|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
4.87e-149 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 416.30 E-value: 4.87e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 1 MTKHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLG 80
Cdd:MTH00189 2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 81 MILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNA 160
Cdd:MTH00189 82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 161 FLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYW 240
Cdd:MTH00189 162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241
|
250
....*....|....*....
gi 288903170 241 HFVDVVWIFLFISIYWWGY 259
Cdd:MTH00189 242 HFVDVVWLFLYVSIYWWGS 260
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
16-257 |
1.64e-120 |
|
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: 343.73 E-value: 1.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 16 LTGSIGAFCFTAGMAAYFNKYDQ-YLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMILFILSEVFFFLA 94
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGpLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 95 FFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLATICLGVYFTLL 174
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 175 QGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFVDVVWIFLFISI 254
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 288903170 255 YWW 257
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
4-259 |
1.26e-117 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 337.08 E-value: 1.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKY--DQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGM 81
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 82 ILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAF 161
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 162 LATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWH 241
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 288903170 242 FVDVVWIFLFISIYWWGY 259
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
69-257 |
2.24e-50 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 163.48 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 69 HTAKVESGMRLGMILFILSEVFFFLAFFWAYFHSALSpsieigAVWTPVGIQGINPfSVPLLNTVVLLSSGVTITWAHHC 148
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 149 ILAGYWTDTCNAFLATICLGVYFTLLQGFEYKVAS---FTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHF 225
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 288903170 226 SKKHHFGFEASAWYWHFVDVVWIFLFISIYWW 257
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
79-258 |
5.83e-06 |
|
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: 45.71 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 79 LGMILFILSEVFFFLAFFWAYFhsALSPSieigavwTPVGIQGINPFSVP--LLNTVVLLSSGVTITWAHHCILAGYWTD 156
Cdd:TIGR02842 3 FGFWLYLMSDCILFATLFATYA--VLSNN-------TAGGPSGKEIFDLPfvLVETFLLLLSSITFGFAMLAMNKKNKKM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 157 TCNAFLATICLGVYFTLLQGFEYK---VASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGF 233
Cdd:TIGR02842 74 VILWLAITFLLGLGFIGMEIYEFYhliAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRL 153
|
170 180
....*....|....*....|....*
gi 288903170 234 EASAWYWHFVDVVWIFLFISIYWWG 258
Cdd:TIGR02842 154 ACLSLFWHFLDIVWICVFTFVYLLG 178
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
4.87e-149 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 416.30 E-value: 4.87e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 1 MTKHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLG 80
Cdd:MTH00189 2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 81 MILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNA 160
Cdd:MTH00189 82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 161 FLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYW 240
Cdd:MTH00189 162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241
|
250
....*....|....*....
gi 288903170 241 HFVDVVWIFLFISIYWWGY 259
Cdd:MTH00189 242 HFVDVVWLFLYVSIYWWGS 260
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
1-255 |
3.70e-140 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 393.78 E-value: 3.70e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 1 MTKHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLG 80
Cdd:MTH00155 1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 81 MILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNA 160
Cdd:MTH00155 81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 161 FLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYW 240
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240
|
250
....*....|....*
gi 288903170 241 HFVDVVWIFLFISIY 255
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.98e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 376.98 E-value: 1.98e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00118 6 HPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLA 163
Cdd:MTH00118 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 164 TICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFV 243
Cdd:MTH00118 166 TILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 288903170 244 DVVWIFLFISIYWWG 258
Cdd:MTH00118 246 DVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
1-259 |
4.43e-133 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 376.15 E-value: 4.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 1 MTKHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLG 80
Cdd:MTH00141 1 MTRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 81 MILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNA 160
Cdd:MTH00141 81 FILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 161 FLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYW 240
Cdd:MTH00141 161 LGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYW 240
|
250
....*....|....*....
gi 288903170 241 HFVDVVWIFLFISIYWWGY 259
Cdd:MTH00141 241 HFVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
3-258 |
1.87e-123 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 351.72 E-value: 1.87e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 3 KHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMI 82
Cdd:MTH00039 4 QHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 83 LFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFL 162
Cdd:MTH00039 84 LFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 163 ATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHF 242
Cdd:MTH00039 164 LTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHF 243
|
250
....*....|....*.
gi 288903170 243 VDVVWIFLFISIYWWG 258
Cdd:MTH00039 244 VDVVWLFLYVCIYWWG 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
16-257 |
1.64e-120 |
|
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: 343.73 E-value: 1.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 16 LTGSIGAFCFTAGMAAYFNKYDQ-YLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMILFILSEVFFFLA 94
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMHGYGGpLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 95 FFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLATICLGVYFTLL 174
Cdd:cd01665 81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 175 QGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFVDVVWIFLFISI 254
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240
|
...
gi 288903170 255 YWW 257
Cdd:cd01665 241 YWW 243
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
1-258 |
2.64e-120 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 343.69 E-value: 2.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 1 MTKHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLG 80
Cdd:MTH00219 4 FQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 81 MILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNA 160
Cdd:MTH00219 84 MILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 161 FLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYW 240
Cdd:MTH00219 164 LLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYW 243
|
250
....*....|....*...
gi 288903170 241 HFVDVVWIFLFISIYWWG 258
Cdd:MTH00219 244 HFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
5.10e-120 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 342.90 E-value: 5.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00130 6 HAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLA 163
Cdd:MTH00130 86 FITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 164 TICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFV 243
Cdd:MTH00130 166 TILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 288903170 244 DVVWIFLFISIYWWG 258
Cdd:MTH00130 246 DVVWLFLYISIYWWG 260
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
4-259 |
1.26e-117 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 337.08 E-value: 1.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKY--DQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGM 81
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYsgNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 82 ILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAF 161
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 162 LATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWH 241
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*...
gi 288903170 242 FVDVVWIFLFISIYWWGY 259
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
4-258 |
1.43e-116 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 334.39 E-value: 1.43e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00099 6 HAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLA 163
Cdd:MTH00099 86 FIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 164 TICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFV 243
Cdd:MTH00099 166 TILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 288903170 244 DVVWIFLFISIYWWG 258
Cdd:MTH00099 246 DVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.77e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 334.02 E-value: 1.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00075 6 HAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLA 163
Cdd:MTH00075 86 FITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 164 TICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFV 243
Cdd:MTH00075 166 TIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFV 245
|
250
....*....|....*
gi 288903170 244 DVVWIFLFISIYWWG 258
Cdd:MTH00075 246 DVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
4-258 |
9.67e-113 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 324.78 E-value: 9.67e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00024 6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLA 163
Cdd:MTH00024 86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 164 TICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFV 243
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245
|
250
....*....|....*
gi 288903170 244 DVVWIFLFISIYWWG 258
Cdd:MTH00024 246 DVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
1-258 |
1.01e-110 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 319.47 E-value: 1.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 1 MTKHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLG 80
Cdd:MTH00009 1 MIRQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 81 MILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNA 160
Cdd:MTH00009 81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 161 FLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYW 240
Cdd:MTH00009 161 LILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYW 240
|
250
....*....|....*...
gi 288903170 241 HFVDVVWIFLFISIYWWG 258
Cdd:MTH00009 241 HFVDVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
2.48e-109 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 315.96 E-value: 2.48e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00052 7 HPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLA 163
Cdd:MTH00052 87 FIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 164 TICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFV 243
Cdd:MTH00052 167 TVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFV 246
|
250
....*....|....*
gi 288903170 244 DVVWIFLFISIYWWG 258
Cdd:MTH00052 247 DVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
4-258 |
1.57e-98 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 290.04 E-value: 1.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAG----------- 152
Cdd:MTH00028 86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTgnpaslekgtq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 153 -------------------------YWTDTCNAFLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVI 207
Cdd:MTH00028 166 giegpnpsngappdpqkgptfllsdFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 288903170 208 IGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFVDVVWIFLFISIYWWG 258
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
3-258 |
6.93e-86 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 256.51 E-value: 6.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 3 KHPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYD--QYLMYLGFFLILLTMVQWWRDVTREATFQGKHTAKVESGMRLG 80
Cdd:PLN02194 6 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 81 MILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYWTDTCNA 160
Cdd:PLN02194 86 SILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 161 FLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYW 240
Cdd:PLN02194 166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245
|
250
....*....|....*...
gi 288903170 241 HFVDVVWIFLFISIYWWG 258
Cdd:PLN02194 246 HFVDVVWLFLFVSIYWWG 263
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
4-259 |
1.20e-70 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 217.52 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 4 HPFHIVDASPWPLTGSIGAFCFTAGMAAYFNKYDQYLMYLGFFLILLTMVQWWRDVTREAtFQGKHTAKVESGMRLGMIL 83
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 84 FILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQGINPFSVPLLNTVVLLSSGVTITWAHHCILAGYwTDTCNAFLA 163
Cdd:MTH00083 82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 164 TICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFV 243
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240
|
250
....*....|....*.
gi 288903170 244 DVVWIFLFISIYWWGY 259
Cdd:MTH00083 241 DVVWLFLFVFVYWWSY 256
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
69-257 |
4.46e-67 |
|
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: 205.90 E-value: 4.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 69 HTAKVESGMRLGMILFILSEVFFFLAFFWAYFHSALSPSIEIGAvwtpvgiqGINPFSVPLLNTVVLLSSGVTITWAHHC 148
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 149 ILAGYWTDTC--NAFLATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFS 226
Cdd:cd00386 73 LAARRGNRKKarLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 288903170 227 KKHHFGFEASAWYWHFVDVVWIFLFISIYWW 257
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
69-257 |
2.24e-50 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 163.48 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 69 HTAKVESGMRLGMILFILSEVFFFLAFFWAYFHSALSpsieigAVWTPVGIQGINPfSVPLLNTVVLLSSGVTITWAHHC 148
Cdd:COG1845 8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS------APDWPAGAELLDL-PLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 149 ILAGYWTDTCNAFLATICLGVYFTLLQGFEYKVAS---FTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHF 225
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 288903170 226 SKKHHFGFEASAWYWHFVDVVWIFLFISIYWW 257
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
78-255 |
1.01e-22 |
|
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: 91.53 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 78 RLGMILFILSEVFFFLAFFWAYF-HSALSPSIeigavwTPVGIQGINPFSvPLLNTVVLLSSGVTITWAHHCILAGYWTD 156
Cdd:cd02862 10 KLGMWVFILSELLAFGALFIAYAvYRALYPEL------FAAGSAHLDLLL-GALNTLVLLTSSFTVALAVRAARAGRRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 157 TCNAFLATICLGVYFTLLQGFEYK---VASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGF 233
Cdd:cd02862 83 ARRWLAAAVLLGLVFLVIKYFEYAhkiAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGV 162
|
170 180
....*....|....*....|..
gi 288903170 234 EASAWYWHFVDVVWIFLFISIY 255
Cdd:cd02862 163 EAAALYWHMVDLVWIVLFPLLY 184
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
75-257 |
1.16e-19 |
|
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: 83.57 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 75 SGMRLGMILFILSEVFFFLAFFWAYFHSALSpsieiGAVWTPVGIQGINpfsVPLLNTVVLLSSGVTITWAHHCILAGYW 154
Cdd:cd02865 7 SPGWWGLWVFMAVEGTLFALLISAYFMRMTS-----GDWQPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 155 TDTCNAFLATICLGVYFTLLQGFEYKVASF---TIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHF 231
Cdd:cd02865 79 VLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRL 158
|
170 180
....*....|....*....|....*.
gi 288903170 232 GFEASAWYWHFVDVVWIFLFISIYWW 257
Cdd:cd02865 159 PVELCALYWHFLLLVWLVLLALLYGT 184
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
69-257 |
2.29e-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: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 69 HTAKVESGMRLGMILFILSEVFFFLAFFWAYFHSALSPSIEIGAVWTPVGIQgINPFSVPL----LNTVVLLSSGVTITW 144
Cdd:cd02864 1 REPFKVSWGKAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALR-IGHFNIPLvliaIMTFILITSSGTMAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 145 AHHCILAGYWTDTCNAFLATICLGVYFTLLQGFEY---------KVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISV 215
Cdd:cd02864 80 AVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvRPWGNPWGAAQFGASFFMITGFHGTHVTIGVIYLII 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 288903170 216 MYYRHIYFHFSKKHHFG-FEASAWYWHFVDVVWIFLFISIYWW 257
Cdd:cd02864 160 IARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
83-255 |
3.61e-13 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 66.48 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 83 LFILSEVFFFLAFFWAYFHSALSPSIEIGAvwtpvgiqginPFSVPLLNTVVLLSSGVTITWAHHCILagywTDTCNAFL 162
Cdd:MTH00049 59 LFILSEVIIFGSLLVCCLWFDDWSYISLSS-----------SLEIPFVGCFLLLGSSITVTAYHHLLG----WKYCDLFL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 163 -ATICLGVYFTLLQGFEYKVASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMyyrhIYFHFSKKHHFGFEASAWYWH 241
Cdd:MTH00049 124 yLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTL----LLVGSSSFGVYRSTVLTWYWH 199
|
170
....*....|....
gi 288903170 242 FVDVVWIFLFISIY 255
Cdd:MTH00049 200 FVDYIWLLVYLIVY 213
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
69-255 |
7.83e-13 |
|
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: 64.95 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 69 HTAKVESGMRLGMILFILSEVFFFLAFFWAYFhsALSPSIEIGAvwtpvgiQGINPFSVPL--LNTVVLLSSGVTITWAH 146
Cdd:cd02863 1 HHTNTGSKKILGFWIYLMSDCILFATLFATYA--VLSGNTAGGP-------PGHELFELPLvfIETFLLLLSSFTCGLAM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 147 HCILAGYWTDTCNAFLATICLGVYFTLLQGFEYK---VASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYF 223
Cdd:cd02863 72 IAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHhliAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKR 151
|
170 180 190
....*....|....*....|....*....|..
gi 288903170 224 HFSKKHHFGFEASAWYWHFVDVVWIFLFISIY 255
Cdd:cd02863 152 GLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
79-258 |
5.83e-06 |
|
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: 45.71 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 79 LGMILFILSEVFFFLAFFWAYFhsALSPSieigavwTPVGIQGINPFSVP--LLNTVVLLSSGVTITWAHHCILAGYWTD 156
Cdd:TIGR02842 3 FGFWLYLMSDCILFATLFATYA--VLSNN-------TAGGPSGKEIFDLPfvLVETFLLLLSSITFGFAMLAMNKKNKKM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 157 TCNAFLATICLGVYFTLLQGFEYK---VASFTIADSVYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGF 233
Cdd:TIGR02842 74 VILWLAITFLLGLGFIGMEIYEFYhliAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRL 153
|
170 180
....*....|....*....|....*
gi 288903170 234 EASAWYWHFVDVVWIFLFISIYWWG 258
Cdd:TIGR02842 154 ACLSLFWHFLDIVWICVFTFVYLLG 178
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
129-258 |
1.01e-05 |
|
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: 44.85 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 129 LLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLATICLGVYFTLLQGFE---YKVASFTIADSVYGSCFYLATGFHGFH 205
Cdd:TIGR02897 56 LIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCH 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 288903170 206 VIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFVDVVWIFLFISIYWWG 258
Cdd:TIGR02897 136 VTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
115-258 |
1.64e-03 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 38.61 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288903170 115 TPVGIQGINPFSVP--LLNTVVLLSSGVTITWAHHCILAGYWTDTCNAFLATICLGVYFTLLQGFEYK---VASFTIADS 189
Cdd:PRK10663 54 TAGGPTGKDIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHhliVEGMGPDRS 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288903170 190 VYGSCFYLATGFHGFHVIIGTTFISVMYYRHIYFHFSKKHHFGFEASAWYWHFVDVVWIFLFISIYWWG 258
Cdd:PRK10663 134 GFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
|
|
| |
