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Conserved domains on  [gi|2540861025|ref|WP_297001092|]
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MULTISPECIES: cytochrome o ubiquinol oxidase subunit III [unclassified Thalassospira]

Protein Classification

cytochrome (ubi)quinol oxidase subunit III( domain architecture ID 10120725)

cytochrome (ubi)quinol oxidase subunit III, a component of the four-subunit heme-copper oxidases, cytochrome o ubiquinol oxidase and cytochrome aa3 quinol oxidase, which catalyzes reduction of oxygen to water acting as a proton pump

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 18-203 3.54e-87

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: 254.86  E-value: 3.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  18 EEHHPETGTMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVA 97
Cdd:cd02863     1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  98 GTQLWLAITGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRR 177
Cdd:cd02863    81 KVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160

                         170       180
                  ....*....|....*....|....*.
gi 2540861025 178 LMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:cd02863   161 LFCLSLFWHFLDIVWIFVFTVVYLLG 186
 
Name Accession Description Interval E-value
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 18-203 3.54e-87

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: 254.86  E-value: 3.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  18 EEHHPETGTMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVA 97
Cdd:cd02863     1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  98 GTQLWLAITGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRR 177
Cdd:cd02863    81 KVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160

                         170       180
                  ....*....|....*....|....*.
gi 2540861025 178 LMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:cd02863   161 LFCLSLFWHFLDIVWIFVFTVVYLLG 186
CyoC TIGR02842
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ...
 26-205 1.98e-86

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: 252.56  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  26 TMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAI 105
Cdd:TIGR02842   1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 106 TGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFW 185
Cdd:TIGR02842  81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160

                         170       180
                  ....*....|....*....|
gi 2540861025 186 HFLDVIWIGVFSVVYLLGVL 205
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 18-205 4.17e-80

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 237.76  E-value: 4.17e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  18 EEHHPETGTM--LGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGN 95
Cdd:PRK10663   15 EHGHHDAGATkvFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  96 VAGTQLWLAITGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENK 175
Cdd:PRK10663   95 KSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNR 174

                         170       180       190
                  ....*....|....*....|....*....|
gi 2540861025 176 RRLMCLSMFWHFLDVIWIGVFSVVYLLGVL 205
Cdd:PRK10663  175 TRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
20-202 3.76e-67

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 204.31  E-value: 3.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  20 HHPETGTMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGT 99
Cdd:COG1845    10 PERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 100 QLWLAITGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLM 179
Cdd:COG1845    90 RLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169

                         170       180
                  ....*....|....*....|...
gi 2540861025 180 CLSMFWHFLDVIWIGVFSVVYLL 202
Cdd:COG1845   170 AAALYWHFVDVVWIFLFALVYLL 192
COX3 pfam00510
Cytochrome c oxidase subunit III;
25-204 1.91e-09

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 55.49  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  25 GTMLGFWIYLMSDCLIFAILFATY---------TVLGQNYAAGPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKGN 95
Cdd:pfam00510  75 GLNLGMILFIISEVFFFLGIFWAFfhsalsptvELGAQWPPVGIHPVNPFEVPL--LNTIILLSSGVTVTYAHHSLIEGN 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  96 VAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENK 175
Cdd:pfam00510 153 RKQALQGLILTILLAVYFTGLQAMEY---TEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHH 229

                         170       180
                  ....*....|....*....|....*....
gi 2540861025 176 RRLMCLSMFWHFLDVIWIGVFSVVYLLGV 204
Cdd:pfam00510 230 FGFEAAILYWHFVDVVWLFLYVSVYWWGS 258
 
Name Accession Description Interval E-value
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 18-203 3.54e-87

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: 254.86  E-value: 3.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  18 EEHHPETGTMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVA 97
Cdd:cd02863     1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  98 GTQLWLAITGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRR 177
Cdd:cd02863    81 KVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160

                         170       180
                  ....*....|....*....|....*.
gi 2540861025 178 LMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:cd02863   161 LFCLSLFWHFLDIVWIFVFTVVYLLG 186
CyoC TIGR02842
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ...
 26-205 1.98e-86

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: 252.56  E-value: 1.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  26 TMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAI 105
Cdd:TIGR02842   1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 106 TGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFW 185
Cdd:TIGR02842  81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160

                         170       180
                  ....*....|....*....|
gi 2540861025 186 HFLDVIWIGVFSVVYLLGVL 205
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 18-205 4.17e-80

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 237.76  E-value: 4.17e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  18 EEHHPETGTM--LGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGN 95
Cdd:PRK10663   15 EHGHHDAGATkvFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  96 VAGTQLWLAITGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENK 175
Cdd:PRK10663   95 KSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQVARRGLTSTNR 174

                         170       180       190
                  ....*....|....*....|....*....|
gi 2540861025 176 RRLMCLSMFWHFLDVIWIGVFSVVYLLGVL 205
Cdd:PRK10663  175 TRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
20-202 3.76e-67

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 204.31  E-value: 3.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  20 HHPETGTMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGT 99
Cdd:COG1845    10 PERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRAARRGDRKGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 100 QLWLAITGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLM 179
Cdd:COG1845    90 RLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVE 169

                         170       180
                  ....*....|....*....|...
gi 2540861025 180 CLSMFWHFLDVIWIGVFSVVYLL 202
Cdd:COG1845   170 AAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 27-205 6.10e-47

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: 152.70  E-value: 6.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  27 MLGFWIYLMSDCLIFAILFATYTVL-GQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAI 105
Cdd:TIGR02897  11 ILGFWIFLGAEIALFATLFATYLVLqHGGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMII 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 106 TGLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFW 185
Cdd:TIGR02897  91 TLLLGAGFVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYW 170

                         170       180
                  ....*....|....*....|
gi 2540861025 186 HFLDVIWIGVFSVVYLLGVL 205
Cdd:TIGR02897 171 HFLDVVWVFIFTAVYLIGMV 190
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 25-202 3.38e-46

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: 150.43  E-value: 3.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  25 GTMLGFWIYLMSDCLIFAILFATYTVLGQNYAAGPA-PADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWL 103
Cdd:cd00386     8 GGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGaGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 104 AITGLFGIAFVGLEIYEFHHLwslGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSM 183
Cdd:cd00386    88 LLTILLGLAFLGLQAYEYSHL---IFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHHLGLEAAAL 164

                         170
                  ....*....|....*....
gi 2540861025 184 FWHFLDVIWIGVFSVVYLL 202
Cdd:cd00386   165 YWHFVDVVWLFLFPLVYLW 183
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 28-202 5.69e-25

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: 96.15  E-value: 5.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  28 LGFWIYLMSDCLIFAILFATYTV-LGQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAIT 106
Cdd:cd02862    11 LGMWVFILSELLAFGALFIAYAVyRALYPELFAAGSAHLDLLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 107 GLFGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWH 186
Cdd:cd02862    91 VLLGLVFLVIKYFEYAHKIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWH 170

                         170
                  ....*....|....*.
gi 2540861025 187 FLDVIWIGVFSVVYLL 202
Cdd:cd02862   171 MVDLVWIVLFPLLYLV 186
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 29-202 1.60e-14

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: 68.55  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  29 GFWIYLMSDCLIFAILFATYTVLgQNYAAGPAPADLFDLELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGL 108
Cdd:cd02865    12 GLWVFMAVEGTLFALLISAYFMR-MTSGDWQPGAPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLARLGLALAGA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 109 FGIAFVGLEIYEFHHLWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFL 188
Cdd:cd02865    91 LALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFL 170

                         170
                  ....*....|....
gi 2540861025 189 DVIWIGVFSVVYLL 202
Cdd:cd02865   171 LLVWLVLLALLYGT 184
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 25-200 5.95e-13

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: 65.23  E-value: 5.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  25 GTMLGFWIYLMSDCLIFAILFAT--YTVLGQNYA-------AGPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKGN 95
Cdd:cd01665    62 GLRLGMILFILSEVMFFFSFFWAffHSSLSPSVElggtwppVGIEPLNPFGIPL--LNTIILLSSGATVTWAHHALLLGN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  96 VAGTQLWLAITGLFGIAFVGLEIYEFHHLwslGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENK 175
Cdd:cd01665   140 RKKAILGLILTILLGVYFTGLQAYEYYEA---SFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHH 216

                         170       180
                  ....*....|....*....|....*
gi 2540861025 176 RRLMCLSMFWHFLDVIWIGVFSVVY 200
Cdd:cd01665   217 LGFEAAIWYWHFVDVVWLFLFVFVY 241
COX3 pfam00510
Cytochrome c oxidase subunit III;
25-204 1.91e-09

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 55.49  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  25 GTMLGFWIYLMSDCLIFAILFATY---------TVLGQNYAAGPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKGN 95
Cdd:pfam00510  75 GLNLGMILFIISEVFFFLGIFWAFfhsalsptvELGAQWPPVGIHPVNPFEVPL--LNTIILLSSGVTVTYAHHSLIEGN 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  96 VAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENK 175
Cdd:pfam00510 153 RKQALQGLILTILLAVYFTGLQAMEY---TEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHH 229

                         170       180
                  ....*....|....*....|....*....
gi 2540861025 176 RRLMCLSMFWHFLDVIWIGVFSVVYLLGV 204
Cdd:pfam00510 230 FGFEAAILYWHFVDVVWLFLYVSVYWWGS 258
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 72-203 1.28e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 53.36  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  72 INTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhLWSlGATPMRSGFLSAFYTLVATHGLHV 151
Cdd:MTH00141  130 LNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEY--YEA-SFSIADGVYGSTFFVLTGFHGLHV 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2540861025 152 TFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00141  207 IIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 72-203 9.48e-08

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 50.88  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  72 INTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHV 151
Cdd:MTH00039  131 LNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEY---YDAPFTIADSVYGSTFFVATGFHGLHV 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2540861025 152 TFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00039  208 IIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWG 259
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 103-203 1.13e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 50.84  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 103 LAITGLFGIAFVGLEIYEFHHLwSLGATPmrSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLS 182
Cdd:MTH00028  199 LLMTILLGIIFTGLQAFEYKEA-SFAISD--SVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAI 275

                          90       100
                  ....*....|....*....|.
gi 2540861025 183 MFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00028  276 WYWHFVDVVWLFLYVFVYWWG 296
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 73-200 3.55e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 49.02  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  73 NTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHVT 152
Cdd:MTH00155  131 NTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEY---YEAPFTIADSVYGSTFFMATGFHGLHVI 207

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540861025 153 FGIIWL-VTLMvqvaqrglivenkRRLMCLSM------------FWHFLDVIWIGVFSVVY 200
Cdd:MTH00155  208 IGTTFLlVCLI-------------RHLNNHFSsnhhfgfeaaawYWHFVDVVWLFLYISIY 255
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 24-203 1.58e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 47.44  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  24 TGTMLGFWIYLMSDCLIFAILF--------ATYTVLGQNYAA-GPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKG 94
Cdd:MTH00024   77 QGLKYGMLLFILSEVLFFFSFFwaffhsslAPAVELGVVWPPqGINPLNPFSVPL--LNTAVLLSSGATVTWAHHAIISG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  95 NVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVEN 174
Cdd:MTH00024  155 KRKEAILGLFLTVFLGVLFTGLQAIEY---YEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQ 231

                         170       180
                  ....*....|....*....|....*....
gi 2540861025 175 KRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00024  232 HVGFEAASWYWHFVDVVWLFLYLCIYWWG 260
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 72-203 2.59e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 46.51  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  72 INTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHV 151
Cdd:MTH00189  131 LNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEY---YEAPFTIADSVYGSTFFVATGFHGLHV 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2540861025 152 TFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00189  208 IIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 259
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 58-203 4.11e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 45.94  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  58 GPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFL 137
Cdd:MTH00052  121 GVDPLNPFSVPL--LNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAMEY---YEAPFTISDSVYG 195

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540861025 138 SAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00052  196 STFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 27-202 4.31e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 45.68  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  27 MLGFWIYLMSDCLIFAILFATyTVLGQNYAAGPAPadlFDLELVAINTSMLLFSSITY-GF-AMLAMEKGNvagtqLWLA 104
Cdd:MTH00049   54 ESAFWLFILSEVIIFGSLLVC-CLWFDDWSYISLS---SSLEIPFVGCFLLLGSSITVtAYhHLLGWKYCD-----LFLY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025 105 ITGLFGIAFVGLEIYEFHhlwSLGATPMRSGFLSAFYTLVATHGLHVTFGIIWLVTLMVQvaqrGLIVENKRRLMCLSMF 184
Cdd:MTH00049  125 LTILLGLLFVVLQVFEFE---ESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLLLV----GSSSFGVYRSTVLTWY 197

                         170
                  ....*....|....*...
gi 2540861025 185 WHFLDVIWIGVFSVVYLL 202
Cdd:MTH00049  198 WHFVDYIWLLVYLIVYVC 215
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 58-203 8.03e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 45.33  E-value: 8.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  58 GPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFHHlwslgaTPMR---S 134
Cdd:MTH00118  120 GIKPLNPFEVPL--LNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYYE------APFTisdS 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540861025 135 GFLSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00118  192 VYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 57-203 1.73e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 44.37  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  57 AGPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFHHLwslGATPMRSGF 136
Cdd:MTH00130  119 TGITTLDPFEVPL--LNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEA---PFTIADGVY 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540861025 137 LSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00130  194 GSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 57-203 2.19e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 43.97  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  57 AGPAPADLFDLELvaINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGF 136
Cdd:MTH00075  119 TGITPLDPFEVPL--LNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTLLQAMEY---YEAPFTIADGVY 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540861025 137 LSAFYTLVATHGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00075  194 GSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 67-203 3.20e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 43.56  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  67 LELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFHHLwslGATPMRSGFLSAFYTLVAT 146
Cdd:MTH00099  127 LEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYYEA---PFTISDGIYGSTFFMATGF 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2540861025 147 HGLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00099  204 HGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 72-203 8.95e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 42.13  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  72 INTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHV 151
Cdd:MTH00009  130 LNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEY---IEAPFTIADSVYGSTFFVATGFHGLHV 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2540861025 152 TFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00009  207 LIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWG 258
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 72-203 1.07e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 41.70  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  72 INTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFhhlWSLGATPMRSGFLSAFYTLVATHGLHV 151
Cdd:MTH00219  133 LNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEY---LEASFSISDSVYGTTFFVATGFHGLHV 209

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2540861025 152 TFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:MTH00219  210 IIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 261
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 73-200 1.10e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 41.87  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  73 NTSMLLFS--SITYGFAMLAMekgNVAGTQLWLAITGLFGIAFVGLEIYEFHHL---WSLGAtpmrsgFLSAFYTLVATH 147
Cdd:MTH00083  129 NTIILLSSgvSVTWSHHSLCL---SNKSCTNSLLLTCFLGLYFTSFQLMEYKEAsfsISDSI------YGSIFYLGTGFH 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2540861025 148 GLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVY 200
Cdd:MTH00083  200 GIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVY 252
PLN02194 PLN02194
cytochrome-c oxidase
 68-203 1.40e-04

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 41.57  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540861025  68 ELVAINTSMLLFSSITYGFAMLAMEKGNVAGTQLWLAITGLFGIAFVGLEIYEFHHLwslGATPMRSGFLSAFYTLVATH 147
Cdd:PLN02194  131 EIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQA---PFTISDSIYGSTFFLATGFH 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2540861025 148 GLHVTFGIIWLVTLMVQVAQRGLIVENKRRLMCLSMFWHFLDVIWIGVFSVVYLLG 203
Cdd:PLN02194  208 GFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWG 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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