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Conserved domains on  [gi|1488175478|ref|YP_009472127|]
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cytochrome c oxidase subunit 3 (mitochondrion) [Arabidopsis thaliana]

Protein Classification

cytochrome c oxidase subunit 3 family protein( domain architecture ID 201)

cytochrome c oxidase (CcO) subunit 3 family protein is not required for catalytic activity but may play a role in the assembly of the heme-copper oxidase (such as CcO and cytochrome bo(3) ubiquinol oxidase) multimer complex

CATH:  1.20.120.80
Gene Ontology:  GO:0070069|GO:0009055
PubMed:  8083153|12907296
SCOP:  3000671

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 ...
 1-265 4.60e-158

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: 439.87  E-value: 4.60e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  81 GLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEK 160
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|....*
gi 1488175478 241 AAWYWHFVDVVWLFLFVSIYWWGGI 265
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWGGI 265
 
Name Accession Description Interval E-value
PLN02194 PLN02194
cytochrome-c oxidase
 1-265 4.60e-158

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 439.87  E-value: 4.60e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  81 GLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEK 160
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|....*
gi 1488175478 241 AAWYWHFVDVVWLFLFVSIYWWGGI 265
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWGGI 265
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-262 1.29e-126

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: 359.14  E-value: 1.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  19 ISGSLGALATTVGGVMYMHSFqGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYGFILFIVSEVMFFF 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGY-GGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  99 AFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTG 178
Cdd:cd01665    80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 179 FQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVS 258
Cdd:cd01665   160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239


                  ....
gi 1488175478 259 IYWW 262
Cdd:cd01665   240 VYWW 243
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-263 9.02e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 340.16  E-value: 9.02e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYGF 86
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  87 ILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYAL 166
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 1488175478 247 FVDVVWLFLFVSIYWWG 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-262 3.34e-52

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 168.49  E-value: 3.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  71 EGHHTKVVQLGLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAveiggiWPPKGIEVLDPWeIPFLNTLILLSSGAAVTWA 150
Cdd:COG1845     5 EAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDLP-LPLINTLLLLLSSFTVALA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 151 HHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQ---APFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYL 227
Cdd:COG1845    78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1488175478 228 GHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWW 262
Cdd:COG1845   158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 137-263 8.46e-11

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 59.48  E-value: 8.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 137 TLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGME---YYQAPFTISDSIYGSTFFLATGFHGFHVII 213
Cdd:TIGR02897  59 TFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTL 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1488175478 214 GtLFLIICGIRQYLGH-LTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWG 263
Cdd:TIGR02897 139 G-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
PLN02194 PLN02194
cytochrome-c oxidase
 1-265 4.60e-158

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 439.87  E-value: 4.60e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
Cdd:PLN02194    1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  81 GLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEK 160
Cdd:PLN02194   81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
Cdd:PLN02194  161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240

                         250       260
                  ....*....|....*....|....*
gi 1488175478 241 AAWYWHFVDVVWLFLFVSIYWWGGI 265
Cdd:PLN02194  241 AAWYWHFVDVVWLFLFVSIYWWGGI 265
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 5-263 9.48e-131

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 370.44  E-value: 9.48e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSfqGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRY 84
Cdd:MTH00118    4 QAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHY--NSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  85 GFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVY 164
Cdd:MTH00118   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 1488175478 245 WHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00118  242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 5-263 5.41e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 365.84  E-value: 5.41e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHsfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRY 84
Cdd:MTH00189    3 QAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFH--YNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  85 GFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVY 164
Cdd:MTH00189   81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
Cdd:MTH00189  161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                         250
                  ....*....|....*....
gi 1488175478 245 WHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00189  241 WHFVDVVWLFLYVSIYWWG 259
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 7-260 7.62e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 365.27  E-value: 7.62e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGarLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYGF 86
Cdd:MTH00155    4 HPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMN--LLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  87 ILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYAL 166
Cdd:MTH00155   82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
Cdd:MTH00155  162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWH 241

                         250
                  ....*....|....
gi 1488175478 247 FVDVVWLFLFVSIY 260
Cdd:MTH00155  242 FVDVVWLFLYISIY 255
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-262 1.29e-126

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: 359.14  E-value: 1.29e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  19 ISGSLGALATTVGGVMYMHSFqGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYGFILFIVSEVMFFF 98
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGY-GGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  99 AFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTG 178
Cdd:cd01665    80 SFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 179 FQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVS 258
Cdd:cd01665   160 LQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVF 239


                  ....
gi 1488175478 259 IYWW 262
Cdd:cd01665   240 VYWW 243
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-263 1.30e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 349.86  E-value: 1.30e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
Cdd:MTH00052    1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQ--SWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  81 GLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEK 160
Cdd:MTH00052   79 GLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
Cdd:MTH00052  159 EAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEA 238

                         250       260
                  ....*....|....*....|...
gi 1488175478 241 AAWYWHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00052  239 AAWYWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 5-264 1.79e-120

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 344.18  E-value: 1.79e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHsfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRY 84
Cdd:MTH00141    2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFH--GGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  85 GFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVY 164
Cdd:MTH00141   80 GFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
Cdd:MTH00141  160 GLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWY 239

                         250       260
                  ....*....|....*....|
gi 1488175478 245 WHFVDVVWLFLFVSIYWWGG 264
Cdd:MTH00141  240 WHFVDVVWLFLYLSIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 3-263 1.55e-119

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 342.12  E-value: 1.55e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   3 ESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHsfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGL 82
Cdd:MTH00024    2 SKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFH--YGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  83 RYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRA 162
Cdd:MTH00024   80 KYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 163 VYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 242
Cdd:MTH00024  160 ILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAAS 239

                         250       260
                  ....*....|....*....|.
gi 1488175478 243 WYWHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00024  240 WYWHFVDVVWLFLYLCIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-263 9.02e-119

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 340.16  E-value: 9.02e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYGF 86
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  87 ILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYAL 166
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*..
gi 1488175478 247 FVDVVWLFLFVSIYWWG 263
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWG 257
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 5-263 4.09e-117

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 335.97  E-value: 4.09e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHsFQGGArLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRY 84
Cdd:MTH00130    4 QAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFH-FHSTT-LMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  85 GFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVY 164
Cdd:MTH00130   82 GMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
Cdd:MTH00130  162 SLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 1488175478 245 WHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00130  242 WHFVDVVWLFLYISIYWWG 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 5-263 1.84e-116

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 334.39  E-value: 1.84e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRY 84
Cdd:MTH00099    4 QTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNS--TTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  85 GFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVY 164
Cdd:MTH00099   82 GMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
Cdd:MTH00099  162 ALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 1488175478 245 WHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00099  242 WHFVDVVWLFLYVSIYWWG 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 4-264 1.23e-113

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 327.07  E-value: 1.23e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   4 SQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFqgGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLR 83
Cdd:MTH00039    2 THQHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGD--SILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  84 YGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAV 163
Cdd:MTH00039   80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 164 YALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAW 243
Cdd:MTH00039  160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239

                         250       260
                  ....*....|....*....|.
gi 1488175478 244 YWHFVDVVWLFLFVSIYWWGG 264
Cdd:MTH00039  240 YWHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 5-263 1.62e-113

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 326.70  E-value: 1.62e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSfqGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRY 84
Cdd:MTH00075    4 QAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHF--GSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  85 GFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVY 164
Cdd:MTH00075   82 GMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244
Cdd:MTH00075  162 SLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWY 241

                         250
                  ....*....|....*....
gi 1488175478 245 WHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00075  242 WHFVDVVWLFLYVSIYWWG 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-263 2.23e-111

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 321.35  E-value: 2.23e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQL 80
Cdd:MTH00219    1 MMFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYN--LDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  81 GLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEK 160
Cdd:MTH00219   79 GLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 161 RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEA 240
Cdd:MTH00219  159 EAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEA 238

                         250       260
                  ....*....|....*....|...
gi 1488175478 241 AAWYWHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00219  239 AAWYWHFVDVVWLFLYVSIYWWG 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-263 6.27e-97

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 284.81  E-value: 6.27e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   6 RHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFqgGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYG 85
Cdd:MTH00009    3 RQPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGY--GTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  86 FILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYA 165
Cdd:MTH00009   81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 166 LVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYW 245
Cdd:MTH00009  161 LILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYW 240

                         250
                  ....*....|....*...
gi 1488175478 246 HFVDVVWLFLFVSIYWWG 263
Cdd:MTH00009  241 HFVDVVWIFLYLCIYWWG 258
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 7-263 4.60e-96

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 283.88  E-value: 4.60e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHsfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGLRYGF 86
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFH--YSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  87 ILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEK------ 160
Cdd:MTH00028   84 LLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNPaslekg 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 161 ------------------------------RAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFH 210
Cdd:MTH00028  164 tqgiegpnpsngappdpqkgptfllsdfrtNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLH 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1488175478 211 VIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWG 263
Cdd:MTH00028  244 VLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 7-263 2.04e-71

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 219.83  E-value: 2.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478   7 HSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGARLLSLglIFILYTMFVWWRDVLREStLEGHHTKVVQLGLRYGF 86
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSL--LYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  87 ILFIVSEVMFFFAFFWAFFHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYaL 166
Cdd:MTH00083   80 ILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTNS-L 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWH 246
Cdd:MTH00083  159 LLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWH 238

                         250
                  ....*....|....*..
gi 1488175478 247 FVDVVWLFLFVSIYWWG 263
Cdd:MTH00083  239 FVDVVWLFLFVFVYWWS 255
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 74-262 7.85e-67

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 205.52  E-value: 7.85e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  74 HTKVVQLGLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAVEIGgiwppkgiEVLDPWEIPFLNTLILLSSGAAVTWAHHA 153
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 154 ILAGKEKR--AVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLT 231
Cdd:cd00386    73 LAARRGNRkkARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1488175478 232 KEHHVGFEAAAWYWHFVDVVWLFLFVSIYWW 262
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-262 3.34e-52

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 168.49  E-value: 3.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  71 EGHHTKVVQLGLRYGFILFIVSEVMFFFAFFWAFFHSSLAPAveiggiWPPKGIEVLDPWeIPFLNTLILLSSGAAVTWA 150
Cdd:COG1845     5 EAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAP------DWPAGAELLDLP-LPLINTLLLLLSSFTVALA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 151 HHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQ---APFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYL 227
Cdd:COG1845    78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALR 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1488175478 228 GHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWW 262
Cdd:COG1845   158 GGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 127-260 1.56e-27

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: 104.62  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 127 LDPWeIPFLNTLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYY---QAPFTISDSIYGSTFFLA 203
Cdd:cd02862    49 LDLL-LGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAhkiAAGIDPDAGLFFTLYFLL 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1488175478 204 TGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIY 260
Cdd:cd02862   128 TGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 133-262 3.07e-19

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 82.42  E-value: 3.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 133 PFLNTLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPF---TISDSIYGSTFFLATGFHGF 209
Cdd:cd02865    52 LSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYLLTGLHGL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1488175478 210 HVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWW 262
Cdd:cd02865   132 HVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 134-260 1.09e-16

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: 75.74  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 134 FLNTLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGME---YYQAPFTISDSIYGSTFFLATGFHGFH 210
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1488175478 211 VIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIY 260
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 137-262 1.50e-14

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: 70.22  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 137 TLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEY-----------YQAPFTISdsIYGSTFFLATG 205
Cdd:cd02864    67 TFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkliveegvrpWGNPWGAA--QFGASFFMITG 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1488175478 206 FHGFHVIIGTLFLIICGIRQYLGHLTKE-HHVGFEAAAWYWHFVDVVWLFLFVSIYWW 262
Cdd:cd02864   145 FHGTHVTIGVIYLIIIARKVWRGKYQRIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 45-260 3.61e-12

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 63.78  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478  45 LLSLGLIFILYTMFVWWrdvlrestleghhtKVVQLGLRY--GFILFIVSEVMFFFaffwaffhsSLAPAVEIGGIWPPK 122
Cdd:MTH00049   28 LVFLILWVLLIVIFVSD--------------GLVQVKHHYesAFWLFILSEVIIFG---------SLLVCCLWFDDWSYI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 123 GIEvlDPWEIPFLNTLILLSSGAAVTWAHHAIlagKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFL 202
Cdd:MTH00049   85 SLS--SSLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 203 ATGFHGFHVIIGTLFLIIcgirqyLGHLTKEHHVGF--EAAAWYWHFVDVVWLFLFVSIY 260
Cdd:MTH00049  160 TVGLHFSHVVLGVVGLST------LLLVGSSSFGVYrsTVLTWYWHFVDYIWLLVYLIVY 213
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 137-263 8.46e-11

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 59.48  E-value: 8.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 137 TLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGME---YYQAPFTISDSIYGSTFFLATGFHGFHVII 213
Cdd:TIGR02897  59 TFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTL 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1488175478 214 GtLFLIICGIRQYLGH-LTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWG 263
Cdd:TIGR02897 139 G-IVWAICLLIQIQRRgLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 128-265 9.92e-09

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 54.02  E-value: 9.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488175478 128 DPWEIPFL--NTLILLSSGAAVTWAHHAILAGKEKRAVYALVATVLLALvftGFQGMEYYQAPFTISD------SIYGST 199
Cdd:PRK10663   62 DIFELPFVlvETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGA---GFIGMEIYEFHHLIVEgmgpdrSGFLSA 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488175478 200 FFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGGI 265
Cdd:PRK10663  139 FFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
 
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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