REP_BCTVC
ID REP_BCTVC Reviewed; 358 AA.
AC P14991; O39485; Q91J25;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE AltName: Full=40.8 kDa protein;
DE AltName: Full=Protein C1;
GN ORFNames=C1;
OS Beet curly top virus (strain California/Logan) (BCTV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Curtovirus.
OX NCBI_TaxID=268960;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH NCBI_TaxID=4071; Capsicum (peppers).
OH NCBI_TaxID=3650; Cucurbitaceae.
OH NCBI_TaxID=4005; Linum.
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Infectious clone pBCT028;
RX PubMed=16453696; DOI=10.1002/j.1460-2075.1986.tb04424.x;
RA Stanley J., Markham P.G., Callis R.J., Pinner M.S.;
RT "The nucleotide sequence of an infectious clone of the geminivirus beet
RT curly top virus.";
RL EMBO J. 5:1761-1767(1986).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=Infectious clone pBCT028;
RA Stanley J.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bisaro D.M., Hormuzdi S.G.;
RL Submitted (MAY-2001) 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 (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; M24597; AAA42751.2; -; Genomic_DNA.
DR EMBL; AF379637; AAK59260.1; -; Genomic_DNA.
DR PIR; S28360; S28360.
DR SMR; P14991; -.
DR Proteomes; UP000006542; 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 GO; GO:0039684; P:rolling circle single-stranded viral DNA replication; IDA:UniProtKB.
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..358
FT /note="Replication-associated protein"
FT /id="PRO_0000222201"
FT REGION 143..153
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 156..176
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 15..19
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 57..62
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 103..106
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT ACT_SITE 103
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 49
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 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 222..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 34
FT /note="G -> R (in strain: Infectious clone pBCT028)"
FT VARIANT 93
FT /note="G -> R (in strain: Infectious clone pBCT028)"
FT VARIANT 144
FT /note="E -> D (in strain: Infectious clone pBCT028)"
FT VARIANT 176
FT /note="A -> P (in strain: Infectious clone pBCT028)"
FT VARIANT 249
FT /note="L -> P (in strain: Infectious clone pBCT028)"
SQ SEQUENCE 358 AA; 40695 MW; 760FE1B9329F6FF2 CRC64;
MPPTKRFRIQ AKNIFLTYPQ CSLSKEEALE QIQGIQLSSN KKYIKIAREL HEDGQPHLHV
LLQLEGKVQI TNIRLFDLVS PTRSAHFHPN IQGAKSSSDV KSYVDKDGDT IEWGEFQIDG
RSARGGQQTA NDSYAKALNA TSLEQALQIL KEEQPKDYFL QHHNLLNNAQ KIFQRAPDPW
TPLFPLSSFT NVPEEMQEWA DAYFGVDAAA RPLRYNSIIV EGDSRTGKTM WARSLGAHNY
ITGHLDFSLR TYYDEVEYNV IDDVDPTYLK MKHWKHLIGA QKEWQTNLKY GKPRVIKGGI
PCIILCNPGP ESSYQQFLEK PENEALKSWT LHNSTFCKLQ GPLFNNQAAA SSQGDSTL
