|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-261 |
3.23e-173 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 477.68 E-value: 3.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-261 |
3.31e-133 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 376.37 E-value: 3.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHY--NSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 84 VLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQAL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 164 FITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2029229567 244 FVDVVWLFLYVSIYWWGS 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 |
2.08e-122 |
|
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: 348.35 E-value: 2.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 18 LTGALSALLMTSGLIMWFHYNSMSLLTLG-LTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRYGMVLFIVSEVFFFAG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFLgLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 97 FFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLGVYFTLL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 177 QASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2029229567 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-259 |
7.31e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 157.32 E-value: 7.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 70 HRTPIVQKGLRYGMVLFIVSEVFF-FAGFFWAFYHSSLAPtpelggcWPPTGIIPLNPLeVPLLNTSVLLASGVSITWAH 148
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 149 HSLMEGNRKHMLQALFITISLGVYFTLLQASEYYE---TSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHY 225
Cdd:COG1845 79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158
|
170 180 190
....*....|....*....|....*....|....
gi 2029229567 226 HFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
127-260 |
2.44e-11 |
|
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: 61.02 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 127 LEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLG---VYFTLLQASEYYETSFTISDGVYGSTFFMATGF 203
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029229567 204 HGLHVIIGsTFLIVCFLRQLHYH-FTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 132 HGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-261 |
3.23e-173 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 477.68 E-value: 3.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
2.00e-167 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 462.88 E-value: 2.00e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
3.74e-154 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 429.57 E-value: 3.74e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
2.44e-151 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 422.23 E-value: 2.44e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-261 |
2.62e-150 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 419.76 E-value: 2.62e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRY 81
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 82 GMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 162 ALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWY 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 2029229567 242 WHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
3-257 |
5.38e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 393.39 E-value: 5.38e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRYG 82
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 83 MVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 163 LFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYW 242
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2029229567 243 HFVDVVWLFLYVSIY 257
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
2.78e-134 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 379.23 E-value: 2.78e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRYGMVL 85
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 86 FIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 166 TISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2029229567 246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-261 |
3.31e-133 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 376.37 E-value: 3.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHY--NSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 84 VLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQAL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 164 FITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 2029229567 244 FVDVVWLFLYVSIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-261 |
2.48e-132 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 374.45 E-value: 2.48e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQtHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00039 1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00039 80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
1.18e-126 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 359.87 E-value: 1.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00219 2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00219 82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWGS 262
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-259 |
2.08e-122 |
|
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: 348.35 E-value: 2.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 18 LTGALSALLMTSGLIMWFHYNSMSLLTLG-LTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRYGMVLFIVSEVFFFAG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFLgLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 97 FFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLGVYFTLL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 177 QASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2029229567 257 YWW 259
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-261 |
5.54e-117 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 335.57 E-value: 5.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
5.05e-115 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 330.60 E-value: 5.05e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00052 2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
Cdd:MTH00052 82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 161 QALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241
|
250 260
....*....|....*....|.
gi 2029229567 241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
6-261 |
8.52e-115 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 329.87 E-value: 8.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRYGMVL 85
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 86 FIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 166 TISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 2029229567 246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
1-261 |
6.15e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 288.50 E-value: 6.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLR 80
Cdd:MTH00028 1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 81 YGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGN----- 155
Cdd:MTH00028 81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 156 -------------------------------RKHMLQALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFH 204
Cdd:MTH00028 161 ekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2029229567 205 GLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00028 241 GLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
4-260 |
8.80e-87 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 259.21 E-value: 8.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 4 QTHAYHMVNPSPWPLTGALSALLMTSGLIMWFH--YNSMSLLTLGLTTNLLTMYQWWRDVIREGTFQGHRTPIVQKGLRY 81
Cdd:PLN02194 5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 82 GMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
Cdd:PLN02194 85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 162 ALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWY 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
|
250
....*....|....*....
gi 2029229567 242 WHFVDVVWLFLYVSIYWWG 260
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-261 |
3.90e-73 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 224.06 E-value: 3.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHYNSMSLLTLGLTTNLLTMYQWWRDVIREGtFQGHRTPIVQKGLRYGMVL 85
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 86 FIVSEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGIIPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKhMLQALFI 165
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKS-CTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 166 TISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 2029229567 246 DVVWLFLYVSIYWWGS 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 ... |
72-259 |
3.38e-65 |
|
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: 201.28 E-value: 3.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 72 TPIVQKGLRYGMVLFIVSEVFFFAGFFWAFYHSSLAPTPELGgcwpptgiIPLNPLEVPLLNTSVLLASGVSITWAHHSL 151
Cdd:cd00386 2 TASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHASL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 152 M--EGNRKHMLQALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHYHFTS 229
Cdd:cd00386 74 AarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTP 153
|
170 180 190
....*....|....*....|....*....|
gi 2029229567 230 NHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd00386 154 RHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-259 |
7.31e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 157.32 E-value: 7.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 70 HRTPIVQKGLRYGMVLFIVSEVFF-FAGFFWAFYHSSLAPtpelggcWPPTGIIPLNPLeVPLLNTSVLLASGVSITWAH 148
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 149 HSLMEGNRKHMLQALFITISLGVYFTLLQASEYYE---TSFTISDGVYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLHY 225
Cdd:COG1845 79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158
|
170 180 190
....*....|....*....|....*....|....
gi 2029229567 226 HFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
131-257 |
6.30e-21 |
|
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: 86.91 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 131 LLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLGVYFTLLQASEYYE---TSFTISDGVYGSTFFMATGFHGLH 207
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2029229567 208 VIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
80-259 |
1.04e-17 |
|
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: 78.70 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 80 RYGMVLFIVSEVFFFAGFFWAfYHSSLAPTPELGGCWPPTGIIPLNPLEVPL----LNTSVLLASGVSITWAHHSLMEGN 155
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIA-YMTARISTTEPWPLPSDVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 156 RKHMLQALFITISLGVYFTLLQASEYyeTSFTISDGV-----------YGSTFFMATGFHGLHVIIGSTFLIVCFLRQLH 224
Cdd:cd02864 89 RKAAARLMLATALLGATFVGMQAFEW--TKLIVEEGVrpwgnpwgaaqFGASFFMITGFHGTHVTIGVIYLIIIARKVWR 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 2029229567 225 YHFTSNHHF-GFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02864 167 GKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
131-257 |
2.21e-16 |
|
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: 74.97 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 131 LLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLGVYFTLLQASE---YYETSFTISDGVYGSTFFMATGFHGLH 207
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2029229567 208 VIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
126-257 |
2.28e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 75.34 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 126 PLEVPLLNTSVLLASGVSITWAHHSLmegNRKHMLQALFITISLGVYFTLLQASEYYETSFTISDGVYGSTFFMATGFHG 205
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2029229567 206 LHVIIGSTFLIVCFLRQLHYHFTSNHHFgfeaAAWYWHFVDVVWLFLYVSIY 257
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
123-259 |
2.64e-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: 239216 Cd Length: 184 Bit Score: 74.71 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 123 PLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLGVYFTLLQASEYYETSF---TISDGVYGSTFFM 199
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 200 ATGFHGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
127-260 |
2.44e-11 |
|
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: 61.02 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 127 LEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLG---VYFTLLQASEYYETSFTISDGVYGSTFFMATGF 203
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGagfVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029229567 204 HGLHVIIGsTFLIVCFLRQLHYH-FTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 132 HGCHVTLG-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
131-261 |
4.41e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 49.01 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029229567 131 LLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITISLGVYFTllqASEYYETSFTISDGvYG-------STFFMATGF 203
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAFFALVGT 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029229567 204 HGLHVIIGSTFLIVCFLRQLHYHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:PRK10663 146 HGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
