|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
3.01e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 396.55 E-value: 3.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00153 22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-216 |
3.15e-127 |
|
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: 367.58 E-value: 3.15e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:cd01663 15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:cd01663 95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:cd01663 175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-216 |
1.14e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 221.54 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 3 AGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 83 PPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLFV 162
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1114634449 163 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-216 |
4.89e-43 |
|
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: 149.65 E-value: 4.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 3 AGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:pfam00115 13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 83 PPSFLLLLASSGveaGAGTGWTVYPPLasnlahagASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQfQTPLFV 162
Cdd:pfam00115 92 VLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1114634449 163 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFG 216
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
7-216 |
5.96e-37 |
|
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: 136.14 E-value: 5.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 7 GTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSF 86
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 87 LLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLFVWSVL 166
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1114634449 167 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
3.01e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 396.55 E-value: 3.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00153 22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
4.57e-132 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 380.98 E-value: 4.57e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00116 24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00116 104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00116 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
2.69e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 376.32 E-value: 2.69e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00167 24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-216 |
3.15e-127 |
|
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: 367.58 E-value: 3.15e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:cd01663 15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:cd01663 95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:cd01663 175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
8.74e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 360.01 E-value: 8.74e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00183 24 AWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00183 104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00183 184 FVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
5.22e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 358.10 E-value: 5.22e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00077 24 AWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00077 104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00077 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-216 |
2.95e-121 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 353.42 E-value: 2.95e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00103 24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00103 104 LLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00103 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
5.24e-120 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 350.18 E-value: 5.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00142 22 AWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00142 102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00142 182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
2-216 |
5.74e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 345.04 E-value: 5.74e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 2 WAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00223 22 WSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 82 LPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLF 161
Cdd:MTH00223 102 LPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLF 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1114634449 162 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00223 182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
3.88e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 320.24 E-value: 3.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00037 24 AWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00037 104 LIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00037 184 FVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-216 |
2.26e-104 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 310.30 E-value: 2.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00007 21 VWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00007 101 LLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00007 181 FVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
7.38e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 299.05 E-value: 7.38e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00184 26 AFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00184 106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00184 186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
9.45e-99 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 296.35 E-value: 9.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00182 26 AGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00182 106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00182 186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-216 |
6.64e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 285.81 E-value: 6.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 2 WAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00079 26 WSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 82 LPPSFLLLLASSGVEAGAGTGWTVYPPLaSNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLF 161
Cdd:MTH00079 106 LPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLF 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1114634449 162 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00079 185 VWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
9.40e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 276.12 E-value: 9.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 1 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 80
Cdd:MTH00026 25 ALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 81 LLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPL 160
Cdd:MTH00026 105 LLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1114634449 161 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00026 185 FVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
2-216 |
4.17e-79 |
|
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: 243.98 E-value: 4.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 2 WAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPlMIGAPDMAFPRMNNMSFWL 81
Cdd:cd00919 14 VALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 82 LPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLF 161
Cdd:cd00919 93 FPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLF 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1114634449 162 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:cd00919 173 VWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFG 227
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-216 |
1.14e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 221.54 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 3 AGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 83 PPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLFV 162
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1114634449 163 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-216 |
7.08e-66 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 211.07 E-value: 7.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 2 WAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 81
Cdd:MTH00048 26 WSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 82 LPPSFLLLLASsgVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITqFQTPLF 161
Cdd:MTH00048 106 LVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSII 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1114634449 162 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:MTH00048 183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-216 |
2.86e-59 |
|
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: 193.57 E-value: 2.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 7 GTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSF 86
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 87 LLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLFVWSVL 166
Cdd:cd01662 104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1114634449 167 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:cd01662 184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFG 233
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-216 |
4.89e-43 |
|
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: 149.65 E-value: 4.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 3 AGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPvMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 82
Cdd:pfam00115 13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 83 PPSFLLLLASSGveaGAGTGWTVYPPLasnlahagASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQfQTPLFV 162
Cdd:pfam00115 92 VLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1114634449 163 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFG 216
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
7-216 |
5.96e-37 |
|
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: 136.14 E-value: 5.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 7 GTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSF 86
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 87 LLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLFVWSVL 166
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1114634449 167 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
31-216 |
1.44e-35 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 132.37 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 31 YNVIVTAHAFVMIFFMVMPVMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLA 110
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114634449 111 SNLAHAGASVDLTIFSLHLAGISSILGAINFITTIMNMKPAAITQFQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 190
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180
....*....|....*....|....*.
gi 1114634449 191 NLNTTFFDPAGGGDPILYQHLFWFFG 216
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWG 283
|
|
|