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Conserved domains on  [gi|183448060|pdb|2K2C|A]
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Chain A, RING finger and CHY zinc finger domain-containing protein 1

Protein Classification

CHY zinc finger protein( domain architecture ID 10527495)

CHY zinc finger protein may bind zinc ions though conserved cysteine and histidine residues; similar to Schizosaccharomyces pombe protein C18H10.09 and protein C3B9.05

Gene Ontology:  GO:0008270
PubMed:  11179890|12665246

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-CHY pfam05495
CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many ...
 20-93 5.52e-22

CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many conserved cysteine and histidine residues. We have named this domain after the N-terminal motif CXHY. This domain can be found in isolation in some proteins, but is also often associated with pfam00097. One of the proteins in this family is a mitochondrial intermembrane space protein called Hot13. This protein is involved in the assembly of small TIM complexes.


:

Pssm-ID: 461665  Cd Length: 75  Bit Score: 82.79  E-value: 5.52e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2K2C_A         20 CEHYDRGCLLKAPCCDKLYTCRLCHDNNED-HQLDRFKVKEVQCINCEKIQHAQQTCEECSTLFGEYYCDICHLF 93
Cdd:pfam05495   1 CKHYHRNCKLRCPCCGKWYPCRLCHDEVEDeHPLDRYAVTEMLCMLCDTEQPVAVLCGNCGVTFAEYFCPICKLY 75
 
Name Accession Description Interval E-value
zf-CHY pfam05495
CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many ...
 20-93 5.52e-22

CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many conserved cysteine and histidine residues. We have named this domain after the N-terminal motif CXHY. This domain can be found in isolation in some proteins, but is also often associated with pfam00097. One of the proteins in this family is a mitochondrial intermembrane space protein called Hot13. This protein is involved in the assembly of small TIM complexes.


Pssm-ID: 461665  Cd Length: 75  Bit Score: 82.79  E-value: 5.52e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2K2C_A         20 CEHYDRGCLLKAPCCDKLYTCRLCHDNNED-HQLDRFKVKEVQCINCEKIQHAQQTCEECSTLFGEYYCDICHLF 93
Cdd:pfam05495   1 CKHYHRNCKLRCPCCGKWYPCRLCHDEVEDeHPLDRYAVTEMLCMLCDTEQPVAVLCGNCGVTFAEYFCPICKLY 75
 
Name Accession Description Interval E-value
zf-CHY pfam05495
CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many ...
 20-93 5.52e-22

CHY zinc finger; This family of domains are likely to bind to zinc ions. They contain many conserved cysteine and histidine residues. We have named this domain after the N-terminal motif CXHY. This domain can be found in isolation in some proteins, but is also often associated with pfam00097. One of the proteins in this family is a mitochondrial intermembrane space protein called Hot13. This protein is involved in the assembly of small TIM complexes.


Pssm-ID: 461665  Cd Length: 75  Bit Score: 82.79  E-value: 5.52e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2K2C_A         20 CEHYDRGCLLKAPCCDKLYTCRLCHDNNED-HQLDRFKVKEVQCINCEKIQHAQQTCEECSTLFGEYYCDICHLF 93
Cdd:pfam05495   1 CKHYHRNCKLRCPCCGKWYPCRLCHDEVEDeHPLDRYAVTEMLCMLCDTEQPVAVLCGNCGVTFAEYFCPICKLY 75
 
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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