REP_TGMVY
ID REP_TGMVY Reviewed; 352 AA.
AC P03567;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE AltName: Full=Protein AC1;
DE AltName: Full=Protein AL1;
GN ORFNames=AC1, AL1;
OS Tomato golden mosaic virus (strain Yellow vein) (TGMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=223341;
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16453557; DOI=10.1002/j.1460-2075.1984.tb02114.x;
RA Hamilton W.D.O., Stein V.E., Coutts R.H.A., Buck K.W.;
RT "Complete nucleotide sequence of the infectious cloned DNA components of
RT tomato golden mosaic virus: potential coding regions and regulatory
RT sequences.";
RL EMBO J. 3:2197-2205(1984).
RN [2]
RP INTERACTION WITH ZEA MAYS RBR1.
RX PubMed=9271385; DOI=10.1128/mcb.17.9.5077;
RA Ach R.A., Durfee T., Miller A.B., Taranto P., Hanley-Bowdoin L.,
RA Zambryski P.C., Gruissem W.;
RT "RRB1 and RRB2 encode maize retinoblastoma-related proteins that interact
RT with a plant D-type cyclin and geminivirus replication protein.";
RL Mol. Cell. Biol. 17:5077-5086(1997).
RN [3]
RP SUBUNIT, AND INTERACTION WITH THE REPLICATION ENHANCER PROTEIN.
RX PubMed=8794317; DOI=10.1128/jvi.70.10.6790-6795.1996;
RA Settlage S.B., Miller A.B., Hanley-Bowdoin L.;
RT "Interactions between geminivirus replication proteins.";
RL J. Virol. 70:6790-6795(1996).
RN [4]
RP INTERACTION WITH ZEA MAYS RBR1 AND ARABIDOPSIS RBR1.
RX PubMed=10880461; DOI=10.1093/emboj/19.13.3485;
RA Kong L.-J., Orozco B.M., Roe J.L., Nagar S., Ou S., Feiler H.S., Durfee T.,
RA Miller A.B., Gruissem W., Robertson D., Hanley-Bowdoin L.;
RT "A geminivirus replication protein interacts with the retinoblastoma
RT protein through a novel domain to determine symptoms and tissue specificity
RT of infection in plants.";
RL EMBO J. 19:3485-3495(2000).
RN [5]
RP SUBUNIT.
RX PubMed=10692401; DOI=10.1074/jbc.275.9.6114;
RA Orozco B.M., Kong L.-J., Batts L.A., Elledge S., Hanley-Bowdoin L.;
RT "The multifunctional character of a geminivirus replication protein is
RT reflected by its complex oligomerization properties.";
RL J. Biol. Chem. 275:6114-6122(2000).
RN [6]
RP INTERACTION WITH ARABIDOPSIS THALIANA GRIK1; GRIMP AND HISTONE H3.
RX PubMed=12172024; DOI=10.1105/tpc.003681;
RA Kong L.-J., Hanley-Bowdoin L.;
RT "A geminivirus replication protein interacts with a protein kinase and a
RT motor protein that display different expression patterns during plant
RT development and infection.";
RL Plant Cell 14:1817-1832(2002).
RN [7]
RP INTERACTION WITH ZEA MAYS RBR1, AND MUTAGENESIS OF LYS-144; GLU-145;
RP GLU-146; ALA-147 AND LEU-148.
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).
RN [8]
RP INTERACTION WITH ARABIDOPSIS THALIANA GRIK1 AND GRIK2.
RX PubMed=17041027; DOI=10.1104/pp.106.088476;
RA Shen W., Hanley-Bowdoin L.;
RT "Geminivirus infection up-regulates the expression of two Arabidopsis
RT protein kinases related to yeast SNF1- and mammalian AMPK-activating
RT kinases.";
RL Plant Physiol. 142:1642-1655(2006).
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). Interacts with host
CC GRIK1, GRIK2, GRIMP and histone H3. {ECO:0000250,
CC ECO:0000269|PubMed:10692401, ECO:0000269|PubMed:10880461,
CC ECO:0000269|PubMed:12172024, ECO:0000269|PubMed:15078963,
CC ECO:0000269|PubMed:17041027, ECO:0000269|PubMed:8794317,
CC ECO:0000269|PubMed:9271385}.
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; K02029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A04170; QQCVL1.
DR SMR; P03567; -.
DR IntAct; P03567; 2.
DR PRIDE; P03567; -.
DR Proteomes; UP000007405; 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 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..352
FT /note="Replication-associated protein"
FT /id="PRO_0000222213"
FT REGION 144..154
FT /note="Binding to RBR1"
FT REGION 157..177
FT /note="Oligomerization"
FT MOTIF 16..20
FT /note="RCR-1"
FT MOTIF 58..63
FT /note="RCR-2"
FT MOTIF 104..107
FT /note="RCR-3"
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"
FT MUTAGEN 144
FT /note="K->A: 58% loss of interaction with RBR. 33% loss of
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
FT MUTAGEN 145
FT /note="E->A: 14% loss of interaction with RBR. No effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
FT MUTAGEN 146
FT /note="E->A: No effect on the interaction with RBR. No
FT effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
FT MUTAGEN 147
FT /note="A->Y: 54% loss of interaction with RBR. Almost
FT complete loss of oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
FT MUTAGEN 148
FT /note="L->G: 64% loss of interaction with RBR. 25% loss of
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
FT MUTAGEN 148
FT /note="L->I: 32% loss of interaction with RBR. Almost no
FT effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
FT MUTAGEN 148
FT /note="L->M: No loss of interaction with RBR. No effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
FT MUTAGEN 148
FT /note="L->V: 69% loss of interaction with RBR. 25% loss of
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:15078963"
SQ SEQUENCE 352 AA; 40332 MW; C33C938E9644B4A4 CRC64;
MPSHPKRFQI NAKNYFLTYP QCSLSKEESL SQLQALNTPI NKKFIKICRE LHEDGQPHLH
VLIQFEGKYC CQNQRFFDLV SPTRSAHFHP NIQRAKSSSD VKTYIDKDGD TLVWGEFQVD
GRSARGGCQT SNDAAAEALN ASSKEEALQI IREKIPEKYL FQFHNLNSNL DRIFDKTPEP
WLPPFHVSSF TNVPDEMRQW AENYFGKSSA ARPERPISII IEGDSRTGKT MWARSLGPHN
YLSGHLDLNS RVYSNKVEYN VIDDVTPQYL KLKHWKELIG AQRDWQTNCK YGKPVQIKGG
IPSIVLCNPG EGASYKVFLD KEENTPLKNW TFHNAKFVFL NSPLYQSSTQ SS
