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Conserved domains on  [gi|489055131|ref|WP_002965291|]
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MULTISPECIES: cytochrome o ubiquinol oxidase subunit III [Brucella]

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 ...
 15-209 9.39e-98

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 PRK10663:

Pssm-ID: 444752  Cd Length: 204  Bit Score: 282.44  E-value: 9.39e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  15 NDHPAHEDHHDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLS 94
Cdd:PRK10663  10 TAHAHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  95 MYKNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGL 174
Cdd:PRK10663  90 MYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGL 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489055131 175 TERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLGVL 209
Cdd:PRK10663 170 TSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
 
Name Accession Description Interval E-value
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 15-209 9.39e-98

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 282.44  E-value: 9.39e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  15 NDHPAHEDHHDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLS 94
Cdd:PRK10663  10 TAHAHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  95 MYKNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGL 174
Cdd:PRK10663  90 MYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGL 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489055131 175 TERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLGVL 209
Cdd:PRK10663 170 TSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 23-207 4.09e-96

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: 277.58  E-value: 4.09e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  23 HHDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSG 102
Cdd:cd02863    2 HTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 103 VLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRV 182
Cdd:cd02863   82 VILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRL 161

                        170       180
                 ....*....|....*....|....*
gi 489055131 183 MCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:cd02863  162 FCLSLFWHFLDIVWIFVFTVVYLLG 186
CyoC TIGR02842
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ...
 30-209 1.11e-95

cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131889  Cd Length: 180  Bit Score: 276.06  E-value: 1.11e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131   30 TLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGV 109
Cdd:TIGR02842   1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  110 TFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFW 189
Cdd:TIGR02842  81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160

                         170       180
                  ....*....|....*....|
gi 489055131  190 HFLDIIWIGVFTLVYLLGVL 209
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
17-206 8.77e-71

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 213.56  E-value: 8.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  17 HPAHEDHHDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMY 96
Cdd:COG1845    3 DVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRAAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  97 KNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTE 176
Cdd:COG1845   83 RGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTP 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 489055131 177 RNRTRVMCLSLFWHFLDIIWIGVFTLVYLL 206
Cdd:COG1845  163 ENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
COX3 pfam00510
Cytochrome c oxidase subunit III;
33-208 4.75e-12

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 63.20  E-value: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131   33 GFWIYLMSDCILFSGLFATY--AVLAHQFAGG----PTGRELFD-LQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLG 105
Cdd:pfam00510  79 GMILFIISEVFFFLGIFWAFfhSALSPTVELGaqwpPVGIHPVNpFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQ 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  106 WLGVTFLLGAAFLAMEIYEFHH---LIVEGAgpdrssFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRV 182
Cdd:pfam00510 159 GLILTILLAVYFTGLQAMEYTEasfTISDGV------YGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGF 232

                         170       180
                  ....*....|....*....|....*.
gi 489055131  183 MCLSLFWHFLDIIWIGVFTLVYLLGV 208
Cdd:pfam00510 233 EAAILYWHFVDVVWLFLYVSVYWWGS 258
 
Name Accession Description Interval E-value
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 15-209 9.39e-98

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 282.44  E-value: 9.39e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  15 NDHPAHEDHHDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLS 94
Cdd:PRK10663  10 TAHAHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  95 MYKNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGL 174
Cdd:PRK10663  90 MYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGL 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489055131 175 TERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLGVL 209
Cdd:PRK10663 170 TSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 23-207 4.09e-96

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: 277.58  E-value: 4.09e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  23 HHDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSG 102
Cdd:cd02863    2 HTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 103 VLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRV 182
Cdd:cd02863   82 VILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRL 161

                        170       180
                 ....*....|....*....|....*
gi 489055131 183 MCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:cd02863  162 FCLSLFWHFLDIVWIFVFTVVYLLG 186
CyoC TIGR02842
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ...
 30-209 1.11e-95

cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131889  Cd Length: 180  Bit Score: 276.06  E-value: 1.11e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131   30 TLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGV 109
Cdd:TIGR02842   1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  110 TFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFW 189
Cdd:TIGR02842  81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160

                         170       180
                  ....*....|....*....|
gi 489055131  190 HFLDIIWIGVFTLVYLLGVL 209
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
17-206 8.77e-71

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 213.56  E-value: 8.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  17 HPAHEDHHDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMY 96
Cdd:COG1845    3 DVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRAAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  97 KNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTE 176
Cdd:COG1845   83 RGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTP 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 489055131 177 RNRTRVMCLSLFWHFLDIIWIGVFTLVYLL 206
Cdd:COG1845  163 ENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 33-206 1.65e-49

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: 159.29  E-value: 1.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  33 GFWIYLMSDCILFSGLFATYAVLAHQFAGGP-TGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTF 111
Cdd:cd00386   12 GMWLFILSEVMLFGSFFWAYFHSRLSPPVEFgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWLLLTI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 112 LLGAAFLAMEIYEFHHLIvegAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHF 191
Cdd:cd00386   92 LLGLAFLGLQAYEYSHLI---FTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHHLGLEAAALYWHF 168

                        170
                 ....*....|....*
gi 489055131 192 LDIIWIGVFTLVYLL 206
Cdd:cd00386  169 VDVVWLFLFPLVYLW 183
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 27-209 2.93e-49

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 158.87  E-value: 2.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131   27 GSTTLVGFWIYLMSDCILFSGLFATYAVLAHQF-AGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLG 105
Cdd:TIGR02897   7 GRLNILGFWIFLGAEIALFATLFATYLVLQHGGdYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  106 WLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCL 185
Cdd:TIGR02897  87 WMIITLLLGAGFVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIV 166

                         170       180
                  ....*....|....*....|....
gi 489055131  186 SLFWHFLDIIWIGVFTLVYLLGVL 209
Cdd:TIGR02897 167 SLYWHFLDVVWVFIFTAVYLIGMV 190
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 33-206 6.16e-27

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: 101.16  E-value: 6.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  33 GFWIYLMSDCILFSGLFATYAV-LAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTF 111
Cdd:cd02862   12 GMWVFILSELLAFGALFIAYAVyRALYPELFAAGSAHLDLLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAAV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 112 LLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHF 191
Cdd:cd02862   92 LLGLVFLVIKYFEYAHKIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHM 171

                        170
                 ....*....|....*
gi 489055131 192 LDIIWIGVFTLVYLL 206
Cdd:cd02862  172 VDLVWIVLFPLLYLV 186
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 33-205 7.57e-26

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: 99.11  E-value: 7.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  33 GFWIYLMSDCILFSGLFATYAV----------LAHQFAGGPTGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSG 102
Cdd:cd02864   12 MMWFFLLSDAFIFSSFLIAYMTaristtepwpLPSDVFALRIGHFNIPLVLIAIMTFILITSSGTMAMAVNFGYRGNRKA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 103 VLGWLGVTFLLGAAFLAMEIYEFHHLIV-EGAGP-----DRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTE 176
Cdd:cd02864   92 AARLMLATALLGATFVGMQAFEWTKLIVeEGVRPwgnpwGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQR 171

                        170       180       190
                 ....*....|....*....|....*....|
gi 489055131 177 RNRTR-VMCLSLFWHFLDIIWIGVFTLVYL 205
Cdd:cd02864  172 IGRYEiVEIAGLYWHFVDLVWVFIFAFFYL 201
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 24-206 6.25e-20

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: 83.19  E-value: 6.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  24 HDAGSTTLVGFWIYLMSDCILFSGLFATYAVLAHQFAGGPtGRELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGV 103
Cdd:cd02865    3 AGARSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQP-GAPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 104 LGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVM 183
Cdd:cd02865   82 RLGLALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVE 161

                        170       180
                 ....*....|....*....|...
gi 489055131 184 CLSLFWHFLDIIWIGVFTLVYLL 206
Cdd:cd02865  162 LCALYWHFLLLVWLVLLALLYGT 184
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 33-204 7.48e-18

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: 78.71  E-value: 7.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  33 GFWIYLMSDCILFSGLFAT--YAVLAHQFAGG----PTGRELFDLQFV-LVETMLLLVSSLTYGLATLSMYKNNRSGVLG 105
Cdd:cd01665   66 GMILFILSEVMFFFSFFWAffHSSLSPSVELGgtwpPVGIEPLNPFGIpLLNTIILLSSGATVTWAHHALLLGNRKKAIL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 106 WLGVTFLLGAAFLAMEIYEFHHLIVEGAGpdrSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCL 185
Cdd:cd01665  146 GLILTILLGVYFTGLQAYEYYEASFTISD---SVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAA 222

                        170
                 ....*....|....*....
gi 489055131 186 SLFWHFLDIIWIGVFTLVY 204
Cdd:cd01665  223 IWYWHFVDVVWLFLFVFVY 241
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 75-207 9.78e-13

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 64.91  E-value: 9.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  75 LVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFL---AMEIYEFHHLIVEGAgpdrssFLSAFFTLVGTH 151
Cdd:MTH00141 129 LLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTflqAGEYYEASFSIADGV------YGSTFFVLTGFH 202

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489055131 152 GLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00141 203 GLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
COX3 pfam00510
Cytochrome c oxidase subunit III;
33-208 4.75e-12

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 63.20  E-value: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131   33 GFWIYLMSDCILFSGLFATY--AVLAHQFAGG----PTGRELFD-LQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLG 105
Cdd:pfam00510  79 GMILFIISEVFFFLGIFWAFfhSALSPTVELGaqwpPVGIHPVNpFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQ 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  106 WLGVTFLLGAAFLAMEIYEFHH---LIVEGAgpdrssFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRV 182
Cdd:pfam00510 159 GLILTILLAVYFTGLQAMEYTEasfTISDGV------YGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGF 232

                         170       180
                  ....*....|....*....|....*.
gi 489055131  183 MCLSLFWHFLDIIWIGVFTLVYLLGV 208
Cdd:pfam00510 233 EAAILYWHFVDVVWLFLYVSVYWWGS 258
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 94-207 3.02e-09

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 55.46  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  94 SMYKNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHlivEGAGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDG 173
Cdd:MTH00028 186 FLLSDFRTNAVIGLLMTILLGIIFTGLQAFEYKE---ASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQ 262

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489055131 174 LTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00028 263 FTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 32-206 2.46e-08

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 52.23  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  32 VGFWIYLMSDCILFSGLFAT--------YAVLAHQFaggptgrelfdlQFVLVETMLLLVSSLTyglatLSMYKNNRSGV 103
Cdd:MTH00049  55 SAFWLFILSEVIIFGSLLVCclwfddwsYISLSSSL------------EIPFVGCFLLLGSSIT-----VTAYHHLLGWK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 104 LGW--LGVTFLLGAAFLAMEIYEFHHLIVEGAgpdRSSFLSAFFTLVGTHGLHITSGLIWILvlsaMLLRDGLTERNRTR 181
Cdd:MTH00049 118 YCDlfLYLTILLGLLFVVLQVFEFEESGVNSL---DSSYYASCFCTVGLHFSHVVLGVVGLS----TLLLVGSSSFGVYR 190

                        170       180
                 ....*....|....*....|....*
gi 489055131 182 VMCLSLFWHFLDIIWIGVFTLVYLL 206
Cdd:MTH00049 191 STVLTWYWHFVDYIWLLVYLIVYVC 215
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 33-204 3.67e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 51.88  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  33 GFWIYLMSDCILFSGLFATY----AVLAHQFAG--GPTGRELFD-LQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLg 105
Cdd:MTH00083  78 GMILFIFSEFMFFFSIFWTFfdaaLVPVHELGGvwSPIGIHLVNyLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTN- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 106 WLGVTFLLGAAFLAMEIYEFHHLIVegaGPDRSSFLSAFFTLVGTHGLHITSGLIWILVLsamLLRDGLTERNRTRVMCL 185
Cdd:MTH00083 157 SLLLTCFLGLYFTSFQLMEYKEASF---SISDSIYGSIFYLGTGFHGIHVLCGGLFLLFN---LLRLLKSHFNYNHHLGL 230

                        170       180
                 ....*....|....*....|..
gi 489055131 186 ---SLFWHFLDIIWIGVFTLVY 204
Cdd:MTH00083 231 efaILYWHFVDVVWLFLFVFVY 252
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 63-207 5.08e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 51.51  E-value: 5.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  63 PTGRELFD-LQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFL---AMEIYEFHHLIVEGAgpdrs 138
Cdd:MTH00189 117 PTGIEPLNpFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTllqAMEYYEAPFTIADSV----- 191

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055131 139 sFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00189 192 -YGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 259
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 75-207 5.98e-08

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 51.27  E-value: 5.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  75 LVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGpdrSSFLSAFFTLVGTHGLH 154
Cdd:MTH00039 130 LLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIAD---SVYGSTFFVATGFHGLH 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489055131 155 ITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00039 207 VIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWG 259
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 63-204 7.90e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 50.95  E-value: 7.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  63 PTGRELFD-LQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHL---IVEgagpdrS 138
Cdd:MTH00155 116 PKGIIPFNpFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEApftIAD------S 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 139 SFLSAFFTLVGTHGLHITSGLIWILVlsaMLLRdglternrtrvMCLSLF--------------WHFLDIIWIGVFTLVY 204
Cdd:MTH00155 190 VYGSTFFMATGFHGLHVIIGTTFLLV---CLIR-----------HLNNHFssnhhfgfeaaawyWHFVDVVWLFLYISIY 255
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 33-207 7.91e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 51.28  E-value: 7.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  33 GFWIYLMSDCILFSGLFATY--AVLAHQFAGG----PTGRELFD-LQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLG 105
Cdd:MTH00075  82 GMILFITSEVFFFLGFFWAFynSSLAPTPELGecwpPTGITPLDpFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQ 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 106 WLGVTFLLGAAFL---AMEIYEFHHLIVEGAgpdrssFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRV 182
Cdd:MTH00075 162 SLALTIILGLYFTllqAMEYYEAPFTIADGV------YGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGF 235

                        170       180
                 ....*....|....*....|....*
gi 489055131 183 MCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00075 236 EAAAWYWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 75-207 1.36e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 50.56  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  75 LVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFL---AMEIYEFHHLIVEgagpdrSSFLSAFFTLVGTH 151
Cdd:MTH00052 132 LLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTglqAMEYYEAPFTISD------SVYGSTFFVTTGAH 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489055131 152 GLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00052 206 GGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 75-207 3.15e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 49.18  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  75 LVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFLA---MEIYEFHHLIVEGAgpdrssFLSAFFTLVGTH 151
Cdd:MTH00118 131 LLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTAlqaMEYYEAPFTISDSV------YGSTFFVATGFH 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489055131 152 GLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00118 205 GLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 33-207 3.97e-07

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 48.95  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  33 GFWIYLMSDCILFSGLFATY--AVLA--HQFAG--GPTG-RELFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLG 105
Cdd:MTH00099  82 GMILFIISEVFFFAGFFWAFyhSSLAptPELGGcwPPTGiTPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQ 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 106 WLGVTFLLGAAFL---AMEIYEFHHLIVEGAgpdrssFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRV 182
Cdd:MTH00099 162 ALFITILLGLYFTllqASEYYEAPFTISDGI------YGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGF 235

                        170       180
                 ....*....|....*....|....*
gi 489055131 183 MCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00099 236 EAAAWYWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 75-207 5.59e-07

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 48.60  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  75 LVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFL---AMEIYEFHHLIVEgagpdrSSFLSAFFTLVGTH 151
Cdd:MTH00024 131 LLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTglqAIEYYEAPFAISD------SVYGSTFFVATGFH 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489055131 152 GLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00024 205 GLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWG 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 63-207 6.64e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 48.61  E-value: 6.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  63 PTGRELFD-LQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFL---AMEIYEFHHLIVEGAgpdrs 138
Cdd:MTH00130 118 PTGITTLDpFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTflqAMEYYEAPFTIADGV----- 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055131 139 sFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00130 193 -YGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 63-207 6.37e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 45.55  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  63 PTGRE-LFDLQFVLVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFL---AMEIYEFHHLIVEgagpdrS 138
Cdd:MTH00219 119 PTGINpLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTmlqGMEYLEASFSISD------S 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055131 139 SFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00219 193 VYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 75-207 2.26e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 44.06  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131  75 LVETMLLLVSSLTYGLATLSMYKNNRSGVLGWLGVTFLLGAAFLAMEIYEFHHLIVEGAGpdrSSFLSAFFTLVGTHGLH 154
Cdd:MTH00009 129 LLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIAD---SVYGSTFFVATGFHGLH 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489055131 155 ITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHFLDIIWIGVFTLVYLLG 207
Cdd:MTH00009 206 VLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWG 258
PLN02194 PLN02194
cytochrome-c oxidase
 112-207 3.29e-04

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 40.42  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055131 112 LLGAAFLAMEIYEFHHLIVEgagpdrSSFLSAFFTLVGTHGLHITSGLIWILVLSAMLLRDGLTERNRTRVMCLSLFWHF 191
Cdd:PLN02194 174 LVFTGFQGMEYYQAPFTISD------SIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHF 247

                         90
                 ....*....|....*.
gi 489055131 192 LDIIWIGVFTLVYLLG 207
Cdd:PLN02194 248 VDVVWLFLFVSIYWWG 263
 
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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