ID   RFA1_XENLA              Reviewed;         609 AA.
AC   Q01588;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 109.
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;
DE   AltName: Full=Single-stranded DNA-binding protein;
GN   Name=rpa1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=1527163; DOI=10.1083/jcb.119.1.1;
RA   Adachi Y., Laemmli U.K.;
RT   "Identification of nuclear pre-replication centers poised for DNA synthesis
RT   in Xenopus egg extracts: immunolocalization study of replication protein
RT   A.";
RL   J. Cell Biol. 119:1-15(1992).
RN   [2]
RP   INTERACTION WITH RIP.
RX   PubMed=10428972; DOI=10.1093/emboj/18.15.4348;
RA   Jullien D., Goerlich D., Laemmli U.K., Adachi Y.;
RT   "Nuclear import of RPA in Xenopus egg extracts requires a novel protein
RT   XRIPalpha but not importin alpha.";
RL   EMBO J. 18:4348-4358(1999).
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) (By similarity). Interacts with rpain-a
CC       (PubMed:10428972). {ECO:0000250|UniProtKB:P27694,
CC       ECO:0000269|PubMed:10428972}.
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; X67240; CAA47665.1; -; mRNA.
DR   PIR; A43458; A43458.
DR   RefSeq; NP_001081585.1; NM_001088116.1.
DR   AlphaFoldDB; Q01588; -.
DR   SMR; Q01588; -.
DR   BioGRID; 99273; 1.
DR   DNASU; 397937; -.
DR   GeneID; 397937; -.
DR   KEGG; xla:397937; -.
DR   CTD; 397937; -.
DR   Xenbase; XB-GENE-945055; rpa1.L.
DR   OrthoDB; 1189265at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 397937; Expressed in ovary and 19 other tissues.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR   GO; GO:0034502; P:protein localization to chromosome; ISS:UniProtKB.
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   1: Evidence at protein 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_0000097267"
FT   DNA_BIND        188..272
FT                   /note="OB"
FT   ZN_FING         472..494
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          113..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..135
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  67086 MW;  8C0CD1FC026FFADA CRC64;
     MALPQLSEGA ISAMLGGDSS CKPTLQVINI RPINTGNGPP RYRLLMSDGL NTLSSFMLAT
     QLNSLVDNNL LATNCICQVS RFIVNNLKDG RRVIIVMELD VLKSADLVMG KIGNPQPYND
     GQPQPAAPAP ASAPAPAPSK LQNNSAPPPS MNRGTSKLFG GGSLLNTPGG SQSKVVPIAS
     LNPYQSKWTV RARVTNKGQI RTWSNSRGEG KLFSIEMVDE SGEIRATAFN EQADKFFSII
     EVNKVYYFSK GTLKIANKQY TSVKNDYEMT FNSETSVIPC DDSADVPMVQ FEFVSIGELE
     SKNKDTVLDI IGVCKNVEEV TKVTIKSNNR EVSKRSIHLM DSSGKVVSTT LWGEDADKFD
     GSRQPVVAIK GARLSDFGGR SLSVLSSSTV MINPDIPEAF KLRAWFDSEG QVVEGTSISE
     SRGGGTGGGN TNWKSLLEVK NENLGHGEKA DYFTSVATIV YLRKENCLYQ ACPSQDCNKK
     VIDQQNGLFR CEKCNKEFPN FKYRLILSAN IADFGENQWI TCFQESAESI LGQNATYLGE
     LKEKNEQAYD EVFQNANFRS YTFRARVKLE TYNDESRIKA TAVDVKPVDH KEYSRRLIMN
     IRKMATQGV