REP_TYLCI
ID REP_TYLCI Reviewed; 357 AA.
AC P27259;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 yellow leaf curl virus (strain Israel) (TYLCV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=66366;
OH NCBI_TaxID=185024; Cynanchum acutum.
OH NCBI_TaxID=145753; Malva parviflora (Little mallow) (Cheeseweed mallow).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1926771; DOI=10.1016/0042-6822(91)90763-2;
RA Navot N., Pichersky E., Zeidan M., Zamir D., Czosnek H.;
RT "Tomato yellow leaf curl virus: a whitefly-transmitted geminivirus with a
RT single genomic component.";
RL Virology 185:151-161(1991).
RN [2]
RP FUNCTION, AND COFACTOR.
RX PubMed=7732000; DOI=10.1073/pnas.92.9.3879;
RA Laufs J., Traut W., Heyraud F., Matzeit V., Rogers S.G., Schell J.,
RA Gronenborn B.;
RT "In vitro cleavage and joining at the viral origin of replication by the
RT replication initiator protein of tomato yellow leaf curl virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3879-3883(1995).
RN [3]
RP INTERACTION WITH ZEA MAYS RBR1.
RX PubMed=15078963; DOI=10.1128/jvi.78.9.4817-4826.2004;
RA Arguello-Astorga G., Lopez-Ochoa L., Kong L.-J., Orozco B.M.,
RA Settlage S.B., Hanley-Bowdoin L.;
RT "A novel motif in geminivirus replication proteins interacts with the plant
RT retinoblastoma-related protein.";
RL J. Virol. 78:4817-4826(2004).
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:0000269|PubMed:7732000}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7732000};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7732000};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
CC {ECO:0000269|PubMed:7732000};
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; X15656; CAA33688.1; -; Genomic_DNA.
DR PIR; D40779; QQCVC1.
DR SMR; P27259; -.
DR Proteomes; UP000007547; 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 1: Evidence at protein level;
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..357
FT /note="Replication-associated protein"
FT /id="PRO_0000222216"
FT REGION 141..151
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 154..174
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 13..17
FT /note="RCR-1"
FT MOTIF 55..60
FT /note="RCR-2"
FT MOTIF 101..104
FT /note="RCR-3"
FT ACT_SITE 101
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 219..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 357 AA; 40679 MW; 939AB68E1AB3B2A7 CRC64;
MPRLFKIYAK NYFLTYPNCS LSKEEALSQL KKLETPTNKK YIKVCKELHE NGEPHLHVLI
QFEGKYQCKN QRFFDLVSPN RSAHFHPNIQ AAKSSTDVKT YVEKDGNFID FGVSQIDGRS
ARGGQQSAND AYAEALNSGS KSEALNILKE KAPKDYILQF HNLSSNLDRI FSPPLEVYVS
PFLSSSFNQV PDELEEWVAE NVVYSAARPW RPISIVIEGD SRTGKTMWAR SLGPHNYLCG
HLDLSPKVYS NDAWYNVIDD VDPHYLKHFK EFMGAQRDWQ SNTKYGKPIQ IKGGIPTIFL
CNPGPTSSYR EYLDEEKNIS LKNWALKNAT FVTLYEPLFA SINQGPTQDS QEETNKA
