ID U4TTP5_DENPD Unreviewed; 403 AA.
AC U4TTP5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN ORFNames=D910_02312 {ECO:0000313|EMBL:ERL84889.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL84889.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL84889.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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|RuleBase:RU364130}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000256|RuleBase:RU364130}.
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DR EMBL; KB631639; ERL84889.1; -; Genomic_DNA.
DR AlphaFoldDB; U4TTP5; -.
DR STRING; 77166.U4TTP5; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR CDD; cd04474; RPA1_DBD_A; 1.
DR CDD; cd04475; RPA1_DBD_B; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF16900; REPA_OB_2; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
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|RuleBase:RU364130};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Zinc {ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 5..109
FT /note="Replication factor-A protein 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04057"
FT DOMAIN 293..391
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
SQ SEQUENCE 403 AA; 44488 MW; 95C27317BDBB263F CRC64;
MSIELSKGAL ATIMQGGDYI EPIVQVLSIK RMNSGTGQPD KDKFRALLSD GQCTVSFAMM
TAPVYARAGE NGLAKFSIIK IVRFITSVIN NTEGKDSRVL LILDLTVLKD GNELGEKIGN
PVSYSQLNVG PSTNYHQSSA NAIQAAGSPS KKPRLSVPFN ANCGTSSSRA VYAISSLSPF
HNKWIIRAKV INKSDIRKWE NSKGVGQLFS FEIADESSEI KCTAFKELVD QFYDVVQVDK
IYYISKCQIK IASKQFNTVK NDYEIYLTPD TVIEECFMCD LPQIPTNFNF VEIRRIADLH
ANELIDVIGV AKSTSDLQIF TAKSSGREIK KRDVQLVDQS KTVVTLTLWG GQAENFNGNG
NPVISLKNAK IHEFLGGKSL STISSTQMRI NPETKEAFLL KAW
//