|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.79e-179 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 493.51 E-value: 1.79e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLA-VCLLRQIQYHFTSEHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00130 240 WYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-262 |
1.66e-138 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 389.85 E-value: 1.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 6 HAYHMVDPSPWPLTGATAALLLTSGLAVWFHY--HSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 84 IPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 164 ALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYW 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLA-VCFLRLLKYHLTDNHHFGFEAAILYW 239
|
250
....*....|....*....
gi 66276093 244 HFVDVVWLFLYVSIYWWGS 262
Cdd:pfam00510 240 HFVDVVWLFLYVSVYWWGS 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
18-260 |
9.37e-133 |
|
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: 374.54 E-value: 9.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 18 LTGATAALLLTSGLAVWFH-YHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRYGMIPFITSEVFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 97 FFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 177 QAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVS 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLT-VCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239
|
....
gi 66276093 257 IYWW 260
Cdd:cd01665 240 VYWW 243
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
118-260 |
1.95e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 158.47 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 118 PTGITPLDPFeVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAMEYYE---APFTIADGVYG 194
Cdd:COG1845 49 PAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFG 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66276093 195 STFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:COG1845 128 SFFFLLTGFHGLHVIIGLIWLL-VVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
120-261 |
1.14e-12 |
|
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: 64.88 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 120 GITPLDPFEVPLL--NTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAME---YYEAPFTIADGVYG 194
Cdd:TIGR02897 43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66276093 195 STFFVATGFHGLHVIIGTSFLagICLLRQIKYH-FTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWA--ICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.79e-179 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 493.51 E-value: 1.79e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLA-VCLLRQIQYHFTSEHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00130 240 WYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
2.61e-178 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 490.62 E-value: 2.61e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00118 1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00118 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLI-VCLLRLIKFHFTTNHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00118 240 WYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.25e-167 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 463.83 E-value: 1.25e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLL-VCLLRQINFHFTSQHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00075 240 WYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-262 |
9.54e-163 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 451.49 E-value: 9.54e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00099 1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00099 81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLI-VCFLRQLKFHFTSNHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00099 240 WYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
1.91e-161 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 447.88 E-value: 1.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 2 ARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRY 81
Cdd:MTH00189 1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 82 GMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQ 161
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 162 SLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAW 241
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLL-VCLLRQIQGHFTSSHHFGFEAAAW 239
|
250 260
....*....|....*....|.
gi 66276093 242 YWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00189 240 YWHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
6-258 |
6.59e-146 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 408.41 E-value: 6.59e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 6 HAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRYGMIP 85
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 86 FITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLAL 165
Cdd:MTH00155 84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 166 TILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHF 245
Cdd:MTH00155 164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLL-VCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 66276093 246 VDVVWLFLYVSIY 258
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
2.66e-142 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 399.65 E-value: 2.66e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARqaHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00141 1 MTR--NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00141 79 WGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00141 159 QGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLL-VCLVRLLLGHFSTNHHFGFEAAA 237
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00141 238 WYWHFVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-262 |
2.84e-140 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 394.48 E-value: 2.84e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQaHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00039 1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00039 80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLA-VCLFRLINHHFSNNHHFGFEAAA 238
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00039 239 WYWHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-262 |
1.66e-138 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 389.85 E-value: 1.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 6 HAYHMVDPSPWPLTGATAALLLTSGLAVWFHY--HSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRYGM 83
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 84 IPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSL 163
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 164 ALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYW 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLA-VCFLRLLKYHLTDNHHFGFEAAILYW 239
|
250
....*....|....*....
gi 66276093 244 HFVDVVWLFLYVSIYWWGS 262
Cdd:pfam00510 240 HFVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.11e-134 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 380.29 E-value: 1.11e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00219 2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00219 82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLF-VCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 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 ... |
18-260 |
9.37e-133 |
|
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: 374.54 E-value: 9.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 18 LTGATAALLLTSGLAVWFH-YHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRYGMIPFITSEVFFFLG 96
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 97 FFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTL 176
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 177 QAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVS 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLT-VCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239
|
....
gi 66276093 257 IYWW 260
Cdd:cd01665 240 VYWW 243
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
6-262 |
1.23e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 362.62 E-value: 1.23e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 6 HAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRYGMIP 85
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 86 FITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLAL 165
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 166 TILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHF 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLF-VCLLRTWSHHFSTGHHFGFEAAAWYWHF 242
|
250
....*....|....*..
gi 66276093 246 VDVVWLFLYVSIYWWGS 262
Cdd:MTH00009 243 VDVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
1-262 |
2.18e-125 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 356.76 E-value: 2.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLF-VCLLRLLSNQFTRRQHVGFEAAS 239
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00024 240 WYWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
6.77e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 355.64 E-value: 6.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00052 2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAI 160
Cdd:MTH00052 82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 161 QSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAA 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLL-VCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 66276093 241 WYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
8.39e-100 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 293.51 E-value: 8.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 1 MARQAHAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLR 80
Cdd:MTH00028 1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 81 YGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQ----- 155
Cdd:MTH00028 81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 156 -------------------------------RKEAIQSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFH 204
Cdd:MTH00028 161 ekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 66276093 205 GLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 262
Cdd:MTH00028 241 GLHVLVGTTFLI-VCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
4-261 |
2.06e-93 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 275.77 E-value: 2.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 4 QAHAYHMVDPSPWPLTGATAALLLTSGLAVWFH--YHSTTLMTLGLILMLLTMYQWWRDIVREGTYMGHHTPPVQKGLRY 81
Cdd:PLN02194 5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 82 GMIPFITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQ 161
Cdd:PLN02194 85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 162 SLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAW 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLI-ICGIRQYLGHLTKEHHVGFEAAAW 243
|
250 260
....*....|....*....|
gi 66276093 242 YWHFVDVVWLFLYVSIYWWG 261
Cdd:PLN02194 244 YWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-262 |
6.06e-75 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 228.69 E-value: 6.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 6 HAYHMVDPSPWPLTGATAALLLTSGLAVWFHYHSTTLMTLGLILMLLTMYQWWRDIVREGtYMGHHTPPVQKGLRYGMIP 85
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 86 FITSEVFFFLGFFWAFFHSSLAPTPELGGCWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSLMEGQrKEAIQSLAL 165
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 166 TILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLaGICLLRQIKYHFTSQHHFGFEAAAWYWHF 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFL-LFNLLRLLKSHFNYNHHLGLEFAILYWHF 239
|
250
....*....|....*..
gi 66276093 246 VDVVWLFLYVSIYWWGS 262
Cdd:MTH00083 240 VDVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
71-260 |
1.74e-67 |
|
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: 207.06 E-value: 1.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 71 HTPPVQKGLRYGMIPFITSEVFFFLGFFWAFFHSSLAPTPELGgcwpptgiTPLDPFEVPLLNTAVLLASGVTVTWAHHS 150
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 151 LM--EGQRKEAIQSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGTSFLAgICLLRQIKYHF 228
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLL-VVLIRLRRGHF 151
|
170 180 190
....*....|....*....|....*....|..
gi 66276093 229 TSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:cd00386 152 TPRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
118-260 |
1.95e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 158.47 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 118 PTGITPLDPFeVPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAMEYYE---APFTIADGVYG 194
Cdd:COG1845 49 PAGAELLDLP-LPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFG 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66276093 195 STFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:COG1845 128 SFFFLLTGFHGLHVIIGLIWLL-VVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
131-258 |
4.32e-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: 95.38 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 131 LLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAMEYYE---APFTIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 66276093 208 VIIGTSFLaGICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:cd02862 135 VLIGLGIL-LWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
120-258 |
2.93e-19 |
|
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: 82.67 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 120 GITPLDPFEVPL--LNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAME---YYEAPFTIADGVYG 194
Cdd:cd02863 41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66276093 195 STFFVATGFHGLHVIIGtsFLAGICLLRQIKYH-FTSQHHFGFEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:cd02863 121 SAFFTLVGTHGLHVTFG--LIWILVMIIQLKKRgLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
129-260 |
2.80e-18 |
|
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: 80.11 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 129 VPLLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAMEYYEAPF---TIADGVYGSTFFVATGFHG 205
Cdd:cd02865 51 LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHG 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 66276093 206 LHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 260
Cdd:cd02865 131 LHVIGGLVALA-IVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
125-258 |
6.91e-17 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 76.88 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 125 DPFEVPLLNTAVLLASGVTVTWAHHSLmegQRKEAIQSLALTILLGCYFTTLQAMEYYEAPFTIADGVYGSTFFVATGFH 204
Cdd:MTH00049 88 SSLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 66276093 205 GLHVIIGTSFLAGICLLRQIKYHFTSQhhfgfEAAAWYWHFVDVVWLFLYVSIY 258
Cdd:MTH00049 165 FSHVVLGVVGLSTLLLVGSSSFGVYRS-----TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
116-260 |
1.40e-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: 72.92 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 116 WPPTG---ITPLDPFEVPL----LNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAMEYYEapFTI 188
Cdd:cd02864 42 WPLPSdvfALRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTK--LIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 189 ADGV-----------YGSTFFVATGFHGLHVIIGTSFLAGICllRQIKYHfTSQHHFGF---EAAAWYWHFVDVVWLFLY 254
Cdd:cd02864 120 EEGVrpwgnpwgaaqFGASFFMITGFHGTHVTIGVIYLIIIA--RKVWRG-KYQRIGRYeivEIAGLYWHFVDLVWVFIF 196
|
....*.
gi 66276093 255 VSIYWW 260
Cdd:cd02864 197 AFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
120-261 |
1.14e-12 |
|
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: 64.88 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 120 GITPLDPFEVPLL--NTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTTLQAME---YYEAPFTIADGVYG 194
Cdd:TIGR02897 43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66276093 195 STFFVATGFHGLHVIIGTSFLagICLLRQIKYH-FTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWA--ICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
120-262 |
6.63e-10 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 57.48 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66276093 120 GITPLDPFEVP--LLNTAVLLASGVTVTWAHHSLMEGQRKEAIQSLALTILLGCYFTtlqAMEYYEAPFTIADGvYG--- 194
Cdd:PRK10663 57 GPTGKDIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdr 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66276093 195 ----STFFVATGFHGLHVIIGTSFLAgICLLRQIKYHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 262
Cdd:PRK10663 133 sgflSAFFALVGTHGLHVTSGLIWMA-VLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
