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Conserved domains on  [gi|636577122|gb|AIA08889|]
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cytochrome c oxidase subunit 3, partial (mitochondrion) [Exaiptasia diaphana]

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 ...
 1-148 2.42e-81

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 MTH00024:

Pssm-ID: 444752  Cd Length: 261  Bit Score: 240.42  E-value: 2.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00024  84 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGL 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00024 164 FLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQ 231
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-148 2.42e-81

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 240.42  E-value: 2.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00024  84 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGL 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00024 164 FLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQ 231
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-148 4.66e-71

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: 213.53  E-value: 4.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:cd01665   68 ILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGL 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:cd01665  148 ILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNH 215
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-148 4.83e-64

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 196.09  E-value: 4.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122    1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122   81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNH 228
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
35-148 1.12e-31

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 111.48  E-value: 1.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  35 PQGIDPLNPfSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGLTATVILGVIFTGLQAMEYYE---APFAISDSVYG 111
Cdd:COG1845   49 PAGAELLDL-PLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFG 127

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 636577122 112 STFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:COG1845  128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPEN 164
 
Name Accession Description Interval E-value
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 1-148 2.42e-81

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 240.42  E-value: 2.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00024  84 LLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGL 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00024 164 FLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQ 231
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-148 4.01e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 229.68  E-value: 4.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00052  85 ILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00052 165 ALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHH 232
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-148 1.08e-74

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 223.29  E-value: 1.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00118  84 ILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQAL 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00118 164 TLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNH 231
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 2-148 8.31e-72

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 215.99  E-value: 8.31e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   2 LFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGLT 81
Cdd:MTH00189  84 LFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALT 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636577122  82 ATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00189 164 LTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSH 230
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-148 4.66e-71

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: 213.53  E-value: 4.66e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:cd01665   68 ILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILGL 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:cd01665  148 ILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNH 215
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-148 2.42e-70

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 211.96  E-value: 2.42e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00155  82 ILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSL 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00155 162 FFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNH 229
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-148 7.63e-70

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 211.12  E-value: 7.63e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00039  83 ILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQAL 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00039 163 FLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNH 230
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 2-148 6.63e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 208.59  E-value: 6.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   2 LFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGLT 81
Cdd:MTH00141  83 LFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLG 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  82 ATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQF-TRHH 148
Cdd:MTH00141 163 LTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFsTNHH 230
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-148 1.13e-64

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 198.06  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00130  84 ILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSL 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00130 164 TLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEH 231
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-148 4.83e-64

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 196.09  E-value: 4.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122    1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGL 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122   81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:pfam00510 161 ILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNH 228
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-148 7.51e-64

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 195.73  E-value: 7.51e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00075  84 ILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSL 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00075 164 ALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQH 231
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-148 7.11e-61

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 188.40  E-value: 7.11e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00099  84 ILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQAL 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00099 164 FITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNH 231
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-148 1.57e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 187.30  E-value: 1.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00219  85 ILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGL 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00219 165 LFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNH 232
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-148 2.37e-58

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 181.96  E-value: 2.37e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:MTH00009  82 ILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQAL 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00009 162 ILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGH 229
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-148 5.97e-55

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 174.48  E-value: 5.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGE-------- 72
Cdd:MTH00028  84 LLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGnpaslekg 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  73 ----------------------------KTEAINGLTATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLH 124
Cdd:MTH00028 164 tqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLH 243

                        170       180
                 ....*....|....*....|....
gi 636577122 125 VIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00028 244 VLVGTTFLIVCFIRLLSNQFTNSH 267
PLN02194 PLN02194
cytochrome-c oxidase
 1-148 5.81e-48

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 155.59  E-value: 5.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGL 80
Cdd:PLN02194  87 ILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYAL 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:PLN02194 167 VATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEH 234
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 1-148 2.78e-42

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 140.48  E-value: 2.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAVWPPQGIDPLNPFSVPLLNTAVLLSSGATVTWAHHALISGEKtEAINGL 80
Cdd:MTH00083  80 ILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSL 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636577122  81 TATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:MTH00083 159 LLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNH 226
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-148 1.68e-40

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: 133.87  E-value: 1.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   1 LLFILSEVLFFFSFFWAFFHSSIAPNIELGAvwppqgidPLNPFSVPLLNTAVLLSSGATVTWAHHALI--SGEKTEAIN 78
Cdd:cd00386   14 WLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHASLAarRGNRKKARL 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  79 GLTATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:cd00386   86 WLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRH 155
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
35-148 1.12e-31

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 111.48  E-value: 1.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  35 PQGIDPLNPfSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGLTATVILGVIFTGLQAMEYYE---APFAISDSVYG 111
Cdd:COG1845   49 PAGAELLDL-PLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAFG 127

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 636577122 112 STFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRHH 148
Cdd:COG1845  128 SFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPEN 164
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 48-145 5.81e-14

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: 65.34  E-value: 5.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  48 LLNTAVLLSSGATVTWAHHALISGEKTEAINGLTATVILGVIFTGLQAME---YYEAPFAISDSVYGSTFFVATGFHGLH 124
Cdd:cd02863   54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                         90       100
                 ....*....|....*....|.
gi 636577122 125 VIIGTTFLTVCLARLVYHQFT 145
Cdd:cd02863  134 VTFGLIWILVMIIQLKKRGLT 154
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 48-138 1.61e-13

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: 64.18  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  48 LLNTAVLLSSGATVTWAHHALISGEKTEAINGLTATVILGVIFTGLQAMEYYE---APFAISDSVYGSTFFVATGFHGLH 124
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHkiaAGIDPDAGLFFTLYFLLTGFHLLH 134

                         90
                 ....*....|....
gi 636577122 125 VIIGTTFLTVCLAR 138
Cdd:cd02862  135 VLIGLGILLWVAWR 148
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 30-145 9.01e-12

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: 59.69  E-value: 9.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  30 GAVWPPQGIDPLNpfsVPLLNTAVLLSSGATVTWAHHALISGEKTEAINGLTATVILGVIFTGLQAMEYYEAPFAI---S 106
Cdd:cd02865   38 GDWQPGAPLPLPN---LLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWHALNDAGygpT 114

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 636577122 107 DSVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFT 145
Cdd:cd02865  115 SNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYG 153
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 31-147 7.28e-09

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: 52.12  E-value: 7.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122  31 AVWPPQGID----PLNPFSVPL----LNTAVLLSSGATVTWAHHALISGEKTEAINGLTATVILGVIFTGLQAMEY---- 98
Cdd:cd02864   39 TEPWPLPSDvfalRIGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtkli 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 636577122  99 -------YEAPFAISdsVYGSTFFVATGFHGLHVIIGTTFLTVCLARLVYHQFTRH 147
Cdd:cd02864  119 veegvrpWGNPWGAA--QFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRI 172
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 2-133 4.42e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 44.52  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636577122   2 LFILSEVLFFFSFFWAFFHSSIAPNIELGAvwppqgidplnPFSVPLLNTAVLLSSGATVTWAHHALISGEKTEAINglt 81
Cdd:MTH00049  59 LFILSEVIIFGSLLVCCLWFDDWSYISLSS-----------SLEIPFVGCFLLLGSSITVTAYHHLLGWKYCDLFLY--- 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 636577122  82 ATVILGVIFTGLQAMEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLT 133
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLS 176
 
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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