|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
2-262 |
1.58e-157 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 438.03 E-value: 1.58e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 2 RTVLCHPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIK 81
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 82 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAI 161
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 162 LGLSLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASW 241
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 62161345 242 YWHFVDVVWLFLYLCVYWWGS 262
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-260 |
1.40e-114 |
|
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: 328.71 E-value: 1.40e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 20 LGAGGAFLITVGSVMYFHYGLSQ-IMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLLFILSEVLFFFSF 98
Cdd:cd01665 2 LGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 99 FWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQ 178
Cdd:cd01665 82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 179 GIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVY 258
Cdd:cd01665 162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVY 241
|
..
gi 62161345 259 WW 260
Cdd:cd01665 242 WW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
1.28e-111 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 321.67 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGL--SQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 85 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 165 SLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 62161345 245 FVDVVWLFLYLCVYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
81-260 |
4.16e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 157.70 E-value: 4.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 81 KYGMLLFILSEVLFFFSFFWAFFHSSLAPAvelgvvWPPQGVHPLNsFSVPLLNTAVLLSSGATVTWAHHAIISGKREEA 160
Cdd:COG1845 17 KLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLD-LPLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 161 ILGLSLTVFLGVLFTGLQGIEYYE---APFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFE 237
Cdd:COG1845 90 RLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169
|
170 180
....*....|....*....|...
gi 62161345 238 AASWYWHFVDVVWLFLYLCVYWW 260
Cdd:COG1845 170 AAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
1.76e-10 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 58.71 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 132 LLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQGIE---YYEAPFTISDSVYGSTFFMATGFHGFH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 62161345 209 VLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVYWWG 261
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
2-262 |
1.58e-157 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 438.03 E-value: 1.58e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 2 RTVLCHPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIK 81
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 82 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAI 161
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 162 LGLSLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASW 241
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 62161345 242 YWHFVDVVWLFLYLCVYWWGS 262
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.41e-134 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 380.29 E-value: 1.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00052 247 DVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
2.10e-131 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 371.98 E-value: 2.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00118 6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00118 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00118 166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00118 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
2.81e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 363.91 E-value: 2.81e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00189 5 HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00189 85 FITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00189 165 TVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00189 245 DVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
7-258 |
3.65e-124 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 353.33 E-value: 3.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00155 84 FIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00155 164 TIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFV 243
|
250
....*....|..
gi 62161345 247 DVVWLFLYLCVY 258
Cdd:MTH00155 244 DVVWLFLYISIY 255
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
9.25e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 347.65 E-value: 9.25e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
2.24e-120 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 344.02 E-value: 2.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
3.48e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 333.64 E-value: 3.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00075 6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00075 86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00075 166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00075 246 DVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
7-262 |
2.14e-115 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 331.31 E-value: 2.14e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00099 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00099 86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00099 166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00099 246 DVVWLFLYVSIYWWGS 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-260 |
1.40e-114 |
|
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: 328.71 E-value: 1.40e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 20 LGAGGAFLITVGSVMYFHYGLSQ-IMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLLFILSEVLFFFSF 98
Cdd:cd01665 2 LGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 99 FWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQ 178
Cdd:cd01665 82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 179 GIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVY 258
Cdd:cd01665 162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVY 241
|
..
gi 62161345 259 WW 260
Cdd:cd01665 242 WW 243
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
1.80e-114 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 329.03 E-value: 1.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00130 246 DVVWLFLYISIYWWGS 261
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
1.28e-111 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 321.67 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGL--SQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSgnMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 85 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 165 SLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 62161345 245 FVDVVWLFLYLCVYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
1.46e-109 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 316.73 E-value: 1.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 1 MRTVLCHPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGI 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 81 KYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEA 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 161 ILGLSLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAAS 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 62161345 241 WYWHFVDVVWLFLYLCVYWWGS 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
3-262 |
1.37e-108 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 315.47 E-value: 1.37e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 3 TVLCHPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKY 82
Cdd:MTH00028 2 SLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 83 GMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGK------ 156
Cdd:MTH00028 82 GMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasle 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 157 ------------------------------REEAILGLSLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHG 206
Cdd:MTH00028 162 kgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 62161345 207 FHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVYWWGS 262
Cdd:MTH00028 242 LHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-262 |
1.08e-103 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 301.76 E-value: 1.08e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSL 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
7-261 |
2.51e-93 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 275.77 E-value: 2.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFH--YGLSQIMYLGVLVIVMIMFVWWQDVIRESTFQGYHSLVVKQGIKYGM 84
Cdd:PLN02194 7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 85 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGL 164
Cdd:PLN02194 87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 165 SLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWH 244
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
|
250
....*....|....*..
gi 62161345 245 FVDVVWLFLYLCVYWWG 261
Cdd:PLN02194 247 FVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
3.07e-68 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 211.35 E-value: 3.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 7 HPYHLVEPSPWPCLGAGGAFLITVGSVMYFHYGLSQIMYLGVLVIVMIMFVWWQDVIREStFQGYHSLVVKQGIKYGMLL 86
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 87 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVHPLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILgLSL 166
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTNS-LLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 167 TVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFV 246
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 62161345 247 DVVWLFLYLCVYWWGS 262
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
1.54e-61 |
|
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: 191.65 E-value: 1.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 72 HSLVVKQGIKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGvvwppqgvHPLNSFSVPLLNTAVLLSSGATVTWAHHA 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 152 II--SGKREEAILGLSLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFT 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 62161345 230 SRQHVGFEAASWYWHFVDVVWLFLYLCVYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
81-260 |
4.16e-48 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 157.70 E-value: 4.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 81 KYGMLLFILSEVLFFFSFFWAFFHSSLAPAvelgvvWPPQGVHPLNsFSVPLLNTAVLLSSGATVTWAHHAIISGKREEA 160
Cdd:COG1845 17 KLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLD-LPLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 161 ILGLSLTVFLGVLFTGLQGIEYYE---APFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFE 237
Cdd:COG1845 90 RLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169
|
170 180
....*....|....*....|...
gi 62161345 238 AASWYWHFVDVVWLFLYLCVYWW 260
Cdd:COG1845 170 AAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
4.54e-23 |
|
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: 92.68 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 132 LLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQGIEYYE---APFTISDSVYGSTFFMATGFHGFH 208
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 62161345 209 VLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-260 |
2.51e-20 |
|
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: 85.50 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 124 PLNSFSVPLLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQGIEYYEAPF---TISDSVYGSTFFM 200
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 201 ATGFHGFHVLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVYWW 260
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
132-258 |
9.74e-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: 81.13 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 132 LLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQGIE---YYEAPFTISDSVYGSTFFMATGFHGFH 208
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 62161345 209 VLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVY 258
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
127-258 |
1.44e-15 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 73.41 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 127 SFSVPLLNTAVLLSSGATVTWAHHAIISgkrEEAILGLSLTVFLGVLFTGLQGIEYYEAPFTISDSVYGSTFFMATGFHG 206
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLGW---KYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 62161345 207 FHVLVGTTFLIICLIRLKFNQFTSRQHVgfeaASWYWHFVDVVWLFLYLCVY 258
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHFVDYIWLLVYLIVY 213
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
81-260 |
2.34e-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: 72.53 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 81 KYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGVhPLNSFSVPL----LNTAVLLSSGATVTWAHHAIISGK 156
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 157 REEAILGLSLTVFLGVLFTGLQGIEYYE---------APFTISDSVYGSTFFMATGFHGFHVLVGTTFLIICLIRLKFNQ 227
Cdd:cd02864 89 RKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 62161345 228 FTSR-QHVGFEAASWYWHFVDVVWLFLYLCVYWW 260
Cdd:cd02864 169 YQRIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
132-261 |
1.76e-10 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131943 Cd Length: 190 Bit Score: 58.71 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 132 LLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQGIE---YYEAPFTISDSVYGSTFFMATGFHGFH 208
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 62161345 209 VLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVYWWG 261
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
132-262 |
3.08e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 55.56 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161345 132 LLNTAVLLSSGATVTWAHHAIISGKREEAILGLSLTVFLGVLFTGLQGIEYY---EAPFTISDSVYGSTFFMATGFHGFH 208
Cdd:PRK10663 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRSGFLSAFFALVGTHGLH 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 62161345 209 VLVGTTFLIICLIRLKFNQFTSRQHVGFEAASWYWHFVDVVWLFLYLCVYWWGS 262
Cdd:PRK10663 150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
