RFA1_XENTR
ID RFA1_XENTR Reviewed; 609 AA.
AC Q5FW17; Q08D29; Q28ES6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit;
DE Short=RP-A p70;
DE AltName: Full=Replication factor A protein 1;
DE Short=RF-A protein 1;
GN Name=rpa1; ORFNames=TGas057c05.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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). Interacts with rpain-a (By similarity).
CC {ECO:0000250|UniProtKB:P27694, ECO:0000250|UniProtKB:Q01588}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:P27694}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; CR848086; CAJ81527.1; -; mRNA.
DR EMBL; BC089665; AAH89665.1; -; mRNA.
DR EMBL; BC123968; AAI23969.1; -; mRNA.
DR RefSeq; NP_001015732.1; NM_001015732.1.
DR AlphaFoldDB; Q5FW17; -.
DR SMR; Q5FW17; -.
DR STRING; 8364.ENSXETP00000063755; -.
DR PaxDb; Q5FW17; -.
DR DNASU; 548449; -.
DR GeneID; 548449; -.
DR KEGG; xtr:548449; -.
DR CTD; 6117; -.
DR Xenbase; XB-GENE-945047; rpa1.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; Q5FW17; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; Q5FW17; -.
DR Reactome; R-XTR-110312; Translesion synthesis by REV1.
DR Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR Reactome; R-XTR-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-XTR-5655862; Translesion synthesis by POLK.
DR Reactome; R-XTR-5656121; Translesion synthesis by POLI.
DR Reactome; R-XTR-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-XTR-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-XTR-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-XTR-5696400; Dual Incision in GG-NER.
DR Reactome; R-XTR-6782135; Dual incision in TC-NER.
DR Reactome; R-XTR-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
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:0034502; P:protein localization to chromosome; ISS:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 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; IPR007199; Rep_factor-A_N.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 1.
DR Pfam; PF04057; Rep-A_N; 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; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..609
FT /note="Replication protein A 70 kDa DNA-binding subunit"
FT /id="PRO_0000097264"
FT DNA_BIND 189..273
FT /note="OB"
FT REGION 112..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 67180 MW; EE5DA355DFB21505 CRC64;
MALPVLSEGA ISAILGGDSS CKPTLQVINI RSINTGNGPP RYRLLMSDGL NTLSSFMLAT
QLNFLVDNNL LATNCICQVS RFIVNNLKDG RRVIIVMEME VLKSADLVKG KIGNPHPYND
GQGPPQPAAP APASAPPPSK PQNISAPPPP SMNRGASKLF GGGSVVNTPG GSQSKVVPIA
SLNPYQSKWT VRARVTNKGQ IRTWSNSRGE GKLFSIEMVD ESGEIRATAF NEQADKFFSL
IEVNKVYYFS KGTLKIANKQ YTSVKNDYEM TFNSETSVIP CDDSADVPMV QFEFVPIGEL
ESKNKDTVLD IIGICKNAEE VTKVTIRSNN REVSKRNINL MDSSGKVVST TLWGEDADKF
DGSRQPVVAI KGARLSDFGG RSLSVLSSST VMINPDIPEA FKLRAWFDSE GQVVEGTSIS
ESRGGTGGGN TNWKSLLEVK TENLGHGEKA DYFTSVATIV YLRKENCLYQ ACPSQDCNKK
VIDQQNGLFR CEKCDKEFPN YKYRLILSAN IADFGENQWI TCFQESAESI LGQNATYLGE
LKEKNEQAYD EVFQNANFRS YTFRIRVKLE TYNDESRIKA TAMDVKPVDH KEYSRRLIMN
IRKMAAQGV
