|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-221 |
1.94e-128 |
|
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: 371.05 E-value: 1.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
1.16e-125 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 364.57 E-value: 1.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-221 |
1.95e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 236.56 E-value: 1.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLLGNHqiYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-221 |
1.03e-44 |
|
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: 154.27 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLlgNHQIYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSiveVGTGTGWTVYPPLssiqshsgASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLyRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTsffdpsGGGDPVLYQHLF 221
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-221 |
3.70e-38 |
|
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: 139.60 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLLGNHqiYNVLITAHAFLMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFP 81
Cdd:TIGR02882 56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-221 |
1.94e-128 |
|
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: 371.05 E-value: 1.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
1.16e-125 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 364.57 E-value: 1.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
1.58e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 331.26 E-value: 1.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00167 17 TLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00167 95 PRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00167 175 GITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
2.03e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 328.59 E-value: 2.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00116 17 TLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00116 95 PRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00116 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
1.28e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 321.16 E-value: 1.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGnhLLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00223 14 TLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00223 92 PRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00223 172 GMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
1.87e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 313.20 E-value: 1.87e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00142 15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00142 93 PRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00142 173 GMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
1.05e-99 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 299.04 E-value: 1.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00182 19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00182 97 PRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00182 177 GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
3.02e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 295.20 E-value: 3.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00184 19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00184 97 PRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00184 177 GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-221 |
5.85e-98 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 294.10 E-value: 5.85e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00103 17 TLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00103 95 PRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00103 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
2.31e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 292.60 E-value: 2.31e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00183 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00183 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00183 175 AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
2.49e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 292.61 E-value: 2.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00077 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00077 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00077 175 SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
5.77e-97 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 291.73 E-value: 5.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00037 17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00037 95 PRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00037 175 GMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-221 |
3.67e-94 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 284.49 E-value: 3.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00007 14 TLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00007 92 PRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00007 172 GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
5.94e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 276.18 E-value: 5.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGnhLLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00079 18 TLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSiQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00079 96 PRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00079 175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-221 |
2.08e-90 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 275.35 E-value: 2.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00026 18 SLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:MTH00026 96 PRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00026 176 GMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-221 |
6.10e-81 |
|
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: 248.98 E-value: 6.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 1 TLYLIFGAFSGVLGGCMSMLIRMELAQPGNhlLLGNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPiMIGSPDMAF 80
Cdd:cd00919 6 LLYLIFAFVALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 81 PRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNP 160
Cdd:cd00919 83 PRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 161 GQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:cd00919 163 GMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-221 |
1.95e-75 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 236.56 E-value: 1.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLLGNHqiYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-221 |
9.12e-63 |
|
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: 202.81 E-value: 9.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLLGNHqiYNVLITAHAFLMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFP 81
Cdd:cd01662 13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:cd01662 90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:cd01662 170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-221 |
2.11e-58 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 191.81 E-value: 2.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLlgNHQIYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:MTH00048 19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSIVevGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:MTH00048 97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLyRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:MTH00048 175 VFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-221 |
1.03e-44 |
|
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: 154.27 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLlgNHQIYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSiveVGTGTGWTVYPPLssiqshsgASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLyRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTsffdpsGGGDPVLYQHLF 221
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-221 |
3.70e-38 |
|
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: 139.60 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRMELAQPGNHLLLGNHqiYNVLITAHAFLMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFP 81
Cdd:TIGR02882 56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 82 RLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNPG 161
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 162 QSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHLF 221
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-220 |
2.59e-34 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 128.90 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 2 LYLIFGAFSGVLGGCMSMLIRME--LAQPGNHLLLGNHQiYNVLITAHAFLMIFFMVMPVMIGgFGNWFVPIMIGSPDMA 79
Cdd:PRK15017 60 MYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312605671 80 FPRLNNISFWLLPPSLCLLLISSIVEVGTGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRN 159
Cdd:PRK15017 138 FPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRA 217
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312605671 160 PGQSLYRIPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPVLYQHL 220
Cdd:PRK15017 218 PGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278
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