ID   ASF1_NEUCR              Reviewed;         271 AA.
AC   Q7S1X9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Histone chaperone asf-1;
DE   AltName: Full=Anti-silencing function protein 1;
GN   Name=asf-1; ORFNames=NCU09436;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002242; EAA29352.1; -; Genomic_DNA.
DR   RefSeq; XP_958588.1; XM_953495.2.
DR   AlphaFoldDB; Q7S1X9; -.
DR   SMR; Q7S1X9; -.
DR   STRING; 5141.EFNCRP00000009211; -.
DR   EnsemblFungi; EAA29352; EAA29352; NCU09436.
DR   GeneID; 3874735; -.
DR   KEGG; ncr:NCU09436; -.
DR   VEuPathDB; FungiDB:NCU09436; -.
DR   HOGENOM; CLU_060354_0_2_1; -.
DR   InParanoid; Q7S1X9; -.
DR   OMA; SYDEREF; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..271
FT                   /note="Histone chaperone asf-1"
FT                   /id="PRO_0000284039"
FT   REGION          152..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..183
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..255
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   271 AA;  30179 MW;  ECF0AE9B3DBF9C86 CRC64;
     MSVVSLLGVN VMNNPAKFTD KYLFEITFEC LEHLEKDLEW KLTYVGSATS DNYDQELDSL
     LVGPIPVGVN KFIFEAEPPD TKRIPIDELL GVTVILLTCA YDGREFVRVG YYVNNEYESE
     ELINDPPPKP VIEKIRRNVL AEKPRVTRFA IKWDSEASAP PEFPPEQPEA DEVADEEEYG
     ADELAEQSSI ADPAVNGGME VEGQPNGAIV IEEDEMSEDG SVDLENESED ELDGEGDAEG
     ELEQGQDEDI EMGDEMEIDD HPKQQGMAMA Q