ID A1XA40_TYCSV Unreviewed; 74 AA.
AC A1XA40;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=Replication-associated protein {ECO:0000256|ARBA:ARBA00014531};
DE Flags: Fragment;
GN Name=C1 {ECO:0000313|EMBL:ABC71744.1};
OS Tomato yellow leaf curl Sardinia virus (TYLCSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=123735 {ECO:0000313|EMBL:ABC71744.1};
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] {ECO:0000313|EMBL:ABC71744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IT:T538:02 {ECO:0000313|EMBL:ABC71744.1};
RX PubMed=17070885; DOI=10.1016/j.virol.2006.09.030;
RA Garcia-Andres S., Accotto G.P., Navas-Castillo J., Moriones E.;
RT "Founder effect, plant host, and recombination shape the emergent
RT population of begomoviruses that cause the tomato yellow leaf curl disease
RT in the Mediterranean basin.";
RL Virology 359:302-312(2007).
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|ARBA:ARBA00024923}.
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 -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC {ECO:0000256|ARBA:ARBA00006240}.
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DR EMBL; DQ317804; ABC71744.1; -; Genomic_DNA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 Gene3D; 3.40.1310.20; -; 1.
DR InterPro; IPR001301; Gemini_AL1_CLV.
DR InterPro; IPR001191; Gemini_AL1_REP.
DR InterPro; IPR022690; Gemini_AL1_REP_cat-dom.
DR Pfam; PF00799; Gemini_AL1; 1.
DR PRINTS; PR00227; GEMCOATAL1.
DR PRINTS; PR00228; GEMCOATCLVL1.
DR SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601191-2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Geminivirus AL1 replication-associated protein
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00799"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT NON_TER 74
FT /evidence="ECO:0000313|EMBL:ABC71744.1"
SQ SEQUENCE 74 AA; 8682 MW; 9A1B03A4CE6B5E82 CRC64;
MPRSGRFSIK AKNYFLTYPK CDLTKENALS QITNLQTPTN KLFIKICREL HENGEPHLHV
LIQFEGKYNC TNQR
//
