ID   ASF1_DEBHA              Reviewed;         264 AA.
AC   Q6BYE5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Histone chaperone ASF1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=ASF1; OrderedLocusNames=DEHA2A10186g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: Histone chaperone that facilitates histone deposition and
CC       histone exchange and removal during nucleosome assembly and
CC       disassembly. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with histone H3 and histone H4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR   EMBL; CR382133; CAG84737.1; -; Genomic_DNA.
DR   RefSeq; XP_456774.1; XM_456774.1.
DR   AlphaFoldDB; Q6BYE5; -.
DR   SMR; Q6BYE5; -.
DR   STRING; 4959.XP_456774.1; -.
DR   EnsemblFungi; CAG84737; CAG84737; DEHA2A10186g.
DR   GeneID; 2899597; -.
DR   KEGG; dha:DEHA2A10186g; -.
DR   VEuPathDB; FungiDB:DEHA2A10186g; -.
DR   eggNOG; KOG3265; Eukaryota.
DR   HOGENOM; CLU_060354_0_2_1; -.
DR   InParanoid; Q6BYE5; -.
DR   OMA; SYDEREF; -.
DR   OrthoDB; 1334998at2759; -.
DR   Proteomes; UP000000599; Chromosome A.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0006337; P:nucleosome disassembly; IEA:InterPro.
DR   Gene3D; 2.60.40.1490; -; 1.
DR   InterPro; IPR006818; ASF1-like.
DR   InterPro; IPR036747; ASF1-like_sf.
DR   InterPro; IPR017282; Hist_deposition_Asf1.
DR   PANTHER; PTHR12040; PTHR12040; 1.
DR   Pfam; PF04729; ASF1_hist_chap; 1.
DR   PIRSF; PIRSF037759; Histone_Asf1; 1.
DR   SUPFAM; SSF101546; SSF101546; 1.
PE   3: Inferred from homology;
KW   Chaperone; Chromatin regulator; Coiled coil; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..264
FT                   /note="Histone chaperone ASF1"
FT                   /id="PRO_0000284034"
FT   REGION          152..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          165..198
FT                   /evidence="ECO:0000255"
FT   COILED          231..251
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        159..211
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..251
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   264 AA;  30193 MW;  3219B3A35B40A578 CRC64;
     MSIVSLLGIE VLNNPAKFTD PYEFEITFEC LEPLKEDLEW KLTYVGSSRS LDHDQELDSI
     LVGPVPVGIN KFLFQADPPS PELIPASELV SVTVILLSCS YADREFVRVG YYVNNEYDSE
     ELRENPPAKV QVEHVVRNIL AEKPRVTRFN IVWDNEDGNA DEYPPEQQVD EEEEEEEEEE
     EEEDDEEEEE EKDVEGEEGE EGEDAEEAAE VEENGSKEAS KEEDIEEDIE EDIEEDIEED
     IEIEDEEEAK NADQGETPID KVQS