ID   CHZ1_YEAS7              Reviewed;         160 AA.
AC   A6ZQX9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Histone H2A.Z-specific chaperone CHZ1;
GN   Name=CHZ1; ORFNames=SCY_1526;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Forms a chaperone-bound H2A.Z-H2B complex that acts as a
CC       source for SWR1 complex-dependent H2A to H2A.Z histone replacement in
CC       chromatin. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterotrimer with H2A.Z-H2B, stabilizing the
CC       association of the histone dimer. Also, with a lower affinity, forms a
CC       heterotrimer with H2A-H2B (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CHZ1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN62999.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000048; EDN62999.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZQX9; -.
DR   BMRB; A6ZQX9; -.
DR   SMR; A6ZQX9; -.
DR   PRIDE; A6ZQX9; -.
DR   EnsemblFungi; EDN62999; EDN62999; SCY_1526.
DR   HOGENOM; CLU_126134_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019098; Histone_chaperone_domain_CHZ.
DR   Pfam; PF09649; CHZ; 1.
DR   SMART; SM01082; CHZ; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chaperone; Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P40019"
FT   CHAIN           2..160
FT                   /note="Histone H2A.Z-specific chaperone CHZ1"
FT                   /id="PRO_0000330222"
FT   REGION          1..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..108
FT                   /note="Important for H2A.Z-H2B binding"
FT   COMPBIAS        1..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..160
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40019"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40019"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40019"
SQ   SEQUENCE   160 AA;  18409 MW;  470A4829A524E78D CRC64;
     MSDEAKEKRE LESQKESSHN KSEKSVEPKP KRRRRRNYDD YDAEVAKEET KAKNGLTKSE
     NNGTVEDSES DMDDAKLDAL MGNEGEEEED DLAEIDTSNI ITSGRRTRGK VIDYKKTAEE
     LDKKEPSTDS KDDVGYGEKE EDEEDEEDEE DEEDDDFKEQ