ID   J7K151_9GEMI            Unreviewed;       361 AA.
AC   J7K151;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Replication-associated protein {ECO:0000256|RuleBase:RU361249};
DE            Short=Rep {ECO:0000256|RuleBase:RU361249};
DE            EC=3.1.21.- {ECO:0000256|RuleBase:RU361249};
OS   Tomato leaf curl virus.
OC   Viruses; ssDNA viruses; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=28350 {ECO:0000313|EMBL:AFQ62676.1};
RN   [1] {ECO:0000313|EMBL:AFQ62676.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Raebareli {ECO:0000313|EMBL:AFQ62676.1};
RA   Aslam M., Mukherjee S.K.;
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for the replication of viral ssDNA. The closed
CC       circular ssDNA genome is first converted to a superhelical dsDNA.
CC       Rep binds a specific region at the genome origin of replication.
CC       It introduces an endonucleolytic nick within the conserved
CC       sequence 5'-TAATATTAC-3' in the intergenic region of the genome
CC       present in all geminiviruses, thereby initiating the rolling
CC       circle replication (RCR). Following cleavage, binds covalently to
CC       the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives
CC       rise to a free 3'-OH that serves as a primer for the cellular DNA
CC       polymerase. The polymerase synthesizes the (+) strand DNA by
CC       rolling circle mechanism. After one round of replication, a Rep-
CC       catalyzed nucleotidyl transfer reaction releases a circular
CC       single-stranded virus genome, thereby terminating the replication.
CC       Displays origin-specific DNA cleavage, nucleotidyl transferase,
CC       ATPase and helicase activities. {ECO:0000256|RuleBase:RU361249}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361249};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361249};
CC   -!- SUBUNIT: Homooligomer. {ECO:0000256|RuleBase:RU361249}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus
CC       {ECO:0000256|RuleBase:RU361249}.
CC   -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2
CC       is probably involved in metal coordination. RCR-3 is required for
CC       phosphodiester bond cleavage for initiation of RCR.
CC       {ECO:0000256|RuleBase:RU361249}.
CC   -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC       {ECO:0000256|RuleBase:RU361249}.
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DR   EMBL; JX232220; AFQ62676.1; -; Genomic_DNA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR   GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU361249};
KW   Covalent protein-DNA linkage {ECO:0000256|RuleBase:RU361249};
KW   DNA-binding {ECO:0000256|RuleBase:RU361249};
KW   Endonuclease {ECO:0000256|RuleBase:RU361249};
KW   Helicase {ECO:0000256|RuleBase:RU361249};
KW   Host nucleus {ECO:0000256|RuleBase:RU361249};
KW   Hydrolase {ECO:0000256|RuleBase:RU361249};
KW   Metal-binding {ECO:0000256|RuleBase:RU361249};
KW   Multifunctional enzyme {ECO:0000256|RuleBase:RU361249};
KW   Nuclease {ECO:0000256|RuleBase:RU361249};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361249};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU361249};
KW   Transferase {ECO:0000256|RuleBase:RU361249}.
FT   DOMAIN        8    119       Gemini_AL1. {ECO:0000259|Pfam:PF00799}.
FT   DOMAIN      126    230       Gemini_AL1_M. {ECO:0000259|Pfam:PF08283}.
SQ   SEQUENCE   361 AA;  40852 MW;  DE88A7074C30B66D CRC64;
     MASPRRLRVN AKNYFLTYPK CSLTKEEALS QLQTLETPTK KKFIKICREL HEDGSPHIHV
     LIQFEGKYQC KNNRFFDLVS PSRSAHFHPN IQGAKSASDV KAYIDKDGDV LEWGVFQIDG
     RSARGGQHTA NDAYAKAINT GNKDDALNVL KELAPKDYVL QFHNLNTNLD RIFQPPSEVY
     VSPFSISSFD RVPADLVDWV SSNVVCAAAR PFRSISIVIE GDSRTGKTMW ARCLGPHNYL
     CGHLDLSPKV YSNDAWYNVI DDVDPHYLKH FKEFMGAQRD WQSNTKYGKP VMIKGGIPTI
     FLCNKGPNSS YKEYLDEEKN AALKQWAIKN AVFITLEEPL YSGRENIAPT EAEEEHSQEA
     S
//