|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-256 |
1.00e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 362.19 E-value: 1.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 4 LQPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGML 83
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 84 LFIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALL 163
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 164 VTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHF 243
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 1016841407 244 VDIVWLFLFTFMY 256
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
17-258 |
1.81e-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: 1.81e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 17 LMGSLATFTFMLSMINLMHFT-NTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLLFIISEIFFFMS 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 96 FFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTIL 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 176 QMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFM 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1016841407 256 YWW 258
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-260 |
1.74e-100 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 293.55 E-value: 1.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 6 PFHLVTKSPWPLMGSLATFTFMLSMINLMHF--TNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGML 83
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 84 LFIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALL 163
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 164 VTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHF 243
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 1016841407 244 VDIVWLFLFTFMYWWPY 260
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
125-258 |
8.67e-45 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 149.23 E-value: 8.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 125 PLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWEYYQ---APFSISDSIYGTTFFMSTG 201
Cdd:COG1845 56 DLPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTG 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1016841407 202 FHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMYWW 258
Cdd:COG1845 136 FHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
126-256 |
5.45e-11 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 59.96 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 126 LSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWEYYQ---APFSISDSIYGTTFFMSTGF 202
Cdd:TIGR02842 42 LPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFYHliaEGNGPDRSAFLSAFFTLVGT 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1016841407 203 HGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMY 256
Cdd:TIGR02842 122 HGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVY 175
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
4-256 |
1.00e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 362.19 E-value: 1.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 4 LQPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGML 83
Cdd:MTH00155 3 NHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 84 LFIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALL 163
Cdd:MTH00155 83 LFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 164 VTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHF 243
Cdd:MTH00155 163 FTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHF 242
|
250
....*....|...
gi 1016841407 244 VDIVWLFLFTFMY 256
Cdd:MTH00155 243 VDVVWLFLYISIY 255
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
6-258 |
4.25e-113 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 325.39 E-value: 4.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 6 PFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLLF 85
Cdd:MTH00189 6 PFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 86 IISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVT 165
Cdd:MTH00189 86 ITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 166 ILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVD 245
Cdd:MTH00189 166 VILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVD 245
|
250
....*....|...
gi 1016841407 246 IVWLFLFTFMYWW 258
Cdd:MTH00189 246 VVWLFLYVSIYWW 258
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.22e-112 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 324.21 E-value: 1.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 4 LQPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGML 83
Cdd:MTH00118 5 AHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 84 LFIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALL 163
Cdd:MTH00118 85 LFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 164 VTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHF 243
Cdd:MTH00118 165 LTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHF 244
|
250
....*....|....*
gi 1016841407 244 VDIVWLFLFTFMYWW 258
Cdd:MTH00118 245 VDVVWLFLYISIYWW 259
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
5-260 |
9.49e-110 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 316.83 E-value: 9.49e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 5 QPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLL 84
Cdd:MTH00141 4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 85 FIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLV 164
Cdd:MTH00141 84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 165 TILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFV 244
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243
|
250
....*....|....*.
gi 1016841407 245 DIVWLFLFTFMYWWPY 260
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
1-258 |
5.76e-107 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 310.12 E-value: 5.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 1 MTFLQPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKS 80
Cdd:MTH00039 1 MTHQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 81 GMLLFIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQK 160
Cdd:MTH00039 81 GMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 161 ALLVTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWY 240
Cdd:MTH00039 161 ALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWY 240
|
250
....*....|....*...
gi 1016841407 241 WHFVDIVWLFLFTFMYWW 258
Cdd:MTH00039 241 WHFVDVVWLFLYVCIYWW 258
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
17-258 |
1.81e-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: 1.81e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 17 LMGSLATFTFMLSMINLMHFT-NTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLLFIISEIFFFMS 95
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYgGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 96 FFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTIL 175
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 176 QMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFM 255
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 1016841407 256 YWW 258
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
5-258 |
1.85e-105 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 306.33 E-value: 1.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 5 QPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLL 84
Cdd:MTH00219 7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 85 FIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLV 164
Cdd:MTH00219 87 FIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 165 TILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFV 244
Cdd:MTH00219 167 TILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFV 246
|
250
....*....|....
gi 1016841407 245 DIVWLFLFTFMYWW 258
Cdd:MTH00219 247 DVVWLFLYVSIYWW 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
6-258 |
5.02e-103 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 300.10 E-value: 5.02e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 6 PFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLLF 85
Cdd:MTH00099 7 AYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 86 IISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVT 165
Cdd:MTH00099 87 IISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 166 ILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVD 245
Cdd:MTH00099 167 ILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVD 246
|
250
....*....|...
gi 1016841407 246 IVWLFLFTFMYWW 258
Cdd:MTH00099 247 VVWLFLYVSIYWW 259
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
2-258 |
1.43e-100 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 293.97 E-value: 1.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 2 TFLQPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSG 81
Cdd:MTH00024 3 KLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 82 MLLFIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKA 161
Cdd:MTH00024 83 MLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 162 LLVTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYW 241
Cdd:MTH00024 163 LFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYW 242
|
250
....*....|....*..
gi 1016841407 242 HFVDIVWLFLFTFMYWW 258
Cdd:MTH00024 243 HFVDVVWLFLYLCIYWW 259
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
6-260 |
1.74e-100 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 293.55 E-value: 1.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 6 PFHLVTKSPWPLMGSLATFTFMLSMINLMHF--TNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGML 83
Cdd:pfam00510 2 PFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 84 LFIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALL 163
Cdd:pfam00510 82 LFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 164 VTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHF 243
Cdd:pfam00510 162 LTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHF 241
|
250
....*....|....*..
gi 1016841407 244 VDIVWLFLFTFMYWWPY 260
Cdd:pfam00510 242 VDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
5-258 |
6.37e-100 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 292.08 E-value: 6.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 5 QPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLL 84
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 85 FIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLV 164
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 165 TILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFV 244
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....
gi 1016841407 245 DIVWLFLFTFMYWW 258
Cdd:MTH00052 247 DVVWLFLFIFMYWW 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
7-258 |
1.51e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 286.26 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 7 FHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLLFI 86
Cdd:MTH00075 8 FHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 87 ISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTI 166
Cdd:MTH00075 88 TSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 167 LLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDI 246
Cdd:MTH00075 168 ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDV 247
|
250
....*....|..
gi 1016841407 247 VWLFLFTFMYWW 258
Cdd:MTH00075 248 VWLFLYVSIYWW 259
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
6-258 |
1.62e-95 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 280.88 E-value: 1.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 6 PFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLLF 85
Cdd:MTH00130 7 AYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 86 IISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVT 165
Cdd:MTH00130 87 ITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 166 ILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVD 245
Cdd:MTH00130 167 ILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVD 246
|
250
....*....|...
gi 1016841407 246 IVWLFLFTFMYWW 258
Cdd:MTH00130 247 VVWLFLYISIYWW 259
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
5-258 |
4.49e-93 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 274.79 E-value: 4.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 5 QPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLL 84
Cdd:MTH00009 4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 85 FIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLV 164
Cdd:MTH00009 84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 165 TILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFV 244
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243
|
250
....*....|....
gi 1016841407 245 DIVWLFLFTFMYWW 258
Cdd:MTH00009 244 DVVWIFLYLCIYWW 257
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
5-258 |
1.09e-88 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 265.01 E-value: 1.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 5 QPFHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLL 84
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 85 FIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLI-----KKHFSETQ 159
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIgtgnpASLEKGTQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 160 K-------------------------------ALLVTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVM 208
Cdd:MTH00028 166 GiegpnpsngappdpqkgptfllsdfrtnaviGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1016841407 209 IGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMYWW 258
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWW 295
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
7-258 |
3.65e-74 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 226.85 E-value: 3.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 7 FHLVTKSPWPLMGSLATFTFMLSMINLMH--FTNTNMIFLAFVISILTMYQWWRDICREATFQGYHTMIVSKNTKSGMLL 84
Cdd:PLN02194 9 YHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 85 FIISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLV 164
Cdd:PLN02194 89 FIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 165 TILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFV 244
Cdd:PLN02194 169 TVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFV 248
|
250
....*....|....
gi 1016841407 245 DIVWLFLFTFMYWW 258
Cdd:PLN02194 249 DVVWLFLFVSIYWW 262
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
7-260 |
1.90e-62 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 196.72 E-value: 1.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 7 FHLVTKSPWPLMGSLATFTFMLSMINLMHFTNTNMIFLAFVISILTMYQWWRDICREAtFQGYHTMIVSKNTKSGMLLFI 86
Cdd:MTH00083 5 FHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 87 ISEIFFFMSFFWAFFHSSLSPNIEIGSQWPPINIQPFNPLSVPLLNTTILLSSGISITWAHHSLIKKHfSETQKALLVTI 166
Cdd:MTH00083 84 FSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 167 LLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDI 246
Cdd:MTH00083 163 FLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDV 242
|
250
....*....|....
gi 1016841407 247 VWLFLFTFMYWWPY 260
Cdd:MTH00083 243 VWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
70-258 |
4.58e-59 |
|
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: 185.48 E-value: 4.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 70 HTMIVSKNTKSGMLLFIISEIFFFMSFFWAFFHSSLSPNIEIGsqwppiniQPFNPLSVPLLNTTILLSSGISITWAHHS 149
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 150 LIKKH--FSETQKALLVTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFNQFS 227
Cdd:cd00386 73 LAARRgnRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1016841407 228 KSHHFGFEASAWYWHFVDIVWLFLFTFMYWW 258
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
125-258 |
8.67e-45 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 149.23 E-value: 8.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 125 PLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWEYYQ---APFSISDSIYGTTFFMSTG 201
Cdd:COG1845 56 DLPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTG 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1016841407 202 FHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMYWW 258
Cdd:COG1845 136 FHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
130-256 |
1.23e-21 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 88.83 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 130 LLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWEYY---QAPFSISDSIYGTTFFMSTGFHGLH 206
Cdd:cd02862 55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAhkiAAGIDPDAGLFFTLYFLLTGFHLLH 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1016841407 207 VMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMY 256
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
130-256 |
3.24e-18 |
|
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 79.59 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 130 LLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWE---YYQAPFSISDSIYGTTFFMSTGFHGLH 206
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1016841407 207 VMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMY 256
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
79-258 |
1.04e-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: 76.00 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 79 KSGMLLFIISEIFFFMSFFWAFFHSSLSPNIEIG--SQWPPINIQPFN-PLSVPLLNTTILLSSGISITWAHHSLIKKHF 155
Cdd:cd02864 10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPlpSDVFALRIGHFNiPLVLIAIMTFILITSSGTMAMAVNFGYRGNR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 156 SETQKALLVTILLGILFTILQMWEY-----------YQAPFSISdsIYGTTFFMSTGFHGLHVMIGTTFLLMMYIRLNFN 224
Cdd:cd02864 90 KAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRG 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1016841407 225 QFSKSHHFG-FEASAWYWHFVDIVWLFLFTFMYWW 258
Cdd:cd02864 168 KYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
122-258 |
1.32e-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: 239216 Cd Length: 184 Bit Score: 75.48 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 122 PFNPLSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWEYYQAPFSI---SDSIYGTTFFM 198
Cdd:cd02865 45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYL 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 199 STGFHGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMYWW 258
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
125-256 |
6.70e-16 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 74.18 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 125 PLSVPLLNTTILLSSGISITWAHHSLIKKHFSetqKALLVTILLGILFTILQMWEYYQAPFSISDSIYGTTFFMSTGFHG 204
Cdd:MTH00049 89 SLEIPFVGCFLLLGSSITVTAYHHLLGWKYCD---LFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1016841407 205 LHVMIGTtFLLMMYIRLNFNQFSKSHHfgfEASAWYWHFVDIVWLFLFTFMY 256
Cdd:MTH00049 166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
126-256 |
5.45e-11 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 59.96 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 126 LSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWEYYQ---APFSISDSIYGTTFFMSTGF 202
Cdd:TIGR02842 42 LPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAITFLLGLGFIGMEIYEFYHliaEGNGPDRSAFLSAFFTLVGT 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1016841407 203 HGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMY 256
Cdd:TIGR02842 122 HGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFWHFLDIVWICVFTFVY 175
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
126-256 |
3.28e-08 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 52.48 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016841407 126 LSVPLLNTTILLSSGISITWAHHSLIKKHFSETQKALLVTILLGILFTILQMWEYYQ---APFSISDSIYGTTFFMSTGF 202
Cdd:PRK10663 66 LPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHlivEGMGPDRSGFLSAFFALVGT 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1016841407 203 HGLHVMIGTTFLLMMYIRLNFNQFSKSHHFGFEASAWYWHFVDIVWLFLFTFMY 256
Cdd:PRK10663 146 HGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
|
|
| |
