ID   ASF1_EMENI              Reviewed;         279 AA.
AC   Q5B3I9; C8V9S6;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Histone chaperone asf1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=asf1; ORFNames=AN4891;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA60969.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000084; EAA60969.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001303; CBF76538.1; -; Genomic_DNA.
DR   RefSeq; XP_662495.1; XM_657403.1.
DR   AlphaFoldDB; Q5B3I9; -.
DR   SMR; Q5B3I9; -.
DR   STRING; 162425.CADANIAP00005511; -.
DR   EnsemblFungi; CBF76538; CBF76538; ANIA_04891.
DR   EnsemblFungi; EAA60969; EAA60969; AN4891.2.
DR   GeneID; 2872691; -.
DR   KEGG; ani:AN4891.2; -.
DR   VEuPathDB; FungiDB:AN4891; -.
DR   eggNOG; KOG3265; Eukaryota.
DR   HOGENOM; CLU_060354_0_2_1; -.
DR   InParanoid; Q5B3I9; -.
DR   OMA; SYDEREF; -.
DR   OrthoDB; 1259909at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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..279
FT                   /note="Histone chaperone asf1"
FT                   /id="PRO_0000284035"
FT   REGION          151..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          182..246
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        168..182
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..258
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  31125 MW;  7764BF8EA648EF93 CRC64;
     MSVVSLLGVK VLNNPAPFTS SYQFEITFEC LEQLQKDLEW KLTYVGSATS SEYDQELDSL
     LVGPIPVGVN KFIFEADPPD LRRIPTSEIL GVTVILLTCS YDGREFVRVG YYVNNEYDSE
     ELTADPPAKP IIERIRRNIL AEKPRVTRFA IKWDTEESAP AEYPPDQPEA DGLDDDGAAY
     GQEEAELEAA LLKELQEAEK NESTKGEDHD MEGADNGEED ISDAESEDIE DESDDDEDEV
     DEEEGNDADE DVEMGDDSEP KDDNANPAAH HSQQEVMVH