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Conserved domains on  [gi|46241583|gb|AAS82983|]
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cytochrome oxidase subunit III, partial (mitochondrion) [Peromyscus maniculatus]

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 ...
 1-218 5.90e-144

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: 401.80  E-value: 5.90e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00099  15 PWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00099  95 AGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFT 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00099 175 LLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHH 232
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-218 5.90e-144

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 401.80  E-value: 5.90e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00099  15 PWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00099  95 AGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFT 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00099 175 LLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHH 232
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-218 1.20e-110

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 317.43  E-value: 1.20e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583     1 PWPLTGAFSALLLTSGLVMWFHY--NSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVF 78
Cdd:pfam00510  10 PWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    79 FFAGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIY 158
Cdd:pfam00510  90 FFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   159 FTVLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:pfam00510 170 FTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHH 229
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 4-218 7.30e-108

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: 309.83  E-value: 7.30e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   4 LTGAFSALLLTSGLVMWFH-YNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAG 82
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  83 FFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFTVL 162
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46241583 163 QASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHH 216
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
56-218 1.97e-34

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 121.11  E-value: 1.97e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  56 HHTPIVQKGLRYGMILFIVSEVFF-FAGFFWAFYHSSLAPthdlggcWPPTGISPLNPLeVPLLNTSVLLASGVSITWAH 134
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583 135 HSLMEGKRNNMNQALLITILLGIYFTVLQASEY---FETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKY 211
Cdd:COG1845  79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158


                ....*..
gi 46241583 212 HFTSKHH 218
Cdd:COG1845 159 GFTPENH 165
 
Name Accession Description Interval E-value
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-218 5.90e-144

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 401.80  E-value: 5.90e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00099  15 PWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00099  95 AGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFT 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00099 175 LLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHH 232
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-218 7.01e-138

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 386.61  E-value: 7.01e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00118  15 PWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00118  95 LGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFT 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00118 175 ALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHH 232
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-218 2.12e-126

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 357.54  E-value: 2.12e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00130  15 PWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00130  95 LGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFT 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00130 175 FLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHH 232
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-218 5.06e-124

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 351.20  E-value: 5.06e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00189  14 PWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00189  94 LGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFT 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00189 174 LLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHH 231
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-218 1.82e-122

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 347.50  E-value: 1.82e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00075  15 PWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00075  95 LGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFT 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00075 175 LLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHH 232
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-218 6.30e-118

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 335.61  E-value: 6.30e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00155  13 PWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00155  93 ISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00155 173 MLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHH 230
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-218 7.49e-115

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 328.00  E-value: 7.49e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00141  13 PWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00141  93 FAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00141 173 FLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHH 230
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-218 1.20e-110

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 317.43  E-value: 1.20e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583     1 PWPLTGAFSALLLTSGLVMWFHY--NSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVF 78
Cdd:pfam00510  10 PWPLFGSFALLLLTSGLVLWFHGysGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    79 FFAGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIY 158
Cdd:pfam00510  90 FFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   159 FTVLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:pfam00510 170 FTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHH 229
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-218 3.79e-109

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 313.59  E-value: 3.79e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00039  14 PWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00039  94 FAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFT 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00039 174 ALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHH 231
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 4-218 7.30e-108

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: 309.83  E-value: 7.30e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   4 LTGAFSALLLTSGLVMWFH-YNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFFAG 82
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHgYGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  83 FFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFTVL 162
Cdd:cd01665  81 FFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46241583 163 QASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:cd01665 161 QAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHH 216
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-218 2.77e-106

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 306.71  E-value: 2.77e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00219  16 PWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00219  96 FAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFT 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00219 176 MLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHH 233
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-218 3.86e-98

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 285.96  E-value: 3.86e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00009  13 PWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00009  93 FAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00009 173 FLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHH 230
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-218 9.07e-96

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 279.72  E-value: 9.07e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00024  15 PWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00024  95 FSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFT 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00024 175 GLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQH 232
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-218 9.70e-94

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 274.75  E-value: 9.70e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00052  16 PWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFT 160
Cdd:MTH00052  96 FSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFT 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46241583  161 VLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00052 176 GLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHH 233
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-218 9.28e-81

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 243.05  E-value: 9.28e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVFFF 80
Cdd:MTH00028  15 PWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   81 AGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGK------------------- 141
Cdd:MTH00028  95 FAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsn 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  142 -----------------RNNMNQALLITILLGIYFTVLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVC 204
Cdd:MTH00028 175 gappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVC 254

                        250
                 ....*....|....
gi 46241583  205 LLRQLKYHFTSKHH 218
Cdd:MTH00028 255 FIRLLSNQFTNSHH 268
PLN02194 PLN02194
cytochrome-c oxidase
 1-218 1.28e-69

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 213.76  E-value: 1.28e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    1 PWPLTGAFSALLLTSGLVMWFH--YNSYTLMTIGLLTNIMTMYQWWRDIVREGTYQGHHTPIVQKGLRYGMILFIVSEVF 78
Cdd:PLN02194  16 PWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVM 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   79 FFAGFFWAFYHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIY 158
Cdd:PLN02194  96 FFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALV 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  159 FTVLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:PLN02194 176 FTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHH 235
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 8-218 1.47e-59

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 187.47  E-value: 1.47e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583    8 FSALLLTSGLVMWFHYNSYTLMTIGLLTNIMTMYQWWRDIVREGtYQGHHTPIVQKGLRYGMILFIVSEVFFFAGFFWAF 87
Cdd:MTH00083  19 FSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583   88 YHSSLAPTHDLGGCWPPTGISPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKrNNMNQALLITILLGIYFTVLQASEY 167
Cdd:MTH00083  98 FDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSN-KSCTNSLLLTCFLGLYFTSFQLMEY 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 46241583  168 FETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:MTH00083 177 KEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHH 227
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 57-218 8.37e-48

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: 155.05  E-value: 8.37e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  57 HTPIVQKGLRYGMILFIVSEVFFFAGFFWAFYHSSLAPTHDLGgcwpptgiSPLNPLEVPLLNTSVLLASGVSITWAHHS 136
Cdd:cd00386   1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG--------AGLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583 137 LM--EGKRNNMNQALLITILLGIYFTVLQASEYFETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFT 214
Cdd:cd00386  73 LAarRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152


                ....
gi 46241583 215 SKHH 218
Cdd:cd00386 153 PRHH 156
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
56-218 1.97e-34

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 121.11  E-value: 1.97e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  56 HHTPIVQKGLRYGMILFIVSEVFF-FAGFFWAFYHSSLAPthdlggcWPPTGISPLNPLeVPLLNTSVLLASGVSITWAH 134
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAP-------DWPAGAELLDLP-LPLINTLLLLLSSFTVALAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583 135 HSLMEGKRNNMNQALLITILLGIYFTVLQASEY---FETPFSISDGIYGSTFFMATGFHGLHVIIGTTFLMVCLLRQLKY 211
Cdd:COG1845  79 RAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRG 158


                ....*..
gi 46241583 212 HFTSKHH 218
Cdd:COG1845 159 GFTPENH 165
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 117-218 1.94e-10

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: 57.63  E-value: 1.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583 117 LLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFTVLQASEY---FETPFSISDGIYGSTFFMATGFHGLH 193
Cdd:cd02862  55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYahkIAAGIDPDAGLFFTLYFLLTGFHLLH 134

                        90       100
                ....*....|....*....|....*
gi 46241583 194 VIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:cd02862 135 VLIGLGILLWVAWRARRGRYSARDY 159
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 112-206 2.20e-10

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 58.00  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583  112 PLEVPLLNTSVLLASGVSITwAHHSLMEGKRNNMNqaLLITILLGIYFTVLQASEYFETPFSISDGIYGSTFFMATGFHG 191
Cdd:MTH00049  89 SLEIPFVGCFLLLGSSITVT-AYHHLLGWKYCDLF--LYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHF 165

                         90
                 ....*....|....*
gi 46241583  192 LHVIIGTTFLMVCLL 206
Cdd:MTH00049 166 SHVVLGVVGLSTLLL 180
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 117-212 7.32e-10

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: 56.09  E-value: 7.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583 117 LLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFTVLQASEYFE---TPFSISDGIYGSTFFMATGFHGLH 193
Cdd:cd02863  54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHliaEGAGPDRSAFLSAFFTLVGTHGLH 133

                        90
                ....*....|....*....
gi 46241583 194 VIIGtTFLMVCLLRQLKYH 212
Cdd:cd02863 134 VTFG-LIWILVMIIQLKKR 151
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 112-216 1.42e-08

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: 52.89  E-value: 1.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583 112 PLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFTVLQASEYfeTPFSISDGI-----------YG 180
Cdd:cd02864  59 PLVLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEW--TKLIVEEGVrpwgnpwgaaqFG 136

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 46241583 181 STFFMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSK 216
Cdd:cd02864 137 ASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRI 172
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 108-218 1.75e-07

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: 49.29  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46241583 108 SPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGKRNNMNQALLITILLGIYFTVLQASE----YFETPFSISDGiYGSTF 183
Cdd:cd02865  44 APLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAwhalNDAGYGPTSNP-AGSFF 122

                        90       100       110
                ....*....|....*....|....*....|....*
gi 46241583 184 FMATGFHGLHVIIGTTFLMVCLLRQLKYHFTSKHH 218
Cdd:cd02865 123 YLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRR 157
 
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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