ASF1_CANGA
ID ASF1_CANGA Reviewed; 305 AA.
AC Q6FL84;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Histone chaperone ASF1;
DE AltName: Full=Anti-silencing function protein 1;
GN Name=ASF1; OrderedLocusNames=CAGL0L05412g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380958; CAG61980.1; -; Genomic_DNA.
DR RefSeq; XP_449010.1; XM_449010.1.
DR AlphaFoldDB; Q6FL84; -.
DR SMR; Q6FL84; -.
DR STRING; 5478.XP_449010.1; -.
DR EnsemblFungi; CAG61980; CAG61980; CAGL0L05412g.
DR GeneID; 2890789; -.
DR KEGG; cgr:CAGL0L05412g; -.
DR CGD; CAL0135742; CAGL0L05412g.
DR VEuPathDB; FungiDB:CAGL0L05412g; -.
DR eggNOG; KOG3265; Eukaryota.
DR HOGENOM; CLU_060354_0_2_1; -.
DR InParanoid; Q6FL84; -.
DR OMA; SCEDNEQ; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0070775; C:H3 histone acetyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0010698; F:acetyltransferase activator activity; IEA:EnsemblFungi.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR GO; GO:0033523; P:histone H2B ubiquitination; IEA:EnsemblFungi.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IEA:EnsemblFungi.
DR GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR GO; GO:0006337; P:nucleosome disassembly; IEA:EnsemblFungi.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:EnsemblFungi.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
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..305
FT /note="Histone chaperone ASF1"
FT /id="PRO_0000284030"
FT REGION 157..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..206
FT /evidence="ECO:0000255"
FT COMPBIAS 165..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 34610 MW; B77768C11430E810 CRC64;
MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LEPLKNDLEW KLTYVGSSRS LEHDQELDSI
LVGPVPVGVN KFVFTADPPS AELIPASELV SVTVILLSCS YDGREFVRVG YYVNNEYDSE
ELRENPPQKV QVDHIVRNIL AEKPRVTRFN IVWDNENEAD IYPPEQPGVD EEDEAEEEEE
EEEEEEEEEE AEDEEEEVEV DVDGEVDLEN EDDKTDKIID GEEAEDDDDG EEIGDEEDED
DEDDEEGDAQ TETAAPNDKT TDTEKEVRLH DRDEDEKADS SKKLKTENDT AKEPDTAPTP
QDSTN
