ID A0A0L9URR6_PHAAN Unreviewed; 860 AA.
AC A0A0L9URR6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN ORFNames=LR48_Vigan06g071700 {ECO:0000313|EMBL:KOM45411.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM45411.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- FUNCTION: Component of the replication protein A complex (RPA) required
CC for DNA recombination, repair and replication. The activity of RPA is
CC mediated by single-stranded DNA binding and protein interactions.
CC Probably involved in repair of double-strand DNA breaks (DSBs) induced
CC by genotoxic stresses. {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex). {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; CM003376; KOM45411.1; -; Genomic_DNA.
DR RefSeq; XP_017425980.1; XM_017570491.1.
DR AlphaFoldDB; A0A0L9URR6; -.
DR STRING; 3914.A0A0L9URR6; -.
DR EnsemblPlants; KOM45411; KOM45411; LR48_Vigan06g071700.
DR GeneID; 108334613; -.
DR Gramene; KOM45411; KOM45411; LR48_Vigan06g071700.
DR KEGG; var:108334613; -.
DR OMA; NCVAPRV; -.
DR OrthoDB; 276920at2759; -.
DR Proteomes; UP000053144; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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 Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
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 InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR NCBIfam; TIGR00617; rpa1; 1.
DR PANTHER; PTHR23273; REPLICATION FACTOR A 1, RFA1; 1.
DR PANTHER; PTHR23273:SF139; REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT C-RELATED; 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 Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW 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:UP000053144};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 825..839
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 115..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 93700 MW; 41174B0CBD72D509 CRC64;
MAGSLTPGAI KEICGANCSS SLKPVLQVID LKLVQSQQAN NTERYRLILS DGSFYQQGML
ATQMNELVHS GKLQKGSVVR LTQFICNDVQ NRKIIVIIDL DVVVEKCELI GEPVSLPKDG
SVESATGQSG VTPGNSQSLN NRSHSGGMAA RPNMAIPSPD HPRMNAPASS VYSSISNSGS
SYSSNAPPTY PKVETGANLS RSAPFTGSHG DQNMGIRHPQ SETSRPLSNS YARAPQPMYR
QPSPMYTNRG PIGKNEAAPR IIPIAALNPY QNMWTIKARV TAKGELRHYN NARGDGKVFS
FDLLDSDGGQ IRATCFNSVA DQFYNLIEAG KIYLVSRGSV KPAQKNFNHL PNDQELTLDM
TSIIQPCPDD DKSIPKQTFN FRPISEIESL ESNAIVDMIG VVTSISPTAS IMRKNGTETQ
KRTLQLKDMS GRSVELTLWG NFCNVEGQRL QTICDDGKFP VLAIKAVRIN DFNGKSVGTI
MTSLLFIEPD FPEVYTLKRW FEKEGKNVPT LSISKDTSSF PKNDNRKTVS QIKDEKLGTS
EKPDWISVCA TISFMKYDNF CYPGCPIMIG DRQCNKKVTN NGDGKWICDR CNQSVDACDY
RYILSFQIMD HTGVTWVTAF QESGEEIIGV PAKDLYYLKY EEQNDERFAE IIRKVLFSEY
VFKLKVKEET FSDEQRVKAT VVKAEKVNFA SKSRVSLELI DKLLTGKSEG ATTVTNSLSG
NTGLRSVETG QVMPPAYNPI KSSTNSGRDF GMPANQVGQQ YGNQYGNIAS AGAPGAYTSC
TNCGGSGHTS ILCPNVRNPA GQSSGGGFSN RVSYGGSGGG ASGECFKCHQ PGHWARDCPG
SSAATASYGS NTMQGRYGGY
//
