REP_TYCSV
ID REP_TYCSV Reviewed; 359 AA.
AC P27260;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE AltName: Full=Protein C1;
GN ORFNames=C1;
OS Tomato yellow leaf curl Sardinia virus (TYLCSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=123735;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH NCBI_TaxID=185024; Cynanchum acutum.
OH NCBI_TaxID=145753; Malva parviflora (Little mallow) (Cheeseweed mallow).
OH NCBI_TaxID=29728; Sinapis arvensis (Charlock mustard) (Brassica kaber).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840676; DOI=10.1093/nar/19.24.6763;
RA Kheyr-Pour A., Bendahmane M., Matzeit V., Accotto G.P., Crespi S.,
RA Gronenborn B.;
RT "Tomato yellow leaf curl virus from Sardinia is a whitefly-transmitted
RT monopartite geminivirus.";
RL Nucleic Acids Res. 19:6763-6769(1991).
RN [2]
RP FUNCTION.
RX PubMed=1630899; DOI=10.1093/nar/20.13.3279;
RA Ilyina T.V., Koonin E.V.;
RT "Conserved sequence motifs in the initiator proteins for rolling circle DNA
RT replication encoded by diverse replicons from eubacteria, eucaryotes and
RT archaebacteria.";
RL Nucleic Acids Res. 20:3279-3285(1992).
RN [3]
RP ACTIVE SITE, AND MUTAGENESIS OF TYR-103.
RX PubMed=8543063; DOI=10.1016/0014-5793(95)01355-5;
RA Laufs J., Schumacher S., Geisler N., Jupin I., Gronenborn B.;
RT "Identification of the nicking tyrosine of geminivirus Rep protein.";
RL FEBS Lett. 377:258-262(1995).
RN [4]
RP FUNCTION.
RX PubMed=7777563; DOI=10.1073/pnas.92.12.5640;
RA Desbiez C., David C., Mettouchi A., Laufs J., Gronenborn B.;
RT "Rep protein of tomato yellow leaf curl geminivirus has an ATPase activity
RT required for viral DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5640-5644(1995).
RN [5]
RP INTERACTION WITH SOLANUM LYCOPERSICUM PCNA.
RX PubMed=12919743; DOI=10.1016/s0042-6822(03)00234-4;
RA Castillo A.G., Collinet D., Deret S., Kashoggi A., Bejarano E.R.;
RT "Dual interaction of plant PCNA with geminivirus replication accessory
RT protein (Ren) and viral replication protein (Rep).";
RL Virology 312:381-394(2003).
RN [6]
RP CHARACTERIZATION OF THE HELICASE ACTIVITY, AND SUBUNIT.
RX PubMed=16943286; DOI=10.1128/jvi.00924-06;
RA Clerot D., Bernardi F.;
RT "DNA helicase activity is associated with the replication initiator protein
RT rep of tomato yellow leaf curl geminivirus.";
RL J. Virol. 80:11322-11330(2006).
RN [7]
RP STRUCTURE BY NMR OF 4-121.
RX PubMed=12130667; DOI=10.1073/pnas.152342699;
RA Campos-Olivas R., Louis J.M., Clerot D., Gronenborn B., Gronenborn A.M.;
RT "The structure of a replication initiator unites diverse aspects of nucleic
RT acid metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10310-10315(2002).
CC -!- FUNCTION: Essential for the replication of viral ssDNA. The closed
CC circular ssDNA genome is first converted to a superhelical dsDNA. Rep
CC binds a specific region at the genome origin of replication. It
CC introduces an endonucleolytic nick within the conserved sequence 5'-
CC TAATATTAC-3' in the intergenic region of the genome present in all
CC geminiviruses, thereby initiating the rolling circle replication (RCR).
CC Following cleavage, binds covalently to the 5'-phosphate of DNA as a
CC tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a
CC primer for the cellular DNA polymerase. The polymerase synthesizes the
CC (+) strand DNA by rolling circle mechanism. After one round of
CC replication, a Rep-catalyzed nucleotidyl transfer reaction releases a
CC circular single-stranded virus genome, thereby terminating the
CC replication. Displays origin-specific DNA cleavage, nucleotidyl
CC transferase, ATPase and helicase activities.
CC {ECO:0000269|PubMed:1630899, ECO:0000269|PubMed:16943286,
CC ECO:0000269|PubMed:7777563}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000250};
CC -!- SUBUNIT: Homooligomer. Interacts with the replication enhancer protein
CC (REn). Interacts with host retinoblastoma-related protein 1 (RBR1), and
CC may thereby induce the transcription of host replicative enzymes even
CC if the cell is not dividing anymore. Interacts with host PCNA.
CC Interacts with host SCE1 protein. {ECO:0000269|PubMed:12919743}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2 is
CC probably involved in metal coordination. RCR-3 is required for
CC phosphodiester bond cleavage for initiation of RCR (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC {ECO:0000305}.
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DR EMBL; X61153; CAA43466.1; -; Genomic_DNA.
DR PIR; S22593; S22593.
DR RefSeq; NP_620741.1; NC_003828.1.
DR PDB; 1L2M; NMR; -; A=4-121.
DR PDB; 1L5I; NMR; -; A=4-121.
DR PDBsum; 1L2M; -.
DR PDBsum; 1L5I; -.
DR BMRB; P27260; -.
DR SMR; P27260; -.
DR GeneID; 944425; -.
DR KEGG; vg:944425; -.
DR EvolutionaryTrace; P27260; -.
DR Proteomes; UP000002323; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR001301; Gemini_AL1_CLV.
DR InterPro; IPR001191; Gemini_AL1_REP.
DR InterPro; IPR022690; Gemini_AL1_REP_cat-dom.
DR InterPro; IPR022692; Gemini_AL1_REP_central.
DR Pfam; PF00799; Gemini_AL1; 1.
DR Pfam; PF08283; Gemini_AL1_M; 1.
DR PRINTS; PR00227; GEMCOATAL1.
DR PRINTS; PR00228; GEMCOATCLVL1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Covalent protein-DNA linkage; DNA replication;
KW DNA-binding; Endonuclease; Helicase; Host nucleus; Host-virus interaction;
KW Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..359
FT /note="Replication-associated protein"
FT /id="PRO_0000222218"
FT REGION 143..153
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 156..176
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 15..19
FT /note="RCR-1"
FT /evidence="ECO:0000303|PubMed:1630899"
FT MOTIF 57..63
FT /note="RCR-2"
FT /evidence="ECO:0000303|PubMed:1630899"
FT MOTIF 103..106
FT /note="RCR-3"
FT /evidence="ECO:0000303|PubMed:1630899"
FT ACT_SITE 103
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000269|PubMed:8543063"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:7777563"
FT MUTAGEN 103
FT /note="Y->F: Complete loss of replication, DNA cleavage and
FT nucleotidyl transfer activity."
FT /evidence="ECO:0000269|PubMed:8543063"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:1L2M"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:1L2M"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:1L2M"
FT STRAND 56..69
FT /evidence="ECO:0007829|PDB:1L2M"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1L2M"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1L2M"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:1L2M"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1L2M"
SQ SEQUENCE 359 AA; 40734 MW; 9717B4A07C93EFA7 CRC64;
MPRSGRFSIK AKNYFLTYPK CDLTKENALS QITNLQTPTN KLFIKICREL HENGEPHLHI
LIQFEGKYNC TNQRFFDLVS PTRSAHFHPN IQGAKSSSDV KSYIDKDGDV LEWGTFQIDG
RSARGGQQTA NDAYAKAINA GSKSQALDVI KELAPRDYVL HFHNINSNLD KVFQVPPAPY
VSPFLSSSFD QVPDELEHWV SENVMDAAAR PWRPVSIVIE GDSRTGKTTW ARSLGPHNYL
CGHLDLSQKV YSNNAWYNVI DDVDPHYLKH FKEFMGAQRD WQSNTKYGKP IQIKGGIPTI
FLCNPGPQSS FKEYLDEEKN QALKNWATKN AIFVTIHQPL FADTNQNTTS HRQEEASEA
