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Conserved domains on  [gi|2510393924|ref|NP_001408728|]
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HIRA-interacting protein 3 isoform 4 [Mus musculus]

Protein Classification

histone H2A.Z-specific chaperone CHZ1( domain architecture ID 10660960)

histone H2A.Z-specific chaperone CHZ1 forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CHZ smart01082
Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is ...
 383-419 2.24e-06

Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones.


:

Pssm-ID: 198150  Cd Length: 38  Bit Score: 44.32  E-value: 2.24e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2510393924  383 REEAAEVAALDVANIISSTGRPRRRNA-WNPSGEGTSP 419
Cdd:smart01082   1 REEEDELAEIDTSNIISTGRRTRRKTIdFAKAAEPLQA 38
 
Name Accession Description Interval E-value
CHZ smart01082
Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is ...
 383-419 2.24e-06

Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones.


Pssm-ID: 198150  Cd Length: 38  Bit Score: 44.32  E-value: 2.24e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2510393924  383 REEAAEVAALDVANIISSTGRPRRRNA-WNPSGEGTSP 419
Cdd:smart01082   1 REEEDELAEIDTSNIISTGRRTRRKTIdFAKAAEPLQA 38
CHZ pfam09649
Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is ...
 384-417 1.58e-04

Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteriztic of all histone chaperones.


Pssm-ID: 462846  Cd Length: 34  Bit Score: 38.78  E-value: 1.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2510393924 384 EEAAEVAALDVANIISSTGRPRRRNAWNPSGEGT 417
Cdd:pfam09649   1 EEEDELEEIDPSNIISSGRRTRGKVIDFAKAAEK 34
 
Name Accession Description Interval E-value
CHZ smart01082
Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is ...
 383-419 2.24e-06

Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones.


Pssm-ID: 198150  Cd Length: 38  Bit Score: 44.32  E-value: 2.24e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2510393924  383 REEAAEVAALDVANIISSTGRPRRRNA-WNPSGEGTSP 419
Cdd:smart01082   1 REEEDELAEIDTSNIISTGRRTRRKTIdFAKAAEPLQA 38
CHZ pfam09649
Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is ...
 384-417 1.58e-04

Histone chaperone domain CHZ; This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteriztic of all histone chaperones.


Pssm-ID: 462846  Cd Length: 34  Bit Score: 38.78  E-value: 1.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2510393924 384 EEAAEVAALDVANIISSTGRPRRRNAWNPSGEGT 417
Cdd:pfam09649   1 EEEDELEEIDPSNIISSGRRTRGKVIDFAKAAEK 34
 
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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