|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
5.36e-171 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 472.13 E-value: 5.36e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-260 |
3.95e-133 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 376.37 E-value: 3.95e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 6 HSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLL--SLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTlfIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 84 ILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHAL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 164 TLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 1569642037 244 FVDIIWLFLYMTIYWWG 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
7.14e-124 |
|
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: 352.20 E-value: 7.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 18 IFGAAAALLTTSGLIMWFHHNSSQLL-SLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEAFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLlFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 97 FFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTAL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 177 QAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1569642037 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-259 |
8.13e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 159.63 E-value: 8.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 70 HHTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLAptpelGGQWPpTGIKPLNPLeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 150 SITESNRKQAIHALTLTILLGFYFTALQAMEYYE---APFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFH 226
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1569642037 227 FTSNHHFGFEAAAWYWHFVDIIWLFLYMTIYWW 259
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
118-261 |
7.16e-12 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 62.27 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 118 PTGiKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTALQAMEYYEApfsIADG------ 191
Cdd:TIGR02842 34 PSG-KEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFYHL---IAEGngpdrs 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 192 VYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIYWWGA 261
Cdd:TIGR02842 110 AFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLGV 179
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
5.36e-171 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 472.13 E-value: 5.36e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
2.49e-152 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 424.95 E-value: 2.49e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-261 |
5.86e-149 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 416.43 E-value: 5.86e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.77e-148 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 415.30 E-value: 1.77e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-260 |
5.03e-146 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 408.98 E-value: 5.03e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 2 AHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 82 GMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIH 161
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 162 ALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 1569642037 242 WHFVDIIWLFLYMTIYWWG 260
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
3-257 |
1.91e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 386.84 E-value: 1.91e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 3 HQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYG 82
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 83 MILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHA 162
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 163 LTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYW 242
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1569642037 243 HFVDIIWLFLYMTIY 257
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-260 |
3.95e-133 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 376.37 E-value: 3.95e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 6 HSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLL--SLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTlfIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 84 ILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHAL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 164 TLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 1569642037 244 FVDIIWLFLYMTIYWWG 260
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-260 |
6.36e-132 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 373.29 E-value: 6.36e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQaHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00039 1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00039 80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239
|
250 260
....*....|....*....|
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWG 260
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
6-260 |
1.97e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 364.21 E-value: 1.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 6 HSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTL 165
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 166 TILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 1569642037 246 DIIWLFLYMTIYWWG 260
Cdd:MTH00141 244 DVVWLFLYLSIYWWG 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
7.14e-124 |
|
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: 352.20 E-value: 7.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 18 IFGAAAALLTTSGLIMWFHHNSSQLL-SLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEAFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLlFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 97 FFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTAL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 177 QAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1569642037 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.40e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 349.86 E-value: 1.40e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00219 2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00219 82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
8.90e-121 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 345.24 E-value: 8.90e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00052 2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00052 82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-261 |
5.47e-119 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 340.58 E-value: 5.47e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 1 MAHQAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 81 YGMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAI 160
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 161 HALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 1569642037 241 YWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
6-261 |
1.85e-112 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 324.10 E-value: 1.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 6 HSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTL 165
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 166 TILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1569642037 246 DIIWLFLYMTIYWWGA 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
2.14e-93 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 276.95 E-value: 2.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 6 HSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESN---------- 155
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 156 --------------------------RKQAIHALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVI 209
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1569642037 210 IGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIYWWGA 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
4-261 |
9.33e-89 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 264.22 E-value: 9.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 4 QAHSYHMVDPSPWPIFGAAAALLTTSGLIMWFH--HNSSQLLSLGLLSMALVMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
Cdd:PLN02194 5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 82 GMILFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIH 161
Cdd:PLN02194 85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 162 ALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWY 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
|
250 260
....*....|....*....|
gi 1569642037 242 WHFVDIIWLFLYMTIYWWGA 261
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-260 |
2.08e-75 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 229.84 E-value: 2.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 6 HSYHMVDPSPWPIFGAAAALLTTSGLIMWFHHNSSQLLSLGLLSMALVMLQWWRDIVREStFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPTGIKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNrKQAIHALTL 165
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 166 TILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*
gi 1569642037 246 DIIWLFLYMTIYWWG 260
Cdd:MTH00083 241 DVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
71-259 |
7.58e-68 |
|
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: 207.83 E-value: 7.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 71 HTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLAPTPELGgqwpptgiKPLNPLEVPLLNTAILLASGVTVTWAHHS 150
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 151 IT--ESNRKQAIHALTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFT 228
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1569642037 229 SNHHFGFEAAAWYWHFVDIIWLFLYMTIYWW 259
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-259 |
8.13e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 159.63 E-value: 8.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 70 HHTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLAptpelGGQWPpTGIKPLNPLeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 150 SITESNRKQAIHALTLTILLGFYFTALQAMEYYE---APFSIADGVYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFH 226
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1569642037 227 FTSNHHFGFEAAAWYWHFVDIIWLFLYMTIYWW 259
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
131-257 |
9.02e-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: 102.31 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 131 LLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTALQAMEYYE---APFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1569642037 208 VIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIY 257
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
123-259 |
1.49e-21 |
|
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: 88.58 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 123 PLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTALQAMEYYEAPFSI---ADGVYGSTFFV 199
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 200 ATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIYWW 259
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
131-257 |
1.56e-19 |
|
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: 83.44 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 131 LLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTALQAME---YYEAPFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1569642037 208 VIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIY 257
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
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| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
126-257 |
2.53e-18 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 80.73 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 126 PLEVPLLNTAILLASGVTVTWAHHSI-TESNRKQaihaLTLTILLGFYFTALQAMEYYEAPFSIADGVYGSTFFVATGFH 204
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1569642037 205 GLHVIIGSsfltICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIY 257
Cdd:MTH00049 165 FSHVVLGV----VGLSTLLLVGSSSFGVYRSTVLTWYWHFVDYIWLLVYLIVY 213
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|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
126-259 |
5.56e-15 |
|
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: 71.38 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 126 PLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTALQAMEYYEAPFSIADG---------VYGST 196
Cdd:cd02864 59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGAS 138
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1569642037 197 FFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHF-GFEAAAWYWHFVDIIWLFLYMTIYWW 259
Cdd:cd02864 139 FFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
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| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
118-261 |
7.16e-12 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 62.27 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 118 PTGiKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTALQAMEYYEApfsIADG------ 191
Cdd:TIGR02842 34 PSG-KEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFYHL---IAEGngpdrs 109
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 192 VYGSTFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIYWWGA 261
Cdd:TIGR02842 110 AFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLGV 179
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| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
118-261 |
1.46e-10 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 59.02 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569642037 118 PTGiKPLNPLEVPLLNTAILLASGVTVTWAHHSITESNRKQAIHALTLTILLGFYFTAlqaMEYYEAPFSIADGvYG--- 194
Cdd:PRK10663 58 PTG-KDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIG---MEIYEFHHLIVEG-MGpdr 132
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1569642037 195 ----STFFVATGFHGLHVIIGSSFLTICLLRLIKFHFTSNHHFGFEAAAWYWHFVDIIWLFLYMTIYWWGA 261
Cdd:PRK10663 133 sgflSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
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