RFA1_CHICK
ID RFA1_CHICK Reviewed; 614 AA.
AC Q5ZJJ2;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit;
DE Short=RP-A p70;
DE AltName: Full=Replication factor A protein 1;
DE Short=RF-A protein 1;
GN Name=RPA1; ORFNames=RCJMB04_17l6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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:0000250|UniProtKB:P27694}.
CC -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC A complex (RPA). {ECO:0000250|UniProtKB:P27694}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:P27694}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AJ720442; CAG32101.1; -; mRNA.
DR RefSeq; NP_001006221.1; NM_001006221.1.
DR RefSeq; XP_015151236.1; XM_015295750.1.
DR RefSeq; XP_015151237.1; XM_015295751.1.
DR AlphaFoldDB; Q5ZJJ2; -.
DR SMR; Q5ZJJ2; -.
DR STRING; 9031.ENSGALP00000004840; -.
DR PaxDb; Q5ZJJ2; -.
DR Ensembl; ENSGALT00000004849; ENSGALP00000004840; ENSGALG00000003072.
DR GeneID; 417563; -.
DR KEGG; gga:417563; -.
DR CTD; 6117; -.
DR VEuPathDB; HostDB:geneid_417563; -.
DR eggNOG; KOG0851; Eukaryota.
DR GeneTree; ENSGT00390000012403; -.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; Q5ZJJ2; -.
DR OMA; VRVTIWG; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; Q5ZJJ2; -.
DR TreeFam; TF105241; -.
DR Reactome; R-GGA-110312; Translesion synthesis by REV1.
DR Reactome; R-GGA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-GGA-110320; Translesion Synthesis by POLH.
DR Reactome; R-GGA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-GGA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-GGA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-GGA-351451; Homologous recombination repair of replication-dependent double-strand breaks.
DR Reactome; R-GGA-351468; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-353303; Nucleotide Excision Repair.
DR Reactome; R-GGA-5655862; Translesion synthesis by POLK.
DR Reactome; R-GGA-5656121; Translesion synthesis by POLI.
DR Reactome; R-GGA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-GGA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-GGA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-GGA-5696400; Dual Incision in GG-NER.
DR Reactome; R-GGA-6782135; Dual incision in TC-NER.
DR Reactome; R-GGA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-GGA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-GGA-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q5ZJJ2; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000003072; Expressed in spermatid and 13 other tissues.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
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:0034502; P:protein localization to chromosome; ISS:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR Gene3D; 2.40.50.140; -; 4.
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 PANTHER; PTHR23273; PTHR23273; 2.
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; SSF50249; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 2: Evidence at transcript level;
KW DNA replication; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..614
FT /note="Replication protein A 70 kDa DNA-binding subunit"
FT /id="PRO_0000097263"
FT DNA_BIND 194..278
FT /note="OB"
FT REGION 112..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 68001 MW; 21F99B6673CD785C CRC64;
MSVRLSEGAI AAIMQGENVY KPVLQVINTR AIATGNGPPR YRVLMSDGVN TLSSFMLATQ
LNPLVEEERL SAHCICQVNR FIVNSLKDGR RVVILMDLDV LKTADMVGGT VGNPVPYNEG
QGQQRSSAPT ANAAPNKPQQ QDGNLSVAGS AAPKYHAPSN QFSKASAPSS VKTPGGTQSK
VVPIASLNPY QSKWTICARV TQKGQIRTWS NSRGEGKLFS IELVDESGEI RATAFNDQAD
KFFPLIELNK VYYFTKGNLK TANKQYTAVK NDYEITFNNE TSVVPCDDAQ HLPSVQFDFV
SISDLENTPK DSIVDVIGIC KSYEDVTKIV VKASNREVSK RNVHLMDTSG KLVTATLWGN
EAEKFDGSRQ PVIAIKGARV SDFGGRSLSV LSSSTVVVNP DSPEAFKLRG WFDSEGQLLE
CASISDVRGG SASGVNTNWK TLYEAKSERL GQGDKADYFS CVGTIVHLRK ENCMYQACPS
QDCNKKVIDQ QNGLYRCEKC DREFPNFKYR MMLLVTIADS LDYQWVTCFQ ESAEFILGQS
ATFLGELKDK NEQAFEEVFQ NANFNTYEFK IRVKLETYND ESRIKATALD VKPVNYREYS
KRLIASIRRN AQLG