ID   ASF1_CHAGB              Reviewed;         276 AA.
AC   Q2GQS2;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Histone chaperone ASF1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=ASF1; ORFNames=CHGG_09682;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408035; EAQ83278.1; -; Genomic_DNA.
DR   RefSeq; XP_001227609.1; XM_001227608.1.
DR   AlphaFoldDB; Q2GQS2; -.
DR   SMR; Q2GQS2; -.
DR   STRING; 38033.XP_001227609.1; -.
DR   EnsemblFungi; EAQ83278; EAQ83278; CHGG_09682.
DR   GeneID; 4396440; -.
DR   eggNOG; KOG3265; Eukaryota.
DR   HOGENOM; CLU_060354_0_2_1; -.
DR   InParanoid; Q2GQS2; -.
DR   OMA; AADEMNM; -.
DR   OrthoDB; 1334998at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
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; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..276
FT                   /note="Histone chaperone ASF1"
FT                   /id="PRO_0000284031"
FT   REGION          159..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..259
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  30874 MW;  79D4AD33F8706642 CRC64;
     MSVVSLLGVN VINNPAKFTD KYEFEITFEC LEPLQKDLEW KLTYVGSAQS DNYDQELDSL
     LVGPIPVGIN KFVFEADPPD TKRIPIDELL GVTVILLTCA YDGREFVRVG YYVNNEYESD
     ELRDEPPAKP DVEKIRRNVL ANKPRVTRFA IKWLLPAPNS HPSSPRLTSS LTRTSTAPKS
     LPKRRRPRQS RAHGEESADK DAQMEGVEGP DGEGENVAED DELSDDGSVD IEGESEDELL
     EEYEVVDQEG GEAAEGDEME VDKPEPTVHK QEAMVH