ID Q2L8B9_9GEMI Unreviewed; 347 AA.
AC Q2L8B9;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 44.
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};
GN Name=AL1 {ECO:0000313|EMBL:ABC74546.1};
OS Tomato chino La Paz virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=240492 {ECO:0000313|EMBL:ABC74546.1};
RN [1] {ECO:0000313|EMBL:ABC74546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Solanum MM4 {ECO:0000313|EMBL:ABC74546.1};
RA Gregorio-Jorge J., Mauricio-Castillo J.A., Ambriz-Granados S.,
RA Alpuche-Solis A.G., Arguello-Astorga G.R.;
RT "Tomato chino La Paz virus isolated from the weed Solanum rostratum coexist
RT with several begomoviruses in mixed infections.";
RL Submitted (JAN-2006) 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|ARBA:ARBA00024923, 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|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; DQ347949; ABC74546.1; -; 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 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 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.
DR SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
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..120
FT /note="Geminivirus AL1 replication-associated protein
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00799"
FT DOMAIN 127..232
FT /note="Geminivirus AL1 replication-associated protein
FT central"
FT /evidence="ECO:0000259|Pfam:PF08283"
FT ACT_SITE 104
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-1"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
SQ SEQUENCE 347 AA; 39641 MW; A701008D8AE29A78 CRC64;
MPLVPKKFLI NSKNYFLTYP HCSLSKEETL EQLLRLSTPT NKKYIKIARE LHEDGEYHLH
VLIQFEGKFK TQNCRFFDLV SSTRSTHFHP NVQGAKSSTD VKSYVDKDGD TIEWGDFQID
GRSARGGQQT ANDAAAEALN ASSKEEAMRI IKEKLPKEFL FQYHNLFSNL DRVFAKAPEP
WVPPFPISSL TNVPDEMQEW ADDYFGRGAA ARPERPISII IEGDSRTGKT MWARALGPHN
YLSGHLDFNP RVYSNEVEYN VIDDVTPQYL KMKHWKELIG AQRDWQSNCK YGKPVQIKGG
IPSIVLCNPG EGASYKSFLD KEDNAALKDW TIYNAKFIFL NSTLYQA
//
