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Replication-associated protein (Rep) (EC 2.7.7.-) (EC 3.1.21.-) (Protein AC1) (Protein AL1)

 REP_TGMVY               Reviewed;         352 AA.
P03567;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
23-MAY-2018, entry version 83.
RecName: Full=Replication-associated protein;
Short=Rep;
EC=2.7.7.-;
EC=3.1.21.-;
AltName: Full=Protein AC1;
AltName: Full=Protein AL1;
ORFNames=AC1, AL1;
Tomato golden mosaic virus (strain Yellow vein) (TGMV).
Viruses; ssDNA viruses; Geminiviridae; Begomovirus.
NCBI_TaxID=223341;
NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16453557;
Hamilton W.D.O., Stein V.E., Coutts R.H.A., Buck K.W.;
"Complete nucleotide sequence of the infectious cloned DNA components
of tomato golden mosaic virus: potential coding regions and regulatory
sequences.";
EMBO J. 3:2197-2205(1984).
[2]
INTERACTION WITH ZEA MAYS RBR1.
PubMed=9271385; DOI=10.1128/MCB.17.9.5077;
Ach R.A., Durfee T., Miller A.B., Taranto P., Hanley-Bowdoin L.,
Zambryski P.C., Gruissem W.;
"RRB1 and RRB2 encode maize retinoblastoma-related proteins that
interact with a plant D-type cyclin and geminivirus replication
protein.";
Mol. Cell. Biol. 17:5077-5086(1997).
[3]
SUBUNIT, AND INTERACTION WITH THE REPLICATION ENHANCER PROTEIN.
PubMed=8794317;
Settlage S.B., Miller A.B., Hanley-Bowdoin L.;
"Interactions between geminivirus replication proteins.";
J. Virol. 70:6790-6795(1996).
[4]
INTERACTION WITH ZEA MAYS RBR1 AND ARABIDOPSIS RBR1.
PubMed=10880461; DOI=10.1093/emboj/19.13.3485;
Kong L.-J., Orozco B.M., Roe J.L., Nagar S., Ou S., Feiler H.S.,
Durfee T., Miller A.B., Gruissem W., Robertson D., Hanley-Bowdoin L.;
"A geminivirus replication protein interacts with the retinoblastoma
protein through a novel domain to determine symptoms and tissue
specificity of infection in plants.";
EMBO J. 19:3485-3495(2000).
[5]
SUBUNIT.
PubMed=10692401; DOI=10.1074/jbc.275.9.6114;
Orozco B.M., Kong L.-J., Batts L.A., Elledge S., Hanley-Bowdoin L.;
"The multifunctional character of a geminivirus replication protein is
reflected by its complex oligomerization properties.";
J. Biol. Chem. 275:6114-6122(2000).
[6]
INTERACTION WITH ARABIDOPSIS THALIANA GRIK1; GRIMP AND HISTONE H3.
PubMed=12172024; DOI=10.1105/tpc.003681;
Kong L.-J., Hanley-Bowdoin L.;
"A geminivirus replication protein interacts with a protein kinase and
a motor protein that display different expression patterns during
plant development and infection.";
Plant Cell 14:1817-1832(2002).
[7]
INTERACTION WITH ZEA MAYS RBR1, AND MUTAGENESIS OF LYS-144; GLU-145;
GLU-146; ALA-147 AND LEU-148.
PubMed=15078963; DOI=10.1128/JVI.78.9.4817-4826.2004;
Arguello-Astorga G., Lopez-Ochoa L., Kong L.-J., Orozco B.M.,
Settlage S.B., Hanley-Bowdoin L.;
"A novel motif in geminivirus replication proteins interacts with the
plant retinoblastoma-related protein.";
J. Virol. 78:4817-4826(2004).
[8]
INTERACTION WITH ARABIDOPSIS THALIANA GRIK1 AND GRIK2.
PubMed=17041027; DOI=10.1104/pp.106.088476;
Shen W., Hanley-Bowdoin L.;
"Geminivirus infection up-regulates the expression of two Arabidopsis
protein kinases related to yeast SNF1- and mammalian AMPK-activating
kinases.";
Plant Physiol. 142:1642-1655(2006).
-!- FUNCTION: Essential for the replication of viral ssDNA. The closed
circular ssDNA genome is first converted to a superhelical dsDNA.
Rep binds a specific region at the genome origin of replication.
It introduces an endonucleolytic nick within the conserved
sequence 5'-TAATATTAC-3' in the intergenic region of the genome
present in all geminiviruses, thereby initiating the rolling
circle replication (RCR). Following cleavage, binds covalently to
the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives
rise to a free 3'-OH that serves as a primer for the cellular DNA
polymerase. The polymerase synthesizes the (+) strand DNA by
rolling circle mechanism. After one round of replication, a Rep-
catalyzed nucleotidyl transfer reaction releases a circular
single-stranded virus genome, thereby terminating the replication.
Displays origin-specific DNA cleavage, nucleotidyl transferase,
ATPase and helicase activities (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
{ECO:0000250};
-!- SUBUNIT: Homooligomer. Interacts with the replication enhancer
protein (REn). Interacts with host retinoblastoma-related protein
1 (RBR1), and may thereby induce the transcription of host
replicative enzymes even if the cell is not dividing anymore.
Interacts with host PCNA. Interacts with host SCE1 protein (By
similarity). Interacts with host GRIK1, GRIK2, GRIMP and histone
H3. {ECO:0000250, ECO:0000269|PubMed:10692401,
ECO:0000269|PubMed:10880461, ECO:0000269|PubMed:12172024,
ECO:0000269|PubMed:15078963, ECO:0000269|PubMed:17041027,
ECO:0000269|PubMed:8794317, ECO:0000269|PubMed:9271385}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
-!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2
is probably involved in metal coordination. RCR-3 is required for
phosphodiester bond cleavage for initiation of RCR (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; K02029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A04170; QQCVL1.
ProteinModelPortal; P03567; -.
SMR; P03567; -.
IntAct; P03567; 2.
OrthoDB; VOG090000BW; -.
Proteomes; UP000007405; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0039684; P:rolling circle single-stranded viral DNA replication; IDA:UniProtKB.
InterPro; IPR001301; Gemini_AL1_CLV.
InterPro; IPR001191; Gemini_AL1_REP.
InterPro; IPR022690; Gemini_AL1_REP_cat-dom.
InterPro; IPR022692; Gemini_AL1_REP_central.
Pfam; PF00799; Gemini_AL1; 1.
Pfam; PF08283; Gemini_AL1_M; 1.
PRINTS; PR00227; GEMCOATAL1.
PRINTS; PR00228; GEMCOATCLVL1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Covalent protein-DNA linkage;
DNA replication; DNA-binding; Endonuclease; Helicase; Host nucleus;
Host-virus interaction; Hydrolase; Metal-binding;
Multifunctional enzyme; Nuclease; Nucleotide-binding;
Nucleotidyltransferase; Transferase.
CHAIN 1 352 Replication-associated protein.
/FTId=PRO_0000222213.
NP_BIND 223 230 ATP. {ECO:0000255}.
REGION 144 154 Binding to RBR1.
REGION 157 177 Oligomerization.
MOTIF 16 20 RCR-1.
MOTIF 58 63 RCR-2.
MOTIF 104 107 RCR-3.
ACT_SITE 104 104 For DNA cleavage activity. {ECO:0000250}.
METAL 50 50 Divalent metal cation. {ECO:0000255}.
METAL 58 58 Divalent metal cation. {ECO:0000255}.
METAL 60 60 Divalent metal cation. {ECO:0000255}.
METAL 108 108 Divalent metal cation. {ECO:0000255}.
MUTAGEN 144 144 K->A: 58% loss of interaction with RBR.
33% loss of oligomerization.
{ECO:0000269|PubMed:15078963}.
MUTAGEN 145 145 E->A: 14% loss of interaction with RBR.
No effect on oligomerization.
{ECO:0000269|PubMed:15078963}.
MUTAGEN 146 146 E->A: No effect on the interaction with
RBR. No effect on oligomerization.
{ECO:0000269|PubMed:15078963}.
MUTAGEN 147 147 A->Y: 54% loss of interaction with RBR.
Almost complete loss of oligomerization.
{ECO:0000269|PubMed:15078963}.
MUTAGEN 148 148 L->G: 64% loss of interaction with RBR.
25% loss of oligomerization.
{ECO:0000269|PubMed:15078963}.
MUTAGEN 148 148 L->I: 32% loss of interaction with RBR.
Almost no effect on oligomerization.
{ECO:0000269|PubMed:15078963}.
MUTAGEN 148 148 L->M: No loss of interaction with RBR. No
effect on oligomerization.
{ECO:0000269|PubMed:15078963}.
MUTAGEN 148 148 L->V: 69% loss of interaction with RBR.
25% loss of oligomerization.
{ECO:0000269|PubMed:15078963}.
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


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