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Conserved domains on  [gi|1165910789|gb|ARA69019|]
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cytochrome c oxidase subunit III (mitochondrion) [Macrauchenia sp. MW-2017]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like super family cl00211
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-239 6.51e-101

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


The actual alignment was detected with superfamily member MTH00099:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 293.94  E-value: 6.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00099    1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00099   81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00099  161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAA 239
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-239 6.51e-101

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 293.94  E-value: 6.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00099    1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00099   81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00099  161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAA 239
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-239 1.05e-73

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 224.60  E-value: 1.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   6 HAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNL--LTMYQWWRDIVRESTFQG*HTPVVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSllLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  84 VLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1165910789 164 FITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAI 236
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 29-239 4.61e-62

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: 194.27  E-value: 4.61e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  29 SGLIMWFHFNSLSLLSLGLLTNLLT-MYQWWRDIVRESTFQG*HTPVVQKGLRYGMVLFIIS*VLFFTGFFWAF****** 107
Cdd:cd01665    12 LGLVLWMHGYGGPLLLFLGLILLILtMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789 108 ***********************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQALFITISLGVYFTLLQASEYYEASFT 187
Cdd:cd01665    92 PSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFT 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1165910789 188 ISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:cd01665   172 ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAI 223
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-239 6.30e-21

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 86.44  E-value: 6.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  71 HTPVVQKGLRYGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHS 150
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLP-------LINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789 151 LM*ANRKHMLQALFITISLGVYFTLLQASEYYEAS---FTISDGVYGSTFFVATGF****************LRQLKFHF 227
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170
                  ....*....|..
gi 1165910789 228 TSDHHFGFEAAA 239
Cdd:COG1845   161 TPENHTGVEAAA 172
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-239 6.51e-101

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 293.94  E-value: 6.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00099    1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00099   81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHML 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00099  161 QALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAA 239
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-239 3.35e-94

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 276.83  E-value: 3.35e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00118    1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00118   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00118  161 QALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAA 239
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-239 1.25e-87

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 260.06  E-value: 1.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00075    1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00075   81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00075  161 QSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAA 239
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-239 5.73e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 255.84  E-value: 5.73e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00130    1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00130   81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00130  161 QSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAA 239
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-239 6.67e-83

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 247.96  E-value: 6.67e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   2 THQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLRY 81
Cdd:MTH00189    1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  82 GMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQ 161
Cdd:MTH00189   81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQ 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1165910789 162 ALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00189  161 ALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAA 238
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 3-239 1.00e-73

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 224.29  E-value: 1.00e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   3 HQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLRYG 82
Cdd:MTH00155    1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  83 MVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQA 162
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1165910789 163 LFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00155  161 LFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAA 237
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-239 1.05e-73

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 224.60  E-value: 1.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   6 HAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNL--LTMYQWWRDIVRESTFQG*HTPVVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSllLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  84 VLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQAL 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1165910789 164 FITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAI 236
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-239 6.13e-71

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 217.45  E-value: 6.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   6 HAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLRYGMVL 85
Cdd:MTH00141    4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  86 FIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQALFI 165
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1165910789 166 TISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00141  164 TIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAA 237
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-239 3.23e-70

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 215.75  E-value: 3.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQtHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00039    1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00039   80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00039  160 QALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAA 238
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-239 6.37e-67

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 207.33  E-value: 6.37e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00219    2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00219   82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQ 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00219  162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAA 240
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-239 1.14e-62

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 196.51  E-value: 1.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00024    1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00024   81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00024  161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAAS 239
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 29-239 4.61e-62

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: 194.27  E-value: 4.61e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  29 SGLIMWFHFNSLSLLSLGLLTNLLT-MYQWWRDIVRESTFQG*HTPVVQKGLRYGMVLFIIS*VLFFTGFFWAF****** 107
Cdd:cd01665    12 LGLVLWMHGYGGPLLLFLGLILLILtMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789 108 ***********************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQALFITISLGVYFTLLQASEYYEASFT 187
Cdd:cd01665    92 PSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFT 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1165910789 188 ISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:cd01665   172 ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAI 223
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-239 4.00e-61

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 192.70  E-value: 4.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00052    2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHML 160
Cdd:MTH00052   82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1165910789 161 QALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00052  162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAA 240
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-239 7.78e-59

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 186.58  E-value: 7.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   6 HAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLRYGMVL 85
Cdd:MTH00009    4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  86 FIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQALFI 165
Cdd:MTH00009   84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALIL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1165910789 166 TISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00009  164 TVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAA 237
PLN02194 PLN02194
cytochrome-c oxidase
 4-239 4.98e-43

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 146.35  E-value: 4.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   4 QTHAYHMVNPSPWP***********SGLIMWFHFNS--LSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLRY 81
Cdd:PLN02194    5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHPFQggARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  82 GMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANRKHMLQ 161
Cdd:PLN02194   85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVY 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1165910789 162 ALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:PLN02194  165 ALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAA 242
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-238 1.24e-42

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 146.37  E-value: 1.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   1 MTHQTHAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVRESTFQG*HTPVVQKGLR 80
Cdd:MTH00028    1 MSLVYHPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  81 YGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*AN----- 155
Cdd:MTH00028   81 LGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpasl 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789 156 -------------------------------RKHMLQALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF* 204
Cdd:MTH00028  161 ekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTH 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1165910789 205 ***************LRQLKFHFTSDHHFGFEAA 238
Cdd:MTH00028  241 GLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAA 274
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-239 4.34e-32

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 117.75  E-value: 4.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789   6 HAYHMVNPSPWP***********SGLIMWFHFNSLSLLSLGLLTNLLTMYQWWRDIVREStFQG*HTPVVQKGLRYGMVL 85
Cdd:MTH00083    3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  86 FIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHSLM*ANrKHMLQALFI 165
Cdd:MTH00083   82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1165910789 166 TISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFTSDHHFGFEAAA 239
Cdd:MTH00083  161 TCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAI 234
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 71-239 5.35e-31

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: 112.68  E-value: 5.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  71 HTPVVQKGLRYGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHS 150
Cdd:cd00386     1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAY--------FHSRLSPPVEFGAGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789 151 LM*A--NRKHMLQALFITISLGVYFTLLQASEYYEASFTISDGVYGSTFFVATGF****************LRQLKFHFT 228
Cdd:cd00386    73 LAARrgNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                         170
                  ....*....|.
gi 1165910789 229 SDHHFGFEAAA 239
Cdd:cd00386   153 PRHHLGLEAAA 163
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
71-239 6.30e-21

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 86.44  E-value: 6.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789  71 HTPVVQKGLRYGMVLFIIS*VLFFTGFFWAF*****************************LLNTSVLLASGVSITWAHHS 150
Cdd:COG1845     8 HAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLP-------LINTLLLLLSSFTVALAVRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1165910789 151 LM*ANRKHMLQALFITISLGVYFTLLQASEYYEAS---FTISDGVYGSTFFVATGF****************LRQLKFHF 227
Cdd:COG1845    81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160

                         170
                  ....*....|..
gi 1165910789 228 TSDHHFGFEAAA 239
Cdd:COG1845   161 TPENHTGVEAAA 172
 
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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