ID   REP10_MDV1              Reviewed;         283 AA.
AC   Q9Z034;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Para-Rep C10;
DE            Short=Rep10;
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 C10;
GN   Name=C10;
OS   Milk vetch dwarf virus (isolate N) (MDV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC   Mulpavirales; Nanoviridae; Nanovirus; Milk vetch dwarf virus.
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) (Lathyrus oleraceus).
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; AB009047; BAA34048.1; -; Genomic_DNA.
DR   SMR; Q9Z034; -.
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   Gene3D; 3.40.1310.20; -; 1.
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.
DR   PROSITE; PS52020; CRESS_DNA_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..283
FT                   /note="Para-Rep C10"
FT                   /id="PRO_0000378528"
FT   DOMAIN          3..96
FT                   /note="CRESS-DNA virus Rep endonuclease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   MOTIF           10..13
FT                   /note="RCR-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   MOTIF           42..44
FT                   /note="RCR-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   MOTIF           51..71
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           79..82
FT                   /note="RCR-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
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:0000255|PROSITE-ProRule:PRU01364"
FT   BINDING         36
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         42
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         172..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   283 AA;  33383 MW;  284EA4E36AE98078 CRC64;
     MPSIRAIHWC FTLNFSGKIP EIVWTADVQY SIWQHERVNH DHLQGYIQMK KQTTLKKMKE
     LLPGAHLEMA RAPKKAIDYC QKKETAIDGP WEYGTWISTG SHKRKLMERF DEDPEEMKLE
     DPGLYRRCLS RVQMTKVREK NSWDYDLRPW QDELLKTIEQ EPDDRTILWV YGPHGGEGKS
     VFAKYLTLKE GWWYTAGGKA TDMLYSYSLD PTCHVCIDIP RCTKEEYINY AVIEQIKNRI
     IINTKYEPCT IRDDGHNVHV IVFANYLPDV TRISEDRIKI IYC
//