ID L0CRA1_9GEMI Unreviewed; 371 AA.
AC L0CRA1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 Turnip curly top virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Turncurtovirus.
OX NCBI_TaxID=859650 {ECO:0000313|EMBL:AGA19537.1};
RN [1] {ECO:0000313|EMBL:AGA19537.1, ECO:0000313|Proteomes:UP000232596}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IR:Hom:H6:Tur:12 {ECO:0000313|EMBL:AGA19537.1},
RC IR:Hom:H8:Tur:12 {ECO:0000313|EMBL:AGA19567.1}, IR:Lap:L16:Tur:12
RC {ECO:0000313|EMBL:AGA19519.1}, and IR:Zaf:Z2-18:Tur:12
RC {ECO:0000313|EMBL:AGA19543.1};
RX PubMed=23225113; DOI=10.1007/s11262-012-0858-y;
RA Razavinejad S., Heydarnejad J., Kamali M., Massumi H., Kraberger S.,
RA Varsani A.;
RT "Genetic diversity and host range studies of turnip curly top virus.";
RL Virus Genes 46:345-353(2013).
RN [2] {ECO:0000313|EMBL:ALR86745.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IR:Hom:Th8:Tur:12 {ECO:0000313|EMBL:ALR86745.1};
RX PubMed=26611911; DOI=10.1007/s00705-015-2686-6;
RA Kamali M., Heydarnejad J., Massumi H., Kvarnheden A., Kraberger S.,
RA Varsani A.;
RT "Molecular diversity of turncurtoviruses in Iran.";
RL Arch. Virol. 161:551-561(2016).
RN [3] {ECO:0000313|EMBL:API65457.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TCTV_IR_CZ7_2013 {ECO:0000313|EMBL:API65457.1};
RA Heydarnejad J., Pouramini N., Kamali M., Massumi H., Farkas K.,
RA Kraberger S., Varsani A.;
RT "Genomes of Beet curly top Iran virus, Oat dwarf virus, Turnip curly top
RT virus and Wheat dwarf virus identified in leafhoppers.";
RL Submitted (JUL-2016) 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|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; KC108896; AGA19519.1; -; Genomic_DNA.
DR EMBL; KC108899; AGA19537.1; -; Genomic_DNA.
DR EMBL; KC108900; AGA19543.1; -; Genomic_DNA.
DR EMBL; KC108904; AGA19567.1; -; Genomic_DNA.
DR EMBL; KT388065; ALR86745.1; -; Genomic_DNA.
DR EMBL; KX533468; API65457.1; -; Genomic_DNA.
DR Proteomes; UP000232596; Genome.
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|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}; Helicase {ECO:0000256|RuleBase:RU361249};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562,
KW ECO:0000256|RuleBase:RU361249};
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|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..243
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 371 AA; 42103 MW; 637A232FB2D33802 CRC64;
MPRTPRQYRI HAKNIFLTYP HCHLTKEEAL LQLQAIQCPS TKKFIRICRE RHDNGEPHLH
VLIQFEGKIQ LYNPRHFDLR DGGSGRICHP NIQGAKSSSD VKSYIEKDGD YIDWGEFQID
ARSARGGQQT ANDACAEALN SGTAEAALAV IREKLPKDYI FQFHNLKPNL AAIFNPPPVG
YVPKYNHTQF VLTDDILDWL ESNFFLEESN SPAGPSKYKV IPSIDRPKSI IIEGPSRTGK
TLWARSLGSH NYITGHLDFS TKVYNDDVSY NVIDDVDPHY LKMKHWKHLI GAQKEWQTNL
KYGKPRIIKG GIPSIILCNP GDGASYQNFL DKPENEALKS WSLQNSVFTT IEEPLFNITS
DQEVEDSTPS L
//
