ID   CHZ1_SCLS1              Reviewed;         121 AA.
AC   A7ER98;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Histone H2A.Z-specific chaperone chz1;
GN   Name=chz1; ORFNames=SS1G_07852;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476630; EDN91990.1; -; Genomic_DNA.
DR   RefSeq; XP_001591226.1; XM_001591176.1.
DR   AlphaFoldDB; A7ER98; -.
DR   GeneID; 5487620; -.
DR   KEGG; ssl:SS1G_07852; -.
DR   InParanoid; A7ER98; -.
DR   OMA; HYLTTYI; -.
DR   Proteomes; UP000001312; 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..121
FT                   /note="Histone H2A.Z-specific chaperone chz1"
FT                   /id="PRO_0000330220"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..121
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   121 AA;  13081 MW;  9E5D253F0C4E7F4C CRC64;
     MSAQTGSTNV SADKGKGKSV AEPQDVTMGE GEDSSSEDDV RSQGLKTAAR EHYLTTYIAE
     EVEEEASDNE IDKSNIIQGR RTRGKKIDFA AAAKDLPAED DEDEDDDFQS EGEDDDEMGG
     N