ID   CHZ1_CANGA              Reviewed;         148 AA.
AC   Q6FWW0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Histone H2A.Z-specific chaperone CHZ1;
GN   Name=CHZ1; OrderedLocusNames=CAGL0C02475g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380949; CAG58190.1; -; Genomic_DNA.
DR   RefSeq; XP_445284.1; XM_445284.1.
DR   AlphaFoldDB; Q6FWW0; -.
DR   SMR; Q6FWW0; -.
DR   STRING; 5478.XP_445284.1; -.
DR   EnsemblFungi; CAG58190; CAG58190; CAGL0C02475g.
DR   GeneID; 2886809; -.
DR   KEGG; cgr:CAGL0C02475g; -.
DR   CGD; CAL0127340; CAGL0C02475g.
DR   VEuPathDB; FungiDB:CAGL0C02475g; -.
DR   eggNOG; ENOG502SCUM; Eukaryota.
DR   HOGENOM; CLU_126134_1_0_1; -.
DR   InParanoid; Q6FWW0; -.
DR   OMA; RRNYDDY; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
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..148
FT                   /note="Histone H2A.Z-specific chaperone CHZ1"
FT                   /id="PRO_0000330206"
FT   REGION          1..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..91
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..148
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   148 AA;  16232 MW;  81CC12B7625F6373 CRC64;
     MSEEKEVKPV VAENAEVPAK VEKKKRRRRN YDDYDAEVTE SEKKKSKPSE ASGKAGAAAA
     GDSDSESDID DAKLDRLESN EDEEEDDLAE IDTSNIITTG RRTRGKIIDY KKTAKELDAS
     EQKTDSAATE AAPGAADDEE DDDADFKE