ID J5RHH5_SACK1 Unreviewed; 621 AA.
AC J5RHH5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN Name=YAR007C {ECO:0000313|EMBL:EJT41601.1};
GN Synonyms=SKDI01G0760 {ECO:0000313|EMBL:CAI4054628.1};
GN ORFNames=SKDI_01G0760 {ECO:0000313|EMBL:CAI4054628.1}, SKUD_190206
GN {ECO:0000313|EMBL:EJT41601.1};
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT41601.1, ECO:0000313|Proteomes:UP000002753};
RN [1] {ECO:0000313|EMBL:EJT41601.1, ECO:0000313|Proteomes:UP000002753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC {ECO:0000313|EMBL:EJT41601.1};
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2] {ECO:0000313|EMBL:EJT41601.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT41601.1};
RA Cliften P.F., Johnston M.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000002753}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
RN [4] {ECO:0000313|EMBL:EJT41601.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT41601.1};
RA Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAI4054628.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4054628.1};
RA Byrne P K.;
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: As part of the replication protein A (RPA/RP-A), a single-
CC stranded DNA-binding heterotrimeric complex, may play an essential role
CC in DNA replication, recombination and repair. Binds and stabilizes
CC single-stranded DNA intermediates, preventing complementary DNA
CC reannealing and recruiting different proteins involved in DNA
CC metabolism. {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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OX365896; CAI4054628.1; -; Genomic_DNA.
DR EMBL; AACI03001999; EJT41601.1; -; Genomic_DNA.
DR AlphaFoldDB; J5RHH5; -.
DR STRING; 226230.J5RHH5; -.
DR HOGENOM; CLU_012393_2_0_1; -.
DR Proteomes; UP000002753; Unassembled WGS sequence.
DR Proteomes; UP001162087; Chromosome 1.
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:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
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 GO; GO:0009059; P:macromolecule biosynthetic process; IEA:UniProt.
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; 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:UP000002753};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 198..267
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 305..400
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT DOMAIN 466..611
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
SQ SEQUENCE 621 AA; 70121 MW; 895CC488F7CBC832 CRC64;
MSSVQLSKGD FHSIFTNKRR YDNPTGGVYQ VYNTRKSDGA NSNRKNLIMI SDGVYHMKAL
LRNQAASKFQ SMELQRGDII RVIIAEPAIV RERKKYVLLV DDFELVQSRA EMVNQASTFL
DNYFSERPNE TLKDEDISDN GNVTNQTNIG NLGVGDMLHS NSNLNANEKK FVNEGSNSQK
SRPIFAIEQL SPYQNVWTIK ARVSYKGEIK TWHNQRGDGK LFNVNFLDTS GEIRATAFND
FATKFNEILQ EGKVYYVSKA KLQPAKPQFT NLTHPYELNL DRDTVVEECF DESNVPKTHF
NFIKLDAIQN QEVNSNVDVL GIIQTINPQF ELTSRAGKKF DRRDITIVDD SGFSISVGLW
NQQALDFNLP EGSVAAIKGV RVTDFGGKSL SMGFSSTLIP NPEIPEAYAL KGWYDSKGRN
ANFTTLKQEP GVGGQSAASL TKFIAQRITI ARAQAENLGR SEKGDFFSAK AAISFLKVDN
FAYPACSNEN CNKKVLEQPD GTWRCEKCDT NNASPNWRYI LTISIIDETN QLWLTLFDDQ
AKQLLGVDAN TLMSLKEEDP NEFTKITQSI QMNEYDFRIR AREDTYNDQS RIRYTVANLH
SLNYKAEADY LADELSKALL A
//
