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Conserved domains on  [gi|1366020089|ref|XP_024162480|]
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LOW QUALITY PROTEIN: cytochrome c oxidase subunit 3 [Rosa chinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like super family cl00211
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 182-444 7.38e-164

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.


The actual alignment was detected with superfamily member PLN02194:

Pssm-ID: 444752  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
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
 
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
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
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
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
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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