ID T1EG41_HELRO Unreviewed; 640 AA.
AC T1EG41;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN Name=20195543 {ECO:0000313|EnsemblMetazoa:HelroP114692};
GN ORFNames=HELRODRAFT_114692 {ECO:0000313|EMBL:ESN95542.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP114692, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESN95542.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP114692}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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: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; AMQM01006806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB097519; ESN95542.1; -; Genomic_DNA.
DR RefSeq; XP_009026408.1; XM_009028160.1.
DR AlphaFoldDB; T1EG41; -.
DR STRING; 6412.T1EG41; -.
DR EnsemblMetazoa; HelroT114692; HelroP114692; HelroG114692.
DR GeneID; 20195543; -.
DR KEGG; hro:HELRODRAFT_114692; -.
DR CTD; 20195543; -.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; T1EG41; -.
DR OMA; FNSYAML; -.
DR OrthoDB; 1122034at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005662; C:DNA replication factor A complex; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
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:UP000015101};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 6..103
FT /note="Replication factor-A protein 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04057"
FT DOMAIN 217..290
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 332..427
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT DOMAIN 486..631
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
FT REGION 149..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 71225 MW; 64DDE79BCED6D74D CRC64;
MAKFTLTANS LEKVMSGLPC EKPVVQVLGH KKIVGAGQGP ERFRLLLSDG VHTVSSVMLA
TQLNDKVTSG QIDINAVVRL DKYICNIIQA EKRVVVVLEL TVLGVSSIVG GKIGNPQPYK
QQAAGELTNS NVTAATAAAD LRQQLPLQAQ NNNSNNNSGF SGKSQFDNTS AKQQQQRTQS
STSSSVSQQI NKNNSSMLDT PSKITSISSL NPYLNRWTIK ARVTQKSSIK TWSNSKGEGK
LFSMNLIDQS GEIRATLFKN EVDKFFDMIE VNKVYFIRKA QLKIANKQFS NLNNDFELTF
TGETEVIPCA DGEDCDDDGQ QLPSISFNFV GIDKFEQMQP NVIVDVIAVV KDCGDLKVVT
QRQSNKEIKK RDITLVDQSK VQVTLTLWGD YAESFKAEGN PVLAIKGVRL TDFGGRSLSQ
SNNSQILENP DFPECHSLRG WFDNVGCSAE YSEYKKEQTS SFGGPLLYKT MLESKNELHD
GEAANYFMAT ATIPVFKKDN SLYKACPQPD CNKKVVDCGN SSYRCEKCSK EFGTFKWRLI
LQMNISDFTE SQWVTAFNEV AETILNIKAD ELGALKDTDS TRFDQVFTNA SFSTFTFKLR
SKVEKYNDES RLKTACIQAT PISYADENKR LILILEKYLQ
//
