NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|162312271|ref|NP_001018829|]
View 

protein ess1 [Schizosaccharomyces pombe]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 6-154 5.07e-65

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: 195.43  E-value: 5.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312271    6 LNLNAELTGVKNLAPKDEESFYYAFKVQCSGCREIHDNAIEISRSETHSIPGSKGEANLIWTCKNCRKTCSFVIE-GPFS 84
Cdd:pfam05907   1 LQIKAELENVTSLQPADTPPFEYTFKVKCTSCREEHPKWVYISRFEEVEISGSRGEANFVWKCKFCKRESSATIIpETPK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312271   85 PYN--DSQETKKVLVLECRGCELVEFIPQGEWIANGAeSNTLFDEIVLED-DWYDYDENASSEVSITNLEWSI 154
Cdd:pfam05907  81 PYTaeDSGKFKPILAFDCRGLEPVEFSPRGGWIVEGA-SGTKFEDVDLSEgEWYDYDEKAGEEVSITELEWEF 152
 
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 ...
 6-154 5.07e-65

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: 195.43  E-value: 5.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312271    6 LNLNAELTGVKNLAPKDEESFYYAFKVQCSGCREIHDNAIEISRSETHSIPGSKGEANLIWTCKNCRKTCSFVIE-GPFS 84
Cdd:pfam05907   1 LQIKAELENVTSLQPADTPPFEYTFKVKCTSCREEHPKWVYISRFEEVEISGSRGEANFVWKCKFCKRESSATIIpETPK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312271   85 PYN--DSQETKKVLVLECRGCELVEFIPQGEWIANGAeSNTLFDEIVLED-DWYDYDENASSEVSITNLEWSI 154
Cdd:pfam05907  81 PYTaeDSGKFKPILAFDCRGLEPVEFSPRGGWIVEGA-SGTKFEDVDLSEgEWYDYDEKAGEEVSITELEWEF 152
 
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 ...
 6-154 5.07e-65

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: 195.43  E-value: 5.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312271    6 LNLNAELTGVKNLAPKDEESFYYAFKVQCSGCREIHDNAIEISRSETHSIPGSKGEANLIWTCKNCRKTCSFVIE-GPFS 84
Cdd:pfam05907   1 LQIKAELENVTSLQPADTPPFEYTFKVKCTSCREEHPKWVYISRFEEVEISGSRGEANFVWKCKFCKRESSATIIpETPK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312271   85 PYN--DSQETKKVLVLECRGCELVEFIPQGEWIANGAeSNTLFDEIVLED-DWYDYDENASSEVSITNLEWSI 154
Cdd:pfam05907  81 PYTaeDSGKFKPILAFDCRGLEPVEFSPRGGWIVEGA-SGTKFEDVDLSEgEWYDYDEKAGEEVSITELEWEF 152
 
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