|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 514.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00153 33 LLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00153 113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00153 193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00153 273 YAMLAIGLLGFIVW 286
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-254 |
9.11e-162 |
|
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: 456.94 E-value: 9.11e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:cd01663 26 LLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:cd01663 106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:cd01663 186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:cd01663 266 YAMLSIGILGFIVW 279
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-254 |
2.21e-98 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 296.06 E-value: 2.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:TIGR02891 29 LLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:TIGR02891 108 SFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSIL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:TIGR02891 188 ILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMV 266
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:TIGR02891 267 YATVAIGFLSFGVW 280
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-254 |
1.15e-96 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 292.80 E-value: 1.15e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:COG0843 38 LLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:COG0843 117 SLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSIL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:COG0843 197 ILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMV 275
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:COG0843 276 LATVAIAFLSFLVW 289
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-254 |
5.39e-62 |
|
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: 200.49 E-value: 5.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:pfam00115 22 LLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSiveNGAGTGWTVYPPLSAgiahaggsVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLdRMPLFVWSVVITAIL 160
Cdd:pfam00115 101 SF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:pfam00115 169 ILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSV 241
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:pfam00115 242 LAFWLIAFLGFLVW 255
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 514.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00153 33 LLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00153 113 SSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAIL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00153 193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00153 273 YAMLAIGLLGFIVW 286
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-254 |
9.11e-162 |
|
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: 456.94 E-value: 9.11e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:cd01663 26 LLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:cd01663 106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:cd01663 186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:cd01663 266 YAMLSIGILGFIVW 279
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
1.14e-153 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 437.57 E-value: 1.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00167 35 LLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00167 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTIL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00167 195 LLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMV 274
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00167 275 WAMMAIGLLGFIVW 288
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
2.36e-151 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 431.45 E-value: 2.36e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00142 33 LLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00142 113 SAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAIL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00142 193 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMI 272
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00142 273 YAMLSIGLLGFIVW 286
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
9.23e-151 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 430.28 E-value: 9.23e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00116 35 LLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00116 115 SSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00116 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMV 274
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00116 275 WAMLSIGFLGFIVW 288
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
1.51e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 427.09 E-value: 1.51e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00223 32 LLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00223 112 SSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00223 192 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMI 271
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00223 272 YAMLSIGVLGFIVW 285
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
1.35e-135 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 391.89 E-value: 1.35e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00037 35 VIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00037 115 SAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00037 195 LLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMV 274
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00037 275 YAMIAIGILGFLVW 288
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-254 |
2.80e-134 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 388.11 E-value: 2.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00007 32 LLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00007 112 SAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00007 192 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMI 271
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00007 272 YAMLGIGVLGFIVW 285
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-254 |
5.20e-134 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 387.70 E-value: 5.20e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00103 35 LLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00103 115 SSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00103 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMV 274
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00103 275 WAMMSIGFLGFIVW 288
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
1.56e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 386.59 E-value: 1.56e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00183 35 LLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00183 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00183 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMV 274
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00183 275 WAMMAIGLLGFIVW 288
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
8.37e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 384.68 E-value: 8.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00077 35 LLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00077 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00077 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMV 274
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00077 275 WAMMSIGLLGFIVW 288
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
2.54e-126 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 368.38 E-value: 2.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00182 37 MLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00182 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00182 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMV 276
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00182 277 YAMLSIGILGFIVW 290
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
4.89e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 362.22 E-value: 4.89e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00184 37 MLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00184 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00184 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMV 276
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00184 277 YAMVSIGILGFIVW 290
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-254 |
3.53e-121 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 354.76 E-value: 3.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 2 LIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLTG 81
Cdd:MTH00079 37 IIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 82 SIVENGAGTGWTVYPPLSAgIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAILL 161
Cdd:MTH00079 117 CFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 162 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIY 241
Cdd:MTH00079 196 VLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVY 275
|
250
....*....|...
gi 347984471 242 AMLAIGLLGFVVW 254
Cdd:MTH00079 276 AILSIGLIGCVVW 288
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
5.00e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 340.07 E-value: 5.00e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00026 36 MLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:MTH00026 116 SSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAIL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00026 196 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMV 275
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00026 276 YAMLAIGVLGFIVW 289
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-254 |
7.07e-104 |
|
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: 309.08 E-value: 7.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:cd00919 24 LLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:cd00919 103 SVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:cd00919 183 LLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMV 261
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:cd00919 262 YAFLAIGFLSFLVW 275
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-254 |
2.21e-98 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 296.06 E-value: 2.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:TIGR02891 29 LLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:TIGR02891 108 SFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSIL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:TIGR02891 188 ILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMV 266
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:TIGR02891 267 YATVAIGFLSFGVW 280
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-254 |
1.15e-96 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 292.80 E-value: 1.15e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:COG0843 38 LLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:COG0843 117 SLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSIL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:COG0843 197 ILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMV 275
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:COG0843 276 LATVAIAFLSFLVW 289
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-254 |
1.59e-84 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 260.77 E-value: 1.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:MTH00048 36 LLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVenGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLdRMPLFVWSVVITAIL 160
Cdd:MTH00048 116 SMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSIL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMI 240
Cdd:MTH00048 193 LLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLV 272
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:MTH00048 273 FAMFSIVCLGSVVW 286
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-254 |
2.49e-82 |
|
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: 254.81 E-value: 2.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:cd01662 30 LLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:cd01662 109 SLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSIL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:cd01662 189 ILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMV 267
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:cd01662 268 YATVAIGFLSFGVW 281
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-254 |
5.39e-62 |
|
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: 200.49 E-value: 5.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:pfam00115 22 LLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSiveNGAGTGWTVYPPLSAgiahaggsVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLdRMPLFVWSVVITAIL 160
Cdd:pfam00115 101 SF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMI 240
Cdd:pfam00115 169 ILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSV 241
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:pfam00115 242 LAFWLIAFLGFLVW 255
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-254 |
1.87e-52 |
|
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: 180.05 E-value: 1.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 1 VLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLT 80
Cdd:TIGR02882 73 LLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 81 GSIVENGAGTGWTVYPPLSAGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAIL 160
Cdd:TIGR02882 152 SFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 161 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKEAFGTLGMI 240
Cdd:TIGR02882 232 IIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMV 310
|
250
....*....|....
gi 347984471 241 YAMLAIGLLGFVVW 254
Cdd:TIGR02882 311 WSTVGIAFLSFLVW 324
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
20-254 |
1.88e-50 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 174.74 E-value: 1.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 20 YNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLLLLLTGSIVENGAGTGWTVYPPLS 99
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 100 AGIAHAGGSVDLSIFSLHLAGASSILGAANFITTVINMRPNGMTLDRMPLFVWSVVITAILLLLSLPVLAGAITMLLTDR 179
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347984471 180 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVW 254
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVW 331
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
13-231 |
1.46e-04 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 42.66 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 13 LIGDDQIYNVIVTAHAFIM-IFFMVMPIMigGFGNWLVPLMLGAPDMAfPRLNNMSFWLLPPSLLLLLTgSIVENGAGTG 91
Cdd:cd01660 37 LPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAV-PILLGQASVL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 92 WTVYPPLsagIAHAGGSVDLSIFSLhlagASSILGAANFITTVINMRPNgmTLDRMPLFVWSVVITAILLLLSLPVLAGA 171
Cdd:cd01660 113 YTFYPPL---QAHPLFYIGAALVVV----GSWISGFAMFVTLWRWKKAN--PGKKVPLATFMVVTTMILWLVASLGVALE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 347984471 172 ITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK 231
Cdd:cd01660 184 VLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK 238
|
|
|