGAPD 92
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 93 MAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNFITTIFNM 172
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 173 RAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 252
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 253 GIVSQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIATVVGGS 332
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 333 LRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCYNEVLGK 412
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63025108 413 IHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAY 477
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-509 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 638.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 8 LYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPvMIGGFGNWFVPLY 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 88 IGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNFIT 167
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 168 TIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 247
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 248 ILPGFGIVSQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIAT 327
Cdd:TIGR02891 240 FLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 328 VVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCYN 407
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 408 EVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDY--HDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKFvg 485
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA-- 476
|
490 500
....*....|....*....|....
gi 63025108 486 wTNDSGHYPSLEWVQASPPAHHTY 509
Cdd:TIGR02891 477 -GANPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-516 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 636.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 4 LTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPvMIGGFGNWF 83
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 84 VPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSM 163
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 164 NFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 243
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 244 VYILILPGFGIVSQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFS 323
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 324 WIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITG 403
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 404 YCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDY--HDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREI 481
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500 510
....*....|....*....|....*....|....*
gi 63025108 482 KFvgwTNDSGHYPSLEWVQASPPAHHTYNELPFVY 516
Cdd:COG0843 484 KA---GGNPWGARTLEWATPSPPPLYNFASIPVVR 515
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-507 |
0e+00 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 561.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 7 WLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGgFGNWFVPL 86
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 87 YIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNFI 166
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 167 TTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYI 246
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 247 LILPGFGIVSQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIA 326
Cdd:cd01662 240 LILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 327 TVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCY 406
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 407 NEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDY--HDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVREIKFV 484
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlpGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDA 478
|
490 500
....*....|....*....|...
gi 63025108 485 gwTNDSGHYPSLEWVQASPPAHH 507
Cdd:cd01662 479 --TGDPWGARTLEWATSSPPPAY 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 520.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 1 MLYLTRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGGFG 80
Cdd:MTH00048 1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 81 NWFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVeqGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSIL 160
Cdd:MTH00048 81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 161 GSMNFITTIFNMRAPGITMdRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 240
Cdd:MTH00048 159 GSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 241 HPEVYILILPGFGIVSQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIK 320
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 321 IFSWIATVVGGSLRTDTPML-WALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFG 399
Cdd:MTH00048 318 VFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 400 KITGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSFAGWNQISSVGSLISIVSVMVFLYLVYDAYVR 479
Cdd:MTH00048 398 LITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVV 477
|
490 500
....*....|....*....|....*....
gi 63025108 480 EIKFVGWTNDSGhypSLEWVQASPPAHHT 508
Cdd:MTH00048 478 KNEVLGLWGSSS---CVVNVLMSPVPYHN 503
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-461 |
1.31e-150 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 437.77 E-value: 1.31e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 15 DIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPvMIGGFGNWFVPLYIGAPDMA 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 95 FPRLNNISFWVLPPSLILLLGSAfveQGVGAGWTVYPPLssvqahsgGSVDAAIFSLHLAGISSILGSMNFITTIFNMRA 174
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 175 PGITMdRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGI 254
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 255 VSQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIATVVGGSLR 334
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 335 -TDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCYNEVLGKI 413
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 63025108 414 HFWLMFIGVNITFFPQHFLGLAGLPRRYS----DYHDSFAGWNQISSVGSLI 461
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
5-515 |
2.00e-139 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 416.77 E-value: 2.00e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 5 TRWLYSTNHKDIGTLYLLFGAFsgMIGTGFS--FLIRLE--LSAPGSM--LGDDHlYNVIITAHGLIMIFFLVMPVMIGG 78
Cdd:TIGR02843 45 NEWLTTVDHKKIGIMYIIVALV--MLLRGFAdaIMMRTQqaLASGGSAgyLPPHH-YDQIFTAHGVIMIFFVAMPFVFGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 79 FgNWFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISS 158
Cdd:TIGR02843 122 M-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 159 ILGSMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWF 238
Cdd:TIGR02843 201 LLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 239 FGHPEVYILILPGFGIVSQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTG 318
Cdd:TIGR02843 281 WGHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 319 IKIFSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWF 398
Cdd:TIGR02843 360 VKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWF 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 399 GKITGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHD-SFAGWNQISSVGSLISIVSVMVFLYLVYDAY 477
Cdd:TIGR02843 440 PKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSI 519
|
490 500 510
....*....|....*....|....*....|....*...
gi 63025108 478 VREIKFVGWTNDSGHYPSLEWVQASPPAHHTYNELPFV 515
Cdd:TIGR02843 520 RDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKV 557
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
7-515 |
1.36e-132 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 399.23 E-value: 1.36e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 7 WLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGgFGNWFVPL 86
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 87 YIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILGSMNFI 166
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 167 TTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYI 246
Cdd:TIGR02882 203 VTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 247 LILPGFGIVSQIIPTFaAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKIFSWIA 326
Cdd:TIGR02882 283 VILPAFGIYSEIISTF-AQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 327 TVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKITGYCY 406
Cdd:TIGR02882 362 TLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 407 NEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHDSfAGW---NQISSVGSLISIVSVMVFLYLVYDAYVREIKF 483
Cdd:TIGR02882 442 NERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPS-DGWfplNLISTIGALLMAIGFIFLVYNIYYSHRKSPRE 520
|
490 500 510
....*....|....*....|....*....|..
gi 63025108 484 VGWTNDSGHypSLEWVQASPPAHHTYNELPFV 515
Cdd:TIGR02882 521 ATGDPWNGR--TLEWATASPPPKYNFAVTPDV 550
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-517 |
3.00e-120 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 368.11 E-value: 3.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 5 TRWLYSTNHKDIGTLYLLFGAFSGMIGTGFSFLIRLE---LSAPGSMLGDDHLYNVIITAHGLIMIFFLVMPVMIGgFGN 81
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 82 WFVPLYIGAPDMAFPRLNNISFWVLPPSLILLLGSAFVEQGVGAGWTVYPPLSSVQAHSGGSVDAAIFSLHLAGISSILG 161
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 162 SMNFITTIFNMRAPGITMDRLPLFVWSILVTTYLLILSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 241
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 242 PEVYILILPGFGIVSQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDSRAYFSAATMIIAVPTGIKI 321
Cdd:PRK15017 285 PEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 322 FSWIATVVGGSLRTDTPMLWALGFVFLFTVGGLTGIVLACSSLDVLLHDTYYVVAHFHYVLSMGAVFALFGGFYYWFGKI 401
Cdd:PRK15017 364 FNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 402 TGYCYNEVLGKIHFWLMFIGVNITFFPQHFLGLAGLPRRYSDYHD-SFAGWNQISSVGSLISIVSVMVFLYLVYDAYVRE 480
Cdd:PRK15017 444 FGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDR 523
|
490 500 510
....*....|....*....|....*....|....*..
gi 63025108 481 IKFVGWTNDSGHYPSLEWVQASPPAHHTYNELPFVYK 517
Cdd:PRK15017 524 DQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
18-475 |
5.23e-25 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 107.76 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 18 TLYLLFGAFsgMIGTGFSFLIRLELSAPGSMLGDDHLYNVIITAHGLIMIFFLVMpVMIGGFGNWFVPLYIGAPDMAfPR 97
Cdd:cd01660 9 HFVVAFLAL--LLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 98 LNNISFWVLPPSLIL-----LLGSAFVEqgvgagWTVYPPLssvQAHSGGSVDAAIFSLHlagiSSILGSMNFITT-IFN 171
Cdd:cd01660 85 LAWAGFWLMVIGTVMaavpiLLGQASVL------YTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLwRWK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 172 MRAPGitmDRLPLFVWSILVTTYL-LILSLPVLAGAITMLLTDRNFNTTffdpagGGDPILFQHLFWFFGHPEVYILILP 250
Cdd:cd01660 152 KANPG---KKVPLATFMVVTTMILwLVASLGVALEVLFQLLPWSLGLVD------TVDVLLSRTLFWWFGHPLVYFWLLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 251 GFGIVSQIIPTFAAKKQIFGYLGMVyAMVSIGILGFIVWAHHMFT-VGMDVDSRAYFSAATMIIAVPTGIKIFSWIATV- 328
Cdd:cd01660 223 AYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLe 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 329 VGGSLRT-------------DTPMLWALGFVFL-FTVGGLTGIVLACSSLDVLLHDTYYVVAHFHyvLSMGAVFAL--FG 392
Cdd:cd01660 302 IAGRLRGgkglfgwiralpwGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALtfMA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025108 393 GFYYWFGKITGYCYNEV-LGKIHFWLMFIGVNITFFPQHFLGLAGLPRR-------YSDYHDSFAGWNQISSVGSLISIV 464
Cdd:cd01660 380 VAYWLVPHLTGRELAAKrLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaeaqygGLPAAGEWAPYQQLMAIGGTILFV 459
|
490
....*....|.
gi 63025108 465 SVMVFLYLVYD 475
Cdd:cd01660 460 SGALFLYILFR 470
|
|
| |
