|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
1.06e-160 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 445.78 E-value: 1.06e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 6 NNQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 86 ILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 166 LMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 2458278129 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
2.57e-126 |
|
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: 358.37 E-value: 2.57e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 20 LTAAIGAMVTASGLTKWFHMFNSSLMLN-GMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMILFISSEVLFFVS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFlGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 99 FFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLMTVILGLYFTCL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 179 QGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2458278129 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
1.47e-125 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 357.11 E-value: 1.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 9 PYHLVDKSPWPLTAAIGAMVTASGLTKWFHMF--NSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 87 LFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLL 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 167 MTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 2458278129 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
2.01e-55 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 176.58 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 72 LHTMFVSKGLRLGMILFISSEVLFFVSFFWAYFHSMMApiielgMTWPPEGIKPFNPmQVPLLNTVILLSSGITVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 152 SLMESNYSESWQSLLMTVILGLYFTCLQGYEY---WESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2458278129 229 FSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
83-259 |
8.62e-09 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 54.09 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 83 LGMILFISSEVLFFVSFFWAYFhsmmapIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESW 162
Cdd:TIGR02897 12 LGFWIFLGAEIALFATLFATYL------VLQHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 163 QSLLMTVILGLYFTCLQGYE---YWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEA 239
Cdd:TIGR02897 86 FWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFI 165
|
170 180
....*....|....*....|
gi 2458278129 240 AAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 166 VSLYWHFLDVVWVFIFTAVY 185
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-259 |
1.06e-160 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 445.78 E-value: 1.06e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 6 NNQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGM 85
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 86 ILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSL 165
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 166 LMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWH 245
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 2458278129 246 FVDVVWLFLYISIY 259
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-261 |
1.42e-145 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 407.80 E-value: 1.42e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 4 TYNNQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRL 83
Cdd:MTH00118 2 THQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 84 GMILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQ 163
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 164 SLLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWY 243
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*...
gi 2458278129 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWW 259
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
4-261 |
2.32e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 394.73 E-value: 2.32e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 4 TYNNQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRL 83
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 84 GMILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQ 163
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 164 SLLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWY 243
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*...
gi 2458278129 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWW 258
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
9-261 |
4.50e-137 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 386.39 E-value: 4.50e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 9 PYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMILF 88
Cdd:MTH00039 6 PYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 89 ISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLMT 168
Cdd:MTH00039 86 ITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 169 VILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00039 166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVD 245
|
250
....*....|...
gi 2458278129 249 VVWLFLYISIYWW 261
Cdd:MTH00039 246 VVWLFLYVCIYWW 258
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
9.23e-136 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 383.09 E-value: 9.23e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 8 QPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMIL 87
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 88 FISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLM 167
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 168 TVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*
gi 2458278129 248 DVVWLFLYISIYWWS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWG 258
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
2-261 |
1.04e-132 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 375.28 E-value: 1.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 2 MTTYNNQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGL 81
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 82 RLGMILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSES 161
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 162 WQSLLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAA 241
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|
gi 2458278129 242 WYWHFVDVVWLFLYISIYWW 261
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWW 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
9-261 |
1.09e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 367.55 E-value: 1.09e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 9 PYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMILF 88
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 89 ISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLMT 168
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 169 VILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|...
gi 2458278129 249 VVWLFLYISIYWW 261
Cdd:MTH00130 247 VVWLFLYISIYWW 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-261 |
2.05e-129 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 367.13 E-value: 2.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 4 TYNNQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRL 83
Cdd:MTH00099 2 THQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 84 GMILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQ 163
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 164 SLLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWY 243
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250
....*....|....*...
gi 2458278129 244 WHFVDVVWLFLYISIYWW 261
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWW 259
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
10-261 |
1.80e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 362.14 E-value: 1.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 10 YHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMILFI 89
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 90 SSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLMTV 169
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 170 ILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|..
gi 2458278129 250 VWLFLYISIYWW 261
Cdd:MTH00075 248 VWLFLYVSIYWW 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-261 |
2.57e-126 |
|
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: 358.37 E-value: 2.57e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 20 LTAAIGAMVTASGLTKWFHMFNSSLMLN-GMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMILFISSEVLFFVS 98
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGPLLLFlGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 99 FFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLMTVILGLYFTCL 178
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 179 QGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVDVVWLFLYISI 258
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 2458278129 259 YWW 261
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
1.47e-125 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 357.11 E-value: 1.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 9 PYHLVDKSPWPLTAAIGAMVTASGLTKWFHMF--NSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMI 86
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 87 LFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLL 166
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 167 MTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHF 246
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*.
gi 2458278129 247 VDVVWLFLYISIYWWS 262
Cdd:pfam00510 242 VDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
8-261 |
2.01e-117 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 336.42 E-value: 2.01e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 8 QPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMIL 87
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 88 FISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLM 167
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 168 TVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFV 247
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....
gi 2458278129 248 DVVWLFLYISIYWW 261
Cdd:MTH00009 244 DVVWIFLYLCIYWW 257
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
9-261 |
6.52e-117 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 335.18 E-value: 6.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 9 PYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMILF 88
Cdd:MTH00024 7 PYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 89 ISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESWQSLLMT 168
Cdd:MTH00024 87 ILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 169 VILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVD 248
Cdd:MTH00024 167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVD 246
|
250
....*....|...
gi 2458278129 249 VVWLFLYISIYWW 261
Cdd:MTH00024 247 VVWLFLYLCIYWW 259
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-263 |
4.94e-111 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 320.59 E-value: 4.94e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 1 MMTTYnnQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKG 80
Cdd:MTH00052 2 MQQYY--HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 81 LRLGMILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSE 160
Cdd:MTH00052 80 LKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 161 SWQSLLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAA 240
Cdd:MTH00052 160 AIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAA 239
|
250 260
....*....|....*....|...
gi 2458278129 241 AWYWHFVDVVWLFLYISIYWWST 263
Cdd:MTH00052 240 AWYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
8-263 |
1.02e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 288.12 E-value: 1.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 8 QPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSKGLRLGMIL 87
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 88 FISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLM------------- 154
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 155 ---------------ESNYSESWQS--------LLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVI 211
Cdd:MTH00028 166 giegpnpsngappdpQKGPTFLLSDfrtnavigLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2458278129 212 IGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWWST 263
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
2-261 |
1.95e-88 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 263.45 E-value: 1.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 2 MTTYNNQPYHLVDKSPWPLTAAIGAMVTASGLTKWFHMFN--SSLMLNGMMITLLTMYQWWRDITREGTLQGLHTMFVSK 79
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 80 GLRLGMILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYS 159
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 160 ESWQSLLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEA 239
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|..
gi 2458278129 240 AAWYWHFVDVVWLFLYISIYWW 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWW 262
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
10-262 |
1.68e-73 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 224.83 E-value: 1.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 10 YHLVDKSPWPLTAAIGAMVTASGLTKWFHMFNSSLMLNGMMITLLTMYQWWRDITREGtLQGLHTMFVSKGLRLGMILFI 89
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 90 SSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNySESWQSLLMTV 169
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 170 ILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVDV 249
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|...
gi 2458278129 250 VWLFLYISIYWWS 262
Cdd:MTH00083 243 VWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
73-261 |
1.88e-71 |
|
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: 217.07 E-value: 1.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 73 HTMFVSKGLRLGMILFISSEVLFFVSFFWAYFHSMMAPIIELGMtwppegikPFNPMQVPLLNTVILLSSGITVTWAHHS 152
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 153 LM--ESNYSESWQSLLMTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFS 230
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2458278129 231 NNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-261 |
2.01e-55 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 176.58 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 72 LHTMFVSKGLRLGMILFISSEVLFFVSFFWAYFHSMMApiielgMTWPPEGIKPFNPmQVPLLNTVILLSSGITVTWAHH 151
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 152 SLMESNYSESWQSLLMTVILGLYFTCLQGYEY---WESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKH 228
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 2458278129 229 FSNNHHFGFEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
82-259 |
1.37e-24 |
|
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: 96.92 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 82 RLGMILFISSEVLFFVSFFWAYF--HSMMAPIIELGmtwpPEGIKPfnpmQVPLLNTVILLSSGITVTWAHHSLMESNYS 159
Cdd:cd02862 10 KLGMWVFILSELLAFGALFIAYAvyRALYPELFAAG----SAHLDL----LLGALNTLVLLTSSFTVALAVRAARAGRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 160 ESWQSLLMTVILGLYFTCLQGYEY-WEspFTISDSIYGSVFFMA----TGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHH 234
Cdd:cd02862 82 RARRWLAAAVLLGLVFLVIKYFEYaHK--IAAGIDPDAGLFFTLyfllTGFHLLHVLIGLGILLWVAWRARRGRYSARDY 159
|
170 180
....*....|....*....|....*
gi 2458278129 235 FGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:cd02862 160 EGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
87-259 |
1.64e-19 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 83.81 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 87 LFISSEVLFFVSFFWAYFHSMMAPIIELGmtwppegikpfNPMQVPLLNTVILLSSGITVTWAHHSLmesNYSESWQSLL 166
Cdd:MTH00049 59 LFILSEVIIFGSLLVCCLWFDDWSYISLS-----------SSLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 167 MTVILGLYFTCLQGYEYWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLmrhyykhFSNNHHFGF---EAAAWY 243
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLL-------LVGSSSFGVyrsTVLTWY 197
|
170
....*....|....*.
gi 2458278129 244 WHFVDVVWLFLYISIY 259
Cdd:MTH00049 198 WHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
82-261 |
1.10e-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: 239215 Cd Length: 202 Bit Score: 76.00 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 82 RLGMILFISSEVLFFVSFFWAYFHSMMAPIIELGMTWPPEGIkPFNPMQVPL----LNTVILLSSGITVTWAHHSLMESN 157
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 158 YSESWQSLLMTVILGLYFTCLQGYEY-----------WESPFTISdsIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYY 226
Cdd:cd02864 89 RKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWR 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 2458278129 227 KHFSNNHHFG-FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02864 167 GKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
80-261 |
3.45e-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: 74.33 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 80 GLRLGMILFISSEVLFFVSFFWAYFHSMMApiielGMTWPPEgikPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYS 159
Cdd:cd02865 8 PGWWGLWVFMAVEGTLFALLISAYFMRMTS-----GDWQPGA---PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 160 ESWQSLLMTVILGLYFTCLQGYEYWESPF---TISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFG 236
Cdd:cd02865 80 LARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLP 159
|
170 180
....*....|....*....|....*
gi 2458278129 237 FEAAAWYWHFVDVVWLFLYISIYWW 261
Cdd:cd02865 160 VELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
83-259 |
5.23e-16 |
|
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 73.81 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 83 LGMILFISSEVLFFVSFFWAYFhsmmapIIELGMTWPPEGIKPFNPMQVpLLNTVILLSSGITVTWAHHSLMESNYSESW 162
Cdd:cd02863 11 LGFWIYLMSDCILFATLFATYA------VLSGNTAGGPPGHELFELPLV-FIETFLLLLSSFTCGLAMIAMNKNNKKKVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 163 QSLLMTVILGLYFTCLQGYE---YWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEA 239
Cdd:cd02863 84 LWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFC 163
|
170 180
....*....|....*....|
gi 2458278129 240 AAWYWHFVDVVWLFLYISIY 259
Cdd:cd02863 164 LSLFWHFLDIVWIFVFTVVY 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
83-259 |
8.62e-09 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 54.09 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 83 LGMILFISSEVLFFVSFFWAYFhsmmapIIELGMTWPPEGIKPFNPMQVPLLNTVILLSSGITVTWAHHSLMESNYSESW 162
Cdd:TIGR02897 12 LGFWIFLGAEIALFATLFATYL------VLQHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 163 QSLLMTVILGLYFTCLQGYE---YWESPFTISDSIYGSVFFMATGFHGIHVIIGTVFLLTCLMRHYYKHFSNNHHFGFEA 239
Cdd:TIGR02897 86 FWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFI 165
|
170 180
....*....|....*....|
gi 2458278129 240 AAWYWHFVDVVWLFLYISIY 259
Cdd:TIGR02897 166 VSLYWHFLDVVWVFIFTAVY 185
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
133-259 |
3.57e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 52.48 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278129 133 LLNTVILLSSGITVTWAHHSLMESNYSESWQSLLMTVILGLYFTCLQGYEYW---ESPFTISDSIYGSVFFMATGFHGIH 209
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2458278129 210 VIIGTVFLLTCLMRHYYKHFSNNHHFGFEAAAWYWHFVDVVWLFLYISIY 259
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
|
|
|