ID S8CUV6_9LAMI Unreviewed; 832 AA.
AC S8CUV6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN ORFNames=M569_06091 {ECO:0000313|EMBL:EPS68676.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS68676.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS68676.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
CC -!- FUNCTION: Component of the replication protein A complex (RPA) required
CC for DNA recombination, repair and replication. The activity of RPA is
CC mediated by single-stranded DNA binding and protein interactions.
CC Probably involved in repair of double-strand DNA breaks (DSBs) induced
CC by genotoxic stresses. {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex). {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:EPS68676.1}.
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DR EMBL; AUSU01002494; EPS68676.1; -; Genomic_DNA.
DR AlphaFoldDB; S8CUV6; -.
DR OrthoDB; 276920at2759; -.
DR Proteomes; UP000015453; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
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 Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
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 InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR NCBIfam; TIGR00617; rpa1; 1.
DR PANTHER; PTHR23273; REPLICATION FACTOR A 1, RFA1; 1.
DR PANTHER; PTHR23273:SF139; REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT C-RELATED; 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 Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 3: Inferred from homology;
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW 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:UP000015453};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 750..765
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 793..808
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 116..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 90837 MW; 9280C14CE2C714EC CRC64;
MPPVNLTEGA IAALSGGNAQ GTDIKPVLQI AEIRLVNAQN QSNNERYRLL LSDGSFTQQG
MLATQRNDLV RSQKLQKGSI VQLTQFVCNL IQNRMIIIII DLDVIVERCD PIGEPKPYPI
KPDGNASSLP SPQTVNQPSA GNVNPHSSYV GVSPSSVSAP RPPNVGGINR GSDSWEGRNA
HSHDASFSSN MDQSARFNSP NVLPKYPDEG GVSRGLATNY VRPPQQPPYH QQAPSYVNRG
PIARNEAAPR IIPIAALNPY QGRWTIKARV TTKGEMRHYN NPRGDGKVFS FDLLDSEGGE
IRVTCFNAVA DQFYQQIEAG KVYMVSRGTL RPAQKAFNHL NNEHEIVLDN TSTVQHCFEE
DNGSIPQQRF NFRPISDVEG LENNSVVDII GIVSSISPSA TIMRKNGTET QKRNLQLKDM
SGRSVELTLW GSFCNGEGQA LQNMCDSAVH PVLAVKSGRV TDFSGKSVGT FSSSQLFIEP
DFPEAKELRM WFQNEGKVAP AISISRETTA AGGGLRPDAR KTISQIKDEK LGTSEKPDWI
TVSATLTFVK MDNFCYMACP VMIGDRACNK KVVNNGDGKW RCERCDRLSD ECDYRYILQM
QIQDHTGLTW ATAFQESGEE IMGGISAKDL YRLKYDEQDD EKLAEVVRGV LFTRFVFKLK
VKEEMFSDEQ RVKSTVVKAE KVGFKTETRH LLDSIAKLKG ENPPTSSSIT ETAKSSGSNY
SNQYERSGAP PPAAFMAPPN GSMTMMMMHC SSCGGTGHNN SNCPSSATVQ SYGSGNGGMA
PVGGGNVGSG GECFKCHQFG HWARDCPNAG NAPPYASSSR YGVAPKQHVG GF
//
