ASF1_ASPFU
ID ASF1_ASPFU Reviewed; 282 AA.
AC Q4WXX5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Histone chaperone asf1;
DE AltName: Full=Anti-silencing function protein 1;
GN Name=asf1; ORFNames=AFUA_3G11030;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000002; EAL92478.1; -; Genomic_DNA.
DR RefSeq; XP_754516.1; XM_749423.1.
DR PDB; 5ZBA; X-ray; 3.50 A; B=1-154.
DR PDB; 5ZBB; X-ray; 3.60 A; B=1-154.
DR PDBsum; 5ZBA; -.
DR PDBsum; 5ZBB; -.
DR AlphaFoldDB; Q4WXX5; -.
DR SMR; Q4WXX5; -.
DR STRING; 746128.CADAFUBP00003733; -.
DR PRIDE; Q4WXX5; -.
DR EnsemblFungi; EAL92478; EAL92478; AFUA_3G11030.
DR GeneID; 3511719; -.
DR KEGG; afm:AFUA_3G11030; -.
DR VEuPathDB; FungiDB:Afu3g11030; -.
DR eggNOG; KOG3265; Eukaryota.
DR HOGENOM; CLU_060354_0_2_1; -.
DR InParanoid; Q4WXX5; -.
DR OMA; SYDEREF; -.
DR OrthoDB; 1231087at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Chromatin regulator; Coiled coil; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..282
FT /note="Histone chaperone asf1"
FT /id="PRO_0000284027"
FT REGION 151..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..249
FT /evidence="ECO:0000255"
FT COMPBIAS 193..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"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 22..32
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:5ZBA"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5ZBA"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 104..119
FT /evidence="ECO:0007829|PDB:5ZBA"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:5ZBA"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:5ZBA"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5ZBA"
SQ SEQUENCE 282 AA; 31496 MW; A9227787DB2F4C9A CRC64;
MSVVSLLGVK IVNNPAPFLA PYQFEITFEC LEQLQKDLEW KLTYVGSATS SEYDQELDSL
LVGPIPVGVN KFLFEADAPD LKRIPTSEIL GVTVILLTCS YDGREFVRVG YYVNNEYDSE
ELTQDPPAKP IIERIRRNIL AEKPRVTRFA IKWDSEEDAP AEYPPDQPEA DLEDDGAAYG
AEEAELEAAL IRELEEAERE AAKGGDHEME GAEETAGKDD EEEDLSDAES EDIEDESDDE
EDDLDEDEGG DRDEDVEMGD DTESKDTNAA SGHHQQQDIM VH