NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|134837404|gb|EBD75716|]
View 

hypothetical protein GOS_9877204, partial [marine metagenome]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10195321)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions; multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 27-122 8.02e-54

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: 164.74  E-value: 8.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYPQG--------EFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIG 98
Cdd:cd13919    4 VEVTAQQWAWTFRYPGGdgklgtddDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREG 83

                         90       100
                 ....*....|....*....|....
gi 134837404  99 KYPIICAELCGPYHGGMRASIIVE 122
Cdd:cd13919   84 EYEVRCAELCGLGHYRMRATVKVV 107
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 27-122 8.02e-54

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: 164.74  E-value: 8.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYPQG--------EFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIG 98
Cdd:cd13919    4 VEVTAQQWAWTFRYPGGdgklgtddDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREG 83

                         90       100
                 ....*....|....*....|....
gi 134837404  99 KYPIICAELCGPYHGGMRASIIVE 122
Cdd:cd13919   84 EYEVRCAELCGLGHYRMRATVKVV 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
27-130 1.89e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 167.70  E-value: 1.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYP-QGEFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICA 105
Cdd:COG1622  115 VEVTGYQWKWLFRYPdQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCA 194

                         90       100
                 ....*....|....*....|....*
gi 134837404 106 ELCGPYHGGMRASIIVEDKSDYERW 130
Cdd:COG1622  195 ELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 27-132 3.63e-37

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: 125.57  E-value: 3.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404   27 IEVSAMQFAFLFNYPQGEFISG-ELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICA 105
Cdd:TIGR02866  93 VKVTGYQWWWDFEYPESGFTTVnELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCA 172

                          90       100
                  ....*....|....*....|....*..
gi 134837404  106 ELCGPYHGGMRASIIVEDKSDYERWFN 132
Cdd:TIGR02866 173 ELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 52-130 6.68e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 63.03  E-value: 6.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE--DKSDYER 129
Cdd:MTH00140 144 LPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFM--PIVVEavPLEDFVK 221


                 .
gi 134837404 130 W 130
Cdd:MTH00140 222 W 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
52-122 5.12e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 58.58  E-value: 5.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134837404   52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE 122
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM--PIVIE 118
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 27-122 8.02e-54

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: 164.74  E-value: 8.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYPQG--------EFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIG 98
Cdd:cd13919    4 VEVTAQQWAWTFRYPGGdgklgtddDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREG 83

                         90       100
                 ....*....|....*....|....
gi 134837404  99 KYPIICAELCGPYHGGMRASIIVE 122
Cdd:cd13919   84 EYEVRCAELCGLGHYRMRATVKVV 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
27-130 1.89e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 167.70  E-value: 1.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYP-QGEFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICA 105
Cdd:COG1622  115 VEVTGYQWKWLFRYPdQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCA 194

                         90       100
                 ....*....|....*....|....*
gi 134837404 106 ELCGPYHGGMRASIIVEDKSDYERW 130
Cdd:COG1622  195 ELCGTGHAGMRFKVVVVSPEEFDAW 219
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 27-121 7.72e-40

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: 128.90  E-value: 7.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYPQGEFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAE 106
Cdd:cd13915    4 IQVTGRQWMWEFTYPNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTE 83

                         90
                 ....*....|....*
gi 134837404 107 LCGPYHGGMRASIIV 121
Cdd:cd13915   84 YCGTGHSGMIGKVRV 98
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 27-132 3.63e-37

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: 125.57  E-value: 3.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404   27 IEVSAMQFAFLFNYPQGEFISG-ELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICA 105
Cdd:TIGR02866  93 VKVTGYQWWWDFEYPESGFTTVnELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCA 172

                          90       100
                  ....*....|....*....|....*..
gi 134837404  106 ELCGPYHGGMRASIIVEDKSDYERWFN 132
Cdd:TIGR02866 173 ELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 27-120 3.98e-30

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: 104.30  E-value: 3.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYPQGEfISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAE 106
Cdd:cd13842    3 VYVTGVQWSWTFIYPNVR-TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICAE 81

                         90
                 ....*....|....
gi 134837404 107 LCGPYHGGMRASII 120
Cdd:cd13842   82 YCGLGHSYMLGKVE 95
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 27-131 1.60e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 104.07  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYPQGEFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAE 106
Cdd:cd13918   35 VEVEGFQFGWQFEYPNGVTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYE 114

                         90       100
                 ....*....|....*....|....*
gi 134837404 107 LCGPYHGGMRASIIVEDKSDYERWF 131
Cdd:cd13918  115 LCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 27-122 2.62e-28

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: 100.00  E-value: 2.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYP---QGEFISG-ELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPI 102
Cdd:cd04213    4 IEVTGHQWWWEFRYPdepGRGIVTAnELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRG 83

                         90       100
                 ....*....|....*....|
gi 134837404 103 ICAELCGPYHGGMRASIIVE 122
Cdd:cd04213   84 QCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 27-130 1.13e-27

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: 98.63  E-value: 1.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYPQGE-FISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICA 105
Cdd:cd13914    3 IEVEAYQWGWEFSYPEANvTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCA 82

                         90       100
                 ....*....|....*....|....*
gi 134837404 106 ELCGPYHGGMRASIIVEDKSDYERW 130
Cdd:cd13914   83 EYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 29-122 7.06e-17

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: 70.68  E-value: 7.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  29 VSAMQFAFLFNypqgefisgELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELC 108
Cdd:cd13913   15 VVAQAFAFNPN---------EIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYC 85

                         90
                 ....*....|....
gi 134837404 109 GPYHGGMRASIIVE 122
Cdd:cd13913   86 GAGHHNMYGKIIVE 99
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 52-130 7.60e-14

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: 63.74  E-value: 7.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVEDKS--DYER 129
Cdd:cd13912   52 VPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFM--PIVVEAVSleDFLS 129


                 .
gi 134837404 130 W 130
Cdd:cd13912  130 W 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 52-130 6.68e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 63.03  E-value: 6.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE--DKSDYER 129
Cdd:MTH00140 144 LPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFM--PIVVEavPLEDFVK 221


                 .
gi 134837404 130 W 130
Cdd:MTH00140 222 W 222
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 27-122 4.06e-12

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: 58.16  E-value: 4.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFlfnypqgefISGELHVPVDQKISIKMESKDVIHAFWI--PEFRI--KQDIIPGQPTILNFTPTKIGKYPI 102
Cdd:cd13916    3 VAVTGHQWYW---------ELSRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTI 73

                         90       100
                 ....*....|....*....|
gi 134837404 103 ICAELCGPYHGGMRASIIVE 122
Cdd:cd13916   74 LCLEYCGLAHHVMMAEFTVV 93
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
52-122 5.12e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 58.58  E-value: 5.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134837404   52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE 122
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM--PIVIE 118
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 64-122 6.46e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 59.97  E-value: 6.46e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 134837404  64 SKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE 122
Cdd:MTH00047 132 SSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM--PIVIE 188
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 52-135 6.83e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 57.56  E-value: 6.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRASIIVEDKSDYERWF 131
Cdd:MTH00008 144 LPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223


                 ....
gi 134837404 132 NQNN 135
Cdd:MTH00008 224 SSFA 227
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 52-122 2.59e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 56.17  E-value: 2.59e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE 122
Cdd:MTH00080 147 LPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFM--PIAVE 215
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 62-122 3.77e-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: 52.76  E-value: 3.77e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134837404  62 MESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRASIIVE 122
Cdd:cd13917   28 LSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIVE 88
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 52-133 7.86e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 54.60  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE--DKSDYER 129
Cdd:MTH00168 144 LPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFM--PIVVEfvPWETFEN 221


                 ....
gi 134837404 130 WFNQ 133
Cdd:MTH00168 222 WVDS 225
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 9-121 1.33e-09

Cupredoxin-like domain; 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.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 51.82  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404    9 IWAGISQSNNNSGLGETAIEVSAMQFaflfnYPQgefisgELHVPVDQKISIKMESKD-VIHAFWIPEFRIKQDIIPGQP 87
Cdd:pfam13473   7 VLFWLSKPAAAADDPTVEITVKDGGF-----SPS------RITVPAGTPVKLEFKNKDkTPAEFESPDLGIEKVLAPGKT 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 134837404   88 TILNFTPTKIGKYPIICaelcgPYHGGMRASIIV 121
Cdd:pfam13473  76 STITIPPLKPGEYDFFC-----DMHMDAKGKLIV 104
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 63-122 2.12e-09

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: 51.08  E-value: 2.12e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  63 ESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRASIIVE 122
Cdd:cd04223   35 QDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIVE 94
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 50-134 6.44e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 52.40  E-value: 6.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  50 LHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE--DKSDY 127
Cdd:MTH00038 142 LVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFM--PIVIEsvPFNTF 219


                 ....*..
gi 134837404 128 ERWFNQN 134
Cdd:MTH00038 220 ENWVSNF 226
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 50-122 1.97e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 50.20  E-value: 1.97e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 134837404  50 LHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE 122
Cdd:PTZ00047  75 LTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFM--PIVVE 145
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 52-130 2.14e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 50.65  E-value: 2.14e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRASIIVEDKSDYERW 130
Cdd:MTH00185 144 VPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 42-119 7.88e-08

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 49.36  E-value: 7.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  42 QGEF----ISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRA 117
Cdd:MTH00023 141 SGDFrlleVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPI 220


                 ..
gi 134837404 118 SI 119
Cdd:MTH00023 221 VI 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 53-130 8.34e-08

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 48.95  E-value: 8.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  53 PVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE--DKSDYERW 130
Cdd:MTH00098 145 PMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFM--PIVLElvPLKYFEKW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 50-130 9.57e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 49.01  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  50 LHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVEDKS--DY 127
Cdd:MTH00051 146 LIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM--PIVIEGVSldKY 223


                 ...
gi 134837404 128 ERW 130
Cdd:MTH00051 224 INW 226
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 27-100 3.01e-07

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: 45.62  E-value: 3.01e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134837404  27 IEVSAMQFAFLFNYP-QGEFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKY 100
Cdd:cd04212    3 IQVVSLDWKWLFIYPeQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTY 77
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 52-122 3.97e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 47.08  E-value: 3.97e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE 122
Cdd:MTH00076 144 VPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFM--PIVVE 212
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 27-130 4.24e-07

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 47.49  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  27 IEVSAMQFAFLFNYP-QGEFISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICA 105
Cdd:PRK10525 129 IEVVSMDWKWFFIYPeQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISA 208

                         90       100
                 ....*....|....*....|....*.
gi 134837404 106 ELCGPYHGGMR-ASIIVEDKSDYERW 130
Cdd:PRK10525 209 SYSGPGFSGMKfKAIATPDRAEFDQW 234
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 46-135 6.10e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 46.94  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  46 ISGELHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRASIIVEDKS 125
Cdd:MTH00027 172 VDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251

                         90
                 ....*....|
gi 134837404 126 DYERWFNQNN 135
Cdd:MTH00027 252 KYIDWIGRED 261
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 52-130 6.54e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 46.63  E-value: 6.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  52 VPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE--DKSDYER 129
Cdd:MTH00129 144 VPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFM--PIVVEavPLEHFEN 221


                 .
gi 134837404 130 W 130
Cdd:MTH00129 222 W 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 54-122 1.01e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 46.06  E-value: 1.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134837404  54 VDQKISIKMESK--------DVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMraSIIVE 122
Cdd:MTH00117 138 VDHRMVIPMESPirilitaeDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFM--PIVVE 212
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
52-122 1.54e-06

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 44.13  E-value: 1.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134837404  52 VPVDQKISIKMESKDV---IHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICaelcgpyhgGM---RASIIVE 122
Cdd:COG4633   54 VKAGIPVRLNFTRKDPsgcAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPFTC---------GMgmyRGTIVVE 121
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 38-122 7.61e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 43.55  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  38 FNYPQGEFISGE---------LHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELC 108
Cdd:MTH00139 121 YMIPTEDLSSGEfrllevdnrLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEIC 200

                         90
                 ....*....|....
gi 134837404 109 GPYHGGMraSIIVE 122
Cdd:MTH00139 201 GANHSFM--PIVVE 212
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 50-135 5.40e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 40.97  E-value: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134837404  50 LHVPVDQKISIKMESKDVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRASIIVEDKSDYER 129
Cdd:MTH00154 142 LVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFIN 221


                 ....*.
gi 134837404 130 WFNQNN 135
Cdd:MTH00154 222 WIKNMS 227
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 66-124 7.32e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 38.42  E-value: 7.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 134837404  66 DVIHAFWIPEFRIKQDIIPGQPTILNFTPTKIGKYPIICAELCGPYHGGMRASIIVEDK 124
Cdd:PRK02888 577 DLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEMRGRMLVEPK 635
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH