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Database: UniProt
Entry: A0A1S3IF32_LINUN
LinkDB: A0A1S3IF32_LINUN
Original site: A0A1S3IF32_LINUN 
ID   A0A1S3IF32_LINUN        Unreviewed;       265 AA.
AC   A0A1S3IF32;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Replication factor A protein 2 {ECO:0000256|ARBA:ARBA00043137};
GN   Name=LOC106163744 {ECO:0000313|RefSeq:XP_013396875.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013396875.1};
RN   [1] {ECO:0000313|RefSeq:XP_013396875.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26383154;
RA   Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA   Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT   "The Lingula genome provides insights into brachiopod evolution and the
RT   origin of phosphate biomineralization.";
RL   Nat. Commun. 6:8301-8301(2015).
RN   [2] {ECO:0000313|RefSeq:XP_013396875.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC       {ECO:0000256|ARBA:ARBA00007815}.
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DR   RefSeq; XP_013396875.1; XM_013541421.1.
DR   AlphaFoldDB; A0A1S3IF32; -.
DR   STRING; 7574.A0A1S3IF32; -.
DR   EnsemblMetazoa; XM_013541421.1; XP_013396875.1; LOC106163744.
DR   GeneID; 106163744; -.
DR   KEGG; lak:106163744; -.
DR   InParanoid; A0A1S3IF32; -.
DR   OrthoDB; 72010at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:InterPro.
DR   CDD; cd04478; RPA2_DBD_D; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR040260; RFA2-like.
DR   InterPro; IPR014646; Rfa2/RPA32.
DR   InterPro; IPR014892; RPA_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13989:SF16; REPLICATION PROTEIN A 32 KDA SUBUNIT; 1.
DR   PANTHER; PTHR13989; REPLICATION PROTEIN A-RELATED; 1.
DR   Pfam; PF08784; RPA_C; 1.
DR   PIRSF; PIRSF036949; RPA32; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT   DOMAIN          172..258
FT                   /note="Replication protein A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08784"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  29203 MW;  E52E67DB50816EBD CRC64;
     MWNNQGGFSN YDQAGGFDSP GGFSSPQQSS QQSRARTRTQ NIVPVTVAMV HQCQHADEKF
     FIDGIEIAQV TIVGLVRSVQ QGSNRMDYTI DDLTGPPMDV RQFVDIDEAN SEEAERIRSV
     RENTYVRLFG HIRAFQGKKN VVAFRIQPVT DMNELTTHIL EVMQAHMASK MHMEAGDAPA
     KTVAADNTYS GAQGSIPANG LTPIQAQVAQ TISDCRDEQG VSVYEIAKQL EGLTEKAIRS
     AIEFLSSEGH IYSTIDDDHY KATDS
//
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