|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
7.59e-170 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 469.27 E-value: 7.59e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 1 MMQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 81 KYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 161 IRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 63025145 241 WYWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-260 |
1.88e-119 |
|
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: 341.03 E-value: 1.88e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 20 IGACGAFFTTVGGVMYFH-YSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGMLLFILSEVCLFFSF 98
Cdd:cd01665 2 LGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 99 FWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQ 178
Cdd:cd01665 82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 179 AMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMY 258
Cdd:cd01665 162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVY 241
|
..
gi 63025145 259 WW 260
Cdd:cd01665 242 WW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
6.29e-118 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 337.85 E-value: 6.29e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 7 HPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYS--QSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 85 LLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 165 ALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 63025145 245 FVDVVWLFLFTFMYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
1.24e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 161.56 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 71 HHTLIVKQGLKYGMLLFILSEVCLFFSFFWAFFHSSLVptieiGAVWPPrGVDPLDPfSIPLLNTAVLLSSGATVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 151 GIISGKRKEAIRGLALTVILGLIFTGLQAMEYYE---APFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 63025145 228 FTRHHHVGFEAAAWYWHFVDVVWLFLFTFMYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
121-261 |
3.20e-11 |
|
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: 60.64 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 121 GVDPLDPFSIPLL--NTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQAME---YYEAPFTISDSVYG 195
Cdd:TIGR02897 43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025145 196 STFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
7.59e-170 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 469.27 E-value: 7.59e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 1 MMQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00052 1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 81 KYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
Cdd:MTH00052 81 KYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 161 IRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAA 240
Cdd:MTH00052 161 IIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 63025145 241 WYWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00052 241 WYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
2-262 |
1.74e-144 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 405.29 E-value: 1.74e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 2 MQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 82 YGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
Cdd:MTH00024 81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 162 RGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAW 241
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240
|
250 260
....*....|....*....|.
gi 63025145 242 YWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
4.44e-137 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 386.23 E-value: 4.44e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 1 MMQQTyHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00118 1 MTHQA-HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 81 KYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
Cdd:MTH00118 80 RYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 161 IRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAA 240
Cdd:MTH00118 160 IQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 63025145 241 WYWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00118 240 WYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
4.59e-131 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 371.23 E-value: 4.59e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 1 MMQQtyHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00189 1 MHQA--HPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 81 KYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
Cdd:MTH00189 79 RYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 161 IRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAA 240
Cdd:MTH00189 159 IQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAA 238
|
250 260
....*....|....*....|..
gi 63025145 241 WYWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00189 239 WYWHFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
5-258 |
3.33e-129 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 366.04 E-value: 3.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 5 TYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGM 84
Cdd:MTH00155 2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 85 LLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGL 164
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 165 ALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWH 244
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 63025145 245 FVDVVWLFLFTFMY 258
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
7-262 |
3.27e-127 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 361.35 E-value: 3.27e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 7 HPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGMLL 86
Cdd:MTH00039 5 HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 87 FILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLAL 166
Cdd:MTH00039 85 FITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 167 TVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFV 246
Cdd:MTH00039 165 TVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFV 244
|
250
....*....|....*.
gi 63025145 247 DVVWLFLFTFMYWWGS 262
Cdd:MTH00039 245 DVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
2.52e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 349.04 E-value: 2.52e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 2 MQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00075 1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 82 YGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
Cdd:MTH00075 81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 162 RGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAW 241
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 63025145 242 YWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
7-262 |
4.54e-122 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 348.42 E-value: 4.54e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 7 HPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGMLL 86
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 87 FILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLAL 166
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 167 TVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFV 246
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 63025145 247 DVVWLFLFTFMYWWGS 262
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
2.63e-120 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 344.05 E-value: 2.63e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 2 MQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00130 1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 82 YGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
Cdd:MTH00130 81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 162 RGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAW 241
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240
|
250 260
....*....|....*....|.
gi 63025145 242 YWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
20-260 |
1.88e-119 |
|
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: 341.03 E-value: 1.88e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 20 IGACGAFFTTVGGVMYFH-YSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGMLLFILSEVCLFFSF 98
Cdd:cd01665 2 LGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 99 FWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQ 178
Cdd:cd01665 82 FWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 179 AMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMY 258
Cdd:cd01665 162 AYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVY 241
|
..
gi 63025145 259 WW 260
Cdd:cd01665 242 WW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
7-262 |
6.29e-118 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 337.85 E-value: 6.29e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 7 HPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYS--QSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGM 84
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 85 LLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGL 164
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 165 ALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWH 244
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 63025145 245 FVDVVWLFLFTFMYWWGS 262
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
1-262 |
5.55e-117 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 335.54 E-value: 5.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 1 MMQQTyHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00099 1 MTHQT-HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 81 KYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
Cdd:MTH00099 80 RYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 161 IRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAA 240
Cdd:MTH00099 160 LQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAA 239
|
250 260
....*....|....*....|..
gi 63025145 241 WYWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00099 240 WYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
2-262 |
7.85e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 333.96 E-value: 7.85e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 2 MQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLK 81
Cdd:MTH00028 1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 82 YGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGK----- 156
Cdd:MTH00028 81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 157 -------------------------------RKEAIRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAH 205
Cdd:MTH00028 161 ekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 63025145 206 GGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00028 241 GLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-262 |
2.23e-112 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 324.05 E-value: 2.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 1 MMQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGL 80
Cdd:MTH00219 1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 81 KYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEA 160
Cdd:MTH00219 81 RIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 161 IRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAA 240
Cdd:MTH00219 161 QQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
|
250 260
....*....|....*....|..
gi 63025145 241 WYWHFVDVVWLFLFTFMYWWGS 262
Cdd:MTH00219 241 WYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
7-262 |
7.32e-107 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 309.84 E-value: 7.32e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 7 HPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQGLKYGMLL 86
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 87 FILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLAL 166
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 167 TVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFV 246
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 63025145 247 DVVWLFLFTFMYWWGS 262
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
1-261 |
4.32e-96 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 282.71 E-value: 4.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 1 MMQQTYHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQ--SWVLIIGLTVIVFTMIVWWRDVIREATYQGHHTLIVKQ 78
Cdd:PLN02194 1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 79 GLKYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKRK 158
Cdd:PLN02194 81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 159 EAIRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEA 238
Cdd:PLN02194 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
|
250 260
....*....|....*....|...
gi 63025145 239 AAWYWHFVDVVWLFLFTFMYWWG 261
Cdd:PLN02194 241 AAWYWHFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
6-262 |
1.11e-71 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 220.21 E-value: 1.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 6 YHPYHLVDPSPWPYIGACGAFFTTVGGVMYFHYSQSWVLIIGLTVIVFTMIVWWRDVIREAtYQGHHTLIVKQGLKYGML 85
Cdd:MTH00083 2 FHNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 86 LFILSEVCLFFSFFWAFFHSSLVPTIEIGAVWPPRGVDPLDPFSIPLLNTAVLLSSGATVTWAHHGIISGKrKEAIRGLA 165
Cdd:MTH00083 81 LFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 166 LTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHF 245
Cdd:MTH00083 160 LTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHF 239
|
250
....*....|....*..
gi 63025145 246 VDVVWLFLFTFMYWWGS 262
Cdd:MTH00083 240 VDVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
72-260 |
1.48e-63 |
|
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: 197.04 E-value: 1.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 72 HTLIVKQGLKYGMLLFILSEVCLFFSFFWAFFHSSLVPTIEIGAvwpprgvdPLDPFSIPLLNTAVLLSSGATVTWAHHG 151
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 152 II--SGKRKEAIRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFT 229
Cdd:cd00386 73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 63025145 230 RHHHVGFEAAAWYWHFVDVVWLFLFTFMYWW 260
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
71-260 |
1.24e-49 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 161.56 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 71 HHTLIVKQGLKYGMLLFILSEVCLFFSFFWAFFHSSLVptieiGAVWPPrGVDPLDPfSIPLLNTAVLLSSGATVTWAHH 150
Cdd:COG1845 7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDL-PLPLINTLLLLLSSFTVALAVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 151 GIISGKRKEAIRGLALTVILGLIFTGLQAMEYYE---APFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHH 227
Cdd:COG1845 80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159
|
170 180 190
....*....|....*....|....*....|...
gi 63025145 228 FTRHHHVGFEAAAWYWHFVDVVWLFLFTFMYWW 260
Cdd:COG1845 160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
132-258 |
2.02e-26 |
|
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: 101.54 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 132 LLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQAMEYYE---APFTISDSVYGSTFFVTTGAHGGH 208
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 63025145 209 VLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMY 258
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
121-258 |
2.97e-23 |
|
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: 93.07 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 121 GVDPLDPFSIPL--LNTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQAME---YYEAPFTISDSVYG 195
Cdd:cd02863 41 GPPGHELFELPLvfIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63025145 196 STFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMY 258
Cdd:cd02863 121 SAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
131-260 |
5.76e-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: 84.34 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 131 PLLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQAMEYYEAPF---TISDSVYGSTFFVTTGAHGG 207
Cdd:cd02865 52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 63025145 208 HVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMYWW 260
Cdd:cd02865 132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
124-260 |
2.15e-16 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 75.23 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 124 PLDPFSIPL----LNTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQAMEYYE---------APFTIS 190
Cdd:cd02864 52 RIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKliveegvrpWGNPWG 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63025145 191 DSVYGSTFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRH-HHVGFEAAAWYWHFVDVVWLFLFTFMYWW 260
Cdd:cd02864 132 AAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
126-258 |
6.20e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.18 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 126 DPFSIPLLNTAVLLSSGATVTWAHHGIISgkrKEAIRGLALTVILGLIFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAH 205
Cdd:MTH00049 88 SSLEIPFVGCFLLLGSSITVTAYHHLLGW---KYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLH 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 63025145 206 GGHVLIGSsFLLVCLYRLVTHHFTRHHHvgfEAAAWYWHFVDVVWLFLFTFMY 258
Cdd:MTH00049 165 FSHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
121-261 |
3.20e-11 |
|
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: 60.64 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 121 GVDPLDPFSIPLL--NTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTGLQAME---YYEAPFTISDSVYG 195
Cdd:TIGR02897 43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025145 196 STFFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMYWWG 261
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
126-262 |
1.69e-09 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 56.33 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025145 126 DPFSIP--LLNTAVLLSSGATVTWAHHGIISGKRKEAIRGLALTVILGLIFTglqAMEYYEAPFTISD------SVYGST 197
Cdd:PRK10663 62 DIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEgmgpdrSGFLSA 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63025145 198 FFVTTGAHGGHVLIGSSFLLVCLYRLVTHHFTRHHHVGFEAAAWYWHFVDVVWLFLFTFMYWWGS 262
Cdd:PRK10663 139 FFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
|
|
| |
