REP_MYMVV
ID REP_MYMVV Reviewed; 361 AA.
AC Q9YPS2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 Mungbean yellow mosaic virus (strain Vigna) (MYMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=223295;
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3915; Vigna mungo (Black gram) (Phaseolus mungo).
OH NCBI_TaxID=157791; Vigna radiata (Mung bean).
OH NCBI_TaxID=3916; Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15290387; DOI=10.1007/s00705-004-0313-z;
RA Karthikeyan A.S., Vanitharani R., Balaji V., Anuradha S.,
RA Thillaichidambaram P., Shivaprasad P.V., Parameswari C., Balamani V.,
RA Saminathan M., Veluthambi K.;
RT "Analysis of an isolate of Mungbean yellow mosaic virus (MYMV) with a
RT highly variable DNA B component.";
RL Arch. Virol. 149:1643-1652(2004).
RN [2]
RP CHARACTERIZATION OF THE HELICASE ACTIVITY.
RX PubMed=17142233; DOI=10.1093/nar/gkl903;
RA Choudhury N.R., Malik P.S., Singh D.K., Islam M.N., Kaliappan K.,
RA Mukherjee S.K.;
RT "The oligomeric Rep protein of Mungbean yellow mosaic India virus (MYMIV)
RT is a likely replicative helicase.";
RL Nucleic Acids Res. 34:6362-6377(2006).
RN [3]
RP FUNCTION, AND INTERACTION WITH THE HOST RAD54 PROTEIN.
RX PubMed=22171001; DOI=10.1096/fj.11-188508;
RA Kaliappan K., Choudhury N.R., Suyal G., Mukherjee S.K.;
RT "A novel role for RAD54: this host protein modulates geminiviral DNA
RT replication.";
RL FASEB J. 26:1142-1160(2012).
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:22171001}.
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). Binds to host RAD54
CC protein to ensure geminiviral replication. {ECO:0000250,
CC ECO:0000269|PubMed:22171001}.
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; AJ132575; CAA10707.1; -; Genomic_DNA.
DR SMR; Q9YPS2; -.
DR Proteomes; UP000007784; 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:0051701; P:biological process involved in interaction with host; IPI:UniProtKB.
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..361
FT /note="Replication-associated protein"
FT /id="PRO_0000320112"
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 MOTIF 57..62
FT /note="RCR-2"
FT MOTIF 103..106
FT /note="RCR-3"
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 220..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ 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
