ID A0A2B4SHC0_STYPI Unreviewed; 664 AA.
AC A0A2B4SHC0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN Name=RPA1 {ECO:0000313|EMBL:PFX28463.1};
GN ORFNames=AWC38_SpisGene6739 {ECO:0000313|EMBL:PFX28463.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX28463.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX28463.1}.
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DR EMBL; LSMT01000082; PFX28463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4SHC0; -.
DR STRING; 50429.A0A2B4SHC0; -.
DR EnsemblMetazoa; XM_022930089.1; XP_022785824.1; LOC111326151.
DR Proteomes; UP000225706; 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 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:UP000225706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 43..147
FT /note="Replication factor-A protein 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04057"
FT DOMAIN 242..323
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 350..449
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT DOMAIN 508..654
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
FT REGION 150..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 74358 MW; EB417BA89332EB3E CRC64;
MLIRNLAGVR VLDERKCHKT AFEYFITRIC RRLQNLQRSL KMLSEGAIQK IISNPVEEHP
QKPVLQILGI KQIQSRGSDG KGNDRYRLVL SDGIHVLTSA MLATQLNEMV TSEQLEVKAV
IQLNKYICNV IQETRKVLIL MDVTVIKPGR EIPGKIGDPK NLNADPSNDR QNPPQQNGNS
APQTMSVGVK AVMANGKSAG GTSRGAGLAS ATYGSHKPLA SRGDNTRSVF PITSLTPYQN
RWTIRVRVTS KPKVRTYNNS RGEGRVFNVD LVDESGEIRA TGFNEAVDKF YDLLELDKVF
YISKCSLRTA NKKFSTIKND YELFLNNDSL IEPCDDTCDL PTMQYNFVEI GDLGNIDADA
LVDILGIVVS ADEVTQITTR TTNRQVSKRD ITLLDRSEKS VRATLWAEEA ETFDEFVGKF
PVLALKGAKV SDFGGRSLSI LGSTNMRINP MDLQEAHSLR GWYENVGKDS NIESLSGLRS
DGGGLGSGYK TFFQMDHENL GMGDKADYFT SKATVLFMKK DNCLYKACPT AECNKKVIDE
GDGNYRCEKC NKTYPNFKYR LLLLTNLADF TGSHWVTCFQ ETAELLLKIT ADELGQMRDS
GDERAFDHIF QEANFKTYIF RIRAKMETYN DETRVKCTAA GVSPLDIMQE GKRMIAEIQK
LRML
//
