REP2_MDV1
ID REP2_MDV1 Reviewed; 282 AA.
AC Q9Z0D4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Para-Rep C2;
DE Short=Rep2;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE EC=3.6.1.-;
DE AltName: Full=Replication-associated protein of non-essential DNA C2;
GN Name=C2;
OS Milk vetch dwarf virus (isolate N) (MDV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Mulpavirales; Nanoviridae; Nanovirus.
OX NCBI_TaxID=291605;
OH NCBI_TaxID=47065; Astragalus sinicus (Chinese milk vetch).
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9880029; DOI=10.1099/0022-1317-79-12-3111;
RA Sano Y., Wada M., Hashimoto Y., Matsumoto T., Kojima M.;
RT "Sequences of ten circular ssDNA components associated with the milk vetch
RT dwarf virus genome.";
RL J. Gen. Virol. 79:3111-3118(1998).
CC -!- FUNCTION: Initiates and terminates the replication only of its own
CC subviral DNA molecule. 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 intergenic region of the genome, thereby initiating the rolling
CC circle replication (RCR). Following cleavage, binds covalently to the
CC 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a
CC free 3'-OH that serves as a primer for the cellular DNA polymerase. The
CC polymerase synthesizes the (+) strand DNA by rolling circle mechanism.
CC After one round of replication, a Rep-catalyzed nucleotidyl transfer
CC reaction releases a circular single-stranded virus genome, thereby
CC terminating the replication. Displays origin-specific DNA cleavage,
CC nucleotidyl transferase, ATPase and helicase activities (By
CC similarity). {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.
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}.
CC -!- CAUTION: This protein is encoded by a subviral DNA that is not present
CC in all isolates of the virus. {ECO:0000305}.
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DR EMBL; AB000921; BAA33981.1; -; Genomic_DNA.
DR SMR; Q9Z0D4; -.
DR Proteomes; UP000008236; 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; Transferase.
FT CHAIN 1..282
FT /note="Para-Rep C2"
FT /id="PRO_0000378522"
FT MOTIF 8..11
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 47..52
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 56..77
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 86..89
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT MOTIF 99..105
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 86
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 47
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 174..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 282 AA; 32682 MW; 6E8CE00C0BB7462E CRC64;
MASKRWCFTL NYKTALERET FISLFSRDEL NYFVCGDEIA PTTGQKHLQG YVSMKKLIRL
GGLKKKFGSI AHWEIAKGDD FQNRDYCTKE TLIAEIGAPV KKGSNRRKIM EIYEEDPEEM
KLRDPDTALR CKAKKLREEY CSEVSVFSLR PWQIELHRAL MEVPDDRTII WAYGPDGGEG
KSTFAKELIK YGWFYTAGGK TQDILYMYAQ DPERNIAFDV PRCSSEMMNY QAMEMMKNRV
FASTKYRPVD LCIRKKVHLI VFANVAPDPT KLSEDRIVII NC
