ASF1L_CAEEL
ID ASF1L_CAEEL Reviewed; 245 AA.
AC Q17603;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 4.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable histone chaperone asf-1-like protein;
DE AltName: Full=Anti-silencing function protein 1-like;
GN Name=asfl-1; ORFNames=C03D6.5;
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; Z75525; CAA99762.3; -; Genomic_DNA.
DR PIR; T18882; T18882.
DR RefSeq; NP_492567.3; NM_060166.5.
DR AlphaFoldDB; Q17603; -.
DR SMR; Q17603; -.
DR BioGRID; 38236; 5.
DR STRING; 6239.C03D6.5; -.
DR EPD; Q17603; -.
DR PaxDb; Q17603; -.
DR PeptideAtlas; Q17603; -.
DR EnsemblMetazoa; C03D6.5.1; C03D6.5.1; WBGene00007277.
DR GeneID; 172812; -.
DR KEGG; cel:CELE_C03D6.5; -.
DR CTD; 172812; -.
DR WormBase; C03D6.5; CE36095; WBGene00007277; asfl-1.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_0_1_1; -.
DR InParanoid; Q17603; -.
DR OMA; KINWDYG; -.
DR OrthoDB; 1334998at2759; -.
DR PhylomeDB; Q17603; -.
DR PRO; PR:Q17603; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00007277; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
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:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
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..245
FT /note="Probable histone chaperone asf-1-like protein"
FT /id="PRO_0000284024"
FT REGION 157..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 245 AA; 27997 MW; 6FF82FA991C3DB50 CRC64;
MASRVNIVQV QILDNPAMFV DKFKMEITFE VFEHLPHDLE WELVYVGSGT SRDFDQVLDS
ALVGPIPEGR HKFVFDAEHP DISKIPVEDI VGVSVLLLRC KYNDQEFINM GWFVANEYTD
EELKENPPAK PLIEKLSRKI ETEDLRVTTF PIRWTDEDPV AEPVDEEANK VFDEDDLMPL
HDDGQDDDEE EEDDDETGPN TEEVDLNESF NERMANAHDG TEQKNGEESM EHDGASGDVE
MGDKH