|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
6.77e-159 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 441.16 E-value: 6.77e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 5 NNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 85 MILFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 165 IMMTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2458278142 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
1.93e-124 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 354.41 E-value: 1.93e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNS--LMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 87 LFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIM 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 167 MTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 2458278142 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.52e-123 |
|
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: 351.43 E-value: 1.52e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 20 LTAAIGAMVTASGLAKWFHMFNNSLMLN-GIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILFISSEVLFFVS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFlGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 99 FFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMTTMLGLYFTLL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 179 QWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2458278142 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
2.85e-53 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 171.19 E-value: 2.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 72 LHTIMVSKGLRWGMILFISSEVLFFVSFFWAYFHsslaptieLGMTFP--PEGIKPFNPmQVPLLNTVVLLSSGITITWA 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFV--------LRASAPdwPAGAELLDL-PLPLINTLLLLLSSFTVALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 150 HHSLMESNYSMSIQGIMMTTMLGLYFTLLQWYEY---WESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYY 226
Cdd:COG1845 78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2458278142 227 MHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
84-259 |
3.17e-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: 55.25 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 84 GMILFISSEVLFFVSFFWAYFhsslapTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQ 163
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYL------VLQHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 164 GIMMTTMLGLYFTLLQWYE---YWESPFTISDSIYGSSFFMATGFHGIHV---IIGTTFLLVCLTRHYYMHFSNNHHFgf 237
Cdd:TIGR02897 87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF-- 164
|
170 180
....*....|....*....|..
gi 2458278142 238 eAAAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 165 -IVSLYWHFLDVVWVFIFTAVY 185
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
6.77e-159 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 441.16 E-value: 6.77e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 5 NNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWG 84
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 85 MILFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQG 164
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 165 IMMTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYW 244
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 2458278142 245 HFVDVVWLFLYISIY 259
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
9-261 |
1.83e-146 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 410.11 E-value: 1.83e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILF 88
Cdd:MTH00118 7 PYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 89 ISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMT 168
Cdd:MTH00118 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 169 TMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00118 167 ILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVD 246
|
250
....*....|...
gi 2458278142 249 VVWLFLYISIYWW 261
Cdd:MTH00118 247 VVWLFLYISIYWW 259
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
9-261 |
1.27e-142 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 400.50 E-value: 1.27e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILF 88
Cdd:MTH00189 6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 89 ISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMT 168
Cdd:MTH00189 86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 169 TMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00189 166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245
|
250
....*....|...
gi 2458278142 249 VVWLFLYISIYWW 261
Cdd:MTH00189 246 VVWLFLYVSIYWW 258
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
1.26e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 387.71 E-value: 1.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 88 FISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMM 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 168 TTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 2458278142 248 DVVWLFLYISIYWWS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWG 258
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
4-261 |
8.20e-136 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 383.31 E-value: 8.20e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 4 INNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRW 83
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 84 GMILFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQ 163
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 164 GIMMTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWY 243
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250
....*....|....*...
gi 2458278142 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWW 258
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
9-261 |
2.35e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 371.75 E-value: 2.35e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILF 88
Cdd:MTH00099 7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 89 ISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMT 168
Cdd:MTH00099 87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 169 TMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00099 167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246
|
250
....*....|...
gi 2458278142 249 VVWLFLYISIYWW 261
Cdd:MTH00099 247 VVWLFLYVSIYWW 259
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
8-261 |
3.70e-131 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 371.43 E-value: 3.70e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMIL 87
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 88 FISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMM 167
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 168 TTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....
gi 2458278142 248 DVVWLFLYISIYWW 261
Cdd:MTH00219 247 DVVWLFLYVSIYWW 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
9-261 |
6.61e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 368.32 E-value: 6.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILF 88
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 89 ISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMT 168
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 169 TMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|...
gi 2458278142 249 VVWLFLYISIYWW 261
Cdd:MTH00130 247 VVWLFLYISIYWW 259
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
10-261 |
3.36e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 361.37 E-value: 3.36e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 10 YHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILFI 89
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 90 SSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMTT 169
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 170 MLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|..
gi 2458278142 250 VWLFLYISIYWW 261
Cdd:MTH00075 248 VWLFLYVSIYWW 259
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
1.93e-124 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 354.41 E-value: 1.93e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNS--LMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 87 LFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIM 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 167 MTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 2458278142 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
1.52e-123 |
|
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: 351.43 E-value: 1.52e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 20 LTAAIGAMVTASGLAKWFHMFNNSLMLN-GIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILFISSEVLFFVS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFlGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 99 FFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMTTMLGLYFTLL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 179 QWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2458278142 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-261 |
1.13e-118 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 339.89 E-value: 1.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 88 FISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMM 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 168 TTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....
gi 2458278142 248 DVVWLFLYISIYWW 261
Cdd:MTH00009 244 DVVWIFLYLCIYWW 257
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
9-261 |
2.48e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 334.03 E-value: 2.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 9 PYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMILF 88
Cdd:MTH00024 7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 89 ISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMT 168
Cdd:MTH00024 87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 169 TMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246
|
250
....*....|...
gi 2458278142 249 VVWLFLYISIYWW 261
Cdd:MTH00024 247 VVWLFLYLCIYWW 259
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
8-261 |
5.56e-109 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 315.19 E-value: 5.56e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMIL 87
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 88 FISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMM 167
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 168 TTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....
gi 2458278142 248 DVVWLFLYISIYWW 261
Cdd:MTH00052 247 DVVWLFLFIFMYWW 260
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-261 |
2.98e-96 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 284.27 E-value: 2.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 8 QPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSKGLRWGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 88 FISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMS------ 161
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPASlekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 162 ------------------------------IQGIMMTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVI 211
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrtnaVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2458278142 212 IGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWW 295
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-261 |
1.99e-86 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 258.05 E-value: 1.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 2 MTINNNQPYHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNS--LMLNGIMITMLTMYQWWRDVTREGTLQGLHTIMVSK 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGarLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 80 GLRWGMILFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYS 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 160 MSIQGIMMTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|..
gi 2458278142 240 AAWYWHFVDVVWLFLYISIYWW 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWW 262
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
2.89e-69 |
|
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.
Pssm-ID: 238227 Cd Length: 183 Bit Score: 211.68 E-value: 2.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 73 HTIMVSKGLRWGMILFISSEVLFFVSFFWAYFHSSLAPTIELGMtfppegikPFNPMQVPLLNTVVLLSSGITITWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 153 LM--ESNYSMSIQGIMMTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2458278142 231 NNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
10-262 |
4.17e-68 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 210.97 E-value: 4.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 10 YHLVDKSPWPLTAAIGAMVTASGLAKWFHMFNNSLMLNGIMITMLTMYQWWRDVTREGtLQGLHTIMVSKGLRWGMILFI 89
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 90 SSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIqGIMMTT 169
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 170 MLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|...
gi 2458278142 250 VWLFLYISIYWWS 262
Cdd:MTH00083 243 VWLFLFVFVYWWS 255
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
2.85e-53 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 171.19 E-value: 2.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 72 LHTIMVSKGLRWGMILFISSEVLFFVSFFWAYFHsslaptieLGMTFP--PEGIKPFNPmQVPLLNTVVLLSSGITITWA 149
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFV--------LRASAPdwPAGAELLDL-PLPLINTLLLLLSSFTVALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 150 HHSLMESNYSMSIQGIMMTTMLGLYFTLLQWYEY---WESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYY 226
Cdd:COG1845 78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2458278142 227 MHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
84-259 |
3.90e-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: 87.68 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 84 GMILFISSEVLFFVSFFWAYF-HSSLAP--------TIELGMTfppegikpfnpmqvpLLNTVVLLSSGITITWAHHSLM 154
Cdd:cd02862 12 GMWVFILSELLAFGALFIAYAvYRALYPelfaagsaHLDLLLG---------------ALNTLVLLTSSFTVALAVRAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 155 ESNYSMSIQGIMMTTMLGLYFTLLQWYEY-WEspFTISDSIYGSSFFMA----TGFHGIHVIIGTTFLLVCLTRHYYMHF 229
Cdd:cd02862 77 AGRRRRARRWLAAAVLLGLVFLVIKYFEYaHK--IAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRY 154
|
170 180 190
....*....|....*....|....*....|
gi 2458278142 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 |
1.33e-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: 80.88 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 80 GLRWGMILFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGikpfnpmqVPLLNTVVLLSSGITITWAHHSLMESNYS 159
Cdd:cd02865 8 PGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQPGAPLPLPN--------LLSLNTAVLAASSVAMQWARRAARRNRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 160 MSIQGIMMTTMLGLYFTLLQWYEYWESPF---TISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFG 236
Cdd:cd02865 80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159
|
170 180
....*....|....*....|....*
gi 2458278142 237 FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 160 VELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
87-259 |
2.31e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 75.34 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 87 LFISSEVLFFVSFFWAYFHSSLAPTIELGmtfppegikpfNPMQVPLLNTVVLLSSGITITwAHHSLMESNYSMSIqgIM 166
Cdd:MTH00049 59 LFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 167 MTTMLGLYFTLLQWYEYWESPFTISDSIYGSSFFMATGFHGIHVIIGTtfllVCLTRHYYMHFSNNHHFGFEAAAWYWHF 246
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGV----VGLSTLLLVGSSSFGVYRSTVLTWYWHF 200
|
170
....*....|...
gi 2458278142 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 |
1.02e-15 |
|
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: 73.04 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 84 GMILFISSEVLFFVSFFWAYF--HSSLAPTielgmtfpPEGIKPFNPMQVpLLNTVVLLSSGITITWAHHSLMESNYSMS 161
Cdd:cd02863 12 GFWIYLMSDCILFATLFATYAvlSGNTAGG--------PPGHELFELPLV-FIETFLLLLSSFTCGLAMIAMNKNNKKKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 162 IQGIMMTTMLGLYFTLLQWYE---YWESPFTISDSIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMHFSNNHHFGFE 238
Cdd:cd02863 83 ILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLF 162
|
170 180
....*....|....*....|.
gi 2458278142 239 AAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 163 CLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
84-261 |
1.22e-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: 73.30 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 84 GMILFISSEVLFFVSFFWAYFHSSLAPTIELGMTFPPEGIkPFNPMQVPL----LNTVVLLSSGITITWAHHSLMESNYS 159
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 160 MSIQGIMMTTMLGLYFTLLQWYEY-----------WESPFTISdsIYGSSFFMATGFHGIHVIIGTTFLLVCLTRHYYMH 228
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 2458278142 229 FSNNHHF-GFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 169 YQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
84-259 |
3.17e-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: 55.25 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 84 GMILFISSEVLFFVSFFWAYFhsslapTIELGMTFPPEGIKPFNPMQVPLLNTVVLLSSGITITWAHHSLMESNYSMSIQ 163
Cdd:TIGR02897 13 GFWIFLGAEIALFATLFATYL------VLQHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 164 GIMMTTMLGLYFTLLQWYE---YWESPFTISDSIYGSSFFMATGFHGIHV---IIGTTFLLVCLTRHYYMHFSNNHHFgf 237
Cdd:TIGR02897 87 WMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVtlgIVWAICLLIQIQRRGLTPYTAPKVF-- 164
|
170 180
....*....|....*....|..
gi 2458278142 238 eAAAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 165 -IVSLYWHFLDVVWVFIFTAVY 185
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-259 |
6.94e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 48.62 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278142 133 LLNTVVLLSSGITITWAHHSLMESNYSMSIQGIMMTTMLGLYFTLLQWYEYW---ESPFTISDSIYGSSFFMATGFHGIH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2458278142 210 VIIGTTFLLVCLTRHYYMHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
|
|
| |
