|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 874.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00153 26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKET 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00153 266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00153 346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00153 426 QHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHS 502
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-469 |
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: 754.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:cd01663 19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:cd01663 99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:cd01663 179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:cd01663 259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:cd01663 339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLN-MPSSIEWLQ 469
Cdd:cd01663 419 QHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-432 |
1.37e-167 |
|
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: 481.72 E-value: 1.37e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:TIGR02891 22 LVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeT 240
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-I 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:TIGR02891 340 FVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFP 419
|
410 420 430
....*....|....*....|....*....|....
gi 669633588 401 QHFLGLSGMPRRYSDYPDS--FTSWNIISSFGSY 432
Cdd:TIGR02891 420 MHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-432 |
4.95e-165 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 476.54 E-value: 4.95e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeT 240
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-L 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:COG0843 269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:COG0843 349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428
|
410 420 430
....*....|....*....|....*....|....
gi 669633588 401 QHFLGLSGMPRRYSDYP--DSFTSWNIISSFGSY 432
Cdd:COG0843 429 MHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-432 |
6.78e-116 |
|
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: 347.25 E-value: 6.78e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMiveNGAGTGWTIYPPLSSnaihssssVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFdQMPLFIWA 160
Cdd:pfam00115 94 GAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeT 240
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMN-YSPSILWSLGFVF 319
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 320 LFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFF 399
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 669633588 400 PQHFLGLSGMPRRYS----DYPDSFTSWNIISSFGSY 432
Cdd:pfam00115 395 PMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 874.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00153 26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKET 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00153 266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00153 346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00153 426 QHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHS 502
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-469 |
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: 754.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:cd01663 19 LVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:cd01663 99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:cd01663 179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:cd01663 259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:cd01663 339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLN-MPSSIEWLQ 469
Cdd:cd01663 419 QHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 716.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00167 28 MVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00167 108 SLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00167 188 ILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00167 268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00167 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFP 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00167 428 QHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHT 504
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 712.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00142 26 MVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00142 106 ALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00142 186 VKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00142 266 FGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00142 346 FTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFP 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00142 426 QHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHT 502
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 710.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00223 25 LVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00223 105 SLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00223 185 VKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00223 265 FGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00223 345 FTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFP 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00223 425 QHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHN 501
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 708.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00116 28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00116 108 SFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00116 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00116 268 FGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00116 348 FTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFP 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00116 428 QHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHT 504
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 649.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00103 28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00103 108 SFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00103 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00103 268 FGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00103 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFP 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00103 428 QHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHT 504
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 643.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00007 25 LLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00007 105 ALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00007 185 VVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00007 265 FGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00007 345 FTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFP 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00007 425 QHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHN 501
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 638.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00183 28 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00183 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00183 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00183 268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00183 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFP 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00183 428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHT 504
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 631.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00077 28 MVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00077 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00077 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00077 268 FGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00077 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFP 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00077 428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHT 504
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 629.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00037 28 MVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00037 108 SFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00037 188 VFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00037 268 FGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00037 348 FTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFP 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEW-LQNLPPSEHS 477
Cdd:MTH00037 428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWqYSSFPPSHHT 505
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 588.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00182 30 MIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00182 110 ALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00182 190 ILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00182 270 FGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00182 350 FTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFP 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMP----SSIEWLQNLPPSEH 476
Cdd:MTH00182 430 QHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTgeswASLEWVHSSPPLFH 509
|
.
gi 669633588 477 S 477
Cdd:MTH00182 510 T 510
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 583.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00079 29 MVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSsVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00079 109 SLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSS-VDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00079 188 VFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00079 268 FGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00079 348 FTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFP 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00079 428 LHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHS 504
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 581.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:MTH00184 30 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:MTH00184 110 ALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKET 240
Cdd:MTH00184 190 ILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:MTH00184 270 FGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00184 350 FTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFP 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRII---MFSLNMPSSIEWLQNLPPSEHS 477
Cdd:MTH00184 430 QHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHYPSLEWAQTSPPAHHT 509
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-432 |
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: 514.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:cd00919 17 LLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:cd00919 96 GLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeT 240
Cdd:cd00919 176 VLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-L 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:cd00919 255 FGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:cd00919 335 FTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFP 414
|
410 420 430
....*....|....*....|....*....|..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSY 432
Cdd:cd00919 415 MHFLGLLGMPRRYADYPDGFAPWNFISSVGAF 446
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
2-431 |
4.18e-180 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 514.95 E-value: 4.18e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 2 LGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 81
Cdd:MTH00026 30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 82 LTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWAV 161
Cdd:MTH00026 110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 162 GITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKETF 241
Cdd:MTH00026 190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 242 GCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMN--YSPSILWSLGFVF 319
Cdd:MTH00026 270 GYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMAWALGFIF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 320 LFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFF 399
Cdd:MTH00026 350 LFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFF 429
|
410 420 430
....*....|....*....|....*....|..
gi 669633588 400 PQHFLGLSGMPRRYSDYPDSFTSWNIISSFGS 431
Cdd:MTH00026 430 PQHFLGLAGLPRRYADYPDNFEDFNQISSFGS 461
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-432 |
1.37e-167 |
|
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: 481.72 E-value: 1.37e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:TIGR02891 22 LVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeT 240
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-I 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:TIGR02891 340 FVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFP 419
|
410 420 430
....*....|....*....|....*....|....
gi 669633588 401 QHFLGLSGMPRRYSDYPDS--FTSWNIISSFGSY 432
Cdd:TIGR02891 420 MHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-432 |
4.95e-165 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 476.54 E-value: 4.95e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 160
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeT 240
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-L 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 320
Cdd:COG0843 269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:COG0843 349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428
|
410 420 430
....*....|....*....|....*....|....
gi 669633588 401 QHFLGLSGMPRRYSDYP--DSFTSWNIISSFGSY 432
Cdd:COG0843 429 MHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-432 |
1.28e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 436.42 E-value: 1.28e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 2 LGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 81
Cdd:MTH00048 30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 82 LTLLISSMIVenGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFdQMPLFIWAV 161
Cdd:MTH00048 110 IVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 162 GITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKETF 241
Cdd:MTH00048 187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 242 GCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYS-PSILWSLGFVFL 320
Cdd:MTH00048 267 GYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 321 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 400
Cdd:MTH00048 347 FTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFP 426
|
410 420 430
....*....|....*....|....*....|..
gi 669633588 401 QHFLGLSGMPRRYSDYPDSFTSWNIISSFGSY 432
Cdd:MTH00048 427 MHYFGLCGLPRRVCVYEPSYYWINVVCTVGSF 458
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-432 |
2.81e-142 |
|
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: 417.37 E-value: 2.81e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 2 LGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 81
Cdd:cd01662 24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 82 LTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWAV 161
Cdd:cd01662 103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 162 GITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeTF 241
Cdd:cd01662 183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 242 GCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFLF 321
Cdd:cd01662 262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 322 TIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFPQ 401
Cdd:cd01662 342 VIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPM 421
|
410 420 430
....*....|....*....|....*....|...
gi 669633588 402 HFLGLSGMPRRYSDYP--DSFTSWNIISSFGSY 432
Cdd:cd01662 422 HILGLMGMPRRVYTYLpgPGWDPLNLISTIGAF 454
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-432 |
6.78e-116 |
|
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: 347.25 E-value: 6.78e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 1 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 80
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 81 SLTLLISSMiveNGAGTGWTIYPPLSSnaihssssVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFdQMPLFIWA 160
Cdd:pfam00115 94 GAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 161 VGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeT 240
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 241 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMN-YSPSILWSLGFVF 319
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 320 LFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFF 399
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 669633588 400 PQHFLGLSGMPRRYS----DYPDSFTSWNIISSFGSY 432
Cdd:pfam00115 395 PMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
7-431 |
1.46e-94 |
|
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: 299.08 E-value: 1.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 7 SLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLI 86
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 87 SSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWAVGITAL 166
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 167 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESgKKETFGCLGM 246
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 247 IYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFLFTIGGL 326
Cdd:TIGR02882 310 VWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 327 TGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFPQHFLGL 406
Cdd:TIGR02882 390 TGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGL 469
|
410 420
....*....|....*....|....*..
gi 669633588 407 SGMPRRYSDY--PDSFTSWNIISSFGS 431
Cdd:TIGR02882 470 DGMPRRMYTYspSDGWFPLNLISTIGA 496
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
27-431 |
2.27e-84 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 272.96 E-value: 2.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 27 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSMIVENGAGTGWTIYPPLS 106
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 107 SNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWAVGITALLLLLSLPVLAGAITMLLTDR 186
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 187 NLNTSFFDPAGGGDPILYQHLFWF**********LPGFGMISHIISQESgKKETFGCLGMIYAMMTIGLLGFIVWAHHMF 266
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 267 TIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFLFTIGGLTGVILANSSIDVTLHDTYYV 346
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 347 VAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFPQHFLGLSGMPRRYSDYPD-SFTSWNI 425
Cdd:PRK15017 417 IAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLM 496
|
....*.
gi 669633588 426 ISSFGS 431
Cdd:PRK15017 497 IAASGA 502
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
6-419 |
1.24e-11 |
|
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: 66.54 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 6 LSLLIRTELgmpNSLIGDDQIYNTIVTAHAFIM-IFFMVMPIMigGFGNWLIPLMLGAPDMAfPRMNNMSFWLLPPSlTL 84
Cdd:cd01660 26 LQVLVRTGV---FPLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIG-TV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 85 LISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLhlagissILGAINFITTIINMRINKMtfDQMPLFIWAVGIT 164
Cdd:cd01660 99 MAAVPILLGQASVLYTFYPPLQAHPLFYIGAALVVVGSW-------ISGFAMFVTLWRWKKANPG--KKVPLATFMVVTT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 165 ALLLLLSLPVLAGAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWF**********LPGFGMISHIISQESGKKeTFGCL 244
Cdd:cd01660 170 MILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 245 GMIYAMMTIGLLGFIVWAHHMFT-IGMDTDTRAYFTSATMIIAVPTGIKIFSWLATF-HGTQMNYSPSILW--------- 313
Cdd:cd01660 244 LARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgd 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633588 314 ------SLGFVFlFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSY-LLKIQ 386
Cdd:cd01660 324 pmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKrLALAQ 402
|
410 420 430
....*....|....*....|....*....|....*
gi 669633588 387 FFTMFIGVNLTFFPQHFLGLSGMPRR--YSDYPDS 419
Cdd:cd01660 403 PWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGL 437
|
|
| |
