ID A0A1S3QGM5_SALSA Unreviewed; 348 AA.
AC A0A1S3QGM5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN Name=LOC106592337 {ECO:0000313|RefSeq:XP_014039148.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014039148.1};
RN [1] {ECO:0000313|RefSeq:XP_014039148.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000256|RuleBase:RU364130}.
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DR RefSeq; XP_014039148.1; XM_014183673.1.
DR AlphaFoldDB; A0A1S3QGM5; -.
DR KEGG; sasa:106592337; -.
DR Proteomes; UP000087266; Unplaced.
DR GO; GO:0016605; C:PML body; 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; 2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
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; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
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:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 80..167
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 188..284
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 38281 MW; 491E51FF50FA49C3 CRC64;
MMVGMCNRGI RAVSSPGQGR TLQNQLSAQS HPAAASTASP HNQPGAASSS TRVPAGRGDS
GKKTPIVVPI ACLIPYQTKW TIRARVTKKN NISPWSNPKG EGKLFNFEIV DESGEISVTA
FNKEVDKFFP LLETGKVYYI SEGKVKETNK KYITSKNNYE IILRNVTSIV PCEDDQNLPM
VECDFRPIAQ LEHMEKDDII DVIGVCRSVD DLSRFTARTG REAYKRDIDL MDTSGKAVAV
TLWGEQAEMF DGSVQPIVAV KRARLSDFGG QSVSAIFSSA VMVNPDIPEA HWLRRWYDQE
GHALDCQSLT ELRPAGGGAN TCWKTLSDIK TEQLGQGDKL CSHSVALW
//
