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Conserved domains on  [gi|47156708|gb|AAT12251|]
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cytochrome oxidase subunit 3, partial (mitochondrion) [Staurastrum hexacerum var. aversum]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10108868)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

CATH:  1.20.120.80
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0009055|GO:0009060|GO:0019646
PubMed:  8083153|12907296|10563795
SCOP:  3000671

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 16-191 4.87e-89

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: 260.91  E-value: 4.87e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:cd01665  33 LLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFG 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:cd01665 113 IPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHV 192

                       170
                ....*....|....*.
gi 47156708 176 IIGTIFLVICCIRQYM 191
Cdd:cd01665 193 IIGTIFLTVCLIRLLK 208
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 16-191 4.87e-89

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: 260.91  E-value: 4.87e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:cd01665  33 LLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFG 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:cd01665 113 IPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHV 192

                       170
                ....*....|....*.
gi 47156708 176 IIGTIFLVICCIRQYM 191
Cdd:cd01665 193 IIGTIFLTVCLIRLLK 208
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 15-189 3.22e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 254.49  E-value: 3.22e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   15 TVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 94
Cdd:MTH00118  48 LSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   95 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFH 174
Cdd:MTH00118 128 EVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*
gi 47156708  175 VIIGTIFLVICCIRQ 189
Cdd:MTH00118 208 VIIGSTFLIVCLLRL 222
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-190 5.47e-79

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 236.15  E-value: 5.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708     1 HSSTGGGALLSLGLTVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIG 80
Cdd:pfam00510  31 HGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708    81 AVWPPKGIEAIGPWDIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIY 160
Cdd:pfam00510 111 AQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVY 190

                         170       180       190
                  ....*....|....*....|....*....|
gi 47156708   161 GSTFFLATGFHGFHVIIGTIFLVICCIRQY 190
Cdd:pfam00510 191 GSTFYFATGFHGLHVIIGTAFLAVCFLRLL 220
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
37-188 7.03e-31

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 111.09  E-value: 7.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  37 HHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAptveiGAVWPPkGIEAIGPWdIPFLNTLILLSSGAAVTWAHH 116
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47156708 117 AILAGSQRQAIYGLLATVFLAFIFTAFQGMEY---VEAPFTISDGIYGSTFFLATGFHGFHVIIGTIFLVICCIR 188
Cdd:COG1845  80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVR 154
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 16-191 4.87e-89

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: 260.91  E-value: 4.87e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:cd01665  33 LLILTMFLWWRDVIRESTFGGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVELGGTWPPVGIEPLNPFG 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:cd01665 113 IPLLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHV 192

                       170
                ....*....|....*.
gi 47156708 176 IIGTIFLVICCIRQYM 191
Cdd:cd01665 193 IIGTIFLTVCLIRLLK 208
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 15-189 3.22e-86

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 254.49  E-value: 3.22e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   15 TVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 94
Cdd:MTH00118  48 LSMLLTMLQWWRDIVRESTFQGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGQWPPTGIKPLNPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   95 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFH 174
Cdd:MTH00118 128 EVPLLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*
gi 47156708  175 VIIGTIFLVICCIRQ 189
Cdd:MTH00118 208 VIIGSTFLIVCLLRL 222
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 15-191 1.19e-85

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 252.79  E-value: 1.19e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   15 TVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 94
Cdd:MTH00155  46 IITLLTMFQWWRDVIREGTFQGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIELGMIWPPKGIIPFNPF 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   95 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFH 174
Cdd:MTH00155 126 QIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLH 205

                        170
                 ....*....|....*..
gi 47156708  175 VIIGTIFLVICCIRQYM 191
Cdd:MTH00155 206 VIIGTTFLLVCLIRHLN 222
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 17-191 1.69e-83

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 247.58  E-value: 1.69e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   17 ILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWDI 96
Cdd:MTH00189  49 LLLTMIQWWRDVVRESTFQGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVELGMCWPPTGIEPLNPFEV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   97 PFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHVI 176
Cdd:MTH00189 129 PLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVI 208

                        170
                 ....*....|....*
gi 47156708  177 IGTIFLVICCIRQYM 191
Cdd:MTH00189 209 IGSTFLLVCLLRQIQ 223
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-190 5.47e-79

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 236.15  E-value: 5.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708     1 HSSTGGGALLSLGLTVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIG 80
Cdd:pfam00510  31 HGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTFLGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVELG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708    81 AVWPPKGIEAIGPWDIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIY 160
Cdd:pfam00510 111 AQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISDGVY 190

                         170       180       190
                  ....*....|....*....|....*....|
gi 47156708   161 GSTFFLATGFHGFHVIIGTIFLVICCIRQY 190
Cdd:pfam00510 191 GSTFYFATGFHGLHVIIGTAFLAVCFLRLL 220
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 16-191 8.23e-79

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 235.56  E-value: 8.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:MTH00141  47 LIVLTMFQWWRDIVRESTFQGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEIGCCWPPVGIEPLNPFQ 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:MTH00141 127 VPLLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHV 206

                        170
                 ....*....|....*.
gi 47156708  176 IIGTIFLVICCIRQYM 191
Cdd:MTH00141 207 IIGTTFLLVCLVRLLL 222
PLN02194 PLN02194
cytochrome-c oxidase
 17-191 8.98e-79

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 235.71  E-value: 8.98e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   17 ILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWDI 96
Cdd:PLN02194  53 ILYTMFVWWRDVLRESTLEGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGIEVLDPWEI 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   97 PFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHVI 176
Cdd:PLN02194 133 PFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVI 212

                        170
                 ....*....|....*
gi 47156708  177 IGTIFLVICCIRQYM 191
Cdd:PLN02194 213 IGTLFLIICGIRQYL 227
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 15-188 1.31e-78

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 235.07  E-value: 1.31e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   15 TVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 94
Cdd:MTH00052  49 ITIIFTMVVWWRDVIRESTYQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIGAVWPPRGVDPLNPF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   95 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFH 174
Cdd:MTH00052 129 SVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGH 208

                        170
                 ....*....|....
gi 47156708  175 VIIGTIFLVICCIR 188
Cdd:MTH00052 209 VLIGSSFLLVCLFR 222
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 16-190 2.99e-78

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 234.26  E-value: 2.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:MTH00024  49 VIVGVMFVWWQDVIRESTFQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGINPLNPFS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:MTH00024 129 VPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHV 208

                        170
                 ....*....|....*
gi 47156708  176 IIGTIFLVICCIRQY 190
Cdd:MTH00024 209 IIGTTFLFVCLLRLL 223
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 15-189 4.49e-76

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 228.88  E-value: 4.49e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   15 TVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 94
Cdd:MTH00130  48 ILLLLTMYQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPELGGCWPPTGITTLDPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   95 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFH 174
Cdd:MTH00130 128 EVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*
gi 47156708  175 VIIGTIFLVICCIRQ 189
Cdd:MTH00130 208 VIIGSTFLAVCLLRQ 222
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 16-188 7.60e-75

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 225.76  E-value: 7.60e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:MTH00039  48 LLILTSINWWRDVIREATFQGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEIGVSWPPTGINPINPFL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:MTH00039 128 VPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHV 207

                        170
                 ....*....|...
gi 47156708  176 IIGTIFLVICCIR 188
Cdd:MTH00039 208 IIGTTFLAVCLFR 220
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 18-189 2.97e-74

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 224.22  E-value: 2.97e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   18 LYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWDIP 97
Cdd:MTH00099  51 MLTMYQWWRDIIRESTFQGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPELGGCWPPTGITPLNPLEVP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   98 FLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHVII 177
Cdd:MTH00099 131 LLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVII 210

                        170
                 ....*....|..
gi 47156708  178 GTIFLVICCIRQ 189
Cdd:MTH00099 211 GSTFLIVCFLRQ 222
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 15-191 5.10e-73

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 221.16  E-value: 5.10e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   15 TVILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPW 94
Cdd:MTH00075  48 IIMLLTMFQWWRDIVREGTFQGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPELGECWPPTGITPLDPF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   95 DIPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFH 174
Cdd:MTH00075 128 EVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLH 207

                        170
                 ....*....|....*..
gi 47156708  175 VIIGTIFLVICCIRQYM 191
Cdd:MTH00075 208 VIIGSLFLLVCLLRQIN 224
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 16-191 3.84e-72

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 218.89  E-value: 3.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:MTH00219  50 IIVLTMIQWWRDVIRESTFMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIELGSCWPPTGINPLNPFQ 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:MTH00219 130 VPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHV 209

                        170
                 ....*....|....*.
gi 47156708  176 IIGTIFLVICCIRQYM 191
Cdd:MTH00219 210 IIGTIFLFVCFMRGLM 225
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 16-191 1.32e-63

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 196.98  E-value: 1.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:MTH00009  47 IIILTMIQWWRDVIREGTYMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPELGCSWPPTGIEPLNPFS 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:MTH00009 127 VPLLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHV 206

                        170
                 ....*....|....*.
gi 47156708  176 IIGTIFLVICCIRQYM 191
Cdd:MTH00009 207 LIGSSFLFVCLLRTWS 222
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 16-188 1.20e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 190.66  E-value: 1.20e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   16 VILYTMFVWWRDVVREATYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:MTH00028  49 LIIITASAWWRDVIREGTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDPFA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   96 IPFLNTLILLSSGAAVTWAHHAILAGS------------------------------------QRQAIYGLLATVFLAFI 139
Cdd:MTH00028 129 VPLLNTTILLSSGATVTWAHHAIIGTGnpaslekgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGII 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 47156708  140 FTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHVIIGTIFLVICCIR 188
Cdd:MTH00028 209 FTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIR 257
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 16-188 1.53e-49

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 160.89  E-value: 1.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   16 VILYTMFVWWRDVVREAtYLGHHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEAIGPWD 95
Cdd:MTH00083  46 YLLFISFLWGKDISMEG-LSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVNYLG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   96 IPFLNTLILLSSGAAVTWAHHAILAGSQRQAIYgLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHV 175
Cdd:MTH00083 125 VPLLNTIILLSSGVSVTWSHHSLCLSNKSCTNS-LLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHV 203

                        170
                 ....*....|...
gi 47156708  176 IIGTIFLVICCIR 188
Cdd:MTH00083 204 LCGGLFLLFNLLR 216
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 38-190 5.27e-44

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: 144.27  E-value: 5.27e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  38 HTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAvwppkgieAIGPWDIPFLNTLILLSSGAAVTWAHHA 117
Cdd:cd00386   1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47156708 118 ILA--GSQRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHVIIGTIFLVICCIRQY 190
Cdd:cd00386  73 LAArrGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLR 147
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
37-188 7.03e-31

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 111.09  E-value: 7.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  37 HHTKMVQLGLRYGMILFIVSEVMFFVAFFWAFFHSSLAptveiGAVWPPkGIEAIGPWdIPFLNTLILLSSGAAVTWAHH 116
Cdd:COG1845   7 PHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRAS-----APDWPA-GAELLDLP-LPLINTLLLLLSSFTVALAVR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47156708 117 AILAGSQRQAIYGLLATVFLAFIFTAFQGMEY---VEAPFTISDGIYGSTFFLATGFHGFHVIIGTIFLVICCIR 188
Cdd:COG1845  80 AARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYshlIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVR 154
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 98-184 1.23e-08

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: 52.24  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  98 FLNTLILLSSGAAVTWAHHAILAGSQRQAIYGLLATVFLAFIFTAFQGME---YVEAPFTISDGIYGSTFFLATGFHGFH 174
Cdd:cd02863  54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEfhhLIAEGAGPDRSAFLSAFFTLVGTHGLH 133

                        90
                ....*....|
gi 47156708 175 VIIGTIFLVI 184
Cdd:cd02863 134 VTFGLIWILV 143
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 47-186 1.76e-06

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: 46.34  E-value: 1.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708  47 RYGMILFIVSEVMFFVAFFWAFFHSSLAPTVEIGAVWPPKGIEaIGPWDIPF----LNTLILLSSGAAVTWAHHAILAGS 122
Cdd:cd02864  10 KAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVFALR-IGHFNIPLvliaIMTFILITSSGTMAMAVNFGYRGN 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47156708 123 QRQAIYGLLATVFLAFIFTAFQGMEYVEAPFTISDG---------IYGSTFFLATGFHGFHVIIGTIFLVICC 186
Cdd:cd02864  89 RKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVRpwgnpwgaaQFGASFFMITGFHGTHVTIGVIYLIIIA 161
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 52-184 8.32e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 44.52  E-value: 8.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47156708   52 LFIVSEVMFFVaffwaffhsSLAPTVEIGAVWPPKGIEAigPWDIPFLNTLILLSSGAAVTWAHHaiLAGSQRQAIYgLL 131
Cdd:MTH00049  59 LFILSEVIIFG---------SLLVCCLWFDDWSYISLSS--SLEIPFVGCFLLLGSSITVTAYHH--LLGWKYCDLF-LY 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 47156708  132 ATVFLAFIFTAFQGMEYVEAPFTISDGIYGSTFFLATGFHGFHVIIGTIFLVI 184
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLST 177
 
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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