ID   CHZ1_VANPO              Reviewed;         144 AA.
AC   A7TR90;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Histone H2A.Z-specific chaperone CHZ1;
GN   Name=CHZ1; ORFNames=Kpol_423p13;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480472; EDO15223.1; -; Genomic_DNA.
DR   RefSeq; XP_001643081.1; XM_001643031.1.
DR   AlphaFoldDB; A7TR90; -.
DR   SMR; A7TR90; -.
DR   STRING; 436907.A7TR90; -.
DR   EnsemblFungi; EDO15223; EDO15223; Kpol_423p13.
DR   GeneID; 5543288; -.
DR   KEGG; vpo:Kpol_423p13; -.
DR   eggNOG; ENOG502SCUM; Eukaryota.
DR   HOGENOM; CLU_126134_1_0_1; -.
DR   InParanoid; A7TR90; -.
DR   OMA; RRNYDDY; -.
DR   OrthoDB; 1639357at2759; -.
DR   PhylomeDB; A7TR90; -.
DR   Proteomes; UP000000267; 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   Chaperone; Nucleus; Reference proteome.
FT   CHAIN           1..144
FT                   /note="Histone H2A.Z-specific chaperone CHZ1"
FT                   /id="PRO_0000330221"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  16425 MW;  EBF0D9BBDA032C18 CRC64;
     MAEELKEKRE LEVEEDNTKK DNSDKKSKVK RRRRNYDDLD AEVTKDEKSR KTKSGKSGKN
     GSDSESEVDD AKLDTMISLE DEQEDDLAEI DTSNIIVTGR RTRGKIIDYK KAAEELAAEG
     KISLDEDEDE DDEDAKEDDG EFDE