|
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 ... |
1-229 |
1.37e-142 |
|
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: 407.25 E-value: 1.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:cd01663 80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:cd01663 160 FNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
3.41e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 401.94 E-value: 3.41e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00153 9 NHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00153 87 APDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00153 167 INMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-229 |
7.82e-85 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 261.22 E-value: 7.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQiFMGNHQlYNVVVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIG 80
Cdd:COG0843 14 DHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLG-LLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:COG0843 91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:COG0843 171 LKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
4-229 |
8.66e-51 |
|
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: 170.45 E-value: 8.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 4 DIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIFmgNHQLYNVVVTAHAFIMVFFLVMPAlIGGFGNWFVPLMIGAPD 83
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 84 MAFPRMNNISFWLLPPALLLLVSSAiveSGAGTGWTVYPPLssvqahsgPSVDLAIFSLHLTGISSILGAINFISTIYNM 163
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499017798 164 RAPGLSFhRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTsfydpsGGGDPVLYQHLFWF 229
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWW 205
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-228 |
5.40e-41 |
|
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: 147.69 E-value: 5.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIFMGNHqlYNVVVTAHAFIMVFFLVMPALIGgFGNWFVPLMIG 80
Cdd:TIGR02882 49 DHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:TIGR02882 126 ARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTI 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFW 228
Cdd:TIGR02882 206 LKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFW 273
|
|
|
|
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 ... |
1-229 |
1.37e-142 |
|
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: 407.25 E-value: 1.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:cd01663 80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:cd01663 160 FNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
3.41e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 401.94 E-value: 3.41e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00153 9 NHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00153 87 APDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00153 167 INMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
5.91e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 360.92 E-value: 5.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00167 11 NHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00167 89 APDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00167 169 INMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
1.07e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 360.06 E-value: 1.07e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGnqIFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00223 8 NHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00223 86 APDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00223 166 INMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 234
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
8.00e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 357.87 E-value: 8.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00116 11 NHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00116 89 APDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00116 169 INMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
3.72e-120 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 350.95 E-value: 3.72e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00142 9 NHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00142 87 APDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00142 167 INMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 235
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
1.33e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 327.16 E-value: 1.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00182 13 NHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAML--GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00182 91 APDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00182 171 FNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWF 239
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
3.56e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 326.01 E-value: 3.56e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00184 13 NHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00184 91 APDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00184 171 FNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-229 |
7.25e-109 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 322.24 E-value: 7.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00007 8 NHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00007 86 APDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00007 166 INMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 234
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
8.67e-109 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 322.28 E-value: 8.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00077 11 NHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00077 89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00077 169 INMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWF 237
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
2.11e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 321.39 E-value: 2.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00037 11 NHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00037 89 APDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00037 169 INMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWF 237
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
3.13e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 320.72 E-value: 3.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00183 11 NHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00183 89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00183 169 INMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-229 |
1.20e-107 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 319.14 E-value: 1.20e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00103 11 NHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00103 89 APDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00103 169 INMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
3.00e-102 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 305.45 E-value: 3.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGnqIFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00079 12 NHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSvQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00079 90 APDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00079 169 KNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
4.03e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 295.77 E-value: 4.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00026 12 NHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00026 90 APDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00026 170 MNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
2-229 |
1.36e-90 |
|
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: 274.02 E-value: 1.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 2 HKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPlMIGA 81
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLF--LDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 82 PDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIY 161
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499017798 162 NMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWF 225
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-229 |
7.82e-85 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 261.22 E-value: 7.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQiFMGNHQlYNVVVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIG 80
Cdd:COG0843 14 DHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLG-LLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:COG0843 91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:COG0843 171 LKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-229 |
3.03e-67 |
|
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: 215.14 E-value: 3.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQiFMGNHQlYNVVVTAHAFIMVFFLVMPALIGgFGNWFVPLMIG 80
Cdd:cd01662 6 DHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGND-FLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:cd01662 83 ARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:cd01662 163 LKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWI 231
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-229 |
5.56e-65 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 209.53 E-value: 5.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIFmgNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIG 80
Cdd:MTH00048 12 DHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVesGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:MTH00048 90 LSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499017798 161 YNMRAPGLsFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWF 229
Cdd:MTH00048 168 YSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
4-229 |
8.66e-51 |
|
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: 170.45 E-value: 8.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 4 DIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIFmgNHQLYNVVVTAHAFIMVFFLVMPAlIGGFGNWFVPLMIGAPD 83
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 84 MAFPRMNNISFWLLPPALLLLVSSAiveSGAGTGWTVYPPLssvqahsgPSVDLAIFSLHLTGISSILGAINFISTIYNM 163
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499017798 164 RAPGLSFhRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTsfydpsGGGDPVLYQHLFWF 229
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWW 205
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-228 |
5.40e-41 |
|
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: 147.69 E-value: 5.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRMELAQPGNQIFMGNHqlYNVVVTAHAFIMVFFLVMPALIGgFGNWFVPLMIG 80
Cdd:TIGR02882 49 DHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 81 APDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTI 160
Cdd:TIGR02882 126 ARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTI 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499017798 161 YNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFW 228
Cdd:TIGR02882 206 LKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFW 273
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-228 |
7.75e-40 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 144.69 E-value: 7.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 1 NHKDIGTLYLIFSAFAGIVGTTLSLLIRME--LAQPGNQIFMGNHQlYNVVVTAHAFIMVFFLVMPALIGgFGNWFVPLM 78
Cdd:PRK15017 53 DHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 79 IGAPDMAFPRMNNISFWLLPPALLLLVSSAIVESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFIS 158
Cdd:PRK15017 131 IGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFV 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499017798 159 TIYNMRAPGLSFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFW 228
Cdd:PRK15017 211 TILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
|
|