Master replication protein - Subterranean clover stunt virus (strain F) (SCSV)

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Q9ICP7 (MREP_SCSVF) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 38. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Master replication protein
Short name=M-Rep
EC=2.7.7.-
EC=3.1.21.-
EC=3.6.1.3

Gene names

Name:	DNA-R
Synonyms:	C8

Organism

Subterranean clover stunt virus (strain F) (SCSV) [Reference proteome]

Taxonomic identifier

291607 [NCBI]

Taxonomic lineage

Viruses › ssDNA viruses › Nanoviridae › Nanovirus ›

Virus host

Medicago arabica [TaxID: 70936]
Medicago lupulina [TaxID: 47085]
Medicago minima [TaxID: 70957]
Phaseolus vulgaris (Kidney bean) (French bean) [TaxID: 3885]
Pisum sativum (Garden pea) [TaxID: 3888]
Trifolium cernuum [TaxID: 74509]
Trifolium dubium (Suckling clover) (Lesser trefoil) [TaxID: 97021]
Trifolium glomeratum [TaxID: 74514]
Trifolium pratense (Red clover) [TaxID: 57577]
Trifolium repens (Creeping white clover) [TaxID: 3899]
Trifolium subterraneum (Subterranean clover) [TaxID: 3900]
Vicia faba (Broad bean) (Faba vulgaris) [TaxID: 3906]
Wisteria sinensis [TaxID: 20997]

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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.
Catalytic activity	ATP + H₂O = ADP + phosphate.
Cofactor	Divalent metal cations, possibly magnesium or manganese By similarity.
Subunit structure	Homooligomer Potential. Rep binds to repeated DNA motifs (iterons) By similarity.
Subcellular location	Host nucleus Potential.
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.
Miscellaneous	The genome of nanoviruses is composed of six to eight segments. In addition, some isolates contain subviral DNAs.
Sequence similarities	Belongs to the nanoviridea/circoviridae replication-associated protein family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Host nucleus
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding
Molecular function	Endonuclease Helicase Hydrolase Nuclease Nucleotidyltransferase Transferase
PTM	Covalent protein-DNA linkage
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC DNA replication Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC protein-DNA covalent cross-linking Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, uncoupled Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro RNA helicase activity Inferred from electronic annotation. Source: InterPro endodeoxyribonuclease activity, producing 5'-phosphomonoesters Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotidyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 286

286

Master replication protein

PRO_0000378521

Regions

Nucleotide binding

180 – 188

ATP By similarity

Motif

10 – 13

RCR-1 By similarity

Motif

41 – 46

RCR-2 By similarity

Motif

50 – 70

Nuclear localization signal Potential

Motif

79 – 82

RCR-3 By similarity

Motif

96 – 102

Nuclear localization signal Potential

Sites

Active site

For DNA cleavage activity By similarity

Metal binding

Divalent metal cation Potential

Metal binding

Divalent metal cation Potential

Metal binding

Divalent metal cation Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ICP7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3E49185793F09C58
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FASTA

286

33,281

        10         20         30         40         50         60 
MARQVICWCF TLNNPLAPLS LHESMKYLVY QTEAGDNGTI HYQGYVEMKK RTSLVQMKKL 

        70         80         90        100        110        120 
LPGAHLEKRR GSQGEARAYA MKEDSRVEGP WEFGEFKEVL EDKLRSVMED MKSTGKRPVE 

       130        140        150        160        170        180 
YIEDCCNTYD KSSATLREFR GELKKKQAIE EWQLQRQPWM DEVERLMETK DCRRIIWVYG 

       190        200        210        220        230        240 
PQGGEGKTSY AKHLVKTRDA FYSTGGKTAD IAFAWDHQEL VLFDFPRSFE EYVNYGVIEQ 

       250        260        270        280 
LKNGIVQSGK YQSIVKYCNY VEVIVFANFI PRSGMFSEDR IVIVYA

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References

[1]

"The master rep concept in nanovirus replication: identification of missing genome components and potential for natural genetic reassortment."
Timchenko T., Katul L., Sano Y., de Kouchkovsky F., Vetten H.J., Gronenborn B.
Virology 274:189-195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ290434 Genomic DNA. Translation: CAB96405.1.
RefSeq	NP_620694.1. NC_003812.1.
3D structure databases
ProteinModelPortal	Q9ICP7.
SMR	Q9ICP7. Positions 2-95.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	991157.
Family and domain databases
InterPro	IPR000605. Helicase_SF3_ssDNA/RNA_vir. IPR003365. Viral_rep_N. [Graphical view]
Pfam	PF00910. RNA_helicase. 1 hit. PF02407. Viral_Rep. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MREP_SCSVF

Accession

Primary (citable) accession number: Q9ICP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 7, 2009
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Entry information

Relevant documents