|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
3.16e-161 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 447.32 E-value: 3.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 4 HANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 84 MILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 164 LFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1418579365 244 HFVDVVWLFLYISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
4.13e-131 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 370.97 E-value: 4.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYT--MTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 85 ILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 165 FFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1418579365 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 |
1.17e-122 |
|
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.
Pssm-ID: 238834 Cd Length: 243 Bit Score: 349.12 E-value: 1.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 19 LTGAIGAMTTVSGLVQWFHQYT-MTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGMILFIVSEVFFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 98 FFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSIL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 178 QGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1418579365 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
1.52e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 153.85 E-value: 1.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 71 LHTYVVTIGLRWGMILFIVSEVFFFISFFWAFFHSSLSptielgMTWPPIGINAFNPFqIPLLNTAILLASGVTVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 151 SLMENNHSQTTQSLFFTIILGVYFSILQGYEY---IEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1418579365 228 FSKNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
2.34e-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: 52.55 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 132 LLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSILQGYE---YIEASFTIADAVYGSTFYMATGFHGLH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1418579365 209 VLIGTtFLLICFLRHINFH-FSKNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 136 VTLGI-VWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
3.16e-161 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 447.32 E-value: 3.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 4 HANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWG 83
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 84 MILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQS 163
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 164 LFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYW 243
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 1418579365 244 HFVDVVWLFLYISIY 258
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
5.19e-143 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 401.25 E-value: 5.19e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 3 THANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRW 82
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 83 GMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQ 162
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 163 SLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWY 242
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 1418579365 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
1.59e-141 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 397.42 E-value: 1.59e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 3 THANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRW 82
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 83 GMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQ 162
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 163 SLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWY 242
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 1418579365 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
6.04e-135 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 380.78 E-value: 6.04e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGMIL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 87 FIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFF 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 167 TIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1418579365 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
1.75e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 372.14 E-value: 1.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGMIL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 87 FIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFF 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 167 TIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 1418579365 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
4.13e-131 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 370.97 E-value: 4.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYT--MTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 85 ILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 165 FFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 1418579365 245 FVDVVWLFLYISIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
3-262 |
5.55e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 370.98 E-value: 5.55e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 3 THANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRW 82
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 83 GMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQ 162
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 163 SLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWY 242
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 1418579365 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
2.05e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 369.50 E-value: 2.05e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 1 MSTHANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGL 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 81 RWGMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQT 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 161 TQSLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAA 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1418579365 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
2.43e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 369.48 E-value: 2.43e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 3 THANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRW 82
Cdd:MTH00130 2 AHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 83 GMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQ 162
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 163 SLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWY 242
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 1418579365 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
3.11e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 364.07 E-value: 3.11e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 3 THANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRW 82
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 83 GMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQ 162
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 163 SLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWY 242
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 1418579365 243 WHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWGS 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
1.17e-122 |
|
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.
Pssm-ID: 238834 Cd Length: 243 Bit Score: 349.12 E-value: 1.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 19 LTGAIGAMTTVSGLVQWFHQYT-MTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGMILFIVSEVFFFIS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGgPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 98 FFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSIL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 178 QGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFVDVVWLFLYISI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1418579365 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-262 |
2.99e-119 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 341.05 E-value: 2.99e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGMIL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 87 FIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFF 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 167 TIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1418579365 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
7-262 |
1.00e-110 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 319.78 E-value: 1.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGMIL 86
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 87 FIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFF 166
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 167 TIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 1418579365 247 DVVWLFLYISIYWWGS 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.28e-108 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 314.42 E-value: 1.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 1 MSTHANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 81 RWGMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHSQT 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 161 TQSLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1418579365 241 WYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.19e-92 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 275.02 E-value: 1.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTIGLRWGMIL 86
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 87 FIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHH---------------- 150
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHaiigtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 151 --------------------SLMENNHSQTTQSLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVL 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptFLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1418579365 211 IGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-261 |
6.44e-83 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 249.20 E-value: 6.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 1 MSTHANHPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYT--MTLFILGNIITILTMYQWWRDISREGTFQGLHTYVVTI 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 79 GLRWGMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNHS 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 159 QTTQSLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 1418579365 239 AAWYWHFVDVVWLFLYISIYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
2.52e-70 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 216.75 E-value: 2.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 7 HPFHLVDYSPWPLTGAIGAMTTVSGLVQWFHQYTMTLFILGNIITILTMYQWWRDISREGtFQGLHTYVVTIGLRWGMIL 86
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 87 FIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNPFQIPLLNTAILLASGVTVTWAHHSLMENNhSQTTQSLFF 166
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 167 TIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFV 246
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 1418579365 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 |
3.36e-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: 193.57 E-value: 3.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 72 HTYVVTIGLRWGMILFIVSEVFFFISFFWAFFHSSLSPTIELGMtwppiginAFNPFQIPLLNTAILLASGVTVTWAHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 152 LMENNHS--QTTQSLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHFS 229
Cdd:cd00386 73 LAARRGNrkKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1418579365 230 KNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
1.52e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 153.85 E-value: 1.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 71 LHTYVVTIGLRWGMILFIVSEVFFFISFFWAFFHSSLSptielgMTWPPIGINAFNPFqIPLLNTAILLASGVTVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDLP-LPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 151 SLMENNHSQTTQSLFFTIILGVYFSILQGYEY---IEASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 1418579365 228 FSKNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
1.07e-19 |
|
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: 83.82 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 132 LLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSILQGYEY---IEASFTIADAVYGSTFYMATGFHGLH 208
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1418579365 209 VLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
131-260 |
1.82e-16 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 75.10 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 131 PLLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSILQGYEYIEASF---TIADAVYGSTFYMATGFHGL 207
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1418579365 208 HVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
3.21e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.95 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 127 PFQIPLLNTAILLASGVTVTWAHHSL-MENNHSQttqsLFFTIILGVYFSILQGYEYIEASFTIADAVYGSTFYMATGFH 205
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLgWKYCDLF----LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1418579365 206 GLHVLIGTtfLLICFLRHINFHFSKNHHFgfEAAAWYWHFVDVVWLFLYISIY 258
Cdd:MTH00049 165 FSHVVLGV--VGLSTLLLVGSSSFGVYRS--TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
83-260 |
2.30e-14 |
|
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: 69.84 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 83 GMILFIVSEVFFFISFFWAFFHSSLSPTIELGMTWPPIGINAFNpFQIPL----LNTAILLASGVTVTWAHHSLMENNHS 158
Cdd:cd02864 12 MMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALRIGH-FNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 159 QTTQSLFFTIILGVYFSILQGYEYIE---------ASFTIADAVYGSTFYMATGFHGLHVLIGTTFLLICFLRHINFHF- 228
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYq 170
|
170 180 190
....*....|....*....|....*....|..
gi 1418579365 229 SKNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 260
Cdd:cd02864 171 RIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
128-258 |
4.38e-13 |
|
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: 65.72 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 128 FQIPL--LNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSILQGYE---YIEASFTIADAVYGSTFYMAT 202
Cdd:cd02863 48 FELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLV 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1418579365 203 GFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFVDVVWLFLYISIY 258
Cdd:cd02863 128 GTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
2.34e-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: 52.55 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 132 LLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSILQGYE---YIEASFTIADAVYGSTFYMATGFHGLH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1418579365 209 VLIGTtFLLICFLRHINFH-FSKNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 261
Cdd:TIGR02897 136 VTLGI-VWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
128-262 |
3.34e-07 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 49.39 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 128 FQIP--LLNTAILLASGVTVTWAHHSLMENNHSQTTQSLFFTIILGVYFSILQGYEY---IEASFTIADAVYGSTFYMAT 202
Cdd:PRK10663 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALV 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418579365 203 GFHGLHVLIGTTFLLICFLRHINFHFSKNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 262
Cdd:PRK10663 144 GTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
