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Conserved domains on  [gi|564813664|gb|AHC03922|]
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cytochrome c oxidase subunit III, partial (mitochondrion) [Molothrus rufoaxillaris]

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 ...
 1-149 2.12e-93

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 MTH00118:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 270.67  E-value: 2.12e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHH 149
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-149 2.12e-93

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 270.67  E-value: 2.12e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHH 149
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-149 8.19e-71

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 213.43  E-value: 8.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664    6 HSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPR--LLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564813664   84 ALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHH 146
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-149 1.41e-60

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: 186.95  E-value: 1.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664  18 ILGAASALLTTSGLTMWFH-YNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYGMALFITSEAFFFLG 96
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564813664  97 FFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHH 133
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-149 4.54e-04

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 38.68  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664  70 HHTPTVQKGLRYGMALFITSEAFFFLGFFWAFFHSSLAptpelGGQWPPvGIKPLNPMeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79
 
Name Accession Description Interval E-value
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-149 2.12e-93

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 270.67  E-value: 2.12e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00118   1 MTHQAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00118  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHH 149
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-149 5.71e-83

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 244.25  E-value: 5.71e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00099   1 MTHQTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00099  81 YGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHH 149
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-149 5.62e-80

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 236.97  E-value: 5.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00130   1 MAHQAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00130  81 YGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHH 149
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-149 9.54e-79

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 233.87  E-value: 9.54e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00075   1 MAHQAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00075  81 YGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHH 149
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-149 2.10e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 230.25  E-value: 2.10e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   2 AHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRY 81
Cdd:MTH00189   1 MHQAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564813664  82 GMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00189  81 GMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHH 148
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 3-149 1.07e-73

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 220.44  E-value: 1.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   3 HQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYG 82
Cdd:MTH00155   1 KKNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564813664  83 MALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00155  81 MILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHH 147
COX3 pfam00510
Cytochrome c oxidase subunit III;
6-149 8.19e-71

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 213.43  E-value: 8.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664    6 HSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPR--LLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYGM 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNmtLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564813664   84 ALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHH 146
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 6-149 2.67e-67

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 204.35  E-value: 2.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   6 HSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYGMAL 85
Cdd:MTH00141   4 NPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFIL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564813664  86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00141  84 FIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHH 147
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-149 2.04e-66

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 202.27  E-value: 2.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQaHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00039   1 MTHQ-HPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00039  80 YGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHH 148
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-149 1.06e-62

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 193.08  E-value: 1.06e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00219   2 MFFQTNPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00219  82 IGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHH 150
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-149 3.16e-62

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 191.93  E-value: 3.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00052   2 MQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00052  82 YGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHH 150
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-149 1.53e-61

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 189.96  E-value: 1.53e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   1 MAHQAHSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLR 80
Cdd:MTH00024   1 MSKLYHPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  81 YGMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00024  81 YGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHH 149
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 18-149 1.41e-60

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: 186.95  E-value: 1.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664  18 ILGAASALLTTSGLTMWFH-YNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYGMALFITSEAFFFLG 96
Cdd:cd01665    1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564813664  97 FFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:cd01665   81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHH 133
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 6-149 1.54e-55

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 174.64  E-value: 1.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   6 HSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYGMAL 85
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMIL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564813664  86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHH 147
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 6-149 1.63e-53

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 170.63  E-value: 1.63e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   6 HSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRYGMAL 85
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLL 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564813664  86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHH 149
PLN02194 PLN02194
cytochrome-c oxidase
 4-149 2.86e-44

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 145.96  E-value: 2.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   4 QAHSYHMVDPSPWPILGAASALLTTSGLTMWFH--YNSPRLLILGLLSTILVMFQWWRDIVRESTFQGHHTPTVQKGLRY 81
Cdd:PLN02194   5 QRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRY 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564813664  82 GMALFITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:PLN02194  85 GSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHH 152
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 6-149 1.01e-30

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 110.82  E-value: 1.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664   6 HSYHMVDPSPWPILGAASALLTTSGLTMWFHYNSPRLLILGLLSTILVMFQWWRDIVREStFQGHHTPTVQKGLRYGMAL 85
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMIL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564813664  86 FITSEAFFFLGFFWAFFHSSLAPTPELGGQWPPVGIKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:MTH00083  82 FIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHH 145
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 71-149 8.83e-12

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: 59.52  E-value: 8.83e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564813664  71 HTPTVQKGLRYGMALFITSEAFFFLGFFWAFFHSSLAPTPELGgqwppvgiKPLNPMEVPLLNTAILLASGVTVTWAHH 149
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHA 71
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
70-149 4.54e-04

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 38.68  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813664  70 HHTPTVQKGLRYGMALFITSEAFFFLGFFWAFFHSSLAptpelGGQWPPvGIKPLNPMeVPLLNTAILLASGVTVTWAHH 149
Cdd:COG1845    7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79
 
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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