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

 REP_MYMVV               Reviewed;         361 AA.
Q9YPS2;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 63.
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;
Mungbean yellow mosaic virus (strain Vigna) (MYMV).
Viruses; ssDNA viruses; Geminiviridae; Begomovirus.
NCBI_TaxID=223295;
NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
NCBI_TaxID=3915; Vigna mungo (Black gram) (Phaseolus mungo).
NCBI_TaxID=157791; Vigna radiata (Mung bean).
NCBI_TaxID=3916; Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15290387; DOI=10.1007/s00705-004-0313-z;
Karthikeyan A.S., Vanitharani R., Balaji V., Anuradha S.,
Thillaichidambaram P., Shivaprasad P.V., Parameswari C., Balamani V.,
Saminathan M., Veluthambi K.;
"Analysis of an isolate of Mungbean yellow mosaic virus (MYMV) with a
highly variable DNA B component.";
Arch. Virol. 149:1643-1652(2004).
[2]
CHARACTERIZATION OF THE HELICASE ACTIVITY.
PubMed=17142233; DOI=10.1093/nar/gkl903;
Choudhury N.R., Malik P.S., Singh D.K., Islam M.N., Kaliappan K.,
Mukherjee S.K.;
"The oligomeric Rep protein of Mungbean yellow mosaic India virus
(MYMIV) is a likely replicative helicase.";
Nucleic Acids Res. 34:6362-6377(2006).
[3]
FUNCTION, AND INTERACTION WITH THE HOST RAD54 PROTEIN.
PubMed=22171001; DOI=10.1096/fj.11-188508;
Kaliappan K., Choudhury N.R., Suyal G., Mukherjee S.K.;
"A novel role for RAD54: this host protein modulates geminiviral DNA
replication.";
FASEB J. 26:1142-1160(2012).
-!- 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. {ECO:0000269|PubMed:22171001}.
-!- 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). Binds to host RAD54 protein to ensure geminiviral
replication. {ECO:0000250, ECO:0000269|PubMed:22171001}.
-!- 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; AJ132575; CAA10707.1; -; Genomic_DNA.
ProteinModelPortal; Q9YPS2; -.
SMR; Q9YPS2; -.
Proteomes; UP000007784; 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:0051701; P:interaction with host; IPI:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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; Reference proteome; Transferase.
CHAIN 1 361 Replication-associated protein.
/FTId=PRO_0000320112.
NP_BIND 220 227 ATP. {ECO:0000255}.
REGION 143 153 Binding to RBR1. {ECO:0000250}.
REGION 156 176 Oligomerization. {ECO:0000250}.
MOTIF 15 19 RCR-1.
MOTIF 57 62 RCR-2.
MOTIF 103 106 RCR-3.
ACT_SITE 103 103 For DNA cleavage activity. {ECO:0000250}.
METAL 49 49 Divalent metal cation. {ECO:0000255}.
METAL 57 57 Divalent metal cation. {ECO:0000255}.
METAL 59 59 Divalent metal cation. {ECO:0000255}.
METAL 107 107 Divalent metal cation. {ECO:0000255}.
SEQUENCE 361 AA; 40677 MW; 6327D91D9996D1DF CRC64;
MPRLGRFAIN AKNYFLTYPR CPLTKEDVLE QLLALSTPVN KKFIRVCREL HEDGEPHLHV
LLQFEGKLQT KNERFFDLVS PTRSTHYHPN IQAAKSASDV KSYMDKDGDV LDHGSFQVDG
RSARGGKQSA NDAYAEALNS GSKLQALNIL REKAPKDYIL QFHNLNCNLS RIFADDVPPY
VSPYSLSAFD KVPSYISSWA SENVRDSCAP ERPISIVIEG DSRTGKTMWA RALGPHNYLC
GHLDLNSKIY SNDAWYNVID DVDPHYLKHF KEFMGAQRDW QSNVKYGKPT HIKGGIPTIF
LCNPGPKSSY KEYLDEPDNT ALKLWASKNA EFYTLKEPLF SSVDQGATQG CQEASNSTLS
N


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