|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
1.07e-157 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 438.64 E-value: 1.07e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 3 GYQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRR 82
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 83 GMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQ 162
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 163 SLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWY 242
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 5835520 243 WHFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
6.82e-125 |
|
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: 354.90 E-value: 6.82e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 19 LVGGSAAFTLTVGLVMWFH-YNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVLFIVSEVFFFLA 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 98 FFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 178 QAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 5835520 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
1.11e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 347.48 E-value: 1.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSIS--LMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 85 VLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 165 AITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 5835520 245 FVDVVWLFLYVCIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
119-260 |
5.33e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 152.31 E-value: 5.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 119 PVGVHPLNaFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWEYYE---APFTIADSVYG 195
Cdd:COG1845 49 PAGAELLD-LPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFG 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5835520 196 STFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCIYWW 260
Cdd:COG1845 128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
4.19e-10 |
|
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: 57.56 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 132 LLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWE---YYEAPFTIADSVYGSTFFVATGFHGLH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 5835520 209 V---IIGSTFLMVCLGRQVFYHYTSSHHFgfeAAAWYWHFVDVVWLFLYVCIYWWG 261
Cdd:TIGR02897 136 VtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
1.07e-157 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 438.64 E-value: 1.07e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 3 GYQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRR 82
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 83 GMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQ 162
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 163 SLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWY 242
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 5835520 243 WHFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.06e-151 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 423.21 E-value: 1.06e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 1 MTgYQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGL 80
Cdd:MTH00118 1 MT-HQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 81 RRGMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEA 160
Cdd:MTH00118 80 RYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 161 IQSLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAA 240
Cdd:MTH00118 160 IQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 5835520 241 WYWHFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00118 240 WYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
7-258 |
1.20e-143 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 402.64 E-value: 1.20e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVL 86
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 87 FIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAI 166
Cdd:MTH00155 84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 167 TVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFV 246
Cdd:MTH00155 164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243
|
250
....*....|..
gi 5835520 247 DVVWLFLYVCIY 258
Cdd:MTH00155 244 DVVWLFLYISIY 255
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
2.52e-140 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 394.48 E-value: 2.52e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 87 FIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAI 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 167 TVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 5835520 247 DVVWLFLYVCIYWWGS 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
3.36e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 389.25 E-value: 3.36e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 87 FIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAI 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 167 TVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 5835520 247 DVVWLFLYVCIYWWGS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-262 |
3.52e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 389.12 E-value: 3.52e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 4 YQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRG 83
Cdd:MTH00130 3 HQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 84 MVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQS 163
Cdd:MTH00130 83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 164 LAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYW 243
Cdd:MTH00130 163 LTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 5835520 244 HFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00130 243 HFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
2.32e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 387.18 E-value: 2.32e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 3 GYQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRR 82
Cdd:MTH00075 2 AHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 83 GMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQ 162
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 163 SLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWY 242
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250 260
....*....|....*....|
gi 5835520 243 WHFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-262 |
4.74e-137 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 386.39 E-value: 4.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 4 YQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRG 83
Cdd:MTH00099 3 HQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 84 MVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQS 163
Cdd:MTH00099 83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 164 LAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYW 243
Cdd:MTH00099 163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYW 242
|
250
....*....|....*....
gi 5835520 244 HFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00099 243 HFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
7-262 |
2.53e-131 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 371.78 E-value: 2.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVL 86
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 87 FIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAI 166
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 167 TVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFV 246
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*.
gi 5835520 247 DVVWLFLYVCIYWWGS 262
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
6.16e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 365.65 E-value: 6.16e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 1 MTGYQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 81 RRGMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 161 IQSLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 5835520 241 WYWHFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
3.89e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 363.72 E-value: 3.89e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 1 MTGYQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGL 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 81 RRGMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEA 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 161 IQSLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAA 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 5835520 241 WYWHFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
6.82e-125 |
|
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: 354.90 E-value: 6.82e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 19 LVGGSAAFTLTVGLVMWFH-YNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVLFIVSEVFFFLA 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 98 FFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGL 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 178 QAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCI 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 5835520 258 YWW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-262 |
1.52e-124 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 354.53 E-value: 1.52e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 87 FIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAI 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 167 TVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 5835520 247 DVVWLFLYVCIYWWGS 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
1.11e-121 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 347.48 E-value: 1.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSIS--LMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 85 VLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 165 AITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 5835520 245 FVDVVWLFLYVCIYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.84e-102 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 300.06 E-value: 1.84e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLSGLRRGMVL 86
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 87 FIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGK---------- 156
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 157 --------------------------RTEAIQSLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVI 210
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 5835520 211 IGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS 262
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-261 |
5.71e-87 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 259.60 E-value: 5.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 1 MTGYQPHPWHLVEPSPWPLVGGSAAFTLTVGLVMWFH--YNSISLMILGLVMIVATMIQWWRDVIREATFQGCHTSYVLS 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 79 GLRRGMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRT 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 159 EAIQSLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 5835520 239 AAWYWHFVDVVWLFLYVCIYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
7.71e-71 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 217.90 E-value: 7.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 7 HPWHLVEPSPWPLVGGSAAFTLTVGLVMWFHYNSISLMILGLVMIVATMIQWWRDVIREAtFQGCHTSYVLSGLRRGMVL 86
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 87 FIVSEVFFFLAFFWAFFHSSLAPTVELGVTWPPVGVHPLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRtEAIQSLAI 166
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 167 TVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFV 246
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 5835520 247 DVVWLFLYVCIYWWGS 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 |
1.67e-63 |
|
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: 196.66 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 72 HTSYVLSGLRRGMVLFIVSEVFFFLAFFWAFFHSSLAPTVELGvtwppvgvHPLNAFAVPLLNTAVLLSSGVTVTWAHHA 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 152 LM--EGKRTEAIQSLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYT 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 5835520 230 SSHHFGFEAAAWYWHFVDVVWLFLYVCIYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
119-260 |
5.33e-46 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 152.31 E-value: 5.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 119 PVGVHPLNaFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWEYYE---APFTIADSVYG 195
Cdd:COG1845 49 PAGAELLD-LPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFG 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5835520 196 STFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCIYWW 260
Cdd:COG1845 128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
3.08e-25 |
|
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: 98.46 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 132 LLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWEYYE---APFTIADSVYGSTFFVATGFHGLH 208
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 5835520 209 VIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCIY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-260 |
2.02e-19 |
|
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: 82.80 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 124 PLNAFAVPLLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWEYYEAPF---TIADSVYGSTFFV 200
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 201 ATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCIYWW 260
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
132-258 |
1.00e-17 |
|
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: 78.44 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 132 LLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWE---YYEAPFTIADSVYGSTFFVATGFHGLH 208
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 5835520 209 VIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCIY 258
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
117-260 |
2.90e-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: 72.15 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 117 WPP---VGVHPLNAFAVPL----LNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWEY------- 182
Cdd:cd02864 42 WPLpsdVFALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtklivee 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 183 ----YEAPFTIAdsVYGSTFFVATGFHGLHVIIGSTFLMVCLGRQVFYHYTSSHHFG-FEAAAWYWHFVDVVWLFLYVCI 257
Cdd:cd02864 122 gvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFF 199
|
...
gi 5835520 258 YWW 260
Cdd:cd02864 200 YLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
8.35e-14 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 68.40 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 127 AFAVPLLNTAVLLSSGVTVTWAHHALmeGKRTEAIQsLAITVMLGLYFTGLQAWEYYEAPFTIADSVYGSTFFVATGFHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL--GWKYCDLF-LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 5835520 207 LHVIIGSTFLMVCL--GRQVFYHYTSShhfgfeAAAWYWHFVDVVWLFLYVCIY 258
Cdd:MTH00049 166 SHVVLGVVGLSTLLlvGSSSFGVYRST------VLTWYWHFVDYIWLLVYLIVY 213
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
4.19e-10 |
|
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: 57.56 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 132 LLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWE---YYEAPFTIADSVYGSTFFVATGFHGLH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 5835520 209 V---IIGSTFLMVCLGRQVFYHYTSSHHFgfeAAAWYWHFVDVVWLFLYVCIYWWG 261
Cdd:TIGR02897 136 VtlgIVWAICLLIQIQRRGLTPYTAPKVF---IVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
132-262 |
1.20e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 53.63 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835520 132 LLNTAVLLSSGVTVTWAHHALMEGKRTEAIQSLAITVMLGLYFTGLQAWEYY---EAPFTIADSVYGSTFFVATGFHGLH 208
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 5835520 209 VIIGSTFLMVCLGRQVFYHYTSSHHFGFEAAAWYWHFVDVVWLFLYVCIYWWGS 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
