ID   CHZ1_PICST              Reviewed;         147 AA.
AC   A3LXX5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Histone H2A.Z-specific chaperone CHZ1;
GN   Name=CHZ1; ORFNames=PICST_32972;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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}.
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DR   EMBL; CP000500; ABN67539.1; -; Genomic_DNA.
DR   RefSeq; XP_001385568.1; XM_001385531.1.
DR   AlphaFoldDB; A3LXX5; -.
DR   STRING; 4924.XP_001385568.1; -.
DR   EnsemblFungi; ABN67539; ABN67539; PICST_32972.
DR   GeneID; 4839849; -.
DR   KEGG; pic:PICST_32972; -.
DR   eggNOG; ENOG502SCUM; Eukaryota.
DR   HOGENOM; CLU_126134_0_0_1; -.
DR   InParanoid; A3LXX5; -.
DR   OMA; RRNYDDY; -.
DR   Proteomes; UP000002258; Chromosome 6.
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   Chaperone; Nucleus; Reference proteome.
FT   CHAIN           1..147
FT                   /note="Histone H2A.Z-specific chaperone CHZ1"
FT                   /id="PRO_0000330219"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..97
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..147
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   147 AA;  17250 MW;  41F0ADE6CFB5CA48 CRC64;
     MSEEKKEAVV EPKAEEVKEK EQIEEKEVEE EEGTNKRTSE EKDKKKHKKR RRRQYDDDVP
     KDSETKEAAE DDEEEEDGEF DENNLENEED VEDDLAEIDT ANIITTGRRT RRKVIDFAKA
     AKELDAENGV VREDDEEEED GEFEVKE