ID D5GBQ9_TUBMM Unreviewed; 614 AA.
AC D5GBQ9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN ORFNames=GSTUM_00005528001 {ECO:0000313|EMBL:CAZ81909.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ81909.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ81909.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ81909.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- FUNCTION: As part of the replication protein A (RPA/RP-A), a single-
CC stranded DNA-binding heterotrimeric complex, may play an essential role
CC in DNA replication, recombination and repair. Binds and stabilizes
CC single-stranded DNA intermediates, preventing complementary DNA
CC reannealing and recruiting different proteins involved in DNA
CC metabolism. {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC A complex (RPA). {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364130}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000256|ARBA:ARBA00005690, ECO:0000256|RuleBase:RU364130}.
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DR EMBL; FN430097; CAZ81909.1; -; Genomic_DNA.
DR RefSeq; XP_002837718.1; XM_002837672.1.
DR AlphaFoldDB; D5GBQ9; -.
DR STRING; 656061.D5GBQ9; -.
DR EnsemblFungi; CAZ81909; CAZ81909; GSTUM_00005528001.
DR GeneID; 9182946; -.
DR KEGG; tml:GSTUM_00005528001; -.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; D5GBQ9; -.
DR OMA; FNDQCDA; -.
DR OrthoDB; 1122034at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005662; C:DNA replication factor A complex; IEA:EnsemblFungi.
DR GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0006265; P:DNA topological change; IEA:EnsemblFungi.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0045184; P:establishment of protein localization; IEA:EnsemblFungi.
DR GO; GO:0030491; P:heteroduplex formation; IEA:EnsemblFungi.
DR GO; GO:1902969; P:mitotic DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:EnsemblFungi.
DR GO; GO:0016567; P:protein ubiquitination; IEA:EnsemblFungi.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0043934; P:sporulation; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IEA:EnsemblFungi.
DR CDD; cd04474; RPA1_DBD_A; 1.
DR CDD; cd04475; RPA1_DBD_B; 1.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR InterPro; IPR047192; Euk_RPA1_DBD_C.
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 NCBIfam; TIGR00617; rpa1; 1.
DR PANTHER; PTHR23273; REPLICATION FACTOR A 1, RFA1; 1.
DR PANTHER; PTHR23273:SF4; REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT; 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; Nucleic acid-binding proteins; 4.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|RuleBase:RU364130};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364130};
KW Metal-binding {ECO:0000256|RuleBase:RU364130};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364130};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 7..108
FT /note="Replication factor-A protein 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04057"
FT DOMAIN 197..278
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 307..403
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT DOMAIN 461..606
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
FT REGION 118..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 68483 MW; D036DF4D6A67F111 CRC64;
MANNPCTPGA LQRVFEADIP TPDSFPNPIL QVLQIKSLAA QPGAPERYRV VFSDTQNFIQ
SMLATQATAH VLDGSIEKGC FVQLTNYQAN KVKDKKILIV IGLEVLTQYG KQEKIGEPVS
LEASQRPQAP DRARAAQNEK ASATSFYGNR PAPAPAEQRG VPARQAQPTT TARSSAPSAT
RPNIYPIESL SPYQNRWTIR ARVTYKSPIK LWQNSNRDGR LFNVTLLDES GEVRATGFND
QVDSFYEVLQ EGQVYYISNC KVNFAKKQFS NINNDYELAF ERNTEIEKCN DVDDGIPMAR
FNFVQFSELE SIQNDGIIDV IGVIKEVGEV ASIQSKNTQK SYTKRDVTLV DKSGYSVHIT
TWGKSAEDWE TQLDEIVAFK GVKVSEYGGR SLSMLHSSTM TVNPDIDESH ALRGWYDGQG
RGETFQSHHT GSSAVRTNDP YKTLSQIRDE NLGMGEDPDI FTTKATIVYI KNENFSYPAC
LTPKCNKKVV EIAEGQWKCE KCDITHPNCQ HRYIMTISCS DAFGLAWFSC FDDVGIMIMG
MTADELVELN NQSGGPAFAD AFLQANCKAY VFRCRAKMDV SQGQQRVRYQ VLNAAPVNFA
LEAHKLIGQI KLYS
//
