|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
7.24e-162 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 448.86 E-value: 7.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 5 NNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 85 MILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 165 LMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2473932294 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
4.47e-128 |
|
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: 362.99 E-value: 4.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 20 LTAAIGAMVTASGLAKWFHMFSNSLMFN-GMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMILFISSEVLFFLS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFlGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 99 FFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMITVILGMYFTCL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 179 QWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2473932294 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
8.02e-128 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 362.88 E-value: 8.02e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNS--LMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 87 LFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLM 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 167 ITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 2473932294 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
7.71e-55 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 175.04 E-value: 7.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 72 LHTMLVSKGLRWGMILFISSEVLFFLSFFWAYFHSSLSPTielgmmWPPEGIKPFNPmQVPLLNTVILLSSGITITWSHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 152 SLMESNHSMSIQGLMITVILGMYFTCLQWYEY---WESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2473932294 229 FSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
84-259 |
8.87e-09 |
|
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: 53.71 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 84 GMILFISSEVLFFLSFFWAYFhsslspTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQ 163
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYL------VLQHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 164 GLMITVILGMYFTCLQWYE---YWESPFTISDAIYGSTFFMATGFHGMHV---IIGTTFLLICLTRHYYNHFSNNHHFgf 237
Cdd:TIGR02897 87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF-- 164
|
170 180
....*....|....*....|..
gi 2473932294 238 eAAAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 165 -IVSLYWHFLDVVWVFIFTAVY 185
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
7.24e-162 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 448.86 E-value: 7.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 5 NNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 85 MILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 165 LMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2473932294 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-261 |
1.11e-150 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 420.90 E-value: 1.11e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 4 TNNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRW 83
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 84 GMILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQ 163
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 164 GLMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWY 243
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*...
gi 2473932294 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWW 259
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
9-261 |
6.27e-145 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 406.28 E-value: 6.27e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMILF 88
Cdd:MTH00189 6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 89 ISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMIT 168
Cdd:MTH00189 86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 169 VILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00189 166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245
|
250
....*....|...
gi 2473932294 249 VVWLFLYISIYWW 261
Cdd:MTH00189 246 VVWLFLYVSIYWW 258
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
7.02e-141 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 395.80 E-value: 7.02e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 88 FISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMI 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 168 TVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 2473932294 248 DVVWLFLYISIYWWS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWG 258
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
5-261 |
4.47e-139 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 391.40 E-value: 4.47e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 5 NNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWG 84
Cdd:MTH00039 2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 85 MILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQG 164
Cdd:MTH00039 82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 165 LMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYW 244
Cdd:MTH00039 162 LFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYW 241
|
250
....*....|....*..
gi 2473932294 245 HFVDVVWLFLYISIYWW 261
Cdd:MTH00039 242 HFVDVVWLFLYVCIYWW 258
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
9-261 |
1.72e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 377.18 E-value: 1.72e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMILF 88
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 89 ISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMIT 168
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 169 VILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|...
gi 2473932294 249 VVWLFLYISIYWW 261
Cdd:MTH00130 247 VVWLFLYISIYWW 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-261 |
2.29e-133 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 377.14 E-value: 2.29e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 4 TNNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRW 83
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 84 GMILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQ 163
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 164 GLMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWY 243
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250
....*....|....*...
gi 2473932294 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWW 259
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-261 |
5.13e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 368.73 E-value: 5.13e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 2 MTTNNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGL 81
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 82 RWGMILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMS 161
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 162 IQGLMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAA 241
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|
gi 2473932294 242 WYWHFVDVVWLFLYISIYWW 261
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWW 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
10-261 |
6.34e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 368.30 E-value: 6.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 10 YHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMILFI 89
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 90 SSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMITV 169
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 170 ILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|..
gi 2473932294 250 VWLFLYISIYWW 261
Cdd:MTH00075 248 VWLFLYVSIYWW 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
4.47e-128 |
|
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: 362.99 E-value: 4.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 20 LTAAIGAMVTASGLAKWFHMFSNSLMFN-GMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMILFISSEVLFFLS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFlGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 99 FFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMITVILGMYFTCL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 179 QWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2473932294 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
8.02e-128 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 362.88 E-value: 8.02e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNS--LMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 87 LFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLM 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 167 ITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 2473932294 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-261 |
3.46e-121 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 346.05 E-value: 3.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 88 FISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMI 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 168 TVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....
gi 2473932294 248 DVVWLFLYISIYWW 261
Cdd:MTH00009 244 DVVWIFLYLCIYWW 257
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
9-261 |
4.34e-121 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 345.97 E-value: 4.34e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMILF 88
Cdd:MTH00024 7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 89 ISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQGLMIT 168
Cdd:MTH00024 87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 169 VILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246
|
250
....*....|...
gi 2473932294 249 VVWLFLYISIYWW 261
Cdd:MTH00024 247 VVWLFLYLCIYWW 259
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
2-261 |
3.09e-113 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 325.98 E-value: 3.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 2 MTTNNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGL 81
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 82 RWGMILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMS 161
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 162 IQGLMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAA 241
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|
gi 2473932294 242 WYWHFVDVVWLFLYISIYWW 261
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWW 260
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-261 |
6.48e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 288.50 E-value: 6.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSKGLRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 88 FISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMS------ 161
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASlekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 162 ------------------------------IQGLMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrtnaVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2473932294 212 IGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWW 295
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-261 |
8.44e-90 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 266.91 E-value: 8.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 2 MTTNNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNS--LMFNGMMITLLTMYQWWRDIVRESTFQGLHTMLVSK 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGarLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 80 GLRWGMILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHS 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 160 MSIQGLMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|..
gi 2473932294 240 AAWYWHFVDVVWLFLYISIYWW 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWW 262
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
10-262 |
2.56e-70 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 216.75 E-value: 2.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 10 YHLVDKSPWPLTAAIGAMVTASGLAKWFHMFSNSLMFNGMMITLLTMYQWWRDIVREStFQGLHTMLVSKGLRWGMILFI 89
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 90 SSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIqGLMITV 169
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 170 ILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|...
gi 2473932294 250 VWLFLYISIYWWS 262
Cdd:MTH00083 243 VWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
3.85e-70 |
|
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: 213.60 E-value: 3.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 73 HTMLVSKGLRWGMILFISSEVLFFLSFFWAYFHSSLSPTIELGMmwppegikPFNPMQVPLLNTVILLSSGITITWSHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 153 LM--ESNHSMSIQGLMITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2473932294 231 NNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
7.71e-55 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 175.04 E-value: 7.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 72 LHTMLVSKGLRWGMILFISSEVLFFLSFFWAYFHSSLSPTielgmmWPPEGIKPFNPmQVPLLNTVILLSSGITITWSHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 152 SLMESNHSMSIQGLMITVILGMYFTCLQWYEY---WESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2473932294 229 FSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
84-259 |
5.33e-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: 87.29 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 84 GMILFISSEVLFFLSFFWAYF-HSSLSP--------TIELGMmwppegikpfnpmqvPLLNTVILLSSGITITWSHHSLM 154
Cdd:cd02862 12 GMWVFILSELLAFGALFIAYAvYRALYPelfaagsaHLDLLL---------------GALNTLVLLTSSFTVALAVRAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 155 ESNHSMSIQGLMITVILGMYFTCLQWYEY-WEspFTISDAIYGSTFFMA----TGFHGMHVIIGTTFLLICLTRHYYNHF 229
Cdd:cd02862 77 AGRRRRARRWLAAAVLLGLVFLVIKYFEYaHK--IAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRY 154
|
170 180 190
....*....|....*....|....*....|
gi 2473932294 230 SNNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 155 SARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
80-261 |
3.61e-18 |
|
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: 79.72 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 80 GLRWGMILFISSEVLFFLSFFWAYFHSSLSPTielgmMWPPEgikPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHS 159
Cdd:cd02865 8 PGWWGLWVFMAVEGTLFALLISAYFMRMTSGD-----WQPGA---PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 160 MSIQGLMITVILGMYFTCLQWYEYWESPF---TISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFG 236
Cdd:cd02865 80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159
|
170 180
....*....|....*....|....*
gi 2473932294 237 FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 160 VELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
84-261 |
1.66e-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: 75.62 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 84 GMILFISSEVLFFLSFFWAYFHSSLSPTIELGMMWPPEGIkPFNPMQVPL----LNTVILLSSGITITWSHHSLMESNHS 159
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 160 MSIQGLMITVILGMYFTCLQWYEY-----------WESPFTIsdAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNH 228
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGA--AQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 2473932294 229 FSNNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 169 YQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
87-259 |
4.70e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.57 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 87 LFISSEVLFFLSFFWAYFHSSLSPTIELGmmwppegikpfNPMQVPLLNTVILLSSGITITwSHHSLMESNHSMSIqgLM 166
Cdd:MTH00049 59 LFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 167 ITVILGMYFTCLQWYEYWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLtrhYYNHFSNNHHFGfEAAAWYWHF 246
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLL---LVGSSSFGVYRS-TVLTWYWHF 200
|
170
....*....|...
gi 2473932294 247 VDVVWLFLYISIY 259
Cdd:MTH00049 201 VDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
84-259 |
3.76e-14 |
|
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: 68.81 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 84 GMILFISSEVLFFLSFFWAYFhsSLSPTIELGmmwpPEGIKPFNPMQVpLLNTVILLSSGITITWSHHSLMESNHSMSIQ 163
Cdd:cd02863 12 GFWIYLMSDCILFATLFATYA--VLSGNTAGG----PPGHELFELPLV-FIETFLLLLSSFTCGLAMIAMNKNNKKKVIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 164 GLMITVILGMYFTCLQWYE---YWESPFTISDAIYGSTFFMATGFHGMHVIIGTTFLLICLTRHYYNHFSNNHHFGFEAA 240
Cdd:cd02863 85 WLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCL 164
|
170
....*....|....*....
gi 2473932294 241 AWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 165 SLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
84-259 |
8.87e-09 |
|
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: 53.71 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 84 GMILFISSEVLFFLSFFWAYFhsslspTIELGMMWPPEGIKPFNPMQVPLLNTVILLSSGITITWSHHSLMESNHSMSIQ 163
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYL------VLQHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 164 GLMITVILGMYFTCLQWYE---YWESPFTISDAIYGSTFFMATGFHGMHV---IIGTTFLLICLTRHYYNHFSNNHHFgf 237
Cdd:TIGR02897 87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF-- 164
|
170 180
....*....|....*....|..
gi 2473932294 238 eAAAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 165 -IVSLYWHFLDVVWVFIFTAVY 185
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-259 |
3.01e-06 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 46.70 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932294 133 LLNTVILLSSGITITWSHHSLMESNHSMSIQGLMITVILGMYFTCLQWYEYW---ESPFTISDAIYGSTFFMATGFHGMH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2473932294 210 VIIGTTFLLICLTRHYYNHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
|
|
|