REP_TYCS2
ID REP_TYCS2 Reviewed; 359 AA.
AC Q67620;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 (isolate Spain-2) (TYLCSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=221538;
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Reina J., Cuadrado-Gomez I.M., Jimenez J., Bejarano E.R.;
RT "Characterization of a tomato yellow leaf curl virus isolated from
RT southeast Spain (almeria).";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH HOST SCE1.
RX PubMed=14990696; DOI=10.1128/jvi.78.6.2758-2769.2004;
RA Castillo A.G., Kong L.J., Hanley-Bowdoin L., Bejarano E.R.;
RT "Interaction between a geminivirus replication protein and the plant
RT sumoylation system.";
RL J. Virol. 78:2758-2769(2004).
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 (By similarity).
CC {ECO:0000250}.
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 (By
CC similarity). Interacts with host SCE1 protein. {ECO:0000250,
CC ECO:0000269|PubMed:14990696}.
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; L27708; AAA47955.1; -; Genomic_DNA.
DR SMR; Q67620; -.
DR Proteomes; UP000008266; 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 ATP-binding; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Host nucleus; Host-virus interaction; Hydrolase;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..359
FT /note="Replication-associated protein"
FT /id="PRO_0000320113"
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 MOTIF 57..62
FT /note="RCR-2"
FT MOTIF 103..106
FT /note="RCR-3"
FT ACT_SITE 103
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
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:0000255"
SQ SEQUENCE 359 AA; 41150 MW; 89B54621D40171F3 CRC64;
MAQPKRFQIN AKHYFLTFPK CSLSKEEALE QLLQLQTPTN KKYIKICREL HEDGQPHLHM
LIQFEGKFNC KNNRFFDLVS PTRSAHFHPN IQGAKSSSDV KSYIDKDGDV LEWGTFQIDG
RSARGGQQTA NDAYAKAINA GRKSEALDVI KELAPRDYIL HFHNINSNLN MVFQVPPAPY
VSPFLSSSFD QVPDELEHWV SENVMDVAAR PWRPVSIVIE GDSRTGKTMW ARSLGPHNYL
CGHLDLSQKV YSNNAWYNVI DDVDPHYLKH FKEFMGSQRD WQSNTKYGKP IQIKGGIPTI
FLCNPGPQSS FKEYLDEEKN QTLKNWAIKN AIFVTIHQPL FTNTNQDPTP HRQEETSEA
