NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|818608088|gb|KKS57021|]
View 

MAG: hypothetical protein UV20_C0004G0117 [Candidatus Magasanikbacteria bacterium GW2011_GWA2_42_32]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 139548)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions

CATH:  2.60.40.420
Gene Ontology:  GO:0005507|GO:0009055
PubMed:  21258692|35994119
SCOP:  3000886

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG4633 super family cl28220
Plastocyanin domain containing protein [General function prediction only];
30-127 3.40e-13

Plastocyanin domain containing protein [General function prediction only];


The actual alignment was detected with superfamily member COG4633:

Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 61.47  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818608088  30 QSDKKITQSNGLTVVKLSASRmGVYDPKIIKVKVGTKLRIEGDPESLSGSMDTMIVDGYELSKKVEPGDNI-LEFIADKT 108
Cdd:COG4633   24 PKSAKAAVENGVQEVTITVDG-GGYSPSRITVKAGIPVRLNFTRKDPSGCAEEVVFPDLGISQDLPLGKTVtIEFTPLKP 102

                         90
                 ....*....|....*....
gi 818608088 109 GTYKVHCANGMGNGTLIVE 127
Cdd:COG4633  103 GEYPFTCGMGMYRGTIVVE 121
 
Name Accession Description Interval E-value
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
30-127 3.40e-13

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 61.47  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818608088  30 QSDKKITQSNGLTVVKLSASRmGVYDPKIIKVKVGTKLRIEGDPESLSGSMDTMIVDGYELSKKVEPGDNI-LEFIADKT 108
Cdd:COG4633   24 PKSAKAAVENGVQEVTITVDG-GGYSPSRITVKAGIPVRLNFTRKDPSGCAEEVVFPDLGISQDLPLGKTVtIEFTPLKP 102

                         90
                 ....*....|....*....
gi 818608088 109 GTYKVHCANGMGNGTLIVE 127
Cdd:COG4633  103 GEYPFTCGMGMYRGTIVVE 121
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 52-126 1.29e-04

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: 38.33  E-value: 1.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818608088   52 GVYDPKIIKVKVGTKLRIEGDPESLSGSmdTMIVDGYELSKKVEPGDNI-LEFIADKTGTYKVHCA-NGMGNGTLIV 126
Cdd:pfam13473  30 GGFSPSRITVPAGTPVKLEFKNKDKTPA--EFESPDLGIEKVLAPGKTStITIPPLKPGEYDFFCDmHMDAKGKLIV 104
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 54-117 1.80e-03

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: 35.29  E-value: 1.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818608088  54 YDPKIIKVKVGTKLR-----IEGDPESLSGsmdtMIVDGYELSKKVEPGDNI-LEFIADKTGTYKVHCAN 117
Cdd:cd04223   13 FTPDIIEVKEGDEVTvhltnLEQDEDITHG----FAIPGYNVNLSLEPGETAtVTFVADKPGVYPYYCTE 78
 
Name Accession Description Interval E-value
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
30-127 3.40e-13

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 61.47  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818608088  30 QSDKKITQSNGLTVVKLSASRmGVYDPKIIKVKVGTKLRIEGDPESLSGSMDTMIVDGYELSKKVEPGDNI-LEFIADKT 108
Cdd:COG4633   24 PKSAKAAVENGVQEVTITVDG-GGYSPSRITVKAGIPVRLNFTRKDPSGCAEEVVFPDLGISQDLPLGKTVtIEFTPLKP 102

                         90
                 ....*....|....*....
gi 818608088 109 GTYKVHCANGMGNGTLIVE 127
Cdd:COG4633  103 GEYPFTCGMGMYRGTIVVE 121
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 52-126 1.29e-04

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: 38.33  E-value: 1.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818608088   52 GVYDPKIIKVKVGTKLRIEGDPESLSGSmdTMIVDGYELSKKVEPGDNI-LEFIADKTGTYKVHCA-NGMGNGTLIV 126
Cdd:pfam13473  30 GGFSPSRITVPAGTPVKLEFKNKDKTPA--EFESPDLGIEKVLAPGKTStITIPPLKPGEYDFFCDmHMDAKGKLIV 104
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 54-117 1.80e-03

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: 35.29  E-value: 1.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818608088  54 YDPKIIKVKVGTKLR-----IEGDPESLSGsmdtMIVDGYELSKKVEPGDNI-LEFIADKTGTYKVHCAN 117
Cdd:cd04223   13 FTPDIIEVKEGDEVTvhltnLEQDEDITHG----FAIPGYNVNLSLEPGETAtVTFVADKPGVYPYYCTE 78
PetE COG3794
Plastocyanin [Energy production and conversion];
53-127 2.12e-03

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 34.59  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818608088  53 VYDPKIIKVKVGTKLRIE-GDPES---LSGSMDTMIVDgyelSKKVEPGDNIlEFIADKTGTYKVHCAN--GMgNGTLIV 126
Cdd:COG3794    2 AFEPATLTVKPGDTVTWVnTDSVPhnvTSDDGPDGAFD----SGLLAPGETF-SVTFDEPGTYDYYCTPhpWM-VGTIVV 75


                 .
gi 818608088 127 E 127
Cdd:COG3794   76 G 76
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 59-127 4.57e-03

Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 34.49  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818608088  59 IKVKVGTKLRIE---GDPESLSGSMD--TMIVDGYELSKKVEPGDN-ILEFIADKTGTYKVHC---------ANGMgNGT 123
Cdd:cd11020   35 IRVREGDTVELTltnPGTNTMPHSIDfhAATGPGGGEFTTIAPGETkTFSFKALYPGVFMYHCatapvlmhiANGM-YGA 113


                 ....
gi 818608088 124 LIVE 127
Cdd:cd11020  114 IIVE 117
 
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