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Conserved domains on  [gi|1431981891|gb|RCL70211|]
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cytochrome oxidase subunit III [Bacteroidetes bacterium]

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 ...
 20-326 6.17e-57

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 cd02864:

Pssm-ID: 444752  Cd Length: 202  Bit Score: 183.09  E-value: 6.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  20 PLNASYGKMMMWFFIVSDALTFSGFIVSYGFARFKYANSWPIADEVFtHVPFVHgQELPMIYVAFMTFVLIMSSVTMVLA 99
Cdd:cd02864     3 PFKVSWGKAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVF-ALRIGH-FNIPLVLIAIMTFILITSSGTMAMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 100 VDAGHKMKKAKVTFYMFLTIIGGIIFVGSQAWEWATFIKGDygavktkggnilqfldaetskrvavddfafdfissrnqh 179
Cdd:cd02864    81 VNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEE--------------------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 180 qgyngiwykdegtlptysveeviagmeaspnivirtqilddkghktiltrqesldilkntgvsvvnGANLIENEYGAPLF 259
Cdd:cd02864   122 ------------------------------------------------------------------GVRPWGNPWGAAQF 135

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 260 ANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:cd02864   136 GASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 20-326 6.17e-57

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: 183.09  E-value: 6.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  20 PLNASYGKMMMWFFIVSDALTFSGFIVSYGFARFKYANSWPIADEVFtHVPFVHgQELPMIYVAFMTFVLIMSSVTMVLA 99
Cdd:cd02864     3 PFKVSWGKAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVF-ALRIGH-FNIPLVLIAIMTFILITSSGTMAMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 100 VDAGHKMKKAKVTFYMFLTIIGGIIFVGSQAWEWATFIKGDygavktkggnilqfldaetskrvavddfafdfissrnqh 179
Cdd:cd02864    81 VNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEE--------------------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 180 qgyngiwykdegtlptysveeviagmeaspnivirtqilddkghktiltrqesldilkntgvsvvnGANLIENEYGAPLF 259
Cdd:cd02864   122 ------------------------------------------------------------------GVRPWGNPWGAAQF 135

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 260 ANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:cd02864   136 GASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
20-326 3.35e-37

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 131.51  E-value: 3.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  20 PLNASYGKMMMWFFIVSDALTFSGFIVSYGFARFKYANsWPIADEVFthvpfvhgqelPMIYVAFMTFVLIMSSVTMVLA 99
Cdd:COG1845    10 PERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPD-WPAGAELL-----------DLPLPLINTLLLLLSSFTVALA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 100 VDAGHKMKKAKVTFYMFLTIIGGIIFVGSQAWEWATFIkgdygavktkggnilqfldaetskrvavddfafdfissrnqh 179
Cdd:COG1845    78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLI------------------------------------------ 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 180 qgyngiwykDEGTLPTYSVeeviagmeaspnivirtqilddkghktiltrqesldilkntgvsvvnganlieneygaplF 259
Cdd:COG1845   116 ---------AEGLTPTSNA------------------------------------------------------------F 126

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 260 ANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKsYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:COG1845   127 GSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPEN-HTGVEAAALYWHFVDVVWIFLFALVYLL 192
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 259-324 4.07e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 53.42  E-value: 4.07e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431981891 259 FANFFFFITGFHGFHVFSG--IVLNIIIFFNVIIGTYEKRKSYEMVekvGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00083  188 YGSIFYLGTGFHGIHVLCGglFLLFNLLRLLKSHFNYNHHLGLEFA---ILYWHFVDVVWLFLFVFVY 252
COX3 pfam00510
Cytochrome c oxidase subunit III;
259-324 2.65e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 45.09  E-value: 2.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 259 FANFFFFITGFHGFHVFSGIVLNIIIFFNVIigTYEKRKSYEM-VEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:pfam00510 190 YGSTFYFATGFHGLHVIIGTAFLAVCFLRLL--KYHLTDNHHFgFEAAILYWHFVDVVWLFLYVSVY 254
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 263-326 2.87e-05

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: 44.08  E-value: 2.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKrKSYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:TIGR02897 125 FFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTP-YTAPKVFIVSLYWHFLDVVWVFIFTAVYLI 187
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 20-326 6.17e-57

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: 183.09  E-value: 6.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  20 PLNASYGKMMMWFFIVSDALTFSGFIVSYGFARFKYANSWPIADEVFtHVPFVHgQELPMIYVAFMTFVLIMSSVTMVLA 99
Cdd:cd02864     3 PFKVSWGKAMMWFFLLSDAFIFSSFLIAYMTARISTTEPWPLPSDVF-ALRIGH-FNIPLVLIAIMTFILITSSGTMAMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 100 VDAGHKMKKAKVTFYMFLTIIGGIIFVGSQAWEWATFIKGDygavktkggnilqfldaetskrvavddfafdfissrnqh 179
Cdd:cd02864    81 VNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEE--------------------------------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 180 qgyngiwykdegtlptysveeviagmeaspnivirtqilddkghktiltrqesldilkntgvsvvnGANLIENEYGAPLF 259
Cdd:cd02864   122 ------------------------------------------------------------------GVRPWGNPWGAAQF 135

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 260 ANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:cd02864   136 GASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQRIGRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
20-326 3.35e-37

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 131.51  E-value: 3.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  20 PLNASYGKMMMWFFIVSDALTFSGFIVSYGFARFKYANsWPIADEVFthvpfvhgqelPMIYVAFMTFVLIMSSVTMVLA 99
Cdd:COG1845    10 PERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPD-WPAGAELL-----------DLPLPLINTLLLLLSSFTVALA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 100 VDAGHKMKKAKVTFYMFLTIIGGIIFVGSQAWEWATFIkgdygavktkggnilqfldaetskrvavddfafdfissrnqh 179
Cdd:COG1845    78 VRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLI------------------------------------------ 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 180 qgyngiwykDEGTLPTYSVeeviagmeaspnivirtqilddkghktiltrqesldilkntgvsvvnganlieneygaplF 259
Cdd:COG1845   116 ---------AEGLTPTSNA------------------------------------------------------------F 126

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 260 ANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKsYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:COG1845   127 GSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPEN-HTGVEAAALYWHFVDVVWIFLFALVYLL 192
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 26-326 2.60e-24

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: 97.27  E-value: 2.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  26 GKMMMWFFIVSDALTFSGFIVSYGFARFKYANSWPIAdevfthvpfVHGQELPMIyvAFMTFVLIMSSVTMVLAVDAGHK 105
Cdd:cd00386     9 GRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAG---------LDPLDLPLL--NTNTLLLSGSSVTWAHASLAARR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 106 MKKAKVTFYMFLTIIGGIIFVGSQAWEWATFIkgdygavktkggnilqfldaetskrvavddfafdfissrnqhqgyngi 185
Cdd:cd00386    78 GNRKKARLWLLLTILLGLAFLGLQAYEYSHLI------------------------------------------------ 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 186 wykdegtlptysveeviAGMEASPnivirtqilddkghktiltrqesldilkntgvsvvnganlieneygaplFANFFFF 265
Cdd:cd00386   110 -----------------FTISDSV-------------------------------------------------FGSTFFL 123

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431981891 266 ITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKsYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:cd00386   124 LTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRH-HLGLEAAALYWHFVDVVWLFLFPLVYLW 183
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 26-326 9.97e-18

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: 79.59  E-value: 9.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  26 GKMMMWFFIVSDALTFSGFIVSYGFARFKYAnswpiadEVFTHVPfvhgQELPMIYVAFMTFVLIMSSVTMVLAVDAGHK 105
Cdd:cd02862     9 GKLGMWVFILSELLAFGALFIAYAVYRALYP-------ELFAAGS----AHLDLLLGALNTLVLLTSSFTVALAVRAARA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 106 MKKAKVTFYMFLTIIGGIIFVGSQAWEWAtfikgdygavktkgGNILQFLDAETSkrvavddfafdfissrnqhqgyngi 185
Cdd:cd02862    78 GRRRRARRWLAAAVLLGLVFLVIKYFEYA--------------HKIAAGIDPDAG------------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 186 wykdegtlptysveeviagmeaspnivirtqilddkghktiltrqesldilkntgvsvvnganlieneygapLFANFFFF 265
Cdd:cd02862   119 ------------------------------------------------------------------------LFFTLYFL 126

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431981891 266 ITGFHGFHVFSGIVLNIIIFFNVIIGTYEkRKSYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:cd02862   127 LTGFHLLHVLIGLGILLWVAWRARRGRYS-ARDYEGVEAAALYWHMVDLVWIVLFPLLYLV 186
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 31-325 5.00e-11

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: 60.72  E-value: 5.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891  31 WFFIVSDALTFSGFIVSYGFARFKYANSwPIADEVFthvpfvhgqELPmiYVAFMTFVLIMSSVTMVLAVDAGHKMKKAK 110
Cdd:cd02863    14 WIYLMSDCILFATLFATYAVLSGNTAGG-PPGHELF---------ELP--LVFIETFLLLLSSFTCGLAMIAMNKNNKKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 111 VTFYMFLTIIGGIIFVGSQAWEWATFIkgdygavktkggnilqfldaetskrvavddfafdfissrnqHQGYNgiwykde 190
Cdd:cd02863    82 VILWLIITFLLGLGFVGMEIYEFHHLI-----------------------------------------AEGAG------- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 191 gtlPTYSVeeviagmeaspnivirtqilddkghktiltrqesldilkntgvsvvnganlieneygaplFANFFFFITGFH 270
Cdd:cd02863   114 ---PDRSA------------------------------------------------------------FLSAFFTLVGTH 130

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1431981891 271 GFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFYL 325
Cdd:cd02863   131 GLHVTFGLIWILVMIIQLKKRGLTPDTARRL-FCLSLFWHFLDIVWIFVFTVVYL 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 262-326 3.34e-09

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 55.45  E-value: 3.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431981891 262 FFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKsYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:cd02865   121 FFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRR-RLPVELCALYWHFLLLVWLVLLALLYGT 184
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 263-324 1.35e-08

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: 54.83  E-value: 1.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIG--TYEKRKSYEMVekvGLYWHFVDLVWVFVFTFFY 324
Cdd:cd01665   181 FFMLTGFHGLHVIIGTIFLTVCLIRLLKGhfSSNHHLGFEAA---IWYWHFVDVVWLFLFVFVY 241
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 259-324 4.07e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 53.42  E-value: 4.07e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431981891 259 FANFFFFITGFHGFHVFSG--IVLNIIIFFNVIIGTYEKRKSYEMVekvGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00083  188 YGSIFYLGTGFHGIHVLCGglFLLFNLLRLLKSHFNYNHHLGLEFA---ILYWHFVDVVWLFLFVFVY 252
PLN02194 PLN02194
cytochrome-c oxidase
 258-324 5.38e-06

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 46.97  E-value: 5.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 258 LFANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKrKSYEMVEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:PLN02194  195 IYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTK-EHHVGFEAAAWYWHFVDVVWLFLFVSIY 260
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 263-324 5.46e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 46.81  E-value: 5.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00141  195 FFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGF-EAAAWYWHFVDVVWLFLYLSIY 255
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 263-324 1.45e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 45.73  E-value: 1.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00189  196 FFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGF-EAAAWYWHFVDVVWLFLYVSIY 256
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 259-324 1.59e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 45.56  E-value: 1.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431981891 259 FANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00155  191 YGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGF-EAAAWYWHFVDVVWLFLYISIY 255
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 263-324 1.97e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 45.51  E-value: 1.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00024  197 FFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGF-EAASWYWHFVDVVWLFLYLCIY 257
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 258-324 2.03e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 45.17  E-value: 2.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 258 LFANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYeKRKSYEMVEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00052  193 VYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQF-TRHHHFGFEAAAWYWHFVDVVWLFLFIFMY 258
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 258-324 2.11e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 45.44  E-value: 2.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 258 LFANFFFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00028  228 VYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGL-EAAIWYWHFVDVVWLFLYVFVY 293
COX3 pfam00510
Cytochrome c oxidase subunit III;
259-324 2.65e-05

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 45.09  E-value: 2.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431981891 259 FANFFFFITGFHGFHVFSGIVLNIIIFFNVIigTYEKRKSYEM-VEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:pfam00510 190 YGSTFYFATGFHGLHVIIGTAFLAVCFLRLL--KYHLTDNHHFgFEAAILYWHFVDVVWLFLYVSVY 254
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 263-326 2.87e-05

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: 44.08  E-value: 2.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKrKSYEMVEKVGLYWHFVDLVWVFVFTFFYLV 326
Cdd:TIGR02897 125 FFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTP-YTAPKVFIVSLYWHFLDVVWVFIFTAVYLI 187
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 249-326 6.71e-05

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 43.23  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431981891 249 LIENEYGA--PLFANFFFFITGFHGFHVFSGIV-LNIIIFFNVIIGTYEKRKSYEMVekVGLYWHFVDLVWVFVFTFFYL 325
Cdd:PRK10663  123 LIVEGMGPdrSGFLSAFFALVGTHGLHVTSGLIwMAVLMVQVARRGLTSTNRTRIMC--LSLFWHFLDVVWICVFTVVYL 200


                  .
gi 1431981891 326 V 326
Cdd:PRK10663  201 M 201
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 263-324 1.84e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 42.47  E-value: 1.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00219  198 FFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGF-EAAAWYWHFVDVVWLFLYVSIY 258
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 263-324 1.93e-04

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 42.41  E-value: 1.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00039  196 FFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGF-EAAAWYWHFVDVVWLFLYVCIY 256
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 263-324 7.43e-04

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 40.48  E-value: 7.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00099  197 FFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGF-EAAAWYWHFVDVVWLFLYVSIY 257
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 263-324 8.59e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 40.52  E-value: 8.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00130  197 FFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGF-EAAAWYWHFVDVVWLFLYISIY 257
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 263-324 1.30e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 39.93  E-value: 1.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431981891 263 FFFITGFHGFHVFSG----IVLNIIIFFNVIIGTYekrksYEMVEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00118  197 FFVATGFHGLHVIIGstflIVCLLRLIKFHFTTNH-----HFGFEAAAWYWHFVDVVWLFLYISIY 257
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 263-324 1.43e-03

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 39.82  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00009  195 FFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGF-EAAAWYWHFVDVVWIFLYLCIY 255
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 263-324 1.48e-03

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 39.73  E-value: 1.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431981891 263 FFFITGFHGFHVFSGIVLNIIIFFNVIIGTYEKRKSYEMvEKVGLYWHFVDLVWVFVFTFFY 324
Cdd:MTH00075  197 FFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGF-EAAAWYWHFVDVVWLFLYVSIY 257
 
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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