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Conserved domains on  [gi|5835159|ref|NP_008218|]
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cytochrome c oxidase subunit III (mitochondrion) [Gorilla gorilla]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10791085)

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 MTH00099
cytochrome c oxidase subunit III; Validated
 1-261 6.32e-167

cytochrome c oxidase subunit III; Validated


:

Pssm-ID: 177161  Cd Length: 261  Bit Score: 461.89  E-value: 6.32e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00099   1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-261 6.32e-167

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 461.89  E-value: 6.32e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00099   1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 6.10e-128

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 363.27  E-value: 6.10e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159      6 HAYHMVKPSPWPLTGALSALLMTSGLAMWFHF--HSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     84 ILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    164 LITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 5835159    244 FVDVVWLFLYVSIYWWGS 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 1.64e-122

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: 348.74  E-value: 1.64e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   18 LTGALSALLMTSGLAMWFH-FHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGMILFITSEVFFFAG 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   97 FFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLL 176
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  177 QASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 5835159  257 YWW 259
Cdd:cd01665 241 YWW 243
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 1.01e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.24  E-value: 1.01e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   70 HHTLPVQKGLRYGMILFITSEVFF-FAGFFWAFYHSSLAPtpqlgahWPPTGITPLNPLeVPLLNTSVLLASGVSITWAH 148
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  149 HSLMENNRNQMIQALLITILLGLYFTLLQASEY---FEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMF 225
Cdd:COG1845  79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 5835159  226 HFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 120-260 1.70e-12

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: 64.49  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    120 GITPLNPLEVPLL--NTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASE---YFEAPFTISDGIYG 194
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835159    195 STFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-261 6.32e-167

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 461.89  E-value: 6.32e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00099   1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00099 161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00099 241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-261 2.49e-166

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 460.19  E-value: 2.49e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00118 161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00118 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-261 2.88e-154

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 429.95  E-value: 2.88e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00130   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00130 161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00130 241 YWHFVDVVWLFLYISIYWWGS 261
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-261 1.21e-152

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 425.70  E-value: 1.21e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00075   1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00075  81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00075 161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAW 240

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00075 241 YWHFVDVVWLFLYVSIYWWGS 261
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 3-261 2.73e-149

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 417.07  E-value: 2.73e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     3 HQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYG 82
Cdd:MTH00189   2 HQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    83 MILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQA 162
Cdd:MTH00189  82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   163 LLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYW 242
Cdd:MTH00189 162 LTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYW 241

                        250
                 ....*....|....*....
gi 5835159   243 HFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00189 242 HFVDVVWLFLYVSIYWWGS 260
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 3-257 2.49e-139

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 391.85  E-value: 2.49e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     3 HQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYG 82
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    83 MILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQA 162
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   163 LLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYW 242
Cdd:MTH00155 161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYW 240

                        250
                 ....*....|....*
gi 5835159   243 HFVDVVWLFLYVSIY 257
Cdd:MTH00155 241 HFVDVVWLFLYISIY 255
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-261 6.83e-134

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 378.30  E-value: 6.83e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQsHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00039   1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00039  80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00039 160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAW 239

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00039 240 YWHFVDVVWLFLYVCIYWWGS 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-261 3.12e-132

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 373.84  E-value: 3.12e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     6 HAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGMIL 85
Cdd:MTH00141   4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    86 FITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLI 165
Cdd:MTH00141  84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   166 TILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFV 245
Cdd:MTH00141 164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*.
gi 5835159   246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00141 244 DVVWLFLYLSIYWWGS 259
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-261 6.10e-128

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 363.27  E-value: 6.10e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159      6 HAYHMVKPSPWPLTGALSALLMTSGLAMWFHF--HSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     84 ILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    164 LITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWH 243
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWH 240

                         250
                  ....*....|....*...
gi 5835159    244 FVDVVWLFLYVSIYWWGS 261
Cdd:pfam00510 241 FVDVVWLFLYVSVYWWGS 258
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-261 1.73e-127

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 362.18  E-value: 1.73e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00219   2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00219  82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 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 1.64e-122

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: 348.74  E-value: 1.64e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   18 LTGALSALLMTSGLAMWFH-FHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGMILFITSEVFFFAG 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   97 FFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLL 176
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  177 QASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSI 256
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFV 240


                ...
gi 5835159  257 YWW 259
Cdd:cd01665 241 YWW 243
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-261 2.95e-117

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 336.04  E-value: 2.95e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     6 HAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGMIL 85
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    86 FITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLI 165
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   166 TILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFV 245
Cdd:MTH00009 164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFV 243

                        250
                 ....*....|....*.
gi 5835159   246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00009 244 DVVWIFLYLCIYWWGS 259
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 6-261 1.12e-115

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 332.10  E-value: 1.12e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     6 HAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGMIL 85
Cdd:MTH00024   6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    86 FITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLI 165
Cdd:MTH00024  86 FILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   166 TILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFV 245
Cdd:MTH00024 166 TVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFV 245

                        250
                 ....*....|....*.
gi 5835159   246 DVVWLFLYVSIYWWGS 261
Cdd:MTH00024 246 DVVWLFLYLCIYWWGS 261
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-261 1.60e-113

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 326.75  E-value: 1.60e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     1 MIHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLR 80
Cdd:MTH00052   2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    81 YGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMI 160
Cdd:MTH00052  82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   161 QALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAW 240
Cdd:MTH00052 162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|.
gi 5835159   241 YWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00052 242 YWHFVDVVWLFLFIFMYWWGS 262
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 6-261 2.31e-92

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 274.25  E-value: 2.31e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     6 HAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRYGMIL 85
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    86 FITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHH---------------- 149
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHaiigtgnpaslekgtq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   150 --------------------SLMENNRNQMIQALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVI 209
Cdd:MTH00028 166 giegpnpsngappdpqkgptFLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVL 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5835159   210 IGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
Cdd:MTH00028 246 VGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
PLN02194 PLN02194
cytochrome-c oxidase
 4-260 1.29e-87

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 261.14  E-value: 1.29e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     4 QSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHS--TTLLMLGLLTNMLTMYQWWRDVMRESTYQGHHTLPVQKGLRY 81
Cdd:PLN02194   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    82 GMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQ 161
Cdd:PLN02194  85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   162 ALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWY 241
Cdd:PLN02194 165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWY 244

                        250
                 ....*....|....*....
gi 5835159   242 WHFVDVVWLFLYVSIYWWG 260
Cdd:PLN02194 245 WHFVDVVWLFLFVSIYWWG 263
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-261 5.19e-72

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 220.98  E-value: 5.19e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159     6 HAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSTTLLMLGLLTNMLTMYQWWRDVMREStYQGHHTLPVQKGLRYGMIL 85
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    86 FITSEVFFFAGFFWAFYHSSLAPTPQLGAHWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNrNQMIQALLI 165
Cdd:MTH00083  82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   166 TILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFV 245
Cdd:MTH00083 161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFV 240

                        250
                 ....*....|....*.
gi 5835159   246 DVVWLFLYVSIYWWGS 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 3.11e-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: 203.59  E-value: 3.11e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   71 HTLPVQKGLRYGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGAhwpptgitPLNPLEVPLLNTSVLLASGVSITWAHHS 150
Cdd:cd00386   1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  151 LM--ENNRNQMIQALLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMFHFT 228
Cdd:cd00386  73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 5835159  229 SKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd00386 153 PRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-259 1.01e-48

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 159.24  E-value: 1.01e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   70 HHTLPVQKGLRYGMILFITSEVFF-FAGFFWAFYHSSLAPtpqlgahWPPTGITPLNPLeVPLLNTSVLLASGVSITWAH 148
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  149 HSLMENNRNQMIQALLITILLGLYFTLLQASEY---FEAPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICLIRQLMF 225
Cdd:COG1845  79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 5835159  226 HFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:COG1845 159 GFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 131-257 1.63e-22

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 91.14  E-value: 1.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  131 LLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASEY---FEAPFTISDGIYGSTFFVATGFHGLH 207
Cdd:cd02862  55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5835159  208 VIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLY 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 131-257 1.32e-18

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: 80.75  E-value: 1.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  131 LLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASEYFE---APFTISDGIYGSTFFVATGFHGLH 207
Cdd:cd02863  54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHliaEGAGPDRSAFLSAFFTLVGTHGLH 133

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5835159  208 VIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIY 257
Cdd:cd02863 134 VTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVY 183
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 123-259 1.47e-17

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: 77.80  E-value: 1.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  123 PLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASEYFEAPF---TISDGIYGSTFFV 199
Cdd:cd02865  45 PLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDagyGPTSNPAGSFFYL 124

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  200 ATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02865 125 LTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 126-257 2.82e-16

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 75.34  E-value: 2.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   126 PLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMiqaLLITILLGLYFTLLQASEYFEAPFTISDGIYGSTFFVATGFHG 205
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVTAYHHLLGWKYCDLF---LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5835159   206 LHVIIGSTFLTICLIRQLMFHFTSKHHFgfeaAAWYWHFVDVVWLFLYVSIY 257
Cdd:MTH00049 166 SHVVLGVVGLSTLLLVGSSSFGVYRSTV----LTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 126-259 7.92e-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: 7.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159  126 PLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASEYFEAPFTISDG---------IYGST 196
Cdd:cd02864  59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGAS 138

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5835159  197 FFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHF-GFEAAAWYWHFVDVVWLFLYVSIYWW 259
Cdd:cd02864 139 FFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 120-260 1.70e-12

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: 64.49  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159    120 GITPLNPLEVPLL--NTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASE---YFEAPFTISDGIYG 194
Cdd:TIGR02897  43 GKMPAELFELPLVliMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYW 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835159    195 STFFVATGFHGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
Cdd:TIGR02897 123 SSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 131-261 8.63e-08

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 51.32  E-value: 8.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835159   131 LLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTllqASEYFEAPFTISDGiYG-------STFFVATGF 203
Cdd:PRK10663  70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFI---GMEIYEFHHLIVEG-MGpdrsgflSAFFALVGT 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 5835159   204 HGLHVIIGSTFLTICLIRQLMFHFTSKHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 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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