|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.31e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 376.90 E-value: 1.31e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00153 29 TSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00153 109 LLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLI 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00153 189 TAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-209 |
1.17e-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: 350.63 E-value: 1.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:cd01663 22 TSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:cd01663 102 LLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:cd01663 182 TAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-209 |
7.18e-70 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 221.92 E-value: 7.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 3 MS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPiMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*LL 82
Cdd:COG0843 36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 83 MSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*ITA 162
Cdd:COG0843 115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2119324121 163 ILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:COG0843 195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-209 |
4.94e-41 |
|
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: 143.87 E-value: 4.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 3 MS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPiMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*LL 82
Cdd:pfam00115 20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 83 MSSSLvnlGVGTGWTVYPPLasniahsgASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLdQTPLFVWSV*ITA 162
Cdd:pfam00115 99 LASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2119324121 163 ILLLLSLPVLAGAITMLLLDRNMNtsffdpAGGGDPILYQHLFWFFG 209
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
6-209 |
4.72e-34 |
|
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: 127.66 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 6 LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGgFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*LLMSS 85
Cdd:TIGR02882 74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 86 SLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*ITAILL 165
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLII 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119324121 166 LLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.31e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 376.90 E-value: 1.31e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00153 29 TSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00153 109 LLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLI 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00153 189 TAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-209 |
1.17e-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: 350.63 E-value: 1.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:cd01663 22 TSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:cd01663 102 LLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:cd01663 182 TAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 230
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
4.83e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 342.43 E-value: 4.83e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00167 31 TALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00167 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00167 191 TTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
3.99e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 337.45 E-value: 3.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00116 31 TALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00116 111 LLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00116 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.60e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 325.78 E-value: 1.60e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00223 28 TSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00223 108 LLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00223 188 TAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
2.98e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 325.14 E-value: 2.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00142 29 TGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00142 109 LLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKI 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00142 189 TAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-209 |
7.06e-102 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 303.73 E-value: 7.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00103 31 TALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00103 111 LLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00103 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-209 |
1.05e-100 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 300.67 E-value: 1.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00007 28 TSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00007 108 LLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00007 188 TVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 236
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.08e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 300.70 E-value: 1.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00077 31 TALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00077 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00077 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.94e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 299.92 E-value: 1.94e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00183 31 TALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00183 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00183 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.96e-99 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 297.51 E-value: 1.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00037 31 TAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00037 111 LLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00037 191 TAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
3.36e-94 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 283.88 E-value: 3.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00079 32 TSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLaSNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00079 112 LILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00079 191 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
1.85e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 277.47 E-value: 1.85e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00182 33 TAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00182 113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00182 193 TAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
5.38e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 275.94 E-value: 5.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00184 33 TAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00184 113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00184 193 TTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-209 |
2.05e-84 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 259.56 E-value: 2.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:MTH00026 32 TAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:MTH00026 112 LLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFI 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00026 192 TAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-209 |
4.69e-78 |
|
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: 240.90 E-value: 4.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 1 TSMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL* 80
Cdd:cd00919 20 GLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGARDLAFPRLNNLSFWLFPPGLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 81 LLMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*I 160
Cdd:cd00919 99 LLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLV 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2119324121 161 TAILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:cd00919 179 TAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFG 227
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-209 |
7.18e-70 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 221.92 E-value: 7.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 3 MS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPiMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*LL 82
Cdd:COG0843 36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 83 MSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*ITA 162
Cdd:COG0843 115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2119324121 163 ILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:COG0843 195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-209 |
4.49e-61 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 198.36 E-value: 4.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 2 SMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*L 81
Cdd:MTH00048 33 SLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 82 LMSSSLvnLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLdQTPLFVWSV*IT 161
Cdd:MTH00048 113 LLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFT 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2119324121 162 AILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:MTH00048 190 SILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-209 |
2.08e-57 |
|
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: 188.56 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 2 SMS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGgFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*L 81
Cdd:cd01662 27 VDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 82 LMSSSLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*IT 161
Cdd:cd01662 106 LNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVT 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2119324121 162 AILLLLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:cd01662 186 SILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFG 233
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-209 |
4.94e-41 |
|
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: 143.87 E-value: 4.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 3 MS*LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPiMIGGFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*LL 82
Cdd:pfam00115 20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 83 MSSSLvnlGVGTGWTVYPPLasniahsgASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLdQTPLFVWSV*ITA 162
Cdd:pfam00115 99 LASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2119324121 163 ILLLLSLPVLAGAITMLLLDRNMNtsffdpAGGGDPILYQHLFWFFG 209
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFG 207
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
6-209 |
4.72e-34 |
|
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: 127.66 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 6 LIRTELGQPGQLIGBSQIYNVVITAHAFIMIFFMVMPIMIGgFGNWM*PLMIGAPDMAFPRMNNMSFWLLPPSL*LLMSS 85
Cdd:TIGR02882 74 LMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNIS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 86 SLVNLGVGTGWTVYPPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*ITAILL 165
Cdd:TIGR02882 153 FVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLII 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2119324121 166 LLSLPVLAGAITMLLLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:TIGR02882 233 IFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWG 276
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
24-209 |
3.94e-32 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 122.35 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 24 YNVVITAHAFIMIFFMVMPIMIGgFGNWM*PLMIGAPDMAFPRMNNMSFWllppSL*LLMSSSLVNLGVG----TGWTVY 99
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFW----FTVVGVILVNVSLGVGefaqTGWLAY 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119324121 100 PPLASNIAHSGASVDLAIFSLHLAGISSILGAIN*ITTTINMRSKKMSLDQTPLFVWSV*ITAILLLLSLPVLAGAITML 179
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253
|
170 180 190
....*....|....*....|....*....|
gi 2119324121 180 LLDRNMNTSFFDPAGGGDPILYQHLFWFFG 209
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWG 283
|
|
|