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Database: UniProt
Entry: A0A395M7C1_9HYPO
LinkDB: A0A395M7C1_9HYPO
Original site: A0A395M7C1_9HYPO 
ID   A0A395M7C1_9HYPO        Unreviewed;       276 AA.
AC   A0A395M7C1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Replication factor a2 {ECO:0000313|EMBL:RFN43787.1};
GN   ORFNames=FIE12Z_11953 {ECO:0000313|EMBL:RFN43787.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN43787.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN43787.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN43787.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC       {ECO:0000256|ARBA:ARBA00007815}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RFN43787.1}.
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DR   EMBL; PXXK01000506; RFN43787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395M7C1; -.
DR   STRING; 2594813.A0A395M7C1; -.
DR   OrthoDB; 5473935at2759; -.
DR   Proteomes; UP000265631; Unassembled WGS sequence.
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; 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   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   Pfam; PF01336; tRNA_anti-codon; 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:UP000265631}.
FT   DOMAIN          75..142
FT                   /note="OB"
FT                   /evidence="ECO:0000259|Pfam:PF01336"
FT   DOMAIN          166..269
FT                   /note="Replication protein A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08784"
FT   REGION          21..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  29566 MW;  500B5354AA6A6203 CRC64;
     MSAYAGFTKT SYGAQGGDDS GGFFAGGSQQ GSQGGGGKSY QDESLRPVTI KQILDAEEAY
     AGADFKIDGS PVTQITFVGQ VRNVQPQPTN ITLKIDDGTG QIEVKKWIDV DKTEDNESSF
     ELESYVRIWG RLKSFNNKRH VGAHVIRPVA EFDEVNYHML EATYVHLYFT KGPLGGQGGG
     ANGDDGMFVD GGNYNDNAGG NTSQSHSKIA GCSPLAKKMF TFMSETPGGN EGVHVNIITS
     STGMSVRDAL TAADELLGQG LIYTTVDDET WAILEY
//
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