RFA1_CAEEL
ID RFA1_CAEEL Reviewed; 655 AA.
AC Q19537;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable replication factor A 73 kDa subunit;
DE AltName: Full=RP-A p73;
DE AltName: Full=Replication factor A protein 1;
DE Short=RF-A protein 1;
GN Name=rpa-1 {ECO:0000312|WormBase:F18A1.5};
GN ORFNames=F18A1.5 {ECO:0000312|WormBase:F18A1.5};
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).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=30383754; DOI=10.1371/journal.pgen.1007653;
RA Janisiw E., Dello Stritto M.R., Jantsch V., Silva N.;
RT "BRCA1-BARD1 associate with the synaptonemal complex and pro-crossover
RT factors and influence RAD-51 dynamics during Caenorhabditis elegans
RT meiosis.";
RL PLoS Genet. 14:e1007653-e1007653(2018).
CC -!- FUNCTION: As part of the heterotrimeric replication protein A complex
CC (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates,
CC that form during DNA replication or upon DNA stress. It prevents their
CC reannealing and in parallel, recruits and activates different proteins
CC and complexes involved in DNA metabolism. Thereby, it plays an
CC essential role both in DNA replication and the cellular response to DNA
CC damage. {ECO:0000250|UniProtKB:P27694}.
CC -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC A complex (RPA). {ECO:0000250}.
CC -!- INTERACTION:
CC Q19537; Q95Y97: rpa-2; NbExp=3; IntAct=EBI-325415, EBI-325404;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30383754}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; BX284602; CCD62042.1; -; Genomic_DNA.
DR PIR; T34219; T34219.
DR RefSeq; NP_495606.1; NM_063205.4.
DR AlphaFoldDB; Q19537; -.
DR SMR; Q19537; -.
DR BioGRID; 39572; 25.
DR DIP; DIP-26609N; -.
DR IntAct; Q19537; 2.
DR STRING; 6239.F18A1.5; -.
DR EPD; Q19537; -.
DR PaxDb; Q19537; -.
DR PeptideAtlas; Q19537; -.
DR PRIDE; Q19537; -.
DR EnsemblMetazoa; F18A1.5.1; F18A1.5.1; WBGene00017546.
DR GeneID; 174238; -.
DR KEGG; cel:CELE_F18A1.5; -.
DR CTD; 174238; -.
DR WormBase; F18A1.5; CE04405; WBGene00017546; rpa-1.
DR eggNOG; KOG0851; Eukaryota.
DR GeneTree; ENSGT00390000012403; -.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; Q19537; -.
DR OMA; YRLLINM; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; Q19537; -.
DR PRO; PR:Q19537; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017546; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:WormBase.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..655
FT /note="Probable replication factor A 73 kDa subunit"
FT /id="PRO_0000097257"
FT DNA_BIND 236..326
FT /note="OB"
FT ZN_FING 518..539
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 195..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 73202 MW; 44E41E7B16E2FB42 CRC64;
MAAIHINHDV FNKYHTNGKL RLTTGYVQEA IENNGYPGHD GIVQVLKGKV EQGEQLGHAF
TFRIRISDGV FQYNALMSAD IDDQIKREVE HLVEGTIIAL TKFEIYDQGE GAKNCFLIKG
YKILSRYHQV LTSPEVKPRS HSGKPDEHKG YRPNIIIEDV WPEAEGMAAD YQENMANPPA
AKAPKREFGE EASYNRAAAP EATRARAVPP PARRTASNTE RGVMPIAMVT PYVSNFKIHG
MVSRKEEIRT FPAKNTKVFN FEITDSNGDT IRCTAFNEVA ESLYTTITEN LSYYLSGGSV
KQANKKFNNT GHDYEITLRS DSIIEAGGEL LAAPKLILKR VKLGEIAGYA GQLIDVLVVV
EKMDPEATEF TSKAGKSLIK REMELIDESG ALVRLTLWGD EATKALVDDY VQKVIAFKGV
IPREFNGGFS LGTGSATRII SVPEIAGVSE LYDWYANVKP TTEVKMMSQA AGGSNEAPRT
IAGLQEMQFG KDSDKGDYAT VKAMITRVNP TNALYRGCAS EGCQKKLVGE NGDYRCEKCN
KNMNKFKWLY MMQFELSDET GQVYVTAFGD SAAKIVGKSA AELGELHDES PDEYNAIFER
LQFVPKMWRL RCKMDSYNEE VRQKMTVYGV DDVNQDKYIE NLKQMIEQMQ QMSDY
