|
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 ... |
3-238 |
7.20e-95 |
|
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: 285.92 E-value: 7.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIA---VLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:cd01663 130 SGPSVDLAIFSLHLAGISSILGAINFITTIFnmrAPGMTLEKMP--LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:cd01663 208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGnpfSTISLD--IWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYV 236
Cdd:cd01663 288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG---GSIKFEtpMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364
|
..
gi 963775344 237 IA 238
Cdd:cd01663 365 VA 366
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
2.73e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 269.82 E-value: 2.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTI---AVLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00153 140 SVDLAIFSLHLAGISSILGAINFITTIinmRSKGMTLDRMP--LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00153 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDV 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00153 298 DTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW-ALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-238 |
4.54e-73 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 231.17 E-value: 4.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:COG0843 143 VGVDLWLLGLALFGVGSILGGVNFIVTILKMrapGMTLMRMP--LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:COG0843 221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGN--PFSTISLdiwYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:COG0843 301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGriRFTTPML---FALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-238 |
2.75e-68 |
|
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: 217.86 E-value: 2.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:TIGR02891 134 VGVDLWLLGLHLLGISSILGAVNFIVTILNMrapGMTLMRMP--LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTH 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:TIGR02891 212 FFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPP 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFM-GNPfsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:TIGR02891 292 LALAFFSAATMLIAVPTGVKVFNWIATLWgGSI--RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
7-238 |
9.99e-53 |
|
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: 175.84 E-value: 9.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 7 VDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTqfydas 86
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 87 FNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDTRAY 166
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQAL 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 963775344 167 FSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:pfam00115 272 FSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343
|
|
|
|
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 ... |
3-238 |
7.20e-95 |
|
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: 285.92 E-value: 7.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIA---VLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:cd01663 130 SGPSVDLAIFSLHLAGISSILGAINFITTIFnmrAPGMTLEKMP--LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:cd01663 208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGnpfSTISLD--IWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYV 236
Cdd:cd01663 288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG---GSIKFEtpMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364
|
..
gi 963775344 237 IA 238
Cdd:cd01663 365 VA 366
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
2.73e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 269.82 E-value: 2.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTI---AVLGVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00153 140 SVDLAIFSLHLAGISSILGAINFITTIinmRSKGMTLDRMP--LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00153 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDV 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00153 298 DTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW-ALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
1.77e-83 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 257.60 E-value: 1.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWC-LFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFYD 84
Cdd:MTH00223 139 SVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLpLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 85 ASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDT 163
Cdd:MTH00223 219 PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKeVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDT 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 963775344 164 RAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTiSLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00223 299 RAYFTAATMIIAVPTGIKVFSWLATIYGSKIKY-EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVA 372
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
3-238 |
1.40e-80 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 249.98 E-value: 1.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00167 139 AGASVDLAIFSLHLAGVSSILGSINFITTIINMkppGITQYQTP--LFVWSILVTTILLLLSLPVLAAAITMLLTDRNLN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGK-LVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00167 217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKkEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00167 297 MDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI-KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
3-238 |
3.91e-78 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 243.85 E-value: 3.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLST-IAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:MTH00116 139 AGASVDLAIFSLHLAGVSSILGAINFITTcINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLE 160
Cdd:MTH00116 219 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMD 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 161 TDTRAYFSAITMMIAIPTGTKIFNWLSTFMGnpfSTISLD--IWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00116 299 VDTRAYFTSATMIIAIPTGIKVFSWLATLHG---GTIKWDppMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVA 375
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
3.33e-77 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 241.51 E-value: 3.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00079 142 SVDLAIFSLHCAGISSILGGINFMVTTKNLrssSISLEHMS--LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQ-TLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00079 220 FDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQsTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDL 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00079 300 DSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLW-VLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVS 375
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
6.94e-76 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 238.08 E-value: 6.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00142 140 SVDLAIFSLHLAGVSSILGAINFITTVINMragGMKFERVP--LFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSF 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00142 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKeVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDV 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFStISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00142 298 DTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVK-YEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVA 373
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
6-238 |
3.97e-73 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 230.94 E-value: 3.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00007 139 SVDLAIFSLHLAGVSSILGAINFITTVINMrwkGLRLERIP--LFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00007 217 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDV 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00007 297 DTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLW-ALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVA 372
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-238 |
4.54e-73 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 231.17 E-value: 4.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:COG0843 143 VGVDLWLLGLALFGVGSILGGVNFIVTILKMrapGMTLMRMP--LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:COG0843 221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGN--PFSTISLdiwYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:COG0843 301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGriRFTTPML---FALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
3-238 |
4.64e-73 |
|
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: 4.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL-GVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:cd00919 127 SGVGVDLAILGLHLAGVSSILGAINFITTILNMrAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTS 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:cd00919 207 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPV 286
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNP--FSTISLdiwYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:cd00919 287 DTRAYFTAATMIIAVPTGIKVFNWLATLWGGRirFDPPML---FALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVA 362
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
3-238 |
6.55e-71 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 225.48 E-value: 6.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00184 141 SGGSVDMAIFSLHLAGISSILGAMNFITTIFNMrapGITMDRMP--LFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLST-SAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00184 219 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTfAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00184 299 MDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLW-AIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVA 377
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
1.92e-70 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 223.94 E-value: 1.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00037 142 SVDLAIFSLHLAGASSILASINFITTIINMrtpGMTFDRLP--LFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00037 220 FDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDV 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00037 300 DTRAYFTAATMIIAVPTGIKVFSWMATLQGSNL-RWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVA 375
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
2.17e-70 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 224.03 E-value: 2.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00183 142 SVDLTIFSLHLAGVSSILGAINFITTIINMkppAISQYQTP--LFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00183 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDV 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00183 300 DTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLW-ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
6-238 |
1.54e-69 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 221.68 E-value: 1.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00103 142 SVDLTIFSLHLAGVSSILGAINFITTIINMkppAMSQYQTP--LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKL-VFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00103 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDV 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00103 300 DTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLW-ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
6-238 |
4.40e-69 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 220.58 E-value: 4.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 6 SVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQF 82
Cdd:MTH00077 142 SVDLTIFSLHLAGVSSILGAINFITTSINMkppSMSQYQTP--LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 83 YDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLS-TSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:MTH00077 220 FDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTyYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNV 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00077 300 DTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLW-ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
3-238 |
7.11e-69 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 220.08 E-value: 7.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00182 141 SGGAVDMAIFSLHLAGVSSILGAINFITTIFNMrapGVTFNRLP--LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLST-SAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00182 219 TTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTfVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00182 299 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLW-AMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVA 377
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-238 |
2.75e-68 |
|
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: 217.86 E-value: 2.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 5 TSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQ 81
Cdd:TIGR02891 134 VGVDLWLLGLHLLGISSILGAVNFIVTILNMrapGMTLMRMP--LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTH 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 82 FYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLET 161
Cdd:TIGR02891 212 FFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPP 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 963775344 162 DTRAYFSAITMMIAIPTGTKIFNWLSTFM-GNPfsTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:TIGR02891 292 LALAFFSAATMLIAVPTGVKVFNWIATLWgGSI--RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
7-238 |
2.88e-67 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 215.70 E-value: 2.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 7 VDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFYDAS 86
Cdd:MTH00048 142 VDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 87 FNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQT-LSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDTRA 165
Cdd:MTH00048 222 GGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHIcLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAV 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 963775344 166 YFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:MTH00048 302 FFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVA 374
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-238 |
6.71e-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: 214.37 E-value: 6.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 7 VDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFY 83
Cdd:cd01662 137 VDYWILGLQFSGIGTLLGAINFIVTILKMrapGMTLMRMP--IFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFF 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 84 DASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDT 163
Cdd:cd01662 215 TNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALV 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 963775344 164 RAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:cd01662 295 NAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLW-AIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVA 368
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
3-238 |
2.11e-63 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 206.40 E-value: 2.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 3 SPTSVDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLN 79
Cdd:MTH00026 140 SGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMrtpGMTMSRIP--LFVWSVFITAILLLLSLPVLAGAITMLLTDRNFN 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 80 TQFYDASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLST-SAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVG 158
Cdd:MTH00026 218 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLfSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 159 LETDTRAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTI-SLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVI 237
Cdd:MTH00026 298 MDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLIfTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVV 377
|
.
gi 963775344 238 A 238
Cdd:MTH00026 378 A 378
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
7-238 |
9.99e-53 |
|
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: 175.84 E-value: 9.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 7 VDLIVFGLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTqfydas 86
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 87 FNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDTRAY 166
Cdd:pfam00115 192 GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQAL 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 963775344 167 FSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWYALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:pfam00115 272 FSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
7-238 |
1.95e-44 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 157.79 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 7 VDLIVFGLAISGISSFLSSVNFLSTIAVL---GVTNGAKPwcLFTWAIVFTAIMLIATLPILTGGLLMLVLDLHLNTQFY 83
Cdd:PRK15017 187 VDYWIWSLQLSGIGTTLTGINFFVTILKMrapGMTMFKMP--VFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFF 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 84 DASFNGDPVLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMTVGLETDT 163
Cdd:PRK15017 265 TNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANV 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 963775344 164 RAYFSAITMMIAIPTGTKIFNWLSTFMGNPFSTISLDIWyALSFIFLFTLGGTTGVVLGNSAIDVALHDTYYVIA 238
Cdd:PRK15017 345 NAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLW-TIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIA 418
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
13-236 |
7.83e-04 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 39.96 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 13 GLAISGISSFLSSVNFLSTIAVLGVTNGAKPWCLFTWAIVFTAIM-LIATLPILTGGLLMLVLDLHLNTQfydasfNGDP 91
Cdd:cd01660 128 GAALVVVGSWISGFAMFVTLWRWKKANPGKKVPLATFMVVTTMILwLVASLGVALEVLFQLLPWSLGLVD------TVDV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 92 VLYQHLFWFFGHPEVYIIILPAFGVISQTLSTSAGKLVFGGPSMILAMGCITVLGSLVWAHHMMT-VGLETDTRAYFSAI 170
Cdd:cd01660 202 LLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 963775344 171 TMMIAIPT-------------------GTKIFNWLSTFMGNPFSTISLdiwyALSFIFlFTLGGTTGVVLGNSAIDVALH 231
Cdd:cd01660 282 TFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLAL----FLAMLM-FIPGGAGGIINASYQLNYVVH 356
|
....*
gi 963775344 232 DTYYV 236
Cdd:cd01660 357 NTAWV 361
|
|
|