ID   ASF1_ASPOR              Reviewed;         285 AA.
AC   Q2UKV7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Histone chaperone asf1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=asf1; ORFNames=AO090003000656;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007155; BAE57808.1; -; Genomic_DNA.
DR   RefSeq; XP_001819810.1; XM_001819758.2.
DR   AlphaFoldDB; Q2UKV7; -.
DR   SMR; Q2UKV7; -.
DR   STRING; 510516.Q2UKV7; -.
DR   PRIDE; Q2UKV7; -.
DR   EnsemblFungi; BAE57808; BAE57808; AO090003000656.
DR   GeneID; 5991793; -.
DR   KEGG; aor:AO090003000656; -.
DR   VEuPathDB; FungiDB:AO090003000656; -.
DR   HOGENOM; CLU_060354_0_2_1; -.
DR   OMA; SYDEREF; -.
DR   Proteomes; UP000006564; Chromosome 2.
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..285
FT                   /note="Histone chaperone asf1"
FT                   /id="PRO_0000284028"
FT   REGION          196..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          183..248
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        196..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..261
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  31924 MW;  DF1C5A012621F2C7 CRC64;
     MSVVSLLGVK IQNNPAPFLA PYQFEITFEC LEQLQKDLEW KLTYVGSATS SEYDQELDSL
     FVGPIPVGVN KFIFEAEAPD LKRIPTSEIL GVTVILLTCS YDGREFVRVG YYVNNEYDSE
     DLSAEPPAKP IIERIRRNIL AEKPRVTRFA IKWDSEESAP AEYPPDQPEA DILEDDSAAY
     GAEEAELEAA LVRELADAER DVKSEDHEME GAEPAIKEEE EEDISDAESE DIEDESDDDE
     EDLDEEEAGD GDEDVEMGDD SEQKDDGPKA DSTNQHSHQP EVMVH