ID   RFA1_CRIFA              Reviewed;         467 AA.
AC   Q23696;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Replication factor A 51 kDa subunit;
DE   AltName: Full=RP-A p51;
DE   AltName: Full=Replication factor-A protein 1;
DE            Short=RF-A protein 1;
DE   AltName: Full=Single-stranded DNA-binding protein P51 subunit;
GN   Name=RPA1;
OS   Crithidia fasciculata.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX   NCBI_TaxID=5656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=CfC1.1;
RX   PubMed=8183313; DOI=10.1016/0166-6851(94)90016-7;
RA   Brown G.W., Hines J.C., Fisher P., Ray D.S.;
RT   "Isolation of the genes encoding the 51-kilodalton and 28-kilodalton
RT   subunits of Crithidia fasciculata replication protein A.";
RL   Mol. Biochem. Parasitol. 63:135-142(1994).
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).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z23163; CAA80682.1; -; Genomic_DNA.
DR   PIR; S38458; S38458.
DR   AlphaFoldDB; Q23696; -.
DR   SMR; Q23696; -.
DR   VEuPathDB; TriTrypDB:CFAC1_300030200; -.
DR   GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; 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:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR   CDD; cd04476; RPA1_DBD_C; 1.
DR   Gene3D; 2.40.50.140; -; 3.
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   Direct protein sequencing; DNA replication; DNA-binding; Metal-binding;
KW   Nucleus; Zinc; Zinc-finger.
FT   CHAIN           1..467
FT                   /note="Replication factor A 51 kDa subunit"
FT                   /id="PRO_0000097258"
FT   DNA_BIND        23..105
FT                   /note="OB"
FT   ZN_FING         313..335
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   467 AA;  52017 MW;  5FA3177877BFFE2A CRC64;
     MHQPGSHQIQ PIDSLTPFLG GKWWIRARVA DKSDIRTWNK PTSQGKLFSF TLIDESAAIR
     ATVFNDAVDT FEPLVVNGQV YYFSGGQVKN ANRRFSNVNN DYELTFDRAS EVILARQDSS
     AAALPMQRYN FVPIELLKQR EVGSLVDVLG VVLKVDEISS ITQKSTGREL IKRNVKIGDM
     SAAVEVTFWN DEAKAWNYPV GTVVALRQLK VGSFDGVTLS STYQTKIDVN PADLPDVKKL
     ATWYVSTGGA NVVSLSSQGL GAGGGGGGEG NRGRKYLDEI QSEGIGRGAK PEYVDVRCVP
     IYFKQDAQWY DACPTCNKKV TEEGAQGDRF RCEKCDATVV PTQRYLVSIQ VTDNVSQVWL
     TLFNEAGVEF FGMEASELKR RAQEDPLYIA KLAQARMNRP VVMRLRVKEE TNANAMTGEE
     SDRLRMSVVR ISEFMPVAGT TEETRRRLAQ NLRSECDDIL RCIEAYV