REP_TPCTV
ID REP_TPCTV Reviewed; 349 AA.
AC Q88888;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE AltName: Full=Protein C1;
GN ORFNames=C1;
OS Tomato pseudo-curly top virus (TPCTV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Topocuvirus.
OX NCBI_TaxID=49267;
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8638404; DOI=10.1006/viro.1996.0264;
RA Briddon R.W., Bedford I.D., Tsai J.H., Markham P.G.;
RT "Analysis of the nucleotide sequence of the treehopper-transmitted
RT geminivirus, tomato pseudo-curly top virus, suggests a recombinant
RT origin.";
RL Virology 219:387-394(1996).
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 (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000250};
CC -!- SUBUNIT: Homooligomer. Interacts with the replication enhancer protein
CC (REn). Interacts with host retinoblastoma-related protein 1 (RBR1), and
CC may thereby induce the transcription of host replicative enzymes even
CC if the cell is not dividing anymore. Interacts with host PCNA.
CC Interacts with host SCE1 protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC {ECO:0000305}.
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DR EMBL; X84735; CAA59223.1; -; Genomic_DNA.
DR RefSeq; NP_620735.1; NC_003825.1.
DR SMR; Q88888; -.
DR GeneID; 944407; -.
DR KEGG; vg:944407; -.
DR Proteomes; UP000007068; Genome.
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 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; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Host nucleus; Host-virus interaction; Hydrolase;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..349
FT /note="Replication-associated protein"
FT /id="PRO_0000323704"
FT REGION 144..154
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 157..177
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 16..20
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 58..63
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 104..107
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT ACT_SITE 104
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 349 AA; 39843 MW; 79EB0D0870C70FE1 CRC64;
MPSNPKRFQI AAKNYFLTYP NCSLSKEEAL DQLQRLQTPT NKKYIKVARE LHENGEPHLH
VLIQFEGKFN CKNQRFFDLV SPTRSTHFHP NIQGAKSSSD VNSYVDKDGD TIEWGEFQID
ARSARGGQQT ANDECAEALN RSSKEEALQI IKEKLPKDFL FCYHNLVSNL DRIFTPAPTP
FVPPFQLSSF TNVPEDMQEW ADDYFGVSAA ARPMRYKSII IEGESRTGKT MWARSLGPHN
YLSGHLDFNS RVYSNSALYN VIDDVTPHYL KLKHWKELIG AQRDWQSNCK YGKPVQIKGG
IPSIVLCNPG GDTSFQDFLD KEENEALKDW TLYNAVFIKL TEPLYDGTV
