|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
7.33e-154 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 428.44 E-value: 7.33e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 4 HSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 84 MILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 164 LMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1812385373 244 HFVDVVWLFLYISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
7.45e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 340.16 E-value: 7.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTF--NINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 85 ILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 165 MMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1812385373 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
1.15e-118 |
|
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: 339.11 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 19 LTGALGAFITAMGLTKWFHTF-NINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGMILFITSEVLFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 98 FFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTM 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 178 QAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1812385373 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
4.74e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.01 E-value: 4.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 71 LHTMKVAVGLRWGMILFITSEVLFFISFFWAFFNSSLAVNvelgmmWPPKGIEPFNPlNIPLLNTIILLSSGITVTWSHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 151 SLMESNYSQAKQSLMMTVILGIYFTTMQAYEYEE---SQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1812385373 228 FSSNHHLGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
128-261 |
1.37e-08 |
|
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: 53.32 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 128 LNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTMQAYE---YEESQFSISDSAYGSTFFMATGF 204
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1812385373 205 HGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
7.33e-154 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 428.44 E-value: 7.33e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 4 HSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 84 MILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 164 LMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1812385373 244 HFVDVVWLFLYISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
1.35e-144 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 405.49 E-value: 1.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 2 LTHSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLR 81
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 82 WGMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAK 161
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 162 QSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAW 241
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1812385373 242 YWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
1.26e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 390.10 E-value: 1.26e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 3 THSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRW 82
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 83 GMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQ 162
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 163 SLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWY 242
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 1812385373 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
4.64e-131 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 371.15 E-value: 4.64e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGMIL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 87 FITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMM 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 167 TVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1812385373 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
3.19e-130 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 369.06 E-value: 3.19e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGMIL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 87 FITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMM 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 167 TVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1812385373 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
3.05e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 361.41 E-value: 3.05e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 1 MLTHSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGL 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 81 RWGMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQA 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 161 KQSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAA 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1812385373 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
2-262 |
8.25e-125 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 355.19 E-value: 8.25e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 2 LTHSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLR 81
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 82 WGMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAK 161
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 162 QSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAW 241
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1812385373 242 YWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
4.59e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 353.28 E-value: 4.59e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 2 LTHSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLR 81
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 82 WGMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAK 161
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 162 QSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAW 241
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1812385373 242 YWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
7.25e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 352.91 E-value: 7.25e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 2 LTHSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLR 81
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 82 WGMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAK 161
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 162 QSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAW 241
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 1812385373 242 YWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
7.45e-119 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 340.16 E-value: 7.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTF--NINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 85 ILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 165 MMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1812385373 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
1.15e-118 |
|
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: 339.11 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 19 LTGALGAFITAMGLTKWFHTF-NINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGMILFITSEVLFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 98 FFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTM 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 178 QAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1812385373 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-262 |
5.32e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 332.96 E-value: 5.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGMIL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 87 FITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMM 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 167 TVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1812385373 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
7-262 |
8.67e-114 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 327.48 E-value: 8.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGMIL 86
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 87 FITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMM 166
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 167 TVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 1812385373 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
8.43e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 317.50 E-value: 8.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 1 MLTHSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 81 RWGMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 161 KQSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1812385373 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
2.19e-96 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 284.65 E-value: 2.19e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAVGLRWGMIL 86
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 87 FITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNY--------- 157
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 158 ---------------------------SQAKQSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVM 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1812385373 211 IGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-261 |
3.33e-85 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 254.97 E-value: 3.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 1 MLTHSNHPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFN--INLMVLGLMIIILTMIQWWRDVTRESTYQGLHTMKVAV 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 79 GLRWGMILFITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYS 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 159 QAKQSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 1812385373 239 AAWYWHFVDVVWLFLYISIYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
2.67e-67 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 209.04 E-value: 2.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 7 HPFHLVDYSPWPLTGALGAFITAMGLTKWFHTFNINLMVLGLMIIILTMIQWWRDVTREStYQGLHTMKVAVGLRWGMIL 86
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 87 FITSEVLFFISFFWAFFNSSLAVNVELGMMWPPKGIEPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNySQAKQSLMM 166
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 167 TVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFV 246
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1812385373 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
5.60e-62 |
|
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: 192.80 E-value: 5.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 72 HTMKVAVGLRWGMILFITSEVLFFISFFWAFFNSSLAVNVELGmmwppkgiEPFNPLNIPLLNTIILLSSGITVTWSHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 152 LM--ESNYSQAKQSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFS 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1812385373 230 SNHHLGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
4.74e-47 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 155.01 E-value: 4.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 71 LHTMKVAVGLRWGMILFITSEVLFFISFFWAFFNSSLAVNvelgmmWPPKGIEPFNPlNIPLLNTIILLSSGITVTWSHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 151 SLMESNYSQAKQSLMMTVILGIYFTTMQAYEYEE---SQFSISDSAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1812385373 228 FSSNHHLGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
128-258 |
1.75e-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: 88.45 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 128 LNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTMQAYEYEEsQFSISDSAYGSTFFMA----TG 203
Cdd:cd02862 51 LLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAH-KIAAGIDPDAGLFFTLyfllTG 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1812385373 204 FHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02862 130 FHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
119-258 |
8.16e-18 |
|
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: 78.82 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 119 PKGIEPFNpLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTMQAYEYEE---SQFSISDSAYG 195
Cdd:cd02863 42 PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHliaEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812385373 196 STFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
7.42e-17 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 76.88 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 127 PLNIPLLNTIILLSSGITVTwSHHSLMESNYSQAkqSLMMTVILGIYFTTMQAYEYEESQFSISDSAYGSTFFMATGFHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDL--FLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1812385373 207 IHVMIGTTFLLICLIRQ--MFYHFSSNhhlgfeAAAWYWHFVDVVWLFLYISIY 258
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGssSFGVYRST------VLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-260 |
6.13e-15 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 71.38 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 124 PFNPLNIPL----LNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTMQAYEY-----EESQFSISD--- 191
Cdd:cd02864 52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtklivEEGVRPWGNpwg 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812385373 192 -SAYGSTFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSS-NHHLGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02864 132 aAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRiGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
123-260 |
9.20e-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: 239216 Cd Length: 184 Bit Score: 70.48 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 123 EPFNPLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTMQAYE----YEESQFSISDsAYGSTF 198
Cdd:cd02865 44 APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAwhalNDAGYGPTSN-PAGSFF 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812385373 199 FMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02865 123 YLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
119-262 |
8.76e-11 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 59.79 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 119 PKGIEPFNpLNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTMQAYEYE---ESQFSISDSAYG 195
Cdd:PRK10663 58 PTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812385373 196 STFFMATGFHGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:PRK10663 137 SAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
128-261 |
1.37e-08 |
|
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: 53.32 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385373 128 LNIPLLNTIILLSSGITVTWSHHSLMESNYSQAKQSLMMTVILGIYFTTMQAYE---YEESQFSISDSAYGSTFFMATGF 204
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1812385373 205 HGIHVMIGTTFLLICLIRQMFYHFSSNHHLGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
