ASF1_CAEEL
ID ASF1_CAEEL Reviewed; 275 AA.
AC Q19326;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable histone chaperone asf-1;
DE AltName: Full=Anti-silencing function protein 1;
GN Name=unc-85 {ECO:0000312|WormBase:F10G7.3};
GN Synonyms=asf-1 {ECO:0000312|WormBase:F10G7.3};
GN ORFNames=F10G7.3 {ECO:0000312|WormBase:F10G7.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; FO081114; CCD69205.1; -; Genomic_DNA.
DR PIR; H88130; H88130.
DR RefSeq; NP_494837.2; NM_062436.4.
DR AlphaFoldDB; Q19326; -.
DR SMR; Q19326; -.
DR BioGRID; 39163; 10.
DR IntAct; Q19326; 1.
DR STRING; 6239.F10G7.3; -.
DR iPTMnet; Q19326; -.
DR EPD; Q19326; -.
DR PaxDb; Q19326; -.
DR PeptideAtlas; Q19326; -.
DR EnsemblMetazoa; F10G7.3.1; F10G7.3.1; WBGene00006817.
DR GeneID; 173809; -.
DR KEGG; cel:CELE_F10G7.3; -.
DR UCSC; F10G7.3; c. elegans.
DR CTD; 173809; -.
DR WormBase; F10G7.3; CE39722; WBGene00006817; unc-85.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_0_2_1; -.
DR InParanoid; Q19326; -.
DR OMA; SYDEREF; -.
DR OrthoDB; 1295345at2759; -.
DR PhylomeDB; Q19326; -.
DR PRO; PR:Q19326; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006817; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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 GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
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..275
FT /note="Probable histone chaperone asf-1"
FT /id="PRO_0000284023"
FT REGION 157..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 31240 MW; 3D468D108F723038 CRC64;
MASRVNIVQV QILDNPAMFV DKFKLEITFE VFEHLPHDLE WELVYVGSGT SRDFDQVLDS
ALVGPIPEGR HKFVFDADHP DISKIPVDDI VGVSVLLLRC KYNDQEFINM GWFVANEYTE
EELKENPPSQ PLIEKLSRKV ETEDLRITTF PIRWTDEDPV AEPVEDEANR VFAEDDLMPL
NDDGQEDDDE EEEDDDEMEA NAEEVDLNES FNERLANALD GAEQKGADEK MEDDGANEDV
DMADDEPGVQ INTDTKVPES MAEPLSDKTN NEMVQ