|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
1.17e-134 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 386.92 E-value: 1.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00153 30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-203 |
9.34e-120 |
|
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: 347.93 E-value: 9.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:cd01663 23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:cd01663 103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:cd01663 183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-203 |
2.90e-66 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 212.29 E-value: 2.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 2 LSLIIRAELGQPG-TLIGNDQiYNVAVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:COG0843 36 LALLMRLQLAGPGlGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:COG0843 114 LLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVT 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:COG0843 194 SILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-203 |
3.86e-38 |
|
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: 136.16 E-value: 3.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 2 LSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 81
Cdd:pfam00115 20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 82 LMSGMvesGVGTGWTVYPPLSAaiahagasVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLdQMPLFVWAVFITA 161
Cdd:pfam00115 99 LASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2250419737 162 ILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHL 203
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
3-203 |
6.05e-33 |
|
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: 124.20 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 3 SLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLL 82
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 83 MSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFITAI 162
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2250419737 163 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANL 271
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
1.17e-134 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 386.92 E-value: 1.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00153 30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-203 |
9.34e-120 |
|
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: 347.93 E-value: 9.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:cd01663 23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:cd01663 103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:cd01663 183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
1.65e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 340.89 E-value: 1.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00167 32 ALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00167 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00167 192 TILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
3.66e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 329.76 E-value: 3.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00142 30 GLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00142 110 LLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKIT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00142 190 AILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 232
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
2.34e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 327.82 E-value: 2.34e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00116 32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00116 112 LLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00116 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
5.18e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 324.24 E-value: 5.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00223 29 SLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00223 109 LLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVT 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00223 189 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 231
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-203 |
1.43e-99 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 297.56 E-value: 1.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00103 32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00103 112 LLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00103 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
2.50e-99 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 297.13 E-value: 2.50e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00037 32 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00037 112 LLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00037 192 AFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHL 234
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-203 |
2.75e-99 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 296.81 E-value: 2.75e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00007 29 SMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00007 109 LVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVIT 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00007 189 VVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 231
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
1.05e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 295.29 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00183 32 ALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00183 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00183 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
1.85e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 294.54 E-value: 1.85e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00077 32 ALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00077 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLIT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00077 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHL 234
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
1.00e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 277.33 E-value: 1.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00079 33 SLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSaAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00079 113 ILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00079 192 VFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHL 234
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
2.26e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 276.70 E-value: 2.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00182 34 AFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00182 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILIT 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00182 194 AFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHL 236
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
1.38e-90 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 274.78 E-value: 1.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00184 34 AFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00184 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVT 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00184 194 TFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 236
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
2.81e-83 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 256.48 E-value: 2.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00026 33 AFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:MTH00026 113 LLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFIT 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00026 193 AILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 235
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-203 |
2.87e-74 |
|
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: 230.88 E-value: 2.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:cd00919 21 LLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:cd00919 100 LLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:cd00919 180 AILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHL 222
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-203 |
2.90e-66 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 212.29 E-value: 2.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 2 LSLIIRAELGQPG-TLIGNDQiYNVAVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:COG0843 36 LALLMRLQLAGPGlGLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFIT 160
Cdd:COG0843 114 LLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVT 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:COG0843 194 SILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-203 |
2.55e-56 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 185.65 E-value: 2.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTL 80
Cdd:MTH00048 33 SLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 81 LLMSgmVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLdQMPLFVWAVFIT 160
Cdd:MTH00048 113 LLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2250419737 161 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:MTH00048 190 SILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHM 232
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-203 |
2.57e-54 |
|
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: 180.08 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 1 SLSLIIRAELGQP-GTLIGNDQiYNVAVTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLT 79
Cdd:cd01662 27 VDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 80 LLLMSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFI 159
Cdd:cd01662 105 LLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2250419737 160 TAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:cd01662 185 TSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHL 228
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-203 |
3.86e-38 |
|
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: 136.16 E-value: 3.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 2 LSLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 81
Cdd:pfam00115 20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 82 LMSGMvesGVGTGWTVYPPLSAaiahagasVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLdQMPLFVWAVFITA 161
Cdd:pfam00115 99 LASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2250419737 162 ILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHL 203
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
20-203 |
4.13e-34 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 127.74 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 20 DQIYnvavTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSGMVESGVGTGWTVYP 99
Cdd:PRK15017 100 DQIF----TAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 100 PLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFITAILLLLSLPVLAGAITMLL 179
Cdd:PRK15017 175 PLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLT 254
|
170 180
....*....|....*....|....
gi 2250419737 180 TDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:PRK15017 255 LDRYLGTHFFTNDMGGNMMMYINL 278
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
3-203 |
6.05e-33 |
|
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: 124.20 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 3 SLIIRAELGQPGTLIGNDQIYNVAVTAHAFVMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLL 82
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250419737 83 MSGMVESGVGTGWTVYPPLSAAIAHAGASVDMGIFSLHLAGVSSILGAVNFMTTVINMRSFGMTLDQMPLFVWAVFITAI 162
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2250419737 163 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 203
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANL 271
|
|
|