|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
1.26e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 334.55 E-value: 1.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 8 GYHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILF 87
Cdd:MTH00141 5 PFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 88 IFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLT 167
Cdd:MTH00141 85 IVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 168 VSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVD 247
Cdd:MTH00141 165 IILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVD 244
|
250
....*....|....*
gi 1181491984 248 VIWVFLFLWVYCWGS 262
Cdd:MTH00141 245 VVWLFLYLSIYWWGS 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
1.65e-105 |
|
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: 305.59 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 19 FVASLGALGMVTGLVKWFHLF-LYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFIFSEVLFFFS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 98 FFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGAYFTML 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 178 QYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWV 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1181491984 258 YCW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
8.84e-98 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 286.61 E-value: 8.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFL--YDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMIL 86
Cdd:pfam00510 3 FHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 87 FIFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLL 166
Cdd:pfam00510 83 FIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 167 TVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFV 246
Cdd:pfam00510 163 TILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFV 242
|
250
....*....|....*.
gi 1181491984 247 DVIWVFLFLWVYCWGS 262
Cdd:pfam00510 243 DVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-258 |
8.26e-39 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 133.82 E-value: 8.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 72 HPVIVMRGLKMGMILFIFSEVLFFFSFFWAFFHASLApsveigSVWPPVGIECLNsWGVPLLNTAVLLGSGVSVTWCHHS 151
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLD-LPLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 152 VKNKVKNEALVAMLLTVSLGAYFTMLQYGEY---VEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHF 228
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|
gi 1181491984 229 SEERHFGMEAAIWYWHFVDVIWVFLFLWVY 258
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVY 190
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
2.02e-07 |
|
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: 49.85 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 132 LLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGA---YFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAgfvGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1181491984 209 VMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWVYCWG 261
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
8-262 |
1.26e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 334.55 E-value: 1.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 8 GYHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILF 87
Cdd:MTH00141 5 PFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 88 IFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLT 167
Cdd:MTH00141 85 IVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 168 VSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVD 247
Cdd:MTH00141 165 IILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVD 244
|
250
....*....|....*
gi 1181491984 248 VIWVFLFLWVYCWGS 262
Cdd:MTH00141 245 VVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
9-258 |
2.29e-114 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 328.68 E-value: 2.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00155 6 FHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00155 86 VSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00155 166 ILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDV 245
|
250
....*....|
gi 1181491984 249 IWVFLFLWVY 258
Cdd:MTH00155 246 VWLFLYISIY 255
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
9-262 |
6.68e-111 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 320.00 E-value: 6.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00189 7 FHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00189 87 TSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00189 167 ILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDV 246
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00189 247 VWLFLYVSIYWWGS 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-260 |
1.65e-105 |
|
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: 305.59 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 19 FVASLGALGMVTGLVKWFHLF-LYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFIFSEVLFFFS 97
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 98 FFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGAYFTML 177
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 178 QYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWV 257
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1181491984 258 YCW 260
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
9-262 |
1.25e-104 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 304.34 E-value: 1.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00039 7 YHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00039 87 TSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00039 167 LLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDV 246
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00039 247 VWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
9-262 |
2.59e-104 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 303.41 E-value: 2.59e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00118 8 YHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00118 88 TSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00118 168 LLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDV 247
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00118 248 VWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
9-262 |
1.87e-100 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 293.62 E-value: 1.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00219 9 YHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00219 89 VSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00219 169 LLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDV 248
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00219 249 VWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-262 |
3.09e-98 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 288.16 E-value: 3.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 1 MTRYGYAgYHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGL 80
Cdd:MTH00099 1 MTHQTHA-YHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 81 KMGMILFIFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEA 160
Cdd:MTH00099 80 RYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 161 LVAMLLTVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAI 240
Cdd:MTH00099 160 LQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 1181491984 241 WYWHFVDVIWVFLFLWVYCWGS 262
Cdd:MTH00099 240 WYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
9-262 |
8.84e-98 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 286.61 E-value: 8.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFL--YDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMIL 86
Cdd:pfam00510 3 FHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 87 FIFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLL 166
Cdd:pfam00510 83 FIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 167 TVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFV 246
Cdd:pfam00510 163 TILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFV 242
|
250
....*....|....*.
gi 1181491984 247 DVIWVFLFLWVYCWGS 262
Cdd:pfam00510 243 DVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
6-262 |
5.30e-97 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 284.72 E-value: 5.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 6 YAGYHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMI 85
Cdd:MTH00024 5 YHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 86 LFIFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAML 165
Cdd:MTH00024 85 LFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 166 LTVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHF 245
Cdd:MTH00024 165 LTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHF 244
|
250
....*....|....*..
gi 1181491984 246 VDVIWVFLFLWVYCWGS 262
Cdd:MTH00024 245 VDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
9-262 |
8.80e-96 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 281.65 E-value: 8.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00130 8 YHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00130 88 TSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00130 168 LLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDV 247
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00130 248 VWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
9-262 |
7.18e-94 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 277.01 E-value: 7.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00075 248 VWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
2.39e-91 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 270.51 E-value: 2.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 1 MTRYGYAGYHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 81 KMGMILFIFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 161 LVAMLLTVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAI 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 1181491984 241 WYWHFVDVIWVFLFLWVYCWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
9-262 |
1.08e-90 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 268.63 E-value: 1.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00009 6 FHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTV 168
Cdd:MTH00009 86 ASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00009 166 LLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDV 245
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00009 246 VWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
6-262 |
1.37e-86 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 259.61 E-value: 1.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 6 YAGYHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMI 85
Cdd:MTH00028 5 YHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 86 LFIFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSV------------- 152
Cdd:MTH00028 85 LFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIigtgnpaslekgt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 153 -----------------------KNKVKNEALVAMLLTVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHV 209
Cdd:MTH00028 165 qgiegpnpsngappdpqkgptflLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1181491984 210 MIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWVYCWGS 262
Cdd:MTH00028 245 LVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
9-261 |
7.67e-71 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 218.38 E-value: 7.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFL--YDLVTLSFICVLICAWMWWRDIIREGTLTGKHPVIVMRGLKMGMIL 86
Cdd:PLN02194 9 YHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 87 FIFSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLL 166
Cdd:PLN02194 89 FIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 167 TVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFV 246
Cdd:PLN02194 169 TVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFV 248
|
250
....*....|....*
gi 1181491984 247 DVIWVFLFLWVYCWG 261
Cdd:PLN02194 249 DVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
9-262 |
2.18e-67 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 209.43 E-value: 2.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 9 YHMVEGSAWPFVASLGALGMVTGLVKWFHLFLYDLVTLSFICVLICAWMWWRDIIREGtLTGKHPVIVMRGLKMGMILFI 88
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 89 FSEVLFFFSFFWAFFHASLAPSVEIGSVWPPVGIECLNSWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNeALVAMLLTV 168
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKS-CTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 169 SLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDV 248
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|....
gi 1181491984 249 IWVFLFLWVYCWGS 262
Cdd:MTH00083 243 VWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
1.07e-55 |
|
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: 177.01 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 72 HPVIVMRGLKMGMILFIFSEVLFFFSFFWAFFHASLAPSVEIGSVwppvgiecLNSWGVPLLNTAVLLGSGVSVTWCHHS 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAG--------LDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 152 VKNKVKN--EALVAMLLTVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHFS 229
Cdd:cd00386 73 LAARRGNrkKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1181491984 230 EERHFGMEAAIWYWHFVDVIWVFLFLWVYCW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
72-258 |
8.26e-39 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 133.82 E-value: 8.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 72 HPVIVMRGLKMGMILFIFSEVLFFFSFFWAFFHASLApsveigSVWPPVGIECLNsWGVPLLNTAVLLGSGVSVTWCHHS 151
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLD-LPLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 152 VKNKVKNEALVAMLLTVSLGAYFTMLQYGEY---VEASYSIADSGYGSSFFLATGFHGAHVMIGSLFLTVCFFRVYFDHF 228
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|
gi 1181491984 229 SEERHFGMEAAIWYWHFVDVIWVFLFLWVY 258
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVY 190
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
127-258 |
4.40e-18 |
|
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: 79.59 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 127 SWGVPLLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGAYFTMLQYGEY---VEASYSIADSGYGSSFFLATG 203
Cdd:cd02862 50 DLLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTG 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1181491984 204 FHGAHVMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWVY 258
Cdd:cd02862 130 FHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
132-258 |
7.15e-15 |
|
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: 70.73 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 132 LLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGAYFTMLQYGE---YVEASYSIADSGYGSSFFLATGFHGAH 208
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1181491984 209 VMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWVY 258
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
135-260 |
2.84e-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: 239215 Cd Length: 202 Bit Score: 66.76 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 135 TAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGAYFTMLQYGEYVE---------ASYSIADSGYGSSFFLATGFH 205
Cdd:cd02864 67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFH 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1181491984 206 GAHVMIGSLFLTVCFFRVYFDHFSEERHFGM-EAAIWYWHFVDVIWVFLFLWVYCW 260
Cdd:cd02864 147 GTHVTIGVIYLIIIARKVWRGKYQRIGRYEIvEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
6.03e-13 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 66.09 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 127 SWGVPLLNTAVLLGSGVSVTWCHHSVKNKvknEALVAMLLTVSLGAYFTMLQYGEYVEASYSIADSGYGSSFFLATGFHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLGWK---YCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1181491984 207 AHVMIGSLFLTVCFfrvYFDHFSEERHFGmEAAIWYWHFVDVIWVFLFLWVY 258
Cdd:MTH00049 166 SHVVLGVVGLSTLL---LVGSSSFGVYRS-TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
2.02e-07 |
|
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: 49.85 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 132 LLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGA---YFTMLQYGEYVEASYSIADSGYGSSFFLATGFHGAH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAgfvGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1181491984 209 VMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWVYCWG 261
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
132-262 |
1.07e-05 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 45.16 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491984 132 LLNTAVLLGSGVSVTWCHHSVKNKVKNEALVAMLLTVSLGAYFTMLQYGEY---VEASYSIADSGYGSSFFLATGFHGAH 208
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFhhlIVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1181491984 209 VMIGSLFLTVCFFRVYFDHFSEERHFGMEAAIWYWHFVDVIWVFLFLWVYCWGS 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
