ID   ASF1_YARLI              Reviewed;         265 AA.
AC   Q6CI62;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Histone chaperone ASF1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=ASF1; OrderedLocusNames=YALI0A01375g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382127; CAG83569.1; -; Genomic_DNA.
DR   RefSeq; XP_499649.1; XM_499649.1.
DR   AlphaFoldDB; Q6CI62; -.
DR   SMR; Q6CI62; -.
DR   STRING; 4952.CAG83569; -.
DR   EnsemblFungi; CAG83569; CAG83569; YALI0_A01375g.
DR   GeneID; 2906074; -.
DR   KEGG; yli:YALI0A01375g; -.
DR   VEuPathDB; FungiDB:YALI0_A01375g; -.
DR   HOGENOM; CLU_060354_0_2_1; -.
DR   InParanoid; Q6CI62; -.
DR   OMA; SYDEREF; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0070775; C:H3 histone acetyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0010698; F:acetyltransferase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IBA:GO_Central.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR   GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR   GO; GO:0033523; P:histone H2B ubiquitination; IEA:EnsemblFungi.
DR   GO; GO:0097043; P:histone H3-K56 acetylation; IEA:EnsemblFungi.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0006337; P:nucleosome disassembly; IEA:EnsemblFungi.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
DR   GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
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; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..265
FT                   /note="Histone chaperone ASF1"
FT                   /id="PRO_0000284041"
FT   REGION          155..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..254
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  29701 MW;  3DC38201EBBB4D58 CRC64;
     MSIVSLLNID VLNNPAPFGS PYEFQITFEC LEPLKHDLEW KLTYVGSSTS FEHDQELDSL
     LVGPVPVGVN KFVFTADPPT VDLIPASELV SVTVIILSCS YNDREFVRVG YYVNNEYDSE
     ELRLNPPPKV QVDHVVRNIL AEKPRVTRFN IVWDNEGEQG EEFPPEQPDA DLEDDEEEYG
     AGEEEEEVEE EVEGETEADA KEDIEAEGEA EAEGDGDGDG DGEDEDLEEA SDEEMEVVDD
     EVGEESEGED DKEDKDDKDD KKDDK