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Conserved domains on  [gi|141620696|gb|ECS58088|]
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hypothetical protein GOS_4150607, 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

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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; ...
 5-102 2.39e-53

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: 162.81  E-value: 2.39e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGN--------FISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTK 76
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDgklgtdddVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTR 81

                         90       100
                 ....*....|....*....|....*.
gi 141620696  77 VGKYPIICAELCGPYHGGMRASIIVE 102
Cdd:cd13919   82 EGEYEVRCAELCGLGHYRMRATVKVV 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; ...
 5-102 2.39e-53

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: 162.81  E-value: 2.39e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGN--------FISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTK 76
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDgklgtdddVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTR 81

                         90       100
                 ....*....|....*....|....*.
gi 141620696  77 VGKYPIICAELCGPYHGGMRASIIVE 102
Cdd:cd13919   82 EGEYEVRCAELCGLGHYRMRATVKVV 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
5-117 2.54e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.93  E-value: 2.54e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGN-FISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPII 83
Cdd:COG1622  113 LTVEVTGYQWKWLFRYPDQGiATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192

                         90       100       110
                 ....*....|....*....|....*....|....
gi 141620696  84 CAELCGPYHGGMRASIIVEEESDYKEWFNKNKKP 117
Cdd:COG1622  193 CAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKAS 226
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-112 2.50e-35

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: 120.18  E-value: 2.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696    3 NNLSIEVSAMQFAFLFNYPKGNFISG-ELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYP 81
Cdd:TIGR02866  89 DALKVKVTGYQWWWDFEYPESGFTTVnELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYY 168

                          90       100       110
                  ....*....|....*....|....*....|.
gi 141620696   82 IICAELCGPYHGGMRASIIVEEESDYKEWFN 112
Cdd:TIGR02866 169 GFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 32-110 5.13e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 62.65  E-value: 5.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE--EESDYKE 109
Cdd:MTH00140 144 LPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFM--PIVVEavPLEDFVK 221


                 .
gi 141620696 110 W 110
Cdd:MTH00140 222 W 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
32-102 1.46e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 59.35  E-value: 1.46e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 141620696   32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
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; ...
 5-102 2.39e-53

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: 162.81  E-value: 2.39e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGN--------FISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTK 76
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDgklgtdddVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTR 81

                         90       100
                 ....*....|....*....|....*.
gi 141620696  77 VGKYPIICAELCGPYHGGMRASIIVE 102
Cdd:cd13919   82 EGEYEVRCAELCGLGHYRMRATVKVV 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
5-117 2.54e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.93  E-value: 2.54e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGN-FISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPII 83
Cdd:COG1622  113 LTVEVTGYQWKWLFRYPDQGiATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192

                         90       100       110
                 ....*....|....*....|....*....|....
gi 141620696  84 CAELCGPYHGGMRASIIVEEESDYKEWFNKNKKP 117
Cdd:COG1622  193 CAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKAS 226
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 5-101 2.67e-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: 129.29  E-value: 2.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGNFISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIIC 84
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFC 81

                         90
                 ....*....|....*..
gi 141620696  85 AELCGPYHGGMRASIIV 101
Cdd:cd13915   82 TEYCGTGHSGMIGKVRV 98
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 3-112 2.50e-35

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: 120.18  E-value: 2.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696    3 NNLSIEVSAMQFAFLFNYPKGNFISG-ELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYP 81
Cdd:TIGR02866  89 DALKVKVTGYQWWWDFEYPESGFTTVnELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYY 168

                          90       100       110
                  ....*....|....*....|....*....|.
gi 141620696   82 IICAELCGPYHGGMRASIIVEEESDYKEWFN 112
Cdd:TIGR02866 169 GFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 5-100 4.24e-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: 103.53  E-value: 4.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGNfISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIIC 84
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR-TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIIC 79

                         90
                 ....*....|....*.
gi 141620696  85 AELCGPYHGGMRASII 100
Cdd:cd13842   80 AEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 5-102 8.90e-30

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: 103.08  E-value: 8.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPK---GNFISG-ELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKY 80
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDepgRGIVTAnELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVY 81

                         90       100
                 ....*....|....*....|..
gi 141620696  81 PIICAELCGPYHGGMRASIIVE 102
Cdd:cd04213   82 RGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 5-111 1.63e-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: 103.30  E-value: 1.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYPKGNFISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIIC 84
Cdd:cd13918   33 LEVEVEGFQFGWQFEYPNGVTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKC 112

                         90       100
                 ....*....|....*....|....*..
gi 141620696  85 AELCGPYHGGMRASIIVEEESDYKEWF 111
Cdd:cd13918  113 YELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 7-110 1.26e-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: 97.48  E-value: 1.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   7 IEVSAMQFAFLFNYPKGN-FISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICA 85
Cdd:cd13914    3 IEVEAYQWGWEFSYPEANvTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCA 82

                         90       100
                 ....*....|....*....|....*
gi 141620696  86 ELCGPYHGGMRASIIVEEESDYKEW 110
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 ...
 24-102 1.41e-16

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: 69.14  E-value: 1.41e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 141620696  24 NFISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVE 102
Cdd:cd13913   21 AFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 32-110 7.14e-15

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: 65.67  E-value: 7.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE--EESDYKE 109
Cdd:cd13912   52 VPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFM--PIVVEavSLEDFLS 129


                 .
gi 141620696 110 W 110
Cdd:cd13912  130 W 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 32-110 5.13e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 62.65  E-value: 5.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE--EESDYKE 109
Cdd:MTH00140 144 LPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFM--PIVVEavPLEDFVK 221


                 .
gi 141620696 110 W 110
Cdd:MTH00140 222 W 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
32-102 1.46e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 59.35  E-value: 1.46e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 141620696   32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM--PIVIE 118
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 44-102 2.65e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 60.35  E-value: 2.65e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 141620696  44 SKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:MTH00047 132 SSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM--PIVIE 188
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 7-102 9.99e-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: 56.62  E-value: 9.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   7 IEVSAMQFAFlfnypkgnfISGELHVPVDQKVSMKMESKDVIHAFWV--PEFRI--KQDIIPGQPTILNFTPTKVGKYPI 82
Cdd:cd13916    3 VAVTGHQWYW---------ELSRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTI 73

                         90       100
                 ....*....|....*....|
gi 141620696  83 ICAELCGPYHGGMRASIIVE 102
Cdd:cd13916   74 LCLEYCGLAHHVMMAEFTVV 93
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 32-115 4.07e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 57.56  E-value: 4.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVEEESDYKEWF 111
Cdd:MTH00008 144 LPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223


                 ....
gi 141620696 112 NKNK 115
Cdd:MTH00008 224 SSFA 227
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 32-110 1.81e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 55.79  E-value: 1.81e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVEEESDYKEW 110
Cdd:MTH00080 147 LPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 42-102 4.44e-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: 52.37  E-value: 4.44e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 141620696  42 MESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVE 102
Cdd:cd13917   28 LSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIVE 88
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 32-102 3.10e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 52.29  E-value: 3.10e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:MTH00168 144 LPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFM--PIVVE 212
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 43-102 1.01e-08

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: 48.77  E-value: 1.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  43 ESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVE 102
Cdd:cd04223   35 QDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIVE 94
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 5-80 1.08e-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: 48.70  E-value: 1.08e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 141620696   5 LSIEVSAMQFAFLFNYPKGNFIS-GELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKY 80
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGIATvNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTY 77
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 33-95 1.15e-08

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 50.87  E-value: 1.15e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 141620696  33 PVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGM 95
Cdd:MTH00098 145 PMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFM 207
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 30-110 2.13e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 50.16  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  30 LHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVEEES--DY 107
Cdd:MTH00051 146 LIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM--PIVIEGVSldKY 223


                 ...
gi 141620696 108 KEW 110
Cdd:MTH00051 224 INW 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 32-102 2.83e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 49.88  E-value: 2.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:MTH00185 144 VPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFM--PIVVE 212
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 30-105 5.28e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 48.28  E-value: 5.28e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 141620696  30 LHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVEEES 105
Cdd:PTZ00047  75 LTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFM--PIVVEAVS 148
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 30-110 6.47e-08

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 48.98  E-value: 6.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  30 LHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVEEESDYKE 109
Cdd:MTH00023 153 LVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIN 232


                 .
gi 141620696 110 W 110
Cdd:MTH00023 233 W 233
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 32-102 7.33e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 48.62  E-value: 7.33e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:MTH00076 144 VPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFM--PIVVE 212
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 26-113 7.95e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 48.87  E-value: 7.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  26 ISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVEEES 105
Cdd:MTH00027 172 VDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251


                 ....*...
gi 141620696 106 DYKEWFNK 113
Cdd:MTH00027 252 KYIDWIGR 259
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 34-102 1.37e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 47.99  E-value: 1.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 141620696  34 VDQKVSMKMESK--------DVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:MTH00117 138 VDHRMVIPMESPirilitaeDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFM--PIVVE 212
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 32-102 3.29e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 47.02  E-value: 3.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:MTH00129 144 VPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFM--PIVVE 212
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 30-102 3.76e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 46.62  E-value: 3.76e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 141620696  30 LHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVE 102
Cdd:MTH00038 142 LVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFM--PIVIE 212
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 5-116 1.16e-06

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 45.56  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696   5 LSIEVSAMQFAFLFNYP-KGNFISGELHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPII 83
Cdd:PRK10525 127 ITIEVVSMDWKWFFIYPeQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGI 206

                         90       100       110
                 ....*....|....*....|....*....|....
gi 141620696  84 CAELCGPYHGGMR-ASIIVEEESDYKEWFNKNKK 116
Cdd:PRK10525 207 SASYSGPGFSGMKfKAIATPDRAEFDQWVAKAKQ 240
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 32-110 4.82e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 43.55  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  32 VPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMraSIIVEEESDYK--E 109
Cdd:MTH00139 144 LPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFM--PIVVEAISPKFflE 221


                 .
gi 141620696 110 W 110
Cdd:MTH00139 222 W 222
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 29-101 6.11e-06

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: 41.80  E-value: 6.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 141620696   29 ELHVPVDQKVSMKMESKD-VIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICaelcgPYHGGMRASIIV 101
Cdd:pfam13473  36 RITVPAGTPVKLEFKNKDkTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC-----DMHMDAKGKLIV 104
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
32-102 6.62e-06

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 42.21  E-value: 6.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 141620696  32 VPVDQKVSMKMESKDV---IHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICaelcgpyhgGM---RASIIVE 102
Cdd:COG4633   54 VKAGIPVRLNFTRKDPsgcAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPFTC---------GMgmyRGTIVVE 121
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 30-114 3.02e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 41.35  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 141620696  30 LHVPVDQKVSMKMESKDVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVEEESDYKE 109
Cdd:MTH00154 142 LVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFIN 221


                 ....*
gi 141620696 110 WFNKN 114
Cdd:MTH00154 222 WIKNM 226
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 46-102 2.02e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 36.49  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 141620696  46 DVIHAFWVPEFRIKQDIIPGQPTILNFTPTKVGKYPIICAELCGPYHGGMRASIIVE 102
Cdd:PRK02888 577 DLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEMRGRMLVE 633
 
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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