ID   CHZ1_ASPNC              Reviewed;         122 AA.
AC   A2QPM6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Histone H2A.Z-specific chaperone chz1;
GN   Name=chz1; ORFNames=An07g09970;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(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; AM270155; CAK45126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QPM6; -.
DR   PaxDb; A2QPM6; -.
DR   EnsemblFungi; CAK45126; CAK45126; An07g09970.
DR   VEuPathDB; FungiDB:An07g09970; -.
DR   HOGENOM; CLU_130004_1_1_1; -.
DR   Proteomes; UP000006706; Chromosome 4L.
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..122
FT                   /note="Histone H2A.Z-specific chaperone chz1"
FT                   /id="PRO_0000330201"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..65
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..113
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   122 AA;  13263 MW;  FB26237477A5E6FC CRC64;
     MGDNNQATTG FDPAANAPDA AAWDKGKGKA TDPTQDMRMD DDESDESEAE EMIDDDDDED
     NDTLEPISSD NIISGGRRTR GKTIDFQAAA ESLKDDGMDE DDDEDDDYVG AGDDDEDNKM
     QD