MREP_FBNY2
ID MREP_FBNY2 Reviewed; 286 AA.
AC O39828;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
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.-;
DE AltName: Full=ATP-dependent helicase C2;
DE AltName: Full=Replication-associated protein 2;
DE Short=Rep2;
GN Name=DNA-R; Synonyms=C2;
OS Faba bean necrotic yellows virus (isolate SV292-88) (FBNYV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Mulpavirales; Nanoviridae; Nanovirus.
OX NCBI_TaxID=291604;
OH NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH NCBI_TaxID=3864; Lens culinaris (Lentil) (Cicer lens).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9217049; DOI=10.1006/viro.1997.8611;
RA Katul L., Maiss E., Morozov S.Y., Vetten H.J.;
RT "Analysis of six DNA components of the faba bean necrotic yellows virus
RT genome and their structural affinity to related plant virus genomes.";
RL Virology 233:247-259(1997).
RN [2]
RP STRUCTURE BY NMR OF 2-95, COFACTOR, AND CHARACTERIZATION.
RX PubMed=17472345; DOI=10.1021/bi700159q;
RA Vega-Rocha S., Gronenborn B., Gronenborn A.M., Campos-Olivas R.;
RT "Solution structure of the endonuclease domain from the master replication
RT initiator protein of the nanovirus faba bean necrotic yellows virus and
RT comparison with the corresponding geminivirus and circovirus structures.";
RL Biochemistry 46:6201-6212(2007).
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.
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;
CC Evidence={ECO:0000305|PubMed:17472345};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:17472345};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
CC {ECO:0000305|PubMed:17472345};
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.
CC -!- MISCELLANEOUS: The genome of nanoviruses is composed of six to eight
CC segments. In addition, some isolates contain subviral DNAs.
CC -!- SIMILARITY: Belongs to the nanoviridea/circoviridae replication-
CC associated protein family. {ECO:0000305}.
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DR EMBL; Y11405; CAA72209.1; -; Genomic_DNA.
DR PDB; 2HWT; NMR; -; A=2-95.
DR PDB; 6H8O; X-ray; 1.15 A; A/B=2-96.
DR PDBsum; 2HWT; -.
DR PDBsum; 6H8O; -.
DR BMRB; O39828; -.
DR SMR; O39828; -.
DR EvolutionaryTrace; O39828; -.
DR Proteomes; UP000008666; 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; IDA:CACAO.
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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Covalent protein-DNA linkage; DNA replication;
KW DNA-binding; Endonuclease; Helicase; Host nucleus; Hydrolase;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..286
FT /note="Master replication protein"
FT /id="PRO_0000318772"
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 186..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:6H8O"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:6H8O"
FT STRAND 40..52
FT /evidence="ECO:0007829|PDB:6H8O"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6H8O"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:6H8O"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:6H8O"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2HWT"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6H8O"
SQ SEQUENCE 286 AA; 33141 MW; FE878BF9336D23CD CRC64;
MARQVICWCF TLNNPLSPLS LHDSMKYLVY QTEQGEAGNI HFQGYIEMKK RTSLAGMKKL
IPGAHFEKRR GTQGEARAYS MKEDTRLEGP WEYGEFVPTI EDKLREVMND MKITGKRPIE
YIEECCNTYD KSASTLREFR GELKKKKAIS SWELQRKPWM GEVDALLQER DGRRIIWVYG
PQGGEGKTSY AKHLVKTRDA FYSTGGKTAD IAFAWDHQEL VLFDFPRSFE EYVNYGVIEQ
LKNGIIQSGK YQSVIKYSDY VEVIVFANFT PRSGMFSEDR IVYVYA
