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Conserved domains on  [gi|490651824|ref|WP_004516818|]
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cytochrome c oxidase subunit II [Haloarcula vallismortis]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11446855)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

CATH:  1.10.287.90|2.60.40.420
EC:  7.1.1.9
Gene Ontology:  GO:0042773|GO:0004129|GO:0005507
SCOP:  4002011|4002191

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
38-243 3.21e-66

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 205.06  E-value: 3.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  38 IWGLNMNLLYVAIPITVLVEGILIYTVWRFR---NQEEALPTQENRRLEVTWTIATAIILLFVGVASYQVMASpyvtAEA 114
Cdd:COG1622   32 IDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHA----LDD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 115 GDQAELQeqdtelITVEAQRYGWTFYYnesswdGEAEVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQ 194
Cdd:COG1622  108 APEDPLT------VEVTGYQWKWLFRY------PDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGR 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490651824 195 YNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWLAEQK 243
Cdd:COG1622  176 VTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQK 224
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
38-243 3.21e-66

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 205.06  E-value: 3.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  38 IWGLNMNLLYVAIPITVLVEGILIYTVWRFR---NQEEALPTQENRRLEVTWTIATAIILLFVGVASYQVMASpyvtAEA 114
Cdd:COG1622   32 IDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHA----LDD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 115 GDQAELQeqdtelITVEAQRYGWTFYYnesswdGEAEVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQ 194
Cdd:COG1622  108 APEDPLT------VEVTGYQWKWLFRY------PDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGR 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490651824 195 YNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWLAEQK 243
Cdd:COG1622  176 VTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQK 224
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-239 7.53e-62

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 189.54  E-value: 7.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEAQRYGWTFYYnesswdGEAEVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGT 207
Cdd:cd13914    3 IEVEAYQWGWEFSY------PEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGE 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490651824 208 YQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWL 239
Cdd:cd13914   77 YQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 45-240 1.20e-60

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 189.90  E-value: 1.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824   45 LLYVAIPITVLVEGILIYTVWRFRNQ-EEALPTQ--ENRRLEVTWTIATAIIllFVGVASYQVMASPYVTaEAGDQAELQ 121
Cdd:TIGR02866  16 VLAVSTLISLLVAALLAYVVWKFRRKgDEEKPSQihGNRRLEYVWTVIPLII--VVGLFAATAKGLLYLE-RPIPKDALK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  122 eqdtelITVEAQRYGWTFYYNESSwdgeaeVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTR 201
Cdd:TIGR02866  93 ------VKVTGYQWWWDFEYPESG------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFN 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490651824  202 ATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWLA 240
Cdd:TIGR02866 161 ADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 78-239 1.27e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 103.09  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  78 ENRRLEVTWTIATAIILLFVGVASYQVMaspYVtaeagdqaeLQEQDTELITVEA---QRYgWTFYY---NESSWD---- 147
Cdd:MTH00140  57 EAQKLETIWTIVPALILVFLALPSLRLL---YL---------LDETNNPLLTVKAighQWY-WSYEYsdfSVIEFDsymv 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 148 GEAEVST------TTD--LKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSG 219
Cdd:MTH00140 124 PENELELgdfrllEVDnrLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGAN 203

                        170       180
                 ....*....|....*....|
gi 490651824 220 HSQMLGTVEVVPQDEYEDWL 239
Cdd:MTH00140 204 HSFMPIVVEAVPLEDFVKWL 223
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
160-230 3.73e-14

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 67.05  E-value: 3.73e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490651824  160 IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVV 230
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
38-243 3.21e-66

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 205.06  E-value: 3.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  38 IWGLNMNLLYVAIPITVLVEGILIYTVWRFR---NQEEALPTQENRRLEVTWTIATAIILLFVGVASYQVMASpyvtAEA 114
Cdd:COG1622   32 IDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHA----LDD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 115 GDQAELQeqdtelITVEAQRYGWTFYYnesswdGEAEVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQ 194
Cdd:COG1622  108 APEDPLT------VEVTGYQWKWLFRY------PDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGR 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490651824 195 YNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWLAEQK 243
Cdd:COG1622  176 VTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQK 224
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-239 7.53e-62

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 189.54  E-value: 7.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEAQRYGWTFYYnesswdGEAEVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGT 207
Cdd:cd13914    3 IEVEAYQWGWEFSY------PEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGE 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490651824 208 YQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWL 239
Cdd:cd13914   77 YQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 45-240 1.20e-60

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 189.90  E-value: 1.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824   45 LLYVAIPITVLVEGILIYTVWRFRNQ-EEALPTQ--ENRRLEVTWTIATAIIllFVGVASYQVMASPYVTaEAGDQAELQ 121
Cdd:TIGR02866  16 VLAVSTLISLLVAALLAYVVWKFRRKgDEEKPSQihGNRRLEYVWTVIPLII--VVGLFAATAKGLLYLE-RPIPKDALK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  122 eqdtelITVEAQRYGWTFYYNESSwdgeaeVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTR 201
Cdd:TIGR02866  93 ------VKVTGYQWWWDFEYPESG------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFN 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490651824  202 ATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWLA 240
Cdd:TIGR02866 161 ADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 128-228 4.64e-38

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 128.57  E-value: 4.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEAQRYGWTFYYNEsswdgeaeVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGT 207
Cdd:cd13842    3 VYVTGVQWSWTFIYPN--------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGT 74

                         90       100
                 ....*....|....*....|.
gi 490651824 208 YQLYCAEYCGSGHSQMLGTVE 228
Cdd:cd13842   75 YTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-239 4.39e-34

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 119.87  E-value: 4.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  90 TAIILLFVGVASYQVMAspYVTaeaGDQAELQEQDTElITVEAQRYGWTFYYnesswdgEAEVSTTTDLKIPANQDVSLR 169
Cdd:cd13918    3 SAIIVISLIVWTYGMLL--YVE---DPPDEADEDALE-VEVEGFQFGWQFEY-------PNGVTTGNTLRVPADTPIALR 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 170 VTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWL 239
Cdd:cd13918   70 VTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-229 6.86e-32

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 112.72  E-value: 6.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEAQRYGWTFYYNesswDGEAEVSTttdLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGT 207
Cdd:cd13915    4 IQVTGRQWMWEFTYP----NGKREINE---LHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGE 76

                         90       100
                 ....*....|....*....|..
gi 490651824 208 YQLYCAEYCGSGHSQMLGTVEV 229
Cdd:cd13915   77 YDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 125-230 4.71e-29

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 105.80  E-value: 4.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 125 TELITVEAQRYGWTFYY-NESSWDGEAEVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRAT 203
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYpGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                         90       100
                 ....*....|....*....|....*..
gi 490651824 204 NTGTYQLYCAEYCGSGHSQMLGTVEVV 230
Cdd:cd13919   81 REGEYEVRCAELCGLGHYRMRATVKVV 107
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 78-239 1.27e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 103.09  E-value: 1.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  78 ENRRLEVTWTIATAIILLFVGVASYQVMaspYVtaeagdqaeLQEQDTELITVEA---QRYgWTFYY---NESSWD---- 147
Cdd:MTH00140  57 EAQKLETIWTIVPALILVFLALPSLRLL---YL---------LDETNNPLLTVKAighQWY-WSYEYsdfSVIEFDsymv 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 148 GEAEVST------TTD--LKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSG 219
Cdd:MTH00140 124 PENELELgdfrllEVDnrLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGAN 203

                        170       180
                 ....*....|....*....|
gi 490651824 220 HSQMLGTVEVVPQDEYEDWL 239
Cdd:MTH00140 204 HSFMPIVVEAVPLEDFVKWL 223
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 125-230 1.32e-24

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 93.84  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 125 TELITVEAQRYGWTFYYNESSWDGeaeVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATN 204
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPGRG---IVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADE 77

                         90       100
                 ....*....|....*....|....*.
gi 490651824 205 TGTYQLYCAEYCGSGHSQMLGTVEVV 230
Cdd:cd04213   78 PGVYRGQCAEFCGASHALMRFKVIAL 103
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 46-241 5.81e-22

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 90.55  E-value: 5.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  46 LYVAIPITVLVEGILIYTVWRFRNQEEALPTQEnrrLEVTWTIATAIILLFVGVASYQVMASpyvtaeagdqaeLQEQDT 125
Cdd:MTH00139  28 MVILIMILSFVGYISLSLMSNKFTSRSLLESQE---VETIWTVLPAFILLFLALPSLRLLYL------------MDEVSD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 126 ELITVEAQRYGWTFYYNESSWD---GEAEVSTTTDLKI--------------PANQDVSLRVTSTDWLHAFHVPGLGLKS 188
Cdd:MTH00139  93 PYLTFKAVGHQWYWSYEYSDFKnlsFDSYMIPTEDLSSgefrllevdnrlvlPYKSNIRALITAADVLHSWTVPSLGVKI 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490651824 189 DAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWLAE 241
Cdd:MTH00139 173 DAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 78-241 4.04e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 88.61  E-value: 4.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  78 ENRRLEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDqaelqeqdtELITVEA---QRYgWTFYYnessWD-GEAEVS 153
Cdd:MTH00038  57 EGQELETIWTIVPAFILIFIALPSLQLL---YLMDEVNN---------PFLTIKAighQWY-WSYEY----TDyNDLEFD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 154 T----TTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEY 215
Cdd:MTH00038 120 SymvpTSDLStglprllevdnrlvLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEI 199

                        170       180
                 ....*....|....*....|....*.
gi 490651824 216 CGSGHSQMLGTVEVVPQDEYEDWLAE 241
Cdd:MTH00038 200 CGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 82-241 9.29e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 87.34  E-value: 9.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  82 LEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQaelqeqDTELITVEAQRYgWTFYYNE-SSWDGEAEVSTTTDLK- 159
Cdd:MTH00168  61 IEFVWTIIPAFILISLALPSLRLL---YLMDEIDKP------DLTIKAVGHQWY-WSYEYTDyNDLEFDSYMVPTQDLSp 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 160 -------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGT 226
Cdd:MTH00168 131 gqfrllevdnrlvLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIV 210

                        170
                 ....*....|....*
gi 490651824 227 VEVVPQDEYEDWLAE 241
Cdd:MTH00168 211 VEFVPWETFENWVDS 225
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 154-230 1.20e-20

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 83.39  E-value: 1.20e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490651824 154 TTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVV 230
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 78-239 1.80e-20

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 87.11  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  78 ENRRLEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAelqeqdtelITVEAQRYGWTFYYNESSWDGE-----AEV 152
Cdd:MTH00023  66 DGTFLEIVWTIIPAVILVFIALPSLKLL---YLMDEVVSPA---------LTIKAIGHQWYWSYEYSDYEGEtlefdSYM 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 153 STTTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGS 218
Cdd:MTH00023 134 VPTSDLNsgdfrllevdnrlvVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGA 213

                        170       180
                 ....*....|....*....|.
gi 490651824 219 GHSQMLGTVEVVPQDEYEDWL 239
Cdd:MTH00023 214 NHSFMPIVIEAVSLDKYINWL 234
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 160-238 6.44e-20

C-terminal domain of Cytochrome c Oxidase subunit II; 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. It 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 82.62  E-value: 6.44e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490651824 160 IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDW 238
Cdd:cd13912   52 VPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 82-243 1.20e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 84.45  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  82 LEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAelqeqdtelITVEAQRYGWTFYYNESSWDGE-----AEVSTTT 156
Cdd:MTH00051  63 IEIIWTLIPAAILIFIAFPSLKLL---YLMDEVIDPA---------LTIKAIGHQWYWSYEYSDYGTDtiefdSYMIPTS 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 157 DLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQ 222
Cdd:MTH00051 131 DLNsgdlrllevdnrliVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSF 210

                        170       180
                 ....*....|....*....|.
gi 490651824 223 MLGTVEVVPQDEYEDWLAEQK 243
Cdd:MTH00051 211 MPIVIEGVSLDKYINWVATQS 231
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 76-240 2.76e-19

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 83.61  E-value: 2.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  76 TQENRRLEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAelqeqdtelITVEAQRYGWTFYYNESSWDG---EAEV 152
Cdd:MTH00098  55 TMDAQEVETIWTILPAIILILIALPSLRIL---YMMDEINNPS---------LTVKTMGHQWYWSYEYTDYEDlsfDSYM 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 153 STTTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGS 218
Cdd:MTH00098 123 IPTSDLKpgelrllevdnrvvLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGS 202

                        170       180
                 ....*....|....*....|..
gi 490651824 219 GHSQMLGTVEVVPQDEYEDWLA 240
Cdd:MTH00098 203 NHSFMPIVLELVPLKYFEKWSA 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 46-238 4.80e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 83.01  E-value: 4.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  46 LYVAIPITVLVEGILIYTVWRFRNQEEALPTQEnrrLEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAelqeqdt 125
Cdd:MTH00185  28 LMIVFLISTLVLYIIVAMVTTKLTNKYILDSQE---IEIVWTILPAIILIMIALPSLRIL---YLMDEINDPH------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 126 elITVEAQRYGWTFYYNESSWDG---EAEVSTTTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKS 188
Cdd:MTH00185  95 --LTIKAMGHQWYWSYEYTDYEQlefDSYMTPTQDLTpgqfrlletdhrmvVPMESPIRVLITAEDVLHSWTVPALGVKM 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490651824 189 DAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDW 238
Cdd:MTH00185 173 DAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 76-240 2.04e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 81.11  E-value: 2.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  76 TQENRRLEVTWTIATAIILLFVGVASYQVMaspYVtaeagdqaeLQEQDTELITVEA---QRYgWTFYY---NESSWDge 149
Cdd:MTH00117  55 TVDAQEVELIWTILPAIVLILLALPSLRIL---YL---------MDEINNPHLTIKAighQWY-WSYEYtdyKDLSFD-- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 150 AEVSTTTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEY 215
Cdd:MTH00117 120 SYMIPTQDLPnghfrllevdhrmvIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEI 199

                        170       180
                 ....*....|....*....|....*
gi 490651824 216 CGSGHSQMLGTVEVVPQDEYEDWLA 240
Cdd:MTH00117 200 CGANHSFMPIVVESVPLKHFENWSS 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 43-239 2.63e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 80.64  E-value: 2.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  43 MNLLyvaIPITVLVEGILIYTVW-----RFRNqeealptqENRRLEVTWTIATAIILLFVGVASYQVMaspYVtaeagdq 117
Cdd:MTH00154  28 MMIL---IMITILVGYMMISLLFnkftnRFLL--------EGQEIEIIWTILPAIILIFIALPSLRLL---YL------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 118 aeLQEQDTELITVEA---QRYgWTFYYNE-----------SSWDGEAE----VSTTTDLKIPANQDVSLRVTSTDWLHAF 179
Cdd:MTH00154  87 --LDEVNNPSITLKTighQWY-WSYEYSDfkniefdsymiPTNELENNgfrlLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 180 HVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWL 239
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 46-238 8.95e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 79.37  E-value: 8.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  46 LYVAIPITVLVEGILIYTVWRFRNQEEALPTQEnrrLEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAelqeqdt 125
Cdd:MTH00129  28 LMIVFLISTLVLYIIVAMVSTKLTNKYILDSQE---IEIIWTVLPAVILILIALPSLRIL---YLMDEINDPH------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 126 elITVEAQRYGWTFYYNESSWDG---EAEVSTTTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKS 188
Cdd:MTH00129  95 --LTIKAMGHQWYWSYEYTDYEDlgfDSYMIPTQDLTpgqfrlleadhrmvVPVESPIRVLVSAEDVLHSWAVPALGVKM 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 490651824 189 DAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDW 238
Cdd:MTH00129 173 DAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 49-239 2.00e-17

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 78.36  E-value: 2.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  49 AIPITVLVEGILIYTVWR-FRNQEEALPTQENRRLEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAelqeqdtel 127
Cdd:MTH00008  27 ALLILTLVLTVVGYAMTSlMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLL---YLMDEVSNPS--------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEA--QRYGWTFYYNE-SSWDGEAEVSTTTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDA 190
Cdd:MTH00008  95 ITLKTigHQWYWSYEYSDfSNLEFDSYMLPTSDLSpgqfrllevdnravLPMQTEIRVLVTAADVIHSWTVPSLGVKVDA 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490651824 191 FPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWL 239
Cdd:MTH00008 175 VPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 76-242 4.27e-16

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 74.82  E-value: 4.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  76 TQENRRLEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAelqeqdtelITVEAQRYGWTFYYNESSWDG---EAEV 152
Cdd:MTH00076  55 TMDAQEIEMVWTIMPAIILIVIALPSLRIL---YLMDEINDPH---------LTVKAIGHQWYWSYEYTDYEDlsfDSYM 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 153 STTTDLK--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGS 218
Cdd:MTH00076 123 IPTQDLTpgqfrllevdnrmvVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGA 202

                        170       180
                 ....*....|....*....|....
gi 490651824 219 GHSQMLGTVEVVPQDEYEDWLAEQ 242
Cdd:MTH00076 203 NHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 78-230 1.28e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 72.68  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  78 ENRRLEVTWTIATAIILLFVgvASYQVMaspYVTAEagdqaeLQEQDTELITVEAQRYGWTF-YYNESSWDgeaevSTTT 156
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVL--CFLNLN---FITSD------LDCFSSETIKVIGHQWYWSYeYSFGGSYD-----SFMT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 157 D--------LKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVE 228
Cdd:MTH00047 109 DdifgvdkpLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188


                 ..
gi 490651824 229 VV 230
Cdd:MTH00047 189 VV 190
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 82-242 2.55e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 73.14  E-value: 2.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  82 LEVTWTIATAIILLFVGVASYQVMaspYVTAEAGDQAELQeqdtelITVEAQRYGWTFYYN---ESSWDGEAEVSTTTDL 158
Cdd:MTH00027  92 IEVIWTLIPAFILILIAFPSLRLL---YIMDECGFSANIT------IKVTGHQWYWSYSYEdygEKNIEFDSYMIPTADL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 159 K--------------IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQML 224
Cdd:MTH00027 163 EfgdlrllevdnrliLPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMP 242

                        170
                 ....*....|....*...
gi 490651824 225 GTVEVVPQDEYEDWLAEQ 242
Cdd:MTH00027 243 IVVESVSLSKYIDWIGRE 260
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
160-230 3.73e-14

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 67.05  E-value: 3.73e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490651824  160 IPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVV 230
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-230 6.06e-13

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 62.78  E-value: 6.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEAQRYGWtfyynesswdgeaEVSTTTdlkIPANQDVSLRVTSTDWLHAFHV--PGLGL--KSDAFPGQYNSLRTRAT 203
Cdd:cd13916    3 VAVTGHQWYW-------------ELSRTE---IPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFD 66

                         90       100
                 ....*....|....*....|....*..
gi 490651824 204 NTGTYQLYCAEYCGSGHSQMLGTVEVV 230
Cdd:cd13916   67 KPGTYTILCLEYCGLAHHVMMAEFTVV 93
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 45-243 1.27e-11

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 63.28  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  45 LLYVAIPITVLVEGIliytVWRFRNQEEALP-----TQENRRLEVTWTIATaIILLFVGVASYQvmaspyvTAEAGDQAE 119
Cdd:PRK10525  51 MLIVVIPAILMAVGF----AWKYRASNKDAKyspnwSHSNKVEAVVWTVPI-LIIIFLAVLTWK-------TTHALEPSK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 120 LQEQDTELITVE--AQRYGWTFYYNESSwdgeaeVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNS 197
Cdd:PRK10525 119 PLAHDEKPITIEvvSMDWKWFFIYPEQG------IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTR 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 490651824 198 LRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVP-QDEYEDWLAEQK 243
Cdd:PRK10525 193 LHLIANEPGTYDGISASYSGPGFSGMKFKAIATPdRAEFDQWVAKAK 239
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 158-235 1.30e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 58.29  E-value: 1.30e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490651824 158 LKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEY 235
Cdd:PTZ00047  75 LTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAY 152
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 30-104 3.44e-10

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 55.42  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824   30 QDSTTDSL--IWGLNMNLLYVAIPITVLVEGILIYTVWRFRNQEEALP---TQENRRLEVTWTIATAIILLFVGVASYQV 104
Cdd:pfam02790  10 QDAASPLMegLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITaryTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 158-230 5.81e-10

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 54.68  E-value: 5.81e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490651824 158 LKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVV 230
Cdd:cd13917   16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIVE 88
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 35-239 6.71e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 57.71  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824  35 DSLIWGLNMnllyvaIPITVLVEGILIYTVWRFRNQEealptQENRRLEVTWTIATAIILLFVGVASYQVMASpyvtaea 114
Cdd:MTH00080  27 CSLLFGEFV------LAFVVFLFLYLISNNFYFKSKK-----IEYQFGELLCSVFPVLILLMQMVPSLSLLYY------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 115 gdqAELQEQDTELiTVEAQRYGWTFYYNESSWD----------------GEAEV-STTTDLKIPANQDVSLRVTSTDWLH 177
Cdd:MTH00080  89 ---YGLMNLDSNL-TVKVTGHQWYWSYEFSDIPglefdsymksldqlrlGEPRLlEVDNRCVLPCDTNIRFCITSSDVIH 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490651824 178 AFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVPQDEYEDWL 239
Cdd:MTH00080 165 SWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 128-223 1.22e-08

The cupredoxin domain of Ubiquinol oxidase subunit II; 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. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 51.39  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEAQRYGWTFYYNESSwdgeaeVSTTTDLKIPANQDVSLRVTSTDWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGT 207
Cdd:cd04212    3 IQVVSLDWKWLFIYPEQG------IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGT 76

                         90
                 ....*....|....*.
gi 490651824 208 YQLYCAEYCGSGHSQM 223
Cdd:cd04212   77 YQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 174-231 6.44e-06

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 43.76  E-value: 6.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490651824 174 DWLHAFHVPGLGLKSDAFPGQYNSLRTRATNTGTYQLYCAEYCGSGHSQMLGTVEVVP 231
Cdd:cd04223   38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIVEP 95
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 128-228 4.51e-05

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 41.83  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490651824 128 ITVEAQRYGWTFYYNEsswdgeAEVSTTTDLKIPANQDVSLRVTSTDW-LHAFHVPGLGLKSDAFPGQYNSLRTR----- 201
Cdd:cd00920    1 ITVTASDWGWSFTYNG------VLLFGPPVLVVPVGDTVRVQFVNKLGeNHSVTIAGFGVPVVAMAGGANPGLVNtlvig 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490651824 202 ----------ATNTGTYQLYCAEYcGSGHSQMLGTVE 228
Cdd:cd00920   75 pgesaevtftTDQAGVYWFYCTIP-GHNHAGMVGTIN 110
 
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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