ID   ASF1_COCIM              Reviewed;         272 AA.
AC   Q1E0W9; J3KCH3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Histone chaperone ASF1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=ASF1; ORFNames=CIMG_03794;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704916; EAS32770.3; -; Genomic_DNA.
DR   RefSeq; XP_001244353.1; XM_001244352.2.
DR   AlphaFoldDB; Q1E0W9; -.
DR   SMR; Q1E0W9; -.
DR   STRING; 246410.Q1E0W9; -.
DR   PRIDE; Q1E0W9; -.
DR   EnsemblFungi; EAS32770; EAS32770; CIMG_03794.
DR   GeneID; 4562957; -.
DR   KEGG; cim:CIMG_03794; -.
DR   VEuPathDB; FungiDB:CIMG_03794; -.
DR   InParanoid; Q1E0W9; -.
DR   OMA; SYDEREF; -.
DR   OrthoDB; 1334998at2759; -.
DR   Proteomes; UP000001261; 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; Coiled coil; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..272
FT                   /note="Histone chaperone ASF1"
FT                   /id="PRO_0000284032"
FT   REGION          152..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          181..206
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        195..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..254
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   272 AA;  30577 MW;  9951ECDA0C54C043 CRC64;
     MSVVSLLGVR VLNNPAAFTA PYEFEITFEC LEQLQKDLEW KLTYVGSATS SEYDQELDSL
     LVGPIPVGVN KFIFEADPPD LKRIPTSEIL GVTVILLTCS YDGREFVRVG YYVNNEYDSE
     ELNKEPPTKP IIERVRRNVL AEKPRVTRFH IKWDTDSDPT EFPPVQPDAD VLEDDGETYG
     AEELELEAAL KRELEELDSQ DADKMDVGEG RDDVDDNESD AGSEDLEGET SGSDDEEEEE
     GFEGEDEDVE MGDDSNPTPD QHQHPNPEVM VH