MREP_BBTVA
ID MREP_BBTVA Reviewed; 286 AA.
AC Q86567;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Master replication protein;
DE Short=M-Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE EC=3.6.1.-;
GN Name=DNA-R; Synonyms=C1;
OS Banana bunchy top virus (isolate Autralia) (BBTV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Mulpavirales; Nanoviridae; Babuvirus.
OX NCBI_TaxID=645099;
OH NCBI_TaxID=4640; Musa.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8445361; DOI=10.1099/0022-1317-74-3-323;
RA Harding R.M., Burns T.M., Hafner G.J., Dietzgen R.G., Dale J.L.;
RT "Nucleotide sequence of one component of the banana bunchy top virus genome
RT contains a putative replicase gene.";
RL J. Gen. Virol. 74:323-328(1993).
CC -!- FUNCTION: Essential for the replication of all genomic viral ssDNA
CC (trans-replication). The closed circular ssDNA genome is first
CC converted to a superhelical dsDNA. Rep binds a specific hairpin at the
CC genome origin of replication. Introduces an endonucleolytic nick within
CC the conserved sequence 5'-A[GT]TATTAC-3' in the intergenic region of
CC the genome, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
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 (Potential). Rep binds to repeated DNA motifs
CC (iterons) (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
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 nanoviridea/circoviridae replication-
CC associated protein family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S56276; AAB25544.1; -; Genomic_DNA.
DR PIR; JQ1960; JQ1960.
DR RefSeq; NP_604483.1; NC_003479.1.
DR SMR; Q86567; -.
DR GeneID; 963871; -.
DR KEGG; vg:963871; -.
DR Proteomes; UP000002339; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0018142; P:protein-DNA covalent cross-linking; IEA:InterPro.
DR GO; GO:0039684; P:rolling circle single-stranded viral DNA replication; IDA:UniProtKB.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR003365; Viral_rep_N.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF02407; Viral_Rep; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Host nucleus; Hydrolase; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..286
FT /note="Master replication protein"
FT /id="PRO_0000379898"
FT MOTIF 10..13
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 41..46
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 50..70
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 79..82
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT MOTIF 96..102
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 79
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 41
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 180..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 33604 MW; 2508FC37F1AEB013 CRC64;
MARYVVCWMF TINNPTTLPV MRDEIKYMVY QVERGQEGTR HVQGYVEMKR RSSLKQMRGF
FPGAHLEKRK GSQEEARSYC MKEDTRIEGP FEFGSFKLSC NDNLFDVIQD MRETHKRPLE
YLYDCPNTFD RSKDTLYRVQ AEMNKTKAMN SWRTSFSAWT SEVENIMAQP CHRRIIWVYG
PNGGEGKTTY AKHLMKTRNA FYSPGGKSLD ICRLYNYEDI VIFDIPRCKE DYLNYGLLEE
FKNGIIQSGK YEPVLKIVEY VEVIVMANFL PKEGIFSEDR IKLVSC
