MREP_SCSVF
ID MREP_SCSVF Reviewed; 286 AA.
AC Q9ICP7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=C8;
OS Subterranean clover stunt virus (strain F) (SCSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Mulpavirales; Nanoviridae; Nanovirus.
OX NCBI_TaxID=291607;
OH NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10936099; DOI=10.1006/viro.2000.0439;
RA Timchenko T., Katul L., Sano Y., de Kouchkovsky F., Vetten H.J.,
RA Gronenborn B.;
RT "The master rep concept in nanovirus replication: identification of missing
RT genome components and potential for natural genetic reassortment.";
RL Virology 274:189-195(2000).
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 -!- 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; AJ290434; CAB96405.1; -; Genomic_DNA.
DR SMR; Q9ICP7; -.
DR Proteomes; UP000006543; 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 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_0000378521"
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; 33281 MW; 3E49185793F09C58 CRC64;
MARQVICWCF TLNNPLAPLS LHESMKYLVY QTEAGDNGTI HYQGYVEMKK RTSLVQMKKL
LPGAHLEKRR GSQGEARAYA MKEDSRVEGP WEFGEFKEVL EDKLRSVMED MKSTGKRPVE
YIEDCCNTYD KSSATLREFR GELKKKQAIE EWQLQRQPWM DEVERLMETK DCRRIIWVYG
PQGGEGKTSY AKHLVKTRDA FYSTGGKTAD IAFAWDHQEL VLFDFPRSFE EYVNYGVIEQ
LKNGIVQSGK YQSIVKYCNY VEVIVFANFI PRSGMFSEDR IVIVYA
