REP_BGYMJ
ID REP_BGYMJ Reviewed; 353 AA.
AC P0CK40; P05175; P87726;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE AltName: Full=40.2 kDa protein;
DE AltName: Full=Protein AC1;
DE AltName: Full=Protein AL1;
GN ORFNames=AC1, AL1;
OS Bean golden yellow mosaic virus (isolate Puerto Rico-Japan) (BGYMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=222449;
OH NCBI_TaxID=260885; Macroptilium lathyroides.
OH NCBI_TaxID=108453; Malvastrum coromandelianum.
OH NCBI_TaxID=3884; Phaseolus lunatus (Lima bean) (Phaseolus limensis).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Puerto Rico-Japan;
RX PubMed=3037283; DOI=10.1111/j.1348-0421.1987.tb03078.x;
RA Morinaga T., Ikegami M., Shimotohno K., Miura K.;
RT "Total nucleotide sequences of the infectious cloned DNAs of bean golden
RT mosaic virus.";
RL Microbiol. Immunol. 31:147-154(1987).
RN [2]
RP FUNCTION, AND INTERACTION WITH THE HOST RAD54 PROTEIN.
RC STRAIN=Mungbean yellow mosaic virus, and Tomato leaf curl virus;
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; D00201; BAA00140.1; -; Genomic_DNA.
DR RefSeq; NP_040770.1; NC_001439.1.
DR SMR; P0CK40; -.
DR PRIDE; P0CK40; -.
DR GeneID; 988086; -.
DR KEGG; vg:988086; -.
DR Proteomes; UP000008769; 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 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..353
FT /note="Replication-associated protein"
FT /id="PRO_0000415532"
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 222..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 353 AA; 40228 MW; FFD9EE57A5811A54 CRC64;
MPPPQRFRVQ SKNYFLTYPR CTIPKEEALS QLQKIHTTTN KKFIKVCEER HDNGEPHLHA
LIQFEGKFIC TNKRLFDLVS TTRSAHFHPN IQGAKSSSDV KEYIDKDGVT IEWGQFQVDG
RSARGGQQSA NDSYAKALNA DSIESALTIL KEEQPKDYVL QNHNIRSNLE RIFFKVPEPW
VPPFPLSSFV NIPVVMQDWV DDYFGRGSAA RPERPISIIV EGDSRTGKTM WARALGPHNY
LSGHLDFNSR VYSNSVEYNV IDDISPNYLK LKHWKELIGA QKDWQSNCKY GKPVQIKGGI
PSIVLCNPGE GSSYKDFLNK EENRALHNWT IHNAIFVTLT APLYQSTAQD CQT
