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Conserved domains on  [gi|1907157518|ref|XP_036020386|]
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CXXC motif containing zinc binding protein isoform X5 [Mus musculus]

Protein Classification

CXXC motif containing zinc binding protein( domain architecture ID 10531319)

CXXC motif containing zinc binding protein binds a Zn2+ ion in a tetrahedral coordination with four thiolate groups from two conserved CxxC motifs

Gene Ontology:  GO:0008270

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CXXC_Zn-b_euk pfam05907
CXXC motif containing zinc binding protein, eukaryotic; This family consists of a number of ...
 3-108 1.12e-49

CXXC motif containing zinc binding protein, eukaryotic; This family consists of a number of eukaryotic proteins including CXXC motif containing zinc binding protein (previously known as UPF0587 protein C1orf123). The crystal structure reveals that the protein binds a Zn2+ ion in a tetrahedral coordination with four Cys residues from two CxxC motifs. CXXC motif containing zinc binding protein was initially identified as an interaction partner for the heavy metal-associated (HMA) domain of CCS (copper chaperone for superoxide dismutase). However, it was shown that only misfolded mutant forms, lacking part of the zinc-binding sites, interact with CCS.


:

Pssm-ID: 461777  Cd Length: 152  Bit Score: 155.37  E-value: 1.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157518   3 MKCGNCGEISEKWQYIRLMDSVALKGGRGSASMVQKCKLCARENSIDILSSTIKAYNAEDNEKFKTIVEFECRGLEPVDF 82
Cdd:pfam05907  27 VKCTSCREEHPKWVYISRFEEVEISGSRGEANFVWKCKFCKRESSATIIPETPKPYTAEDSGKFKPILAFDCRGLEPVEF 106

                          90       100
                  ....*....|....*....|....*.
gi 1907157518  83 QPQAGFAADGvESGTVFSDINLQEKE 108
Cdd:pfam05907 107 SPRGGWIVEG-ASGTKFEDVDLSEGE 131
 
Name Accession Description Interval E-value
CXXC_Zn-b_euk pfam05907
CXXC motif containing zinc binding protein, eukaryotic; This family consists of a number of ...
 3-108 1.12e-49

CXXC motif containing zinc binding protein, eukaryotic; This family consists of a number of eukaryotic proteins including CXXC motif containing zinc binding protein (previously known as UPF0587 protein C1orf123). The crystal structure reveals that the protein binds a Zn2+ ion in a tetrahedral coordination with four Cys residues from two CxxC motifs. CXXC motif containing zinc binding protein was initially identified as an interaction partner for the heavy metal-associated (HMA) domain of CCS (copper chaperone for superoxide dismutase). However, it was shown that only misfolded mutant forms, lacking part of the zinc-binding sites, interact with CCS.


Pssm-ID: 461777  Cd Length: 152  Bit Score: 155.37  E-value: 1.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157518   3 MKCGNCGEISEKWQYIRLMDSVALKGGRGSASMVQKCKLCARENSIDILSSTIKAYNAEDNEKFKTIVEFECRGLEPVDF 82
Cdd:pfam05907  27 VKCTSCREEHPKWVYISRFEEVEISGSRGEANFVWKCKFCKRESSATIIPETPKPYTAEDSGKFKPILAFDCRGLEPVEF 106

                          90       100
                  ....*....|....*....|....*.
gi 1907157518  83 QPQAGFAADGvESGTVFSDINLQEKE 108
Cdd:pfam05907 107 SPRGGWIVEG-ASGTKFEDVDLSEGE 131
 
Name Accession Description Interval E-value
CXXC_Zn-b_euk pfam05907
CXXC motif containing zinc binding protein, eukaryotic; This family consists of a number of ...
 3-108 1.12e-49

CXXC motif containing zinc binding protein, eukaryotic; This family consists of a number of eukaryotic proteins including CXXC motif containing zinc binding protein (previously known as UPF0587 protein C1orf123). The crystal structure reveals that the protein binds a Zn2+ ion in a tetrahedral coordination with four Cys residues from two CxxC motifs. CXXC motif containing zinc binding protein was initially identified as an interaction partner for the heavy metal-associated (HMA) domain of CCS (copper chaperone for superoxide dismutase). However, it was shown that only misfolded mutant forms, lacking part of the zinc-binding sites, interact with CCS.


Pssm-ID: 461777  Cd Length: 152  Bit Score: 155.37  E-value: 1.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157518   3 MKCGNCGEISEKWQYIRLMDSVALKGGRGSASMVQKCKLCARENSIDILSSTIKAYNAEDNEKFKTIVEFECRGLEPVDF 82
Cdd:pfam05907  27 VKCTSCREEHPKWVYISRFEEVEISGSRGEANFVWKCKFCKRESSATIIPETPKPYTAEDSGKFKPILAFDCRGLEPVEF 106

                          90       100
                  ....*....|....*....|....*.
gi 1907157518  83 QPQAGFAADGvESGTVFSDINLQEKE 108
Cdd:pfam05907 107 SPRGGWIVEG-ASGTKFEDVDLSEGE 131
 
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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