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Master replication protein (M-Rep) (EC 2.7.7.-) (EC 3.1.21.-) (EC 3.6.1.3)

 MREP_SCSVF              Reviewed;         286 AA.
Q9ICP7;
07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
15-MAR-2017, entry version 51.
RecName: Full=Master replication protein;
Short=M-Rep;
EC=2.7.7.-;
EC=3.1.21.-;
EC=3.6.1.3;
Name=DNA-R; Synonyms=C8;
Subterranean clover stunt virus (strain F) (SCSV).
Viruses; ssDNA viruses; Nanoviridae; Nanovirus.
NCBI_TaxID=291607;
NCBI_TaxID=70936; Medicago arabica.
NCBI_TaxID=47085; Medicago lupulina.
NCBI_TaxID=70957; Medicago minima.
NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
NCBI_TaxID=3888; Pisum sativum (Garden pea).
NCBI_TaxID=74509; Trifolium cernuum.
NCBI_TaxID=97021; Trifolium dubium (Suckling clover) (Lesser trefoil).
NCBI_TaxID=74514; Trifolium glomeratum.
NCBI_TaxID=57577; Trifolium pratense (Red clover).
NCBI_TaxID=3899; Trifolium repens (Creeping white clover).
NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
NCBI_TaxID=20997; Wisteria sinensis.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10936099; DOI=10.1006/viro.2000.0439;
Timchenko T., Katul L., Sano Y., de Kouchkovsky F., Vetten H.J.,
Gronenborn B.;
"The master rep concept in nanovirus replication: identification of
missing genome components and potential for natural genetic
reassortment.";
Virology 274:189-195(2000).
-!- FUNCTION: Essential for the replication of all genomic viral ssDNA
(trans-replication). 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 conserved sequence 5'-A[GT]TATTAC-3' in 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 (By
similarity). {ECO:0000250}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; AJ290434; CAB96405.1; -; Genomic_DNA.
ProteinModelPortal; Q9ICP7; -.
SMR; Q9ICP7; -.
OrthoDB; VOG090000H6; -.
Proteomes; UP000006543; 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; Reference proteome;
Transferase.
CHAIN 1 286 Master replication protein.
/FTId=PRO_0000378521.
NP_BIND 180 188 ATP. {ECO:0000250}.
MOTIF 10 13 RCR-1. {ECO:0000250}.
MOTIF 41 46 RCR-2. {ECO:0000250}.
MOTIF 50 70 Nuclear localization signal.
{ECO:0000255}.
MOTIF 79 82 RCR-3. {ECO:0000250}.
MOTIF 96 102 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 79 79 For DNA cleavage activity. {ECO:0000250}.
METAL 33 33 Divalent metal cation. {ECO:0000255}.
METAL 41 41 Divalent metal cation. {ECO:0000255}.
METAL 84 84 Divalent metal cation. {ECO:0000255}.
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


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