|
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 ... |
1-244 |
2.69e-90 |
|
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: 275.52 E-value: 2.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:cd01663 3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:cd01663 80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
....
gi 2178351184 241 VPAF 244
Cdd:cd01663 239 LPGF 242
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
1.12e-79 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 248.74 E-value: 1.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00223 9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00223 86 APDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00223 165 IINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 244
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00223 245 LPGF 248
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-244 |
1.48e-71 |
|
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: 227.49 E-value: 1.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:TIGR02891 6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:TIGR02891 82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
....*
gi 2178351184 240 IVPAF 244
Cdd:TIGR02891 240 FLPAF 244
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-244 |
1.78e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 223.08 E-value: 1.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:COG0843 15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:COG0843 91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:COG0843 169 TILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYIL 248
|
....*
gi 2178351184 240 IVPAF 244
Cdd:COG0843 249 ILPAF 253
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-244 |
1.03e-45 |
|
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: 158.51 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 3 RLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIFQGSP 82
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 83 EVVYPRINNFSILILSLSylfVILSLISEFGGGTGWTLYPPLSTSFLslspsstgnLIFGLLISGISSCLTSLNFWTTII 162
Cdd:pfam00115 77 DMAFPRLNALSFWLVVLG---AVLLLASFGGATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTIL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 163 NLRSYYLTLKtMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFfdpifeGDPIFYQHLFWFFGHPEVYILIVP 242
Cdd:pfam00115 145 KRRAPGMTLR-MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGG------GDPLLDQHLFWWFGHPEVYILILP 217
|
..
gi 2178351184 243 AF 244
Cdd:pfam00115 218 AF 219
|
|
|
|
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 ... |
1-244 |
2.69e-90 |
|
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: 275.52 E-value: 2.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:cd01663 3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:cd01663 80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
....
gi 2178351184 241 VPAF 244
Cdd:cd01663 239 LPGF 242
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
1.12e-79 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 248.74 E-value: 1.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00223 9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00223 86 APDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00223 165 IINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 244
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00223 245 LPGF 248
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
7.72e-79 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 246.70 E-value: 7.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00153 10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLI---GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00153 87 APDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILGAINFITT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00153 166 IINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 245
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00153 246 LPGF 249
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
3.51e-73 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 232.26 E-value: 3.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00167 12 HKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00167 89 APDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLA-GNLAHAGASVDLAIFSLHLAGVSSILGSINFITT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00167 168 IINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00167 248 LPGF 251
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
6.79e-73 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 231.52 E-value: 6.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00116 12 HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00116 89 APDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGN-LAHAGASVDLAIFSLHLAGVSSILGAINFITT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00116 168 CINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00116 248 LPGF 251
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-265 |
1.06e-72 |
|
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: 229.34 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFqG 80
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQ---LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSStGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:cd00919 77 ARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:cd00919 156 ILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILI 235
|
250 260
....*....|....*....|....*
gi 2178351184 241 VPAFGIISIIISGILQKIIFGNQSM 265
Cdd:cd00919 236 LPAFGAISEIIPTFSGKPLFGYKLM 260
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
4.72e-72 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 229.18 E-value: 4.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGnriISPENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00079 13 HKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG---LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00079 90 APDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST--LGHPGSSVDLAIFSLHCAGISSILGGINFMVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00079 168 TKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILI 247
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00079 248 LPAF 251
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-244 |
1.48e-71 |
|
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: 227.49 E-value: 1.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:TIGR02891 6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:TIGR02891 82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
....*
gi 2178351184 240 IVPAF 244
Cdd:TIGR02891 240 FLPAF 244
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
2.75e-71 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 227.30 E-value: 2.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00142 10 HKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLL---GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00142 87 APDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS-SNLAHSGGSVDLAIFSLHLAGVSSILGAINFITT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00142 166 VINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 245
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00142 246 LPGF 249
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-244 |
1.78e-69 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 223.08 E-value: 1.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:COG0843 15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:COG0843 91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:COG0843 169 TILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYIL 248
|
....*
gi 2178351184 240 IVPAF 244
Cdd:COG0843 249 ILPAF 253
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
1.19e-68 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 220.47 E-value: 1.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00184 14 HKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSML---GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00184 91 APDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGSVDMAIFSLHLAGISSILGAMNFITT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00184 170 IFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 249
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00184 250 LPGF 253
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-244 |
2.63e-68 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 219.37 E-value: 2.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00103 12 HKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00103 89 APDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGN-LAHAGASVDLTIFSLHLAGVSSILGAINFITT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00103 168 IINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00103 248 LPGF 251
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-244 |
4.60e-67 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 216.31 E-value: 4.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00007 9 HKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQ---LYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSsTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00007 86 APDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPS-VDLAIFSLHLAGVSSILGAINFITT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00007 165 VINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 244
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00007 245 LPGF 248
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
7.73e-67 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 215.96 E-value: 7.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00077 12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSsTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00077 89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGAS-VDLTIFSLHLAGVSSILGAINFITT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00077 168 SINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILI 247
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00077 248 LPGF 251
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
3.33e-66 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 214.02 E-value: 3.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00183 12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00183 89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGN-LAHAGASVDLTIFSLHLAGVSSILGAINFITT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00183 168 IINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00183 248 LPGF 251
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
1.53e-65 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 212.76 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00182 14 HKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAML---GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00182 91 APDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGAVDMAIFSLHLAGVSSILGAINFITT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00182 170 IFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILI 249
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00182 250 LPGF 253
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
6.02e-65 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 210.84 E-value: 6.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00037 12 HKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLL---QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00037 89 APDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLS-SNIAHAGGSVDLAIFSLHLAGASSILASINFITT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00037 168 IINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILI 247
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00037 248 LPGF 251
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-265 |
3.57e-62 |
|
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: 203.20 E-value: 3.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPENqnfYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:cd01662 7 HKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH---YNQIFTMHGTIMIFLFAMP-LVFGLMNYLVPLQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:cd01662 83 ARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSG--LEYSPGVGVDYwILGLQFSGIGTLLGAINFIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:cd01662 161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240
|
250 260
....*....|....*....|....*.
gi 2178351184 240 IVPAFGIISIIISGILQKIIFGNQSM 265
Cdd:cd01662 241 ILPAFGIFSEIVPTFSRKPLFGYRSM 266
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
7.87e-62 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 203.32 E-value: 7.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00026 13 HKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSML---GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00026 90 APDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLA-SIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00026 169 VMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 248
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00026 249 LPGF 252
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-244 |
6.38e-57 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 189.89 E-value: 6.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00048 13 HKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLD---VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 81 SPEVVYPRINNFSILILSLSYLFVILSLIseFGGGTGWTLYPPLSTSFLSLSpSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00048 90 LSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSS-WGVDFLMFSLHLAGVSSLFGSINFICT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTmPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00048 167 IYSAFMTNVFSRT-SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLI 245
|
....
gi 2178351184 241 VPAF 244
Cdd:MTH00048 246 LPGF 249
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-244 |
1.03e-45 |
|
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: 158.51 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 3 RLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIFQGSP 82
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 83 EVVYPRINNFSILILSLSylfVILSLISEFGGGTGWTLYPPLSTSFLslspsstgnLIFGLLISGISSCLTSLNFWTTII 162
Cdd:pfam00115 77 DMAFPRLNALSFWLVVLG---AVLLLASFGGATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTIL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 163 NLRSYYLTLKtMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFfdpifeGDPIFYQHLFWFFGHPEVYILIVP 242
Cdd:pfam00115 145 KRRAPGMTLR-MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGG------GDPLLDQHLFWWFGHPEVYILILP 217
|
..
gi 2178351184 243 AF 244
Cdd:pfam00115 218 AF 219
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-265 |
3.49e-39 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 144.31 E-value: 3.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 1 HKRLGIYYLLSAFIFGISGTLISILIRIE--LYSSGNRIISPENQnfYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIF 78
Cdd:PRK15017 54 HKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 79 QGSPEVVYPRINNFSILILSLSYLFVILSL-ISEFGGgTGWTLYPPLSTsfLSLSPS-STGNLIFGLLISGISSCLTSLN 156
Cdd:PRK15017 131 IGARDVAFPFLNNLSFWFTVVGVILVNVSLgVGEFAQ-TGWLAYPPLSG--IEYSPGvGVDYWIWSLQLSGIGTTLTGIN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 157 FWTTIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEV 236
Cdd:PRK15017 208 FFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEV 287
|
250 260
....*....|....*....|....*....
gi 2178351184 237 YILIVPAFGIISIIISGILQKIIFGNQSM 265
Cdd:PRK15017 288 YILILPVFGVFSEIAATFSRKRLFGYTSL 316
|
|
|