ID   J7K151_9GEMI            Unreviewed;       361 AA.
AC   J7K151;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   02-JUN-2021, entry version 19.
DE   RecName: Full=Replication-associated protein {ECO:0000256|ARBA:ARBA00014531, 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; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; 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. 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:0000256|RuleBase:RU361249}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU361249};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601191-2};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601191-2};
CC       Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
CC       {ECO:0000256|PIRSR:PIRSR601191-2};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|RuleBase:RU361249};
CC   -!- SUBUNIT: Homooligomer. {ECO:0000256|RuleBase:RU361249}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC       ECO:0000256|RuleBase:RU361249}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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.
CC       {ECO:0000256|RuleBase:RU361249}.
CC   -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC       {ECO:0000256|ARBA:ARBA00006240, 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: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   GO; GO:0016032; P:viral process; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361249};
KW   Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124,
KW   ECO:0000256|RuleBase:RU361249};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU361249};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW   ECO:0000256|RuleBase:RU361249};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU361249};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562,
KW   ECO:0000256|RuleBase:RU361249};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361249};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601191-2};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW   ECO:0000256|RuleBase:RU361249};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU361249};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361249};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU361249};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361249}.
FT   DOMAIN          8..119
FT                   /note="Gemini_AL1"
FT                   /evidence="ECO:0000259|Pfam:PF00799"
FT   DOMAIN          126..230
FT                   /note="Gemini_AL1_M"
FT                   /evidence="ECO:0000259|Pfam:PF08283"
FT   ACT_SITE        103
FT                   /note="For DNA cleavage activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-1"
FT   METAL           49
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT   METAL           57
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT   METAL           59
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT   METAL           107
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
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
//