|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
0e+00 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 497.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-261 |
8.96e-142 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 397.94 E-value: 8.96e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 6 HSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSP--YLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGnmTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 84 VLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQAL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 164 TLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1919576645 244 FVDVVWLFLYMTIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
8.79e-132 |
|
Cytochrome c oxidase subunit III. 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. CcO 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, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.
Pssm-ID: 238834 Cd Length: 243 Bit Score: 372.23 E-value: 8.79e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 18 IFGAGAALLTTSGLTMWFH-YNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMVLFITSEAFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 97 FFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTGL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 177 QAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1919576645 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-259 |
1.18e-50 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 164.25 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 70 HHTPTVQKGLRYGMVLFITSEAFFFLGFFWAFFHSSLAptpelGGQWPPvGIKPLNPMeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 150 SIMEANRKQAIQALTLTVLLGFYFTGLQAMEYYE---APFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFH 226
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1919576645 227 FTPNHHFGFEAAAWYWHFVDVVWLFLYMTIYWW 259
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
131-260 |
6.03e-12 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III 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: 131943 Cd Length: 190 Bit Score: 62.95 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 131 LLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTGLQAME---YYEAPFSIADGVYGSTFFVATGFHGLH 207
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1919576645 208 VIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTIYWWG 260
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
0e+00 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 497.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.78e-159 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 443.05 E-value: 1.78e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-261 |
1.95e-158 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 440.32 E-value: 1.95e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
2.29e-156 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 434.94 E-value: 2.29e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-261 |
6.47e-156 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 434.02 E-value: 6.47e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 2 AHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 82 GMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQ 161
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 162 ALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 1919576645 242 WHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
3-257 |
1.70e-147 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 412.27 E-value: 1.70e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 3 HQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 83 MVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQA 162
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 163 LTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYW 242
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1919576645 243 HFVDVVWLFLYMTIY 257
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-261 |
8.96e-142 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 397.94 E-value: 8.96e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 6 HSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSP--YLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGnmTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 84 VLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQAL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 164 TLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1919576645 244 FVDVVWLFLYMTIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-261 |
2.79e-140 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 394.48 E-value: 2.79e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQaHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00039 1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00039 80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
9.61e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 393.10 E-value: 9.61e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 6 HSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMVL 85
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQALTL 165
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 166 TVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1919576645 246 DVVWLFLYMTIYWWGS 261
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
8.79e-132 |
|
Cytochrome c oxidase subunit III. 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. CcO 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, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.
Pssm-ID: 238834 Cd Length: 243 Bit Score: 372.23 E-value: 8.79e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 18 IFGAGAALLTTSGLTMWFH-YNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMVLFITSEAFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 97 FFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTGL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 177 QAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1919576645 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
2.90e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 364.11 E-value: 2.90e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00052 2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00052 82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
4.51e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 363.72 E-value: 4.51e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00219 2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00219 82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-261 |
1.75e-126 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 359.45 E-value: 1.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 1 MAHQAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 81 YGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAI 160
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 161 QALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 1919576645 241 YWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
6-261 |
1.30e-118 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 339.50 E-value: 1.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 6 HSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMVL 85
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQALTL 165
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 166 TVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1919576645 246 DVVWLFLYMTIYWWGS 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
2.57e-99 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 291.97 E-value: 2.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 6 HSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMVL 85
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEAN---------- 155
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 156 --------------------------RKQAIQALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVI 209
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1919576645 210 IGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTIYWWGS 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
4-260 |
2.26e-92 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 273.08 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 4 QAHSYHMVDPSPWPIFGAGAALLTTSGLTMWFH--YNSPYLLIIGLTSTLLVMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
Cdd:PLN02194 5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 82 GMVLFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQ 161
Cdd:PLN02194 85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 162 ALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWY 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
|
250
....*....|....*....
gi 1919576645 242 WHFVDVVWLFLYMTIYWWG 260
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
1.17e-78 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 237.93 E-value: 1.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 6 HSYHMVDPSPWPIFGAGAALLTTSGLTMWFHYNSPYLLIIGLTSTLLVMLQWWRDIVREStFQGHHTPTVQKGLRYGMVL 85
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHHSIMEANrKQAIQALTL 165
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 166 TVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1919576645 246 DVVWLFLYMTIYWWGS 261
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
71-259 |
7.20e-69 |
|
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.
Pssm-ID: 238227 Cd Length: 183 Bit Score: 210.52 E-value: 7.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 71 HTPTVQKGLRYGMVLFITSEAFFFLGFFWAFFHSSLAPTPELGgqwppvgiKPLNPMEVPLLNTAILLASGVTVTWAHHS 150
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 151 IM--EANRKQAIQALTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFT 228
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1919576645 229 PNHHFGFEAAAWYWHFVDVVWLFLYMTIYWW 259
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-259 |
1.18e-50 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 164.25 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 70 HHTPTVQKGLRYGMVLFITSEAFFFLGFFWAFFHSSLAptpelGGQWPPvGIKPLNPMeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 150 SIMEANRKQAIQALTLTVLLGFYFTGLQAMEYYE---APFSIADGVYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFH 226
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1919576645 227 FTPNHHFGFEAAAWYWHFVDVVWLFLYMTIYWW 259
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
131-257 |
1.07e-27 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 105.01 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 131 LLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTGLQAMEYYE---APFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1919576645 208 VIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTIY 257
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
131-257 |
1.91e-21 |
|
Ubiquinol oxidase subunit III subfamily. 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. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 88.45 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 131 LLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTGLQAME---YYEAPFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1919576645 208 VIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTIY 257
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
116-259 |
9.20e-20 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 83.96 E-value: 9.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 116 WPPVGIKPLNpmeVPLLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTGLQAMEYYEAPFSI---ADGV 192
Cdd:cd02865 41 QPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNP 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1919576645 193 YGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTIYWW 259
Cdd:cd02865 118 AGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
126-257 |
3.25e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.95 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 126 PMEVPLLNTAILLASGVTVTWAHHSI-MEANRKQaiqaLTLTVLLGFYFTGLQAMEYYEAPFSIADGVYGSTFFVATGFH 204
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1919576645 205 GLHVIIGStFLLVCLLRLIKFHFTPNHHfgfEAAAWYWHFVDVVWLFLYMTIY 257
Cdd:MTH00049 165 FSHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
80-259 |
4.83e-16 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 74.46 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 80 RYGMVLFITSEAFFFLGFFWAFFHSSLApTPELGGQWPPVGIKPLNPMEVPL----LNTAILLASGVTVTWAHHSIMEAN 155
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIAYMTARIS-TTEPWPLPSDVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 156 RKQAIQALTLTVLLGFYFTGLQAMEYYEAPFSIADG---------VYGSTFFVATGFHGLHVIIGSTFLLVCLLRLIKFH 226
Cdd:cd02864 89 RKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 1919576645 227 FTPNHHFG-FEAAAWYWHFVDVVWLFLYMTIYWW 259
Cdd:cd02864 169 YQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
131-260 |
6.03e-12 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III 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: 131943 Cd Length: 190 Bit Score: 62.95 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 131 LLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTGLQAME---YYEAPFSIADGVYGSTFFVATGFHGLH 207
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1919576645 208 VIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTIYWWG 260
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
131-261 |
9.46e-11 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 59.79 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919576645 131 LLNTAILLASGVTVTWAHHSIMEANRKQAIQALTLTVLLGFYFTglqAMEYYEAPFSIADGvYG-------STFFVATGF 203
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAFFALVGT 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1919576645 204 HGLHVIIGSTFLLVCLLRLIKFHFTPNHHFGFEAAAWYWHFVDVVWLFLYMTIYWWGS 261
Cdd:PRK10663 146 HGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
