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Q9YUD3

- REP_BFDV

UniProt

Q9YUD3 - REP_BFDV

Protein

Replication-associated protein

Gene

Rep

Organism
Beak and feather disease virus (BFDV)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep and/or Rep' binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-AGTATTAC-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. ATPase activity is probably carried by the isoform Rep By similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Divalent metal cations, possibly magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi43 – 431Divalent metal cationSequence Analysis
    Metal bindingi51 – 511Divalent metal cationSequence Analysis
    Active sitei89 – 891For DNA cleavage activityBy similarity
    Metal bindingi93 – 931Divalent metal cationSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1728ATPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW
    2. protein-DNA covalent cross-linking Source: InterPro

    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:
    Replication-associated protein (EC:2.7.7.-, EC:3.1.21.-, EC:3.6.1.3)
    Alternative name(s):
    ATP-dependent helicase Rep
    RepP
    Gene namesi
    Name:Rep
    ORF Names:ORF1
    OrganismiBeak and feather disease virus (BFDV)
    Taxonomic identifieri77856 [NCBI]
    Taxonomic lineageiVirusesssDNA virusesCircoviridaeCircovirus
    Virus hostiGracula [TaxID: 116991]
    Psittaciformes [TaxID: 9223]
    ProteomesiUP000007454: Genome

    Subcellular locationi

    Host nucleus Curated

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Replication-associated proteinPRO_0000319862Add
    BLAST

    Keywords - PTMi

    Covalent protein-DNA linkage

    Interactioni

    Subunit structurei

    Interacts with the capsid protein; this interaction relocates Rep into the nucleus.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9YUD3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi4 – 1310Nuclear localization signalSequence Analysis
    Motifi14 – 174RCR-1By similarity
    Motifi51 – 566RCR-2By similarity
    Motifi60 – 8021Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi89 – 924RCR-3By similarity

    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

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR027417. P-loop_NTPase.
    IPR003365. Viral_rep_N.
    [Graphical view]
    PfamiPF00910. RNA_helicase. 1 hit.
    PF02407. Viral_Rep. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9YUD3-1 [UniParc]FASTAAdd to Basket

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    MPSKEGSGCR RWCFTLNNPT DGEIEFVRSL GPDEFYYAIV GREKGEQGTP    50
    HLQGYFHFKN KKRLSALKKL LPRAHFERAK GSDADNEKYC SKEGDVILTL 100
    GIVARDGHRA FDGAVAAVMS GRKMKEVARE FPEVYVRHGR GLHNLSLLVG 150
    SSPRDFKTEV DVIYGPPGCG KSRWANEQPG TKYYKMRGEW WDGYDGEDVV 200
    VLDDFYGWLP YCEMLRLCDR YPHKVPVKGA FVEFTSKRII ITSNKPPETW 250
    YKEDCDPKPL FRRFTRVWWY NVDKLEQVRP DFLAHPINY 289
    Length:289
    Mass (Da):33,446
    Last modified:May 1, 1999 - v1
    Checksum:iA52614012B831791
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF080560 Genomic DNA. Translation: AAC69861.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF080560 Genomic DNA. Translation: AAC69861.1 .

    3D structure databases

    ProteinModelPortali Q9YUD3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR027417. P-loop_NTPase.
    IPR003365. Viral_rep_N.
    [Graphical view ]
    Pfami PF00910. RNA_helicase. 1 hit.
    PF02407. Viral_Rep. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Psittacine beak and feather disease virus nucleotide sequence analysis and its relationship to porcine circovirus, plant circoviruses, and chicken anaemia virus."
      Bassami M.R., Berryman D., Wilcox G.E., Raidal S.R.
      Virology 249:453-459(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The capsid protein of beak and feather disease virus binds to the viral DNA and is responsible for transporting the replication-associated protein into the nucleus."
      Heath L., Williamson A.L., Rybicki E.P.
      J. Virol. 80:7219-7225(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAPSID PROTEIN.

    Entry informationi

    Entry nameiREP_BFDV
    AccessioniPrimary (citable) accession number: Q9YUD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3