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Para-Rep C3 (Rep3) (EC 2.7.7.-) (EC 3.1.21.-) (EC 3.6.1.3) (Replication-associated protein of non-essential DNA C3)

 REP3_MDV1               Reviewed;         284 AA.
Q9Z0D3;
07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
15-MAR-2017, entry version 59.
RecName: Full=Para-Rep C3;
Short=Rep3;
EC=2.7.7.-;
EC=3.1.21.-;
EC=3.6.1.3;
AltName: Full=Replication-associated protein of non-essential DNA C3;
Name=C3;
Milk vetch dwarf virus (isolate N) (MDV).
Viruses; ssDNA viruses; Nanoviridae; Nanovirus.
NCBI_TaxID=291605;
NCBI_TaxID=47065; Astragalus sinicus (Chinese milk vetch).
NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
NCBI_TaxID=3888; Pisum sativum (Garden pea).
NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9880029;
Sano Y., Wada M., Hashimoto Y., Matsumoto T., Kojima M.;
"Sequences of ten circular ssDNA components associated with the milk
vetch dwarf virus genome.";
J. Gen. Virol. 79:3111-3118(1998).
-!- FUNCTION: Initiates and terminates the replication only of its own
subviral DNA molecule. The closed circular ssDNA genome is first
converted to a superhelical dsDNA. Rep binds a specific hairpin at
the genome origin of replication. Introduces an endonucleolytic
nick within the intergenic region of the genome, thereby
initiating the rolling circle replication (RCR). Following
cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl
ester. The cleavage gives rise to a free 3'-OH that serves as a
primer for the cellular DNA polymerase. The polymerase synthesizes
the (+) strand DNA by rolling circle mechanism. After one round of
replication, a Rep-catalyzed nucleotidyl transfer reaction
releases a circular single-stranded virus genome, thereby
terminating the replication. Displays origin-specific DNA
cleavage, nucleotidyl transferase, ATPase and helicase activities
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
{ECO:0000250};
-!- SUBUNIT: Homooligomer (Potential). Rep binds to repeated DNA
motifs (iterons) (By similarity). {ECO:0000250, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
-!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2
is probably involved in metal coordination. RCR-3 is required for
phosphodiester bond cleavage for initiation of RCR.
-!- MISCELLANEOUS: The genome of nanoviruses is composed of six to
eight segments. In addition, some isolates contain subviral DNAs.
-!- SIMILARITY: Belongs to the nanoviridea/circoviridae replication-
associated protein family. {ECO:0000305}.
-!- CAUTION: This protein is encoded by a subviral DNA that is not
present in all isolates of the virus. {ECO:0000305}.
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EMBL; AB000922; BAA33982.1; -; Genomic_DNA.
ProteinModelPortal; Q9Z0D3; -.
SMR; Q9Z0D3; -.
OrthoDB; VOG090000BW; -.
Proteomes; UP000008236; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042624; F:ATPase activity, uncoupled; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0018142; P:protein-DNA covalent cross-linking; IEA:InterPro.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR003365; Viral_rep_N.
Pfam; PF00910; RNA_helicase; 1.
Pfam; PF02407; Viral_Rep; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Covalent protein-DNA linkage;
DNA replication; DNA-binding; Endonuclease; Helicase; Host nucleus;
Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Transferase.
CHAIN 1 284 Para-Rep C3.
/FTId=PRO_0000378524.
NP_BIND 174 182 ATP. {ECO:0000250}.
MOTIF 11 14 RCR-1. {ECO:0000250}.
MOTIF 42 47 RCR-2. {ECO:0000250}.
MOTIF 51 71 Nuclear localization signal.
{ECO:0000255}.
MOTIF 81 84 RCR-3. {ECO:0000250}.
MOTIF 98 104 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 81 81 For DNA cleavage activity. {ECO:0000250}.
METAL 36 36 Divalent metal cation. {ECO:0000255}.
METAL 42 42 Divalent metal cation. {ECO:0000255}.
METAL 86 86 Divalent metal cation. {ECO:0000255}.
SEQUENCE 284 AA; 33349 MW; C9C880B8459B3355 CRC64;
MPTVQSTCWV FTLNFKGEIP ILPFNERVQY ACWQHERVGH DHLQGFIQMK AQQSLGQMKA
IIPGAHFEKM RALNSDQAKA YAMKEDTRIE GPWEYGKYIK KGSHKRKIME RFEDDPEEMK
IEDPSLYRRC LSRKMTEEQR STAEWNYDMK PWQDQVIQEI EETPDYRKII WVYGPKGGEG
KSTFARYLSL KQGWGYLPGG PTHDMLHIIS GEPKNNWVFD IPRVASEYVN YGVLEQVKNR
VMVNTKYEPI VIRDDNHPVH VIVFANCMPD FTKISEDRMK IVHC


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