ID   RFA2_CRIFA              Reviewed;         258 AA.
AC   Q23697;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Replication protein A 28 kDa subunit;
DE            Short=RP-A p28;
DE   AltName: Full=Replication factor A protein 2;
DE            Short=RF-A protein 2;
GN   Name=RPA2;
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].
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:P15927}.
CC   -!- SUBUNIT: Heterotrimer of 51, 28, and 14 kDa chains.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Also present in
CC       PML nuclear bodies. Redistributes to discrete nuclear foci upon DNA
CC       damage (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase
CC       until mitosis). Phosphorylated upon DNA damage, which promotes its
CC       translocation to nuclear foci (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC       {ECO:0000305}.
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DR   EMBL; Z23164; CAA80683.1; -; Genomic_DNA.
DR   PIR; S38459; S38459.
DR   AlphaFoldDB; Q23697; -.
DR   VEuPathDB; TriTrypDB:CFAC1_060019500; -.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR040260; RFA2-like.
DR   InterPro; IPR014646; Rfa2/RPA32.
DR   InterPro; IPR014892; RPA_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR13989; PTHR13989; 1.
DR   Pfam; PF08784; RPA_C; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PIRSF; PIRSF036949; RPA32; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Nucleus.
FT   CHAIN           1..258
FT                   /note="Replication protein A 28 kDa subunit"
FT                   /id="PRO_0000097269"
FT   DNA_BIND        60..138
FT                   /note="OB"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   258 AA;  27509 MW;  739EF6D581C8B8E6 CRC64;
     MLASQAGSNF SAAASSNGGQ QQQQRRQHPI RPLTIKQMLE AQSVGGGVMV VDGREVTQAT
     VVGRVVGYEN ANMASGGGAI TAKHFGYRIT DNTGMIVVRQ WIDADRAQEP IPLNTHVRAS
     GTVNVWQQSP IVTGTVVSMA DSNEMNYHML DAILTHLRLT QGNKRAAGNI GSGASVQNSA
     AAVGVQNMLP GGDNKVLLTD LLVSFIKQNG HGDAGMSMDE LTMAAQRYSF TPGDVRTAMR
     TLAAEGKVYQ THDNRFNI