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Q66862

- REP1_FBNY2

UniProt

Q66862 - REP1_FBNY2

Protein

Para-Rep C1

Gene

C1

Organism
Faba bean necrotic yellows virus (isolate SV292-88) (FBNYV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Divalent metal cations, possibly magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi33 – 331Divalent metal cationSequence Analysis
    Metal bindingi39 – 391Divalent metal cationSequence Analysis
    Active sitei78 – 781For DNA cleavage activity
    Metal bindingi83 – 831Divalent metal cationSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi176 – 1783ATPCurated

    GO - Molecular functioni

    1. ATPase activity Source: CACAO
    2. ATPase activity, uncoupled Source: InterPro
    3. ATP binding Source: UniProtKB-KW
    4. DNA binding Source: UniProtKB-KW
    5. endodeoxyribonuclease activity, producing 5'-phosphomonoesters Source: InterPro
    6. metal ion binding Source: UniProtKB-KW
    7. nucleotidyltransferase activity Source: CACAO
    8. RNA binding Source: InterPro
    9. RNA helicase activity Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA replication Source: UniProtKB-KW
    3. protein-DNA covalent cross-linking Source: InterPro
    4. viral DNA cleavage involved in viral genome maturation Source: CACAO

    Keywords - Molecular functioni

    Endonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Para-Rep C1 (EC:2.7.7.-, EC:3.1.21.-, EC:3.6.1.3)
    Short name:
    Rep1
    Alternative name(s):
    ATP-dependent helicase C1
    Replication-associated protein of non-essential DNA C1
    Gene namesi
    Name:C1
    ORF Names:ORF1
    OrganismiFaba bean necrotic yellows virus (isolate SV292-88) (FBNYV)
    Taxonomic identifieri291604 [NCBI]
    Taxonomic lineageiVirusesssDNA virusesNanoviridaeNanovirus
    Virus hostiCicer arietinum (Chickpea) (Garbanzo) [TaxID: 3827]
    Lens culinaris (Lentil) (Cicer lens) [TaxID: 3864]
    Phaseolus vulgaris (Kidney bean) (French bean) [TaxID: 3885]
    Vicia faba (Broad bean) (Faba vulgaris) [TaxID: 3906]
    ProteomesiUP000008666: Genome

    Subcellular locationi

    Host nucleus Curated

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781Y → F: Complete loss of DNA cleavage and nucleotidyl transfer activity. 1 Publication
    Mutagenesisi177 – 1771K → A: Complete loss of ATPase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 278278Para-Rep C1PRO_0000222439Add
    BLAST

    Keywords - PTMi

    Covalent protein-DNA linkage

    Interactioni

    Subunit structurei

    Homooligomer Potential. Rep binds to repeated DNA motifs (iterons) By similarity.By similarityCurated

    Structurei

    3D structure databases

    ProteinModelPortaliQ66862.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi8 – 114RCR-1By similarity
    Motifi39 – 446RCR-2By similarity
    Motifi48 – 6922Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi78 – 814RCR-3By similarity
    Motifi95 – 1017Nuclear localization signalSequence Analysis

    Domaini

    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.

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR003365. Viral_rep_N.
    [Graphical view]
    PfamiPF00910. RNA_helicase. 1 hit.
    PF02407. Viral_Rep. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q66862-1 [UniParc]FASTAAdd to Basket

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    MACSNWVFTR NFQGALPLLS FDERVQYAVW QHERGTHDHI QGVIQLKKKA    50
    RFSTVKEIIG GNPHVEKMKG TIEEASAYVQ KEETRVAGPW SYGDLLKRGS 100
    HRRKTMERYL EDPEEMQLKD PDTALRCNAK RLKEDFMKEK TKLQLRPWQK 150
    ELHDLILTEP DDRTIIWVYG PDGGEGKSMF AKELIKYGWF YTAGGKTQDI 200
    LYMYAQDPER NIAFDVPRCS SEMMNYQAME MMKNRCFAST KYRSVDLCCN 250
    KNVHLVVFAN VAYDPTKISE DRIVIINC 278
    Length:278
    Mass (Da):32,382
    Last modified:November 1, 1996 - v1
    Checksum:i4D9F4451F4EA2DED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80879 Genomic DNA. Translation: CAA56847.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80879 Genomic DNA. Translation: CAA56847.1 .

    3D structure databases

    ProteinModelPortali Q66862.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR003365. Viral_rep_N.
    [Graphical view ]
    Pfami PF00910. RNA_helicase. 1 hit.
    PF02407. Viral_Rep. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of a faba bean necrotic yellows virus DNA component containing a putative replicase gene."
      Katul L., Maiss E., Vetten V.J.
      J. Gen. Virol. 76:475-479(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A single Rep protein initiates replication of multiple genome components of faba bean necrotic yellows virus, a single-stranded DNA virus of plants."
      Timchenko T., de Kouchkovsky F., Katul L., David C., Vetten H.J., Gronenborn B.
      J. Virol. 73:10173-10182(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-78 AND LYS-177.
    3. "Nanoviruses: genome organisation and protein function."
      Gronenborn B.
      Vet. Microbiol. 98:103-109(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiREP1_FBNY2
    AccessioniPrimary (citable) accession number: Q66862
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The genome of nanoviruses is composed of six to eight segments. In addition, some isolates contain subviral DNAs.

    Caution

    This protein is encoded by a subviral DNA that is not present in all isolates of the virus.Curated

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3