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Conserved domains on  [gi|1495346005|gb|AYN50470|]
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cytochrome c oxidase subunit III (mitochondrion) [Nestor notabilis]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791089)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 1.17e-179

cytochrome c oxidase subunit III; Provisional


:

Pssm-ID: 177179  Cd Length: 261  Bit Score: 494.08  E-value: 1.17e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00118    1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00118   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00118  161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00118  241 YWHFVDVVWLFLYISIYWWGS 261
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 1.17e-179

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 494.08  E-value: 1.17e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00118    1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00118   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00118  161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00118  241 YWHFVDVVWLFLYISIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 2.91e-138

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 389.08  E-value: 2.91e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   6 HSYHMVDPSPWPLFGAAAALLTTSGLIMWFHH--NSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  84 ILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 164 TMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1495346005 244 FVDVIWLFLYMTIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-259 2.98e-128

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: 363.37  E-value: 2.98e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  18 LFGAAAALLTTSGLIMWFHHNSSQ-LLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYGMILFITSEAFFFLG 96
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  97 FFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQALTMTILLGFYFTAL 176
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 177 QATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFVDVIWLFLYMTI 256
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1495346005 257 YWW 259
Cdd:cd01665   241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 6.84e-49

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.63  E-value: 6.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  70 HHTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLVptpelGGQWPpTGITPLNPLeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 150 SITEGNQNQAIQALTMTILLGFYFTALQATEYYE---APFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFH 226
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1495346005 227 FTPNHHFGFEAAAWYWHFVDVIWLFLYMTIYWW 259
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 1.17e-179

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 494.08  E-value: 1.17e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00118    1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00118   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00118  161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00118  241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-261 6.01e-159

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 441.51  E-value: 6.01e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00130    1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00130   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00130  161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00130  241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-261 2.80e-157

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 437.62  E-value: 2.80e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00099    1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00099   81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00099  161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00099  241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-261 6.93e-155

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 431.48  E-value: 6.93e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00075    1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00075   81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00075  161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00075  241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-261 1.93e-151

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 422.46  E-value: 1.93e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   2 AHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRY 81
Cdd:MTH00189    1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  82 GMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQ 161
Cdd:MTH00189   81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 162 ALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWY 241
Cdd:MTH00189  161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWY 240

                         250       260
                  ....*....|....*....|
gi 1495346005 242 WHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00189  241 WHFVDVVWLFLYVSIYWWGS 260
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 3-257 1.17e-144

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 405.33  E-value: 1.17e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   3 HQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYG 82
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  83 MILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQA 162
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 163 LTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYW 242
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                         250
                  ....*....|....*
gi 1495346005 243 HFVDVIWLFLYMTIY 257
Cdd:MTH00155  241 HFVDVVWLFLYISIY 255
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-261 3.04e-139

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 391.78  E-value: 3.04e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQaHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00039    1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00039   80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00039  160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00039  240 YWHFVDVVWLFLYVCIYWWGS 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 2.91e-138

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 389.08  E-value: 2.91e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   6 HSYHMVDPSPWPLFGAAAALLTTSGLIMWFHH--NSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  84 ILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 164 TMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 1495346005 244 FVDVIWLFLYMTIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-261 5.20e-135

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 381.16  E-value: 5.20e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   6 HSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  86 FITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQALTM 165
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 166 TILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFV 245
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1495346005 246 DVIWLFLYMTIYWWGS 261
Cdd:MTH00141  244 DVVWLFLYLSIYWWGS 259
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-261 6.71e-129

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 365.65  E-value: 6.71e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00219    2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00219   82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00219  162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00219  242 YWHFVDVVWLFLYVSIYWWGS 262
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-259 2.98e-128

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: 363.37  E-value: 2.98e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  18 LFGAAAALLTTSGLIMWFHHNSSQ-LLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYGMILFITSEAFFFLG 96
Cdd:cd01665     1 ILGSFGLLLLALGLVLWMHGYGGPlLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  97 FFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQALTMTILLGFYFTAL 176
Cdd:cd01665    81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 177 QATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFVDVIWLFLYMTI 256
Cdd:cd01665   161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                  ...
gi 1495346005 257 YWW 259
Cdd:cd01665   241 YWW 243
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-261 1.49e-125

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 357.18  E-value: 1.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00052    2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00052   82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00052  162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00052  242 YWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-261 2.22e-123

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 351.75  E-value: 2.22e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   1 MAHQAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLR 80
Cdd:MTH00024    1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  81 YGMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAI 160
Cdd:MTH00024   81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 161 QALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAW 240
Cdd:MTH00024  161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240

                         250       260
                  ....*....|....*....|.
gi 1495346005 241 YWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00024  241 YWHFVDVVWLFLYLCIYWWGS 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-261 1.20e-119

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 342.20  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   6 HSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  86 FITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQALTM 165
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 166 TILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFV 245
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                         250
                  ....*....|....*.
gi 1495346005 246 DVIWLFLYMTIYWWGS 261
Cdd:MTH00009  244 DVVWIFLYLCIYWWGS 259
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 6-261 1.00e-98

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 290.43  E-value: 1.00e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   6 HSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00028    6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  86 FITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGN---------- 155
Cdd:MTH00028   86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtq 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 156 --------------------------QNQAIQALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVI 209
Cdd:MTH00028  166 giegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1495346005 210 IGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFVDVIWLFLYMTIYWWGS 261
Cdd:MTH00028  246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 4-260 3.50e-92

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 272.69  E-value: 3.50e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   4 QAHSYHMVDPSPWPLFGAAAALLTTSGLIMWFH--HNSSQLLTLGLLSIILVMIQWWRDIVREGTFQGHHTPTVQKGLRY 81
Cdd:PLN02194    5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  82 GMILFITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQ 161
Cdd:PLN02194   85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 162 ALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWY 241
Cdd:PLN02194  165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                         250
                  ....*....|....*....
gi 1495346005 242 WHFVDVIWLFLYMTIYWWG 260
Cdd:PLN02194  245 WHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-261 5.25e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 233.69  E-value: 5.25e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005   6 HSYHMVDPSPWPLFGAAAALLTTSGLIMWFHHNSSQLLTLGLLSIILVMIQWWRDIVREGtFQGHHTPTVQKGLRYGMIL 85
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  86 FITSEAFFFLGFFWAFFHSSLVPTPELGGQWPPTGITPLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIqALTM 165
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN-SLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 166 TILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFV 245
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                         250
                  ....*....|....*.
gi 1495346005 246 DVIWLFLYMTIYWWGS 261
Cdd:MTH00083  241 DVVWLFLFVFVYWWSY 256
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 71-259 1.77e-66

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: 204.36  E-value: 1.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  71 HTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLVPTPELGgqwpptgiTPLNPLEVPLLNTAILLASGVTVTWAHHS 150
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 151 IT--EGNQNQAIQALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFHFT 228
Cdd:cd00386    73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1495346005 229 PNHHFGFEAAAWYWHFVDVIWLFLYMTIYWW 259
Cdd:cd00386   153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 6.84e-49

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.63  E-value: 6.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005  70 HHTPTVQKGLRYGMILFITSEAFFFLGFFWAFFHSSLVptpelGGQWPpTGITPLNPLeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845     7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWP-AGAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 150 SITEGNQNQAIQALTMTILLGFYFTALQATEYYE---APFSIADGVYGSTFFVATGFHGLHVIIGSSFLLICLLRLIKFH 226
Cdd:COG1845    80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1495346005 227 FTPNHHFGFEAAAWYWHFVDVIWLFLYMTIYWW 259
Cdd:COG1845   160 FTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 131-257 5.22e-26

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: 100.39  E-value: 5.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 131 LLNTAILLASGVTVTWAHHSITEGNQNQAIQALTMTILLGFYFTALQATEYYE---APFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02862    55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1495346005 208 VIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFVDVIWLFLYMTIY 257
Cdd:cd02862   135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 123-259 5.04e-20

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: 84.73  E-value: 5.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 123 PLNPLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQALTMTILLGFYFTALQATEYYEAPFSI---ADGVYGSTFFV 199
Cdd:cd02865    45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpTSNPAGSFFYL 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 200 ATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFVDVIWLFLYMTIYWW 259
Cdd:cd02865   125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 131-257 2.09e-19

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: 83.06  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 131 LLNTAILLASGVTVTWAHHSITEGNQNQAIQALTMTILLGFYFTALQATE---YYEAPFSIADGVYGSTFFVATGFHGLH 207
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1495346005 208 VIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFVDVIWLFLYMTIY 257
Cdd:cd02863   134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 126-257 6.01e-17

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 76.88  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 126 PLEVPLLNTAILLASGVTVTWAHHSItegNQNQAIQALTMTILLGFYFTALQATEYYEAPFSIADGVYGSTFFVATGFHG 205
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVTAYHHLL---GWKYCDLFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1495346005 206 LHVIIGSsFLLICLLRLIKFHFTPNHHfgfEAAAWYWHFVDVIWLFLYMTIY 257
Cdd:MTH00049  166 SHVVLGV-VGLSTLLLVGSSSFGVYRS---TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 126-259 8.25e-15

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: 70.99  E-value: 8.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 126 PLEVPLLNTAILLASGVTVTWAHHSITEGNQNQAIQALTMTILLGFYFTALQATEYYEAPFSIADG---------VYGST 196
Cdd:cd02864    59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGAS 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1495346005 197 FFVATGFHGLHVIIGSSFLLICLLRLIKFHFTPNHHFG-FEAAAWYWHFVDVIWLFLYMTIYWW 259
Cdd:cd02864   139 FFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEiVEIAGLYWHFVDLVWVFIFAFFYLW 202
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 131-261 1.00e-10

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 59.79  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1495346005 131 LLNTAILLASGVTVTWAHHSITEGNQNQAIQALTMTILLGFYFTALqatEYYEAPFSIADGvYG-------STFFVATGF 203
Cdd:PRK10663   70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGM---EIYEFHHLIVEG-MGpdrsgflSAFFALVGT 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1495346005 204 HGLHVIIGSSFLLICLLRLIKFHFTPNHHFGFEAAAWYWHFVDVIWLFLYMTIYWWGS 261
Cdd:PRK10663  146 HGLHVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
 
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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