ID   ASF1_KLULA              Reviewed;         277 AA.
AC   Q6CN69;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Histone chaperone ASF1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=ASF1; OrderedLocusNames=KLLA0E14938g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99707.1; -; Genomic_DNA.
DR   RefSeq; XP_454620.1; XM_454620.1.
DR   AlphaFoldDB; Q6CN69; -.
DR   SMR; Q6CN69; -.
DR   STRING; 28985.XP_454620.1; -.
DR   EnsemblFungi; CAG99707; CAG99707; KLLA0_E14895g.
DR   GeneID; 2894045; -.
DR   KEGG; kla:KLLA0_E14895g; -.
DR   eggNOG; KOG3265; Eukaryota.
DR   HOGENOM; CLU_060354_0_2_1; -.
DR   InParanoid; Q6CN69; -.
DR   OMA; SCEDNEQ; -.
DR   Proteomes; UP000000598; Chromosome E.
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; IEA:EnsemblFungi.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IEA:EnsemblFungi.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; IEA:EnsemblFungi.
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; Chromatin regulator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..277
FT                   /note="Histone chaperone ASF1"
FT                   /id="PRO_0000284038"
FT   REGION          154..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..204
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..261
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   277 AA;  31534 MW;  3CE6F26370F0BCF6 CRC64;
     MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LEPLKHDLEW KLTYVGSSRS LDHDQELDSI
     LVGPIPVGIN KFKFVADAPS PDLIPASELV SVTVILLSCS YNGKEFVRVG YYVNNEYDLE
     ELRENPPQKV PIDHVVRNIL AEKPRVTRFN IVWDNEGEEE FYPPEQEEPE EEEEEEEDED
     EDEEADEDAE EDLAEEDDVD DGEGEETAPE KKKLKRDPKK STASDVKNDE GESQAESLGP
     EEDEEDEEEA EEIDLEKESD SENDADLPTP QDTTQHK