|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-246 |
1.63e-147 |
|
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: 420.74 E-value: 1.63e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLllGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:cd01663 16 WSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:cd01663 94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:cd01663 174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFS 253
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:cd01663 254 gKKPVFG 260
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-246 |
1.78e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 403.48 E-value: 1.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00153 23 WSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQES 260
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00153 261 gKKETFG 267
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-246 |
1.86e-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: 1.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:TIGR02891 19 AFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:TIGR02891 96 WLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:TIGR02891 176 LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA 255
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:TIGR02891 256 RKPIFG 261
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-246 |
7.47e-95 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 287.79 E-value: 7.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:COG0843 28 VFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:COG0843 105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:COG0843 185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:COG0843 265 RKPLFG 270
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-246 |
2.34e-61 |
|
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: 198.57 E-value: 2.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:pfam00115 12 VWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLvevGAGTGWTVYPPLssiqshsgAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMyRIP 160
Cdd:pfam00115 89 WLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA 230
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:pfam00115 231 GRPLFG 236
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-246 |
1.63e-147 |
|
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: 420.74 E-value: 1.63e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLllGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:cd01663 16 WSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:cd01663 94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:cd01663 174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFS 253
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:cd01663 254 gKKPVFG 260
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-246 |
1.78e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 403.48 E-value: 1.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00153 23 WSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQES 260
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00153 261 gKKETFG 267
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
2-246 |
5.64e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 371.62 E-value: 5.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 2 SGVLGACISMLIRMELAQPGnqLLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFW 81
Cdd:MTH00223 23 SGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 82 LLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPL 161
Cdd:MTH00223 101 LLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 162 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSR 241
Cdd:MTH00223 181 FVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSS 260
|
....*.
gi 451810449 242 K-PVFG 246
Cdd:MTH00223 261 KkEVFG 266
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-246 |
6.62e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 371.70 E-value: 6.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00167 25 WAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00167 103 WLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00167 183 LFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYS 262
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00167 263 gKKEPFG 269
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-242 |
1.27e-125 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 365.95 E-value: 1.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00116 25 WAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00116 103 WLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00116 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYA 262
|
..
gi 451810449 241 RK 242
Cdd:MTH00116 263 GK 264
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-246 |
2.18e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 357.50 E-value: 2.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00142 23 WAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00142 101 WLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00142 181 LFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYS 260
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00142 261 gKKEVFG 267
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-246 |
7.01e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 336.41 E-value: 7.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00182 27 GAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00182 105 WLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00182 185 LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFV 264
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00182 265 aKKQIFG 271
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-246 |
1.45e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 332.95 E-value: 1.45e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00184 27 FAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00184 105 WLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00184 185 LFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFA 264
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00184 265 aKKQIFG 271
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-242 |
1.58e-110 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 327.22 E-value: 1.58e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00103 25 WAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00103 103 WLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00103 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYS 262
|
..
gi 451810449 241 RK 242
Cdd:MTH00103 263 GK 264
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-242 |
2.03e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 327.17 E-value: 2.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00037 25 WAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00037 103 WLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00037 183 LFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYS 262
|
..
gi 451810449 241 RK 242
Cdd:MTH00037 263 GK 264
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-242 |
3.31e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 326.51 E-value: 3.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00077 25 WAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00077 103 WLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00077 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYS 262
|
..
gi 451810449 241 RK 242
Cdd:MTH00077 263 AK 264
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-242 |
9.84e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 325.34 E-value: 9.84e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00183 25 WAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00183 103 WLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00183 183 LFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYS 262
|
..
gi 451810449 241 RK 242
Cdd:MTH00183 263 GK 264
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-243 |
1.09e-107 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 319.93 E-value: 1.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00007 22 WGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00007 100 WLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00007 180 LFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYA 259
|
...
gi 451810449 241 RKP 243
Cdd:MTH00007 260 GKL 262
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-246 |
1.01e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 315.08 E-value: 1.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 2 SGVLGACISMLIRMELAQPGnqLLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFW 81
Cdd:MTH00079 27 SGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 82 LLPPSLCLLLASSLVEVGAGTGWTVYPPLSSiQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPL 161
Cdd:MTH00079 105 LLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 162 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS- 240
Cdd:MTH00079 184 FVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTg 263
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:MTH00079 264 KKEVFG 269
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-246 |
3.32e-102 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 306.94 E-value: 3.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00026 26 LSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00026 104 WLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00026 184 LFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFS 263
|
....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00026 264 yKKQIFG 270
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-246 |
1.86e-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: 1.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:TIGR02891 19 AFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:TIGR02891 96 WLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:TIGR02891 176 LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA 255
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:TIGR02891 256 RKPIFG 261
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-246 |
5.66e-98 |
|
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: 293.67 E-value: 5.66e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPiMIGSPDMAFPRLNNISF 80
Cdd:cd00919 14 VALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:cd00919 91 WLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:cd00919 171 LFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFS 250
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:cd00919 251 GKPLFG 256
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-246 |
7.47e-95 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 287.79 E-value: 7.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:COG0843 28 VFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:COG0843 105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:COG0843 185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:COG0843 265 RKPLFG 270
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
4-246 |
4.88e-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: 254.04 E-value: 4.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 4 VLGACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLL 83
Cdd:cd01662 23 LRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 84 PPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPLFV 163
Cdd:cd01662 100 LFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 164 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSRKP 243
Cdd:cd01662 180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP 259
|
...
gi 451810449 244 VFG 246
Cdd:cd01662 260 LFG 262
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-240 |
1.12e-76 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 240.35 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 2 SGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFW 81
Cdd:MTH00048 27 SGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 82 LLPPSLCLLLASSLVevGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSmYRIPL 161
Cdd:MTH00048 105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 451810449 162 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00048 182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLS 260
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-246 |
2.34e-61 |
|
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: 198.57 E-value: 2.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:pfam00115 12 VWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 81 WLLPPSLCLLLASSLvevGAGTGWTVYPPLssiqshsgAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMyRIP 160
Cdd:pfam00115 89 WLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA 230
|
....*.
gi 451810449 241 RKPVFG 246
Cdd:pfam00115 231 GRPLFG 236
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
9-246 |
6.04e-51 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 175.89 E-value: 6.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 9 ISMLIRMELAQPGNQLLLGNHQvYNVLITAHAILMIFFLVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 88
Cdd:PRK15017 77 IMMRSQQALASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 89 LLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 168
Cdd:PRK15017 155 LVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLC 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 451810449 169 TAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSRKPVFG 246
Cdd:PRK15017 235 ANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFG 312
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
6-246 |
2.99e-50 |
|
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: 173.50 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 6 GACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 85
Cdd:TIGR02882 68 GGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 86 SLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPLFVWS 165
Cdd:TIGR02882 145 GAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 166 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSRKPVF 245
Cdd:TIGR02882 225 TLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLF 304
|
.
gi 451810449 246 G 246
Cdd:TIGR02882 305 G 305
|
|
|