|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
1.60e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 356.98 E-value: 1.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 1 MFRMNPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRI 80
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 81 GMVLFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIM 160
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 161 GLVITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWY 240
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 270267458 241 WHFVDVVWIFLYSFVYMWG 259
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
17-258 |
1.15e-95 |
|
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: 280.56 E-value: 1.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 17 IMGSFGAMFTAFGLVIWFHL-GSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVLFITSEVLFFFG 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 96 FFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITLFLGFFFTLL 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 176 QAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFV 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 270267458 256 YMW 258
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-259 |
1.23e-92 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 273.52 E-value: 1.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 6 PFHLVDASPWPIMGSFGAMFTAFGLVIWFH--LGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMV 83
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 84 LFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLV 163
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 164 ITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHF 243
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 270267458 244 VDVVWIFLYSFVYMWG 259
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-258 |
2.19e-31 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 114.56 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 70 HLLQVMSGLRIGMVLFITSEVLFFFGFFWTFFhsglvpVVELGGVWPPFMLESLDPmAVPLLNTVVLLSSGVSVTYSHYS 149
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 150 VINSNLTDGIMGLVITLFLGFFFTLLQAFEY---VQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHV 226
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 270267458 227 LSNHHIGYECAIWYWHFVDVVWIFLYSFVYMW 258
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
130-259 |
1.97e-07 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 49.95 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 130 LLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITLFLGFFFTLLQAFEY---VQTSFTIADSVYGSIFFMATGFHGFH 206
Cdd:TIGR02842 46 LVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFyhlIAEGNGPDRSAFLSAFFTLVGTHGLH 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 270267458 207 VFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYMWG 259
Cdd:TIGR02842 126 VTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLG 178
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
1.60e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 356.98 E-value: 1.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 1 MFRMNPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRI 80
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 81 GMVLFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIM 160
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 161 GLVITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWY 240
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 270267458 241 WHFVDVVWIFLYSFVYMWG 259
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-256 |
3.33e-106 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 307.88 E-value: 3.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 5 NPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVL 84
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 85 FITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVI 164
Cdd:MTH00155 84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 165 TLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFV 244
Cdd:MTH00155 164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243
|
250
....*....|..
gi 270267458 245 DVVWIFLYSFVY 256
Cdd:MTH00155 244 DVVWLFLYISIY 255
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-260 |
7.06e-102 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 297.02 E-value: 7.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 1 MFRMNPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRI 80
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 81 GMVLFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIM 160
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 161 GLVITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWY 240
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 270267458 241 WHFVDVVWIFLYSFVYMWGG 260
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-259 |
9.01e-102 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 296.86 E-value: 9.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 4 MNPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMV 83
Cdd:MTH00118 5 AHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 84 LFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLV 163
Cdd:MTH00118 85 LFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 164 ITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHF 243
Cdd:MTH00118 165 LTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHF 244
|
250
....*....|....*.
gi 270267458 244 VDVVWIFLYSFVYMWG 259
Cdd:MTH00118 245 VDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
5-260 |
2.72e-99 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 290.25 E-value: 2.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 5 NPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVL 84
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 85 FITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVI 164
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 165 TLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFV 244
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 270267458 245 DVVWIFLYSFVYMWGG 260
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
17-258 |
1.15e-95 |
|
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: 280.56 E-value: 1.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 17 IMGSFGAMFTAFGLVIWFHL-GSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVLFITSEVLFFFG 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 96 FFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITLFLGFFFTLL 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 176 QAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFV 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 270267458 256 YMW 258
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-259 |
1.23e-92 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 273.52 E-value: 1.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 6 PFHLVDASPWPIMGSFGAMFTAFGLVIWFH--LGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMV 83
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHgySGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 84 LFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLV 163
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 164 ITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHF 243
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 270267458 244 VDVVWIFLYSFVYMWG 259
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
6-259 |
4.23e-90 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 267.39 E-value: 4.23e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 6 PFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVLF 85
Cdd:MTH00024 7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 86 ITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVIT 165
Cdd:MTH00024 87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 166 LFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVD 245
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246
|
250
....*....|....
gi 270267458 246 VVWIFLYSFVYMWG 259
Cdd:MTH00024 247 VVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
1.81e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 265.47 E-value: 1.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 6 PFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVLF 85
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 86 ITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVIT 165
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 166 LFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVD 245
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|....
gi 270267458 246 VVWIFLYSFVYMWG 259
Cdd:MTH00130 247 VVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-259 |
2.85e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 265.11 E-value: 2.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 2 FRMNPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIG 81
Cdd:MTH00219 4 FQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 82 MVLFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMG 161
Cdd:MTH00219 84 MILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 162 LVITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYW 241
Cdd:MTH00219 164 LLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYW 243
|
250
....*....|....*...
gi 270267458 242 HFVDVVWIFLYSFVYMWG 259
Cdd:MTH00219 244 HFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
7.17e-89 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 264.35 E-value: 7.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 6 PFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVLF 85
Cdd:MTH00052 8 PYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 86 ITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVIT 165
Cdd:MTH00052 88 IVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 166 LFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVD 245
Cdd:MTH00052 168 VALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVD 247
|
250
....*....|....
gi 270267458 246 VVWIFLYSFVYMWG 259
Cdd:MTH00052 248 VVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
3-259 |
1.35e-88 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 263.51 E-value: 1.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 3 RMNPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGM 82
Cdd:MTH00099 4 QTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 83 VLFITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGL 162
Cdd:MTH00099 84 ILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 163 VITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWH 242
Cdd:MTH00099 164 FITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWH 243
|
250
....*....|....*..
gi 270267458 243 FVDVVWIFLYSFVYMWG 259
Cdd:MTH00099 244 FVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
7-259 |
6.92e-87 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 258.91 E-value: 6.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 7 FHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVLFI 86
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 87 TSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITL 166
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 167 FLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDV 246
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|...
gi 270267458 247 VWIFLYSFVYMWG 259
Cdd:MTH00075 248 VWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
5-259 |
1.25e-82 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 249.60 E-value: 1.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 5 NPFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVL 84
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 85 FITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNL--------- 155
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 156 ---------------------------TDGIMGLVITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVF 208
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfrTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 270267458 209 VGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYMWG 259
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
6-259 |
1.12e-81 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 245.90 E-value: 1.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 6 PFHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVLF 85
Cdd:MTH00009 5 PFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 86 ITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVIT 165
Cdd:MTH00009 85 IASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 166 LFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVD 245
Cdd:MTH00009 165 VLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVD 244
|
250
....*....|....
gi 270267458 246 VVWIFLYSFVYMWG 259
Cdd:MTH00009 245 VVWIFLYLCIYWWG 258
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
7-260 |
3.06e-69 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 214.53 E-value: 3.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 7 FHLVDASPWPIMGSFGAMFTAFGLVIWFH--LGSLFFMFFGVFLIVFTKYVWWRDVVREASSLGFHLLQVMSGLRIGMVL 84
Cdd:PLN02194 9 YHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 85 FITSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVI 164
Cdd:PLN02194 89 FIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 165 TLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFV 244
Cdd:PLN02194 169 TVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFV 248
|
250
....*....|....*.
gi 270267458 245 DVVWIFLYSFVYMWGG 260
Cdd:PLN02194 249 DVVWLFLFVSIYWWGG 264
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-259 |
1.43e-59 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 189.40 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 7 FHLVDASPWPIMGSFGAMFTAFGLVIWFHLGSLFFMFFGVFLIVFTKYVWWRDVVREASSlGFHLLQVMSGLRIGMVLFI 86
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEGLS-GYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 87 TSEVLFFFGFFWTFFHSGLVPVVELGGVWPPFMLESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLtDGIMGLVITL 166
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 167 FLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDV 246
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|...
gi 270267458 247 VWIFLYSFVYMWG 259
Cdd:MTH00083 243 VWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
70-258 |
3.18e-45 |
|
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: 150.05 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 70 HLLQVMSGLRIGMVLFITSEVLFFFGFFWTFFHSGLVPVVELGgvwppfmlESLDPMAVPLLNTVVLLSSGVSVTYSHYS 149
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 150 VI--NSNLTDGIMGLVITLFLGFFFTLLQAFEYVQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVL 227
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 270267458 228 SNHHIGYECAIWYWHFVDVVWIFLYSFVYMW 258
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
70-258 |
2.19e-31 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 114.56 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 70 HLLQVMSGLRIGMVLFITSEVLFFFGFFWTFFhsglvpVVELGGVWPPFMLESLDPmAVPLLNTVVLLSSGVSVTYSHYS 149
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYF------VLRASAPDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 150 VINSNLTDGIMGLVITLFLGFFFTLLQAFEY---VQTSFTIADSVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHV 226
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 270267458 227 LSNHHIGYECAIWYWHFVDVVWIFLYSFVYMW 258
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
130-257 |
5.48e-15 |
|
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: 71.11 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 130 LLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITLFLGFFFTLLQAFEY---VQTSFTIADSVYGSIFFMATGFHGFH 206
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 270267458 207 VFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYM 257
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLYL 185
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
130-259 |
7.24e-12 |
|
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: 62.26 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 130 LLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITLFLGFFFTLLQAFE---YVQTSFTIADSVYGSIFFMATGFHGFH 206
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 270267458 207 VFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYMWG 259
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVYLLG 186
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
121-258 |
1.11e-11 |
|
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: 62.00 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 121 ESLDPMAVPLLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITLFLGFFFTLLQAFEYVQTSF---TIADSVYGSIFF 197
Cdd:cd02865 44 APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFY 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 270267458 198 MATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYMW 258
Cdd:cd02865 124 LLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
192-258 |
2.29e-10 |
|
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: 58.67 E-value: 2.29e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270267458 192 YGSIFFMATGFHGFHVFVGSVFL-LVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYMW 258
Cdd:cd02864 135 FGASFFMITGFHGTHVTIGVIYLiIIARKVWRGKYQRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
124-256 |
6.18e-08 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 51.84 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 124 DPMAVPLLNTVVLLSSGVSVTYSHySVINSNLTDGIMGLVITLFLGFFFTllQAFEYVQTSFTIADSVYGSIFFMATGFH 203
Cdd:MTH00049 88 SSLEIPFVGCFLLLGSSITVTAYH-HLLGWKYCDLFLYLTILLGLLFVVL--QVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 270267458 204 GFHVFVGSVFLLVCLVRMVNGHVLSNHHIgyecAIWYWHFVDVVWIFLYSFVY 256
Cdd:MTH00049 165 FSHVVLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHFVDYIWLLVYLIVY 213
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
130-259 |
1.97e-07 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 49.95 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 130 LLNTVVLLSSGVSVTYSHYSVINSNLTDGIMGLVITLFLGFFFTLLQAFEY---VQTSFTIADSVYGSIFFMATGFHGFH 206
Cdd:TIGR02842 46 LVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFyhlIAEGNGPDRSAFLSAFFTLVGTHGLH 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 270267458 207 VFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYMWG 259
Cdd:TIGR02842 126 VTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVYLLG 178
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
190-259 |
6.63e-06 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 45.54 E-value: 6.63e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 190 SVYGSIFFMATGFHGFHVFVGSVFLLVCLVRMVNGHVLSNHHIGYECAIWYWHFVDVVWIFLYSFVYMWG 259
Cdd:PRK10663 133 SGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
180-259 |
1.38e-05 |
|
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: 44.46 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267458 180 YVQTSFTIADSVYGSIFFMATGFHGFHVFVGsVFLLVCLVRMVNGHVLSNHHIGYECAI-WYWHFVDVVWIFLYSFVYMW 258
Cdd:TIGR02897 109 YASEGVTPQIGSYWSSFFVLLGTHGCHVTLG-IVWAICLLIQIQRRGLTPYTAPKVFIVsLYWHFLDVVWVFIFTAVYLI 187
|
.
gi 270267458 259 G 259
Cdd:TIGR02897 188 G 188
|
|
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