|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 567.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
250 260
....*....|....*....|....*....
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELPLLTN 269
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-252 |
5.28e-165 |
|
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: 466.19 E-value: 5.28e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd01663 236 ILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:cd01663 316 ATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLS 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:cd01663 396 YNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
|
250
....*....|...
gi 1836280632 241 -PMQLSSSIEWLQ 252
Cdd:cd01663 476 nVGEGSTSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-268 |
8.22e-100 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 301.66 E-value: 8.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQV 238
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
250 260 270
....*....|....*....|....*....|.
gi 1836280632 239 -IYPMQlSSSIEWLQNTPPAEHSYSELPLLT 268
Cdd:COG0843 486 gGNPWG-ARTLEWATPSPPPLYNFASIPVVR 515
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-261 |
2.40e-96 |
|
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: 291.43 E-value: 2.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:TIGR02891 317 ATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQV 238
Cdd:TIGR02891 397 YNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476
|
250 260
....*....|....*....|...
gi 1836280632 239 IYPMQLSSSIEWLQNTPPAEHSY 261
Cdd:TIGR02891 477 GANPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-216 |
2.00e-68 |
|
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: 217.83 E-value: 2.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:pfam00115 213 ILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLN-YSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 159
Cdd:pfam00115 292 ATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGR 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836280632 160 VLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSSI 216
Cdd:pfam00115 372 MYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 567.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
250 260
....*....|....*....|....*....
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELPLLTN 269
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-252 |
5.28e-165 |
|
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: 466.19 E-value: 5.28e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd01663 236 ILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:cd01663 316 ATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLS 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:cd01663 396 YNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
|
250
....*....|...
gi 1836280632 241 -PMQLSSSIEWLQ 252
Cdd:cd01663 476 nVGEGSTSLEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-267 |
2.83e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 452.59 E-value: 2.83e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00167 245 ILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00167 325 ATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00167 405 LNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLP 484
|
250 260
....*....|....*....|....*..
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELPLL 267
Cdd:MTH00167 485 VELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-265 |
1.92e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 450.20 E-value: 1.92e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
250 260
....*....|....*....|....*
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELP 265
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
7.56e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 448.79 E-value: 7.56e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00142 243 ILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00142 323 ATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLT 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00142 403 LNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMW 482
|
250 260
....*....|....*....|....*....
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELPLLTN 269
Cdd:MTH00142 483 SSHLSTSLEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
2.11e-157 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 448.00 E-value: 2.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00116 325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00116 405 LHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQ 484
|
250 260
....*....|....*....|....*....
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELPLLTN 269
Cdd:MTH00116 485 PELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-266 |
1.93e-139 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 402.29 E-value: 1.93e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
|
250 260
....*....|....*....|....*..
gi 1836280632 241 PMQLSSSIEWLQNT-PPAEHSYSELPL 266
Cdd:MTH00037 485 PEFSSSSLEWQYSSfPPSHHTFDETPS 511
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-263 |
6.25e-139 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 400.80 E-value: 6.25e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00103 325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00103 405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
|
250 260
....*....|....*....|...
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSE 263
Cdd:MTH00103 485 VELTTTNLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-263 |
3.43e-136 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 393.90 E-value: 3.43e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
250 260
....*....|....*....|...
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSE 263
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
2.62e-134 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 389.30 E-value: 2.62e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00077 245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00077 325 ATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00077 405 LHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLT 484
|
250 260
....*....|....*....|....*....
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELPLLTN 269
Cdd:MTH00077 485 TELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-268 |
7.84e-134 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 387.72 E-value: 7.84e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
250 260
....*....|....*....|....*...
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSELPLLT 268
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIIT 509
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-267 |
9.53e-120 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 352.20 E-value: 9.53e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVI- 239
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIg 486
|
250 260 270
....*....|....*....|....*....|.
gi 1836280632 240 ---YPMQLSSSIEWLQNTPPAEHSYSELPLL 267
Cdd:MTH00182 487 wkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-263 |
1.54e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 346.28 E-value: 1.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00079 245 ILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00079 325 ATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00079 405 YDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLH 484
|
250 260
....*....|....*....|...
gi 1836280632 241 PMQLSSSIEWLQNTPPAEHSYSE 263
Cdd:MTH00079 485 DNYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-267 |
9.18e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 339.50 E-value: 9.18e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVIY 240
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVG 486
|
250 260 270
....*....|....*....|....*....|
gi 1836280632 241 PMQLS---SSIEWLQNTPPAEHSYSELPLL 267
Cdd:MTH00184 487 WVEDSghyPSLEWAQTSPPAHHTYNELPYV 516
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-232 |
9.09e-107 |
|
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: 317.17 E-value: 9.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd00919 233 ILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:cd00919 312 ATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRM 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESL 232
Cdd:cd00919 392 LSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-268 |
8.22e-100 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 301.66 E-value: 8.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQV 238
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
250 260 270
....*....|....*....|....*....|.
gi 1836280632 239 -IYPMQlSSSIEWLQNTPPAEHSYSELPLLT 268
Cdd:COG0843 486 gGNPWG-ARTLEWATPSPPPLYNFASIPVVR 515
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-261 |
2.40e-96 |
|
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: 291.43 E-value: 2.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:TIGR02891 317 ATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQV 238
Cdd:TIGR02891 397 YNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476
|
250 260
....*....|....*....|...
gi 1836280632 239 IYPMQLSSSIEWLQNTPPAEHSY 261
Cdd:TIGR02891 477 GANPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-267 |
3.26e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 282.29 E-value: 3.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLN--YSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTG 158
Cdd:MTH00026 326 ATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 159 LVLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESL------ 232
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyreepf 485
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1836280632 233 ---VTQRQVIYPMQLS----SSIEWLQNTPPAEHSYSELPLL 267
Cdd:MTH00026 486 dinIMAKGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-260 |
2.52e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 271.55 E-value: 2.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00048 243 VLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYS-PAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 159
Cdd:MTH00048 323 YMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 160 VLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQVI 239
Cdd:MTH00048 403 SLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
250 260
....*....|....*....|.
gi 1836280632 240 YPMQLSSSIEWLQNTPPAEHS 260
Cdd:MTH00048 483 GLWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-261 |
2.31e-87 |
|
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: 268.68 E-value: 2.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd01662 239 ILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQRQV 238
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRD 477
|
250 260
....*....|....*....|....*
gi 1836280632 239 IY--PMQlSSSIEWLQNTPPAEHSY 261
Cdd:cd01662 478 ATgdPWG-ARTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-216 |
2.00e-68 |
|
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: 217.83 E-value: 2.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:pfam00115 213 ILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLN-YSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 159
Cdd:pfam00115 292 ATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGR 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836280632 160 VLNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSSI 216
Cdd:pfam00115 372 MYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-265 |
1.52e-58 |
|
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: 197.00 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESgKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:TIGR02882 282 IVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSTIGSSISLLGILFFLF-IIWESLVTQRQ 237
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPRE 520
|
250 260
....*....|....*....|....*...
gi 1836280632 238 VIYPMQLSSSIEWLQNTPPAEHSYSELP 265
Cdd:TIGR02882 521 ATGDPWNGRTLEWATASPPPKYNFAVTP 548
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-265 |
4.05e-53 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 182.83 E-value: 4.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 1 ILILPGFGMISHIISQESgKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:PRK15017 289 ILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 81 ATLHGTQLNYSPAMLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLV 160
Cdd:PRK15017 368 FTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFK 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 161 LNPKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTTWNVVSTIGSSISLLGILFFLFIIWESLVTQ---R 236
Cdd:PRK15017 448 LNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRdqnR 527
|
250 260
....*....|....*....|....*....
gi 1836280632 237 QVIYPMQLSSSIEWLQNTPPAEHSYSELP 265
Cdd:PRK15017 528 DLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
65-233 |
4.54e-14 |
|
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: 71.55 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 65 TMIIAVPTGIKIFSWLATL-------HG-------TQLNYSPAMLWALGFVFL-FTVGGLTGVVLANSSVDIILHDTYYV 129
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeiagrlrGGkglfgwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836280632 130 VAHFHyvLSMGAVFAIMA-GFVHWY-PLFTGLVLNPKWLKS-QFIIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY- 203
Cdd:cd01660 362 PGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPa 439
|
170 180 190
....*....|....*....|....*....|....
gi 1836280632 204 ----TTWNVVSTIGSSISLLGILFFLFIIWESLV 233
Cdd:cd01660 440 agewAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
|
|
|