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Conserved domains on  [gi|490286013|ref|WP_004181805|]
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MULTISPECIES: hypothetical protein [Gammaproteobacteria]

Protein Classification

DnaJ-like cysteine-rich domain-containing protein( domain architecture ID 230175)

DnaJ-like cysteine-rich domain-containing protein contains four repeats of a CxxCxGxG motif and binds zinc ions; similar to Arabidopsis thaliana chloroplastic protein ORANGE involved in chromoplast differentiation

Gene Ontology:  GO:0008270
PubMed:  8617216

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ_CXXCXGXG super family cl47586
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 19-44 4.43e-03

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


The actual alignment was detected with superfamily member pfam00684:

Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 34.46  E-value: 4.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 490286013   19 GFMEVRRPCPDCLGSG--IN--CLQCAGSG 44
Cdd:pfam00684  36 GFFQMQSTCPTCGGTGkiIKdpCKKCKGKG 65
 
Name Accession Description Interval E-value
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 19-44 4.43e-03

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 34.46  E-value: 4.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 490286013   19 GFMEVRRPCPDCLGSG--IN--CLQCAGSG 44
Cdd:pfam00684  36 GFFQMQSTCPTCGGTGkiIKdpCKKCKGKG 65
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 19-44 7.50e-03

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 34.15  E-value: 7.50e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 490286013  19 GFMEVRRPCPDCLGSG--IN--CLQCAGSG 44
Cdd:cd10719   36 GFFQTQTTCPTCGGTGkiIKdpCPKCKGKG 65
 
Name Accession Description Interval E-value
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 19-44 4.43e-03

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 34.46  E-value: 4.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 490286013   19 GFMEVRRPCPDCLGSG--IN--CLQCAGSG 44
Cdd:pfam00684  36 GFFQMQSTCPTCGGTGkiIKdpCKKCKGKG 65
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 19-44 7.50e-03

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 34.15  E-value: 7.50e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 490286013  19 GFMEVRRPCPDCLGSG--IN--CLQCAGSG 44
Cdd:cd10719   36 GFFQTQTTCPTCGGTGkiIKdpCPKCKGKG 65
 
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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