|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
13-266 |
1.25e-115 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 332.14 E-value: 1.25e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 13 HAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTagFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGM 92
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFN--MNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 93 ILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGL 172
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 173 ILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWH 252
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 2307924995 253 FVDVVWLFLYVAVY 266
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
25-268 |
4.26e-113 |
|
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: 325.24 E-value: 4.26e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 25 ILTSFSALTLVVGSTMYFHGYTaGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGMILFIVSEVMFFF 104
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYG-GPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 105 AFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTC 184
Cdd:cd01665 80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 185 FQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVA 264
Cdd:cd01665 160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239
|
....
gi 2307924995 265 VYFW 268
Cdd:cd01665 240 VYWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
13-269 |
2.20e-108 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 313.96 E-value: 2.20e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 13 HAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTAGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGM 92
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 93 ILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGL 172
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 173 ILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWH 252
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 2307924995 253 FVDVVWLFLYVAVYFWG 269
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
77-268 |
8.51e-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: 8.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 77 EGYHTNIVQLGLRYGMILFIVSEVMFFFAFFWAFFASSLTptieigNIWPPKGINTFNaLEIPLVNTLILLGSGVTITYA 156
Cdd:COG1845 5 EAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLD-LPLPLINTLLLLLSSFTVALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 157 HHAITAGLKLEALWGLILTVVLAIIFTCFQAYEY---LNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNL 233
Cdd:COG1845 78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2307924995 234 NQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFW 268
Cdd:COG1845 158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
136-269 |
2.96e-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: 63.72 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 136 LEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTCFQAYE---YLNADFKISDGIYGSCFFMATGF 212
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2307924995 213 HGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFWG 269
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
13-266 |
1.25e-115 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 332.14 E-value: 1.25e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 13 HAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTagFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGM 92
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFN--MNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 93 ILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGL 172
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 173 ILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWH 252
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 2307924995 253 FVDVVWLFLYVAVY 266
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
11-269 |
4.81e-114 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 328.45 E-value: 4.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHgyTAGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:MTH00118 4 QAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFH--YNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 2307924995 251 WHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWG 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
25-268 |
4.26e-113 |
|
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: 325.24 E-value: 4.26e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 25 ILTSFSALTLVVGSTMYFHGYTaGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGMILFIVSEVMFFF 104
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYG-GPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 105 AFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTC 184
Cdd:cd01665 80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 185 FQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVA 264
Cdd:cd01665 160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239
|
....
gi 2307924995 265 VYFW 268
Cdd:cd01665 240 VYWW 243
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
10-269 |
4.33e-112 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 323.46 E-value: 4.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 10 VQRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYtaGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLR 89
Cdd:MTH00189 2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYN--SFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 90 YGMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEAL 169
Cdd:MTH00189 80 YGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 170 WGLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAF 249
Cdd:MTH00189 160 QALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAW 239
|
250 260
....*....|....*....|
gi 2307924995 250 YWHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00189 240 YWHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
11-270 |
1.14e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 319.91 E-value: 1.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYtaGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGG--SFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:MTH00141 80 GFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:MTH00141 160 GLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWY 239
|
250 260
....*....|....*....|
gi 2307924995 251 WHFVDVVWLFLYVAVYFWGG 270
Cdd:MTH00141 240 WHFVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
13-269 |
2.20e-108 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 313.96 E-value: 2.20e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 13 HAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTAGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGM 92
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 93 ILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGL 172
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 173 ILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWH 252
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 2307924995 253 FVDVVWLFLYVAVYFWG 269
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
10-269 |
4.62e-102 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 298.20 E-value: 4.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 10 VQRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTAGFetALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLR 89
Cdd:MTH00024 3 KLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFI--LYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 90 YGMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEAL 169
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 170 WGLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAF 249
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|
gi 2307924995 250 YWHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
11-269 |
1.47e-101 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 296.64 E-value: 1.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTAGFETalLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:MTH00099 4 QTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLT--LGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 2307924995 251 WHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
11-270 |
1.20e-100 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 294.33 E-value: 1.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTagFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:MTH00039 3 HQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDS--ILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250 260
....*....|....*....|
gi 2307924995 251 WHFVDVVWLFLYVAVYFWGG 270
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
11-269 |
6.54e-99 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 290.13 E-value: 6.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTAGFETalLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:MTH00130 4 QAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMT--LGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250
....*....|....*....
gi 2307924995 251 WHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
13-269 |
2.04e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 289.00 E-value: 2.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 13 HAFHLVDPSSMPILTSFSALTLVVGSTMYFHgYTAGFeTALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGM 92
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFH-YSQSW-VLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 93 ILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGL 172
Cdd:MTH00052 85 ILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 173 ILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWH 252
Cdd:MTH00052 165 ALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWH 244
|
250
....*....|....*..
gi 2307924995 253 FVDVVWLFLYVAVYFWG 269
Cdd:MTH00052 245 FVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
11-269 |
2.06e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 288.95 E-value: 2.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTagFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:MTH00075 4 QAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGS--MIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250
....*....|....*....
gi 2307924995 251 WHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
11-271 |
1.94e-93 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 276.54 E-value: 1.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTAGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:PLN02194 5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:PLN02194 85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
|
250 260
....*....|....*....|.
gi 2307924995 251 WHFVDVVWLFLYVAVYFWGGL 271
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWGGI 265
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
11-269 |
6.33e-93 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 274.74 E-value: 6.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 11 QRHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYTAGFETalLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRY 90
Cdd:MTH00219 5 QTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLI--LGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 91 GMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALW 170
Cdd:MTH00219 83 GMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 171 GLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFY 250
Cdd:MTH00219 163 GLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWY 242
|
250
....*....|....*....
gi 2307924995 251 WHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00219 243 WHFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
12-269 |
7.83e-90 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 267.09 E-value: 7.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 12 RHAFHLVDPSSMPILTSFSALTLVVGSTMYFHGYtaGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYG 91
Cdd:MTH00009 3 RQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGY--GTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 92 MILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWG 171
Cdd:MTH00009 81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 172 LILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYW 251
Cdd:MTH00009 161 LILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYW 240
|
250
....*....|....*...
gi 2307924995 252 HFVDVVWLFLYVAVYFWG 269
Cdd:MTH00009 241 HFVDVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
13-269 |
9.24e-84 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 253.07 E-value: 9.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 13 HAFHLVDPSSMPILTSFSALTLVVGSTMYFHgyTAGFETALLGLIGVLACMFLWWRDITREGTLEGYHTNIVQLGLRYGM 92
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFH--YSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 93 ILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAG--------- 163
Cdd:MTH00028 84 LLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTgnpaslekg 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 164 ---------------------------LKLEALWGLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFH 216
Cdd:MTH00028 164 tqgiegpnpsngappdpqkgptfllsdFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2307924995 217 VIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFWG 269
Cdd:MTH00028 244 VLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
13-269 |
5.74e-67 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 208.66 E-value: 5.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 13 HAFHLVDPSSMPILTSFSALTLVVGSTMYFhgYTAGFETALLGLIGVLACMFLWWRDITREGtLEGYHTNIVQLGLRYGM 92
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFF--KYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 93 ILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNALEIPLVNTLILLGSGVTITYAHHAITAGLKlEALWGL 172
Cdd:MTH00083 80 ILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 173 ILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWH 252
Cdd:MTH00083 159 LLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWH 238
|
250
....*....|....*..
gi 2307924995 253 FVDVVWLFLYVAVYFWG 269
Cdd:MTH00083 239 FVDVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
80-268 |
9.42e-57 |
|
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: 180.09 E-value: 9.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 80 HTNIVQLGLRYGMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNiwppkginTFNALEIPLVNTLILLGSGVTITYAHHA 159
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 160 ITAGL--KLEALWGLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFT 237
Cdd:cd00386 73 LAARRgnRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 2307924995 238 TAHHFGFEAAAFYWHFVDVVWLFLYVAVYFW 268
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
77-268 |
8.51e-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: 8.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 77 EGYHTNIVQLGLRYGMILFIVSEVMFFFAFFWAFFASSLTptieigNIWPPKGINTFNaLEIPLVNTLILLGSGVTITYA 156
Cdd:COG1845 5 EAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLD-LPLPLINTLLLLLSSFTVALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 157 HHAITAGLKLEALWGLILTVVLAIIFTCFQAYEY---LNADFKISDGIYGSCFFMATGFHGFHVIIGTIFIIVSLIRLNL 233
Cdd:COG1845 78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2307924995 234 NQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFW 268
Cdd:COG1845 158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
140-266 |
5.08e-21 |
|
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: 87.68 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 140 LVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTCFQAYEYlNADFKISDGIYGSCFFMA----TGFHGF 215
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEY-AHKIAAGIDPDAGLFFTLyfllTGFHLL 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2307924995 216 HVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVY 266
Cdd:cd02862 134 HVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
127-269 |
4.65e-18 |
|
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: 79.59 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 127 PKGINTFNaLEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTCFQAYE---YLNADFKISDGIYG 203
Cdd:cd02863 42 PPGHELFE-LPLVFIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2307924995 204 SCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFWG 269
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVYLLG 186
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
89-268 |
2.98e-17 |
|
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: 77.93 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 89 RYGMILFIVSEVMFFFAFFWAFFASSLTPTIEIGNIWPPKGINTFNaLEIPLV----NTLILLGSGVTITYAHHAITAGL 164
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALRIGH-FNIPLVliaiMTFILITSSGTMAMAVNFGYRGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 165 KLEALWGLILTVVLAIIFTCFQAYEYLNADFKISDG---------IYGSCFFMATGFHGFHVIIGTIFIIvsLIRLNLNQ 235
Cdd:cd02864 89 RKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLI--IIARKVWR 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 2307924995 236 FTTAHHFGF---EAAAFYWHFVDVVWLFLYVAVYFW 268
Cdd:cd02864 167 GKYQRIGRYeivEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
135-266 |
8.06e-17 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 76.88 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 135 ALEIPLVNTLILLGSGVTITYAHHAItaGLKLEALWgLILTVVLAIIFTCFQAYEYLNADFKISDGIYGSCFFMATGFHG 214
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLL--GWKYCDLF-LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2307924995 215 FHVIIGTIfIIVSLIRLNLNQFTTAHHfgfEAAAFYWHFVDVVWLFLYVAVY 266
Cdd:MTH00049 166 SHVVLGVV-GLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
139-268 |
5.43e-13 |
|
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: 65.85 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 139 PLVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTCFQAYE--YLNADFKISDG-IYGSCFFMATGFHGF 215
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAwhALNDAGYGPTSnPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2307924995 216 HVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFW 268
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
136-269 |
2.96e-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: 63.72 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 136 LEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTCFQAYE---YLNADFKISDGIYGSCFFMATGF 212
Cdd:TIGR02897 52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGT 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2307924995 213 HGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFWG 269
Cdd:TIGR02897 132 HGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
127-271 |
9.56e-10 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 57.10 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307924995 127 PKGINTFNaLEIPLVNTLILLGSGVTITYAHHAITAGLKLEALWGLILTVVLAIIFTCFQAYEY---LNADFKISDGIYG 203
Cdd:PRK10663 58 PTGKDIFE-LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2307924995 204 SCFFMATGFHGFHVIIGTIFIIVSLIRLNLNQFTTAHHFGFEAAAFYWHFVDVVWLFLYVAVYFWGGL 271
Cdd:PRK10663 137 SAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
|
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