|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
182-444 |
7.38e-164 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 461.83 E-value: 7.38e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 182 DQQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGL 261
Cdd:PLN02194 3 ESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 262 RYGFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRA 341
Cdd:PLN02194 83 RYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 342 VYALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 421
Cdd:PLN02194 163 VYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 242
|
250 260
....*....|....*....|...
gi 1366020089 422 WYWHFVDVVRLFPFVSIYWWGGI 444
Cdd:PLN02194 243 WYWHFVDVVWLFLFVSIYWWGGI 265
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
198-441 |
2.99e-133 |
|
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: 383.40 E-value: 2.99e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 198 ISGSLGALATTVGGVMYMHpFQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRYGFIPFIVSEVMFLF 277
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMH-GYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 278 AFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYALVATVSLALVFTG 357
Cdd:cd01665 80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 358 FQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVRLFPFVS 437
Cdd:cd01665 160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239
|
....
gi 1366020089 438 IYWW 441
Cdd:cd01665 240 VYWW 243
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
186-442 |
3.15e-126 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 365.97 E-value: 3.15e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 186 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRYGF 265
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 266 IPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYAL 345
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 346 VATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 425
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 1366020089 426 FVDVVRLFPFVSIYWWG 442
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
250-441 |
1.17e-51 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 172.34 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 250 EGHHTKAVQLGLRYGFIPFIVSEVMFLFAFFrasshSSLAPTVEIGGIWPPkGIGVLDPReIPFLNTPILLSSGAAVTWA 329
Cdd:COG1845 5 EAPHAPERRSPGKLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDLP-LPLINTLLLLLSSFTVALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 330 HHAILAGKEKRAVYALVATVSLALVFTGFQGMEYYQ---APFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYL 406
Cdd:COG1845 78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1366020089 407 GHLTKEHHVGFEAAAWYWHFVDVVRLFPFVSIYWW 441
Cdd:COG1845 158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| YMF19 |
pfam02326 |
Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant ... |
2-82 |
3.03e-24 |
|
Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant and algae mitochondrial F-ATPases (EC:3.6.1.34).
Pssm-ID: 396760 Cd Length: 84 Bit Score: 95.93 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 2 PQLDKFTYFTQFFWSCLFLFTFYIPICNdgDGFLGISRILKLRNRLVSQRG----NNTRSNDPNSLEEILRKG-FSTGVS 76
Cdd:pfam02326 1 PQLDKFTYFTQFFWLCLFFFTFYIFLLN--FILPKISRILKLRKKLLSSLIssklGKEQSLLGVSKDSLLANSsLSTSNS 78
|
....*.
gi 1366020089 77 YMYSSL 82
Cdd:pfam02326 79 YLYSSL 84
|
|
| YMF19_C |
pfam06449 |
ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the ... |
93-143 |
1.11e-17 |
|
ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the F0 complex of mitochondrial F-ATPases from plants. This family is found in conjunction with pfam02326.
Pssm-ID: 368914 Cd Length: 51 Bit Score: 76.65 E-value: 1.11e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1366020089 93 DLLGKGRKITLISCFGEISGSRGMERNIFDLISKSSYSTSSNPGWVIACRN 143
Cdd:pfam06449 1 DLFGKRRIITFIECFGEISGSRGMERNIFYLISKSSYNTSSNPGWGITCRN 51
|
|
| ATP8 |
MTH00169 |
ATP synthase F0 subunit 8; Provisional |
1-72 |
1.69e-04 |
|
ATP synthase F0 subunit 8; Provisional
Pssm-ID: 214446 Cd Length: 67 Bit Score: 39.57 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1366020089 1 MPQLDKFTYFTQFFWSCLFLFTFYipicndgdgFLGISRILKlrnRLVSQRGNNTRSNDPNSLE------EILRKGFS 72
Cdd:MTH00169 1 MPQLDSVTYLTQYIWTLIILFFLF---------SLLVNYILP---KIQQQLVIRTKGVNSVEGKkerpkiEIFKKLFD 66
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
182-444 |
7.38e-164 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 461.83 E-value: 7.38e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 182 DQQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGL 261
Cdd:PLN02194 3 ESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 262 RYGFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRA 341
Cdd:PLN02194 83 RYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 342 VYALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 421
Cdd:PLN02194 163 VYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 242
|
250 260
....*....|....*....|...
gi 1366020089 422 WYWHFVDVVRLFPFVSIYWWGGI 444
Cdd:PLN02194 243 WYWHFVDVVWLFLFVSIYWWGGI 265
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
184-442 |
1.96e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 397.40 E-value: 1.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 184 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRY 263
Cdd:MTH00118 4 QAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFH--YNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 264 GFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVY 343
Cdd:MTH00118 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 344 ALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:MTH00118 162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 1366020089 424 WHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00118 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
184-442 |
6.13e-138 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 395.88 E-value: 6.13e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 184 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRY 263
Cdd:MTH00189 3 QAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFH--YNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 264 GFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVY 343
Cdd:MTH00189 81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 344 ALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:MTH00189 161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240
|
250
....*....|....*....
gi 1366020089 424 WHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00189 241 WHFVDVVWLFLYVSIYWWG 259
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
198-441 |
2.99e-133 |
|
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: 383.40 E-value: 2.99e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 198 ISGSLGALATTVGGVMYMHpFQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRYGFIPFIVSEVMFLF 277
Cdd:cd01665 1 ILGSFGLLLLALGLVLWMH-GYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 278 AFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYALVATVSLALVFTG 357
Cdd:cd01665 80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 358 FQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVRLFPFVS 437
Cdd:cd01665 160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239
|
....
gi 1366020089 438 IYWW 441
Cdd:cd01665 240 VYWW 243
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
186-439 |
5.85e-130 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 375.29 E-value: 5.85e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 186 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRYGF 265
Cdd:MTH00155 4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFH--QFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 266 IPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYAL 345
Cdd:MTH00155 82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 346 VATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 425
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241
|
250
....*....|....
gi 1366020089 426 FVDVVRLFPFVSIY 439
Cdd:MTH00155 242 FVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
183-442 |
4.50e-128 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 371.05 E-value: 4.50e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 183 QQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLR 262
Cdd:MTH00052 4 QYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQ--SWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 263 YGFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAV 342
Cdd:MTH00052 82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 343 YALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAW 422
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241
|
250 260
....*....|....*....|
gi 1366020089 423 YWHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWG 261
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
184-443 |
1.30e-127 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 369.60 E-value: 1.30e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 184 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRY 263
Cdd:MTH00141 2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFH--GGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 264 GFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVY 343
Cdd:MTH00141 80 GFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 344 ALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:MTH00141 160 GLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWY 239
|
250 260
....*....|....*....|
gi 1366020089 424 WHFVDVVRLFPFVSIYWWGG 443
Cdd:MTH00141 240 WHFVDVVWLFLYLSIYWWGS 259
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
186-442 |
3.15e-126 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 365.97 E-value: 3.15e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 186 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRYGF 265
Cdd:pfam00510 1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 266 IPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYAL 345
Cdd:pfam00510 81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 346 VATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 425
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240
|
250
....*....|....*..
gi 1366020089 426 FVDVVRLFPFVSIYWWG 442
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
181-442 |
1.40e-125 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 364.46 E-value: 1.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 181 RDQQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLG 260
Cdd:MTH00024 1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFH--YGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 261 LRYGFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKR 340
Cdd:MTH00024 79 LKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 341 AVYALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAA 420
Cdd:MTH00024 159 AILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAA 238
|
250 260
....*....|....*....|..
gi 1366020089 421 AWYWHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00024 239 SWYWHFVDVVWLFLYLCIYWWG 260
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
184-442 |
7.75e-125 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 362.54 E-value: 7.75e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 184 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpFQGgATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRY 263
Cdd:MTH00130 4 QAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFH-FHS-TTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 264 GFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVY 343
Cdd:MTH00130 82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 344 ALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:MTH00130 162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241
|
250
....*....|....*....
gi 1366020089 424 WHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00130 242 WHFVDVVWLFLYISIYWWG 260
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
184-442 |
6.64e-123 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 357.88 E-value: 6.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 184 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRY 263
Cdd:MTH00099 4 QTHAYHMVNPSPWPLTGALSALLMTSGLIMWFH--FNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 264 GFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVY 343
Cdd:MTH00099 82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 344 ALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:MTH00099 162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241
|
250
....*....|....*....
gi 1366020089 424 WHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00099 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
184-442 |
7.91e-121 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 352.51 E-value: 7.91e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 184 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRY 263
Cdd:MTH00075 4 QAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFH--FGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 264 GFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVY 343
Cdd:MTH00075 82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 344 ALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:MTH00075 162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241
|
250
....*....|....*....
gi 1366020089 424 WHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00075 242 WHFVDVVWLFLYVSIYWWG 260
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
183-443 |
2.19e-119 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 348.64 E-value: 2.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 183 QQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFqgGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLR 262
Cdd:MTH00039 2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGD--SILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 263 YGFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAV 342
Cdd:MTH00039 80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 343 YALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAW 422
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239
|
250 260
....*....|....*....|.
gi 1366020089 423 YWHFVDVVRLFPFVSIYWWGG 443
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWGS 260
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
184-442 |
1.01e-116 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 342.15 E-value: 1.01e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 184 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRY 263
Cdd:MTH00219 5 QTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYN--LDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 264 GFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVY 343
Cdd:MTH00219 83 GMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 344 ALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:MTH00219 163 GLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWY 242
|
250
....*....|....*....
gi 1366020089 424 WHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00219 243 WHFVDVVWLFLYVSIYWWG 261
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
185-442 |
2.79e-103 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 307.92 E-value: 2.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 185 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFqgGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRYG 264
Cdd:MTH00009 3 RQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGY--GTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 265 FIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYA 344
Cdd:MTH00009 81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 345 LVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 424
Cdd:MTH00009 161 LILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYW 240
|
250
....*....|....*...
gi 1366020089 425 HFVDVVRLFPFVSIYWWG 442
Cdd:MTH00009 241 HFVDVVWIFLYLCIYWWG 258
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
186-442 |
4.71e-97 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 293.13 E-value: 4.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 186 HSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGATLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKAVQLGLRYGF 265
Cdd:MTH00028 6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFH--YSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 266 IPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEK------ 339
Cdd:MTH00028 84 LLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPaslekg 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 340 ------------------------------RAVYALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFH 389
Cdd:MTH00028 164 tqgiegpnpsngappdpqkgptfllsdfrtNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1366020089 390 VIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVRLFPFVSIYWWG 442
Cdd:MTH00028 244 VLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
186-442 |
2.45e-71 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 225.61 E-value: 2.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 186 HSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGATLLSLglIFILYTMFVWWRDVLREStLEGHHTKAVQLGLRYGF 265
Cdd:MTH00083 3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSL--LYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 266 IPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIWPPKGIGVLDPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYaL 345
Cdd:MTH00083 80 ILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTNS-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 346 VATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 425
Cdd:MTH00083 159 LLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWH 238
|
250
....*....|....*..
gi 1366020089 426 FVDVVRLFPFVSIYWWG 442
Cdd:MTH00083 239 FVDVVWLFLFVFVYWWS 255
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
253-441 |
2.12e-70 |
|
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: 220.54 E-value: 2.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 253 HTKAVQLGLRYGFIPFIVSEVMFLFAFFRASSHSSLAPTVEIGGIwppkgigvLDPREIPFLNTPILLSSGAAVTWAHHA 332
Cdd:cd00386 1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAG--------LDPLDLPLLNTNTLLLSGSSVTWAHAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 333 ILAGKEKR--AVYALVATVSLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLT 410
Cdd:cd00386 73 LAARRGNRkkARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152
|
170 180 190
....*....|....*....|....*....|.
gi 1366020089 411 KEHHVGFEAAAWYWHFVDVVRLFPFVSIYWW 441
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
250-441 |
1.17e-51 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 172.34 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 250 EGHHTKAVQLGLRYGFIPFIVSEVMFLFAFFrasshSSLAPTVEIGGIWPPkGIGVLDPReIPFLNTPILLSSGAAVTWA 329
Cdd:COG1845 5 EAPHAPERRSPGKLGMWLFLASEVMLFAALF-----AAYFVLRASAPDWPA-GAELLDLP-LPLINTLLLLLSSFTVALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 330 HHAILAGKEKRAVYALVATVSLALVFTGFQGMEYYQ---APFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYL 406
Cdd:COG1845 78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1366020089 407 GHLTKEHHVGFEAAAWYWHFVDVVRLFPFVSIYWW 441
Cdd:COG1845 158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
268-439 |
7.97e-25 |
|
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: 100.77 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 268 FIVSEVMFLFAFFRA-SSHSSLAPTVEiggiwpPKGIGVLDPReIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYALV 346
Cdd:cd02862 16 FILSELLAFGALFIAyAVYRALYPELF------AAGSAHLDLL-LGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 347 ATVSLALVFTGFQGMEYY---QAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 423
Cdd:cd02862 89 AAVLLGLVFLVIKYFEYAhkiAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALY 168
|
170
....*....|....*.
gi 1366020089 424 WHFVDVVRLFPFVSIY 439
Cdd:cd02862 169 WHMVDLVWIVLFPLLY 184
|
|
| YMF19 |
pfam02326 |
Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant ... |
2-82 |
3.03e-24 |
|
Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant and algae mitochondrial F-ATPases (EC:3.6.1.34).
Pssm-ID: 396760 Cd Length: 84 Bit Score: 95.93 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 2 PQLDKFTYFTQFFWSCLFLFTFYIPICNdgDGFLGISRILKLRNRLVSQRG----NNTRSNDPNSLEEILRKG-FSTGVS 76
Cdd:pfam02326 1 PQLDKFTYFTQFFWLCLFFFTFYIFLLN--FILPKISRILKLRKKLLSSLIssklGKEQSLLGVSKDSLLANSsLSTSNS 78
|
....*.
gi 1366020089 77 YMYSSL 82
Cdd:pfam02326 79 YLYSSL 84
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
268-441 |
1.75e-18 |
|
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: 82.80 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 268 FIVSEVMFLFAFFRASSHSSLAPTVeiggiWPPKGIGVLDpreIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYALVA 347
Cdd:cd02865 16 FMAVEGTLFALLISAYFMRMTSGDW-----QPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 348 TVSLALVFTGFQGMEYYQAPF---TISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 424
Cdd:cd02865 88 AGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYW 167
|
170
....*....|....*..
gi 1366020089 425 HFVDVVRLFPFVSIYWW 441
Cdd:cd02865 168 HFLLLVWLVLLALLYGT 184
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|
| YMF19_C |
pfam06449 |
ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the ... |
93-143 |
1.11e-17 |
|
ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the F0 complex of mitochondrial F-ATPases from plants. This family is found in conjunction with pfam02326.
Pssm-ID: 368914 Cd Length: 51 Bit Score: 76.65 E-value: 1.11e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1366020089 93 DLLGKGRKITLISCFGEISGSRGMERNIFDLISKSSYSTSSNPGWVIACRN 143
Cdd:pfam06449 1 DLFGKRRIITFIECFGEISGSRGMERNIFYLISKSSYNTSSNPGWGITCRN 51
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|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
313-439 |
2.23e-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: 68.42 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 313 FLNTPILLSSGAAVTWAHHAILAGKEKRAVYALVATVSLALVFTGFQGME---YYQAPFTISDSIYGSTFFLATGFHGFH 389
Cdd:cd02863 54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1366020089 390 VIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVRLFPFVSIY 439
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
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|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
268-441 |
1.34e-12 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 66.37 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 268 FIVSEVMFLFAFFRASSHSSLAPTVEIGGIwPPKGIGVldPREIPFLNTPILLSSGAAVTWAHHAILAGKEKRAVYALVA 347
Cdd:cd02864 22 FIFSSFLIAYMTARISTTEPWPLPSDVFAL-RIGHFNI--PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 348 TVSLALVFTGFQGMEY-----------YQAPFTISdsIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKE-HHV 415
Cdd:cd02864 99 TALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIgRYE 176
|
170 180
....*....|....*....|....*.
gi 1366020089 416 GFEAAAWYWHFVDVVRLFPFVSIYWW 441
Cdd:cd02864 177 IVEIAGLYWHFVDLVWVFIFAFFYLW 202
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|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
224-439 |
3.40e-12 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 65.32 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 224 LLSLGLIFILYTMFVWWRDVLREstlegHHTKAvqlglryGFIPFIVSEVM----FLFA--FFRASSHSSLAptveiggi 297
Cdd:MTH00049 28 LVFLILWVLLIVIFVSDGLVQVK-----HHYES-------AFWLFILSEVIifgsLLVCclWFDDWSYISLS-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 298 wppkgigvlDPREIPFLNTPILLSSGAAVTWAHHAIlagKEKRAVYALVATVSLALVFTGFQGMEYYQAPFTISDSIYGS 377
Cdd:MTH00049 88 ---------SSLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1366020089 378 TFFLATGFHGFHVIIGTLFLIIcgirqyLGHLTKEHHVGF--EAAAWYWHFVDVVRLFPFVSIY 439
Cdd:MTH00049 156 SCFCTVGLHFSHVVLGVVGLST------LLLVGSSSFGVYrsTVLTWYWHFVDYIWLLVYLIVY 213
|
|
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
310-444 |
6.72e-06 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 46.70 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366020089 310 EIPFL--NTPILLSSGAAVTWAHHAILAGKEKRAVYALVATVSLALvftGFQGMEYYQAPFTISD------SIYGSTFFL 381
Cdd:PRK10663 65 ELPFVlvETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGA---GFIGMEIYEFHHLIVEgmgpdrSGFLSAFFA 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1366020089 382 ATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVRLFPFVSIYWWGGI 444
Cdd:PRK10663 142 LVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
|
|
| ATP8 |
MTH00169 |
ATP synthase F0 subunit 8; Provisional |
1-72 |
1.69e-04 |
|
ATP synthase F0 subunit 8; Provisional
Pssm-ID: 214446 Cd Length: 67 Bit Score: 39.57 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1366020089 1 MPQLDKFTYFTQFFWSCLFLFTFYipicndgdgFLGISRILKlrnRLVSQRGNNTRSNDPNSLE------EILRKGFS 72
Cdd:MTH00169 1 MPQLDSVTYLTQYIWTLIILFFLF---------SLLVNYILP---KIQQQLVIRTKGVNSVEGKkerpkiEIFKKLFD 66
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