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P05400

- POL_CERV

UniProt

P05400 - POL_CERV

Protein

Enzymatic polyprotein

Gene

ORF V

Organism
Carnation etched ring virus (CERV)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Encodes for at least two polypeptides: protease (PR) and reverse transcriptase (RT). The protease processes the polyprotein in cis. Reverse transcriptase is multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated, and reverse-transcribed inside the nucleocapsid. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA) By similarity.By similarity

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei34 – 341

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. endonuclease activity Source: UniProtKB-KW
    3. RNA binding Source: InterPro
    4. RNA-directed DNA polymerase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

    Protein family/group databases

    MEROPSiA03.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enzymatic polyprotein
    Including the following 3 domains:
    Aspartic protease (EC:3.4.23.-)
    Endonuclease
    Reverse transcriptase (EC:2.7.7.49)
    Gene namesi
    ORF Names:ORF V
    OrganismiCarnation etched ring virus (CERV)
    Taxonomic identifieri10640 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesCaulimoviridaeCaulimovirus
    Virus hostiDianthus caryophyllus (Carnation) (Clove pink) [TaxID: 3570]
    ProteomesiUP000008446: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 659659Enzymatic polyproteinPRO_0000222055Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP05400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini252 – 436185Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 180180ProteaseBy similarityAdd
    BLAST

    Domaini

    The polymerase/reverse transcriptase (RT) and ribonuclease H (RH) domains are structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RH domain stabilizes the association of RT with primer-template By similarity.By similarity

    Sequence similaritiesi

    Contains 1 peptidase A3A domain.Curated
    Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation

    Family and domain databases

    InterProiIPR000588. Pept_A3A.
    IPR000477. RT_dom.
    [Graphical view]
    PfamiPF02160. Peptidase_A3. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view]
    PRINTSiPR00731. CAULIMOPTASE.
    PROSITEiPS50878. RT_POL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05400-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLRNRTNPN SIYVKGILKF PGYQTNLDLH CYVDTGSSLC MASKYVIPEE    50
    YWQTAEKPLN IKIANGKIIQ LTKVCSKLPI RLGGERFLIP TLFQQESGID 100
    LLLGNNFCQL YSPFIQYTDR IYFHLNKQSV IIGKITKAYQ YGVKGFLESM 150
    KKKSKVNRPE PINITSNQHL FLEEGGNHVD EMLYEIQISK FSAIEEMLER 200
    VSSENPIDPE KSKQWMTATI ELIDPKTVVK VKPMSYSPSD REEFDRQIKE 250
    LLELKVIKPS KSTHMSPAFL VENEAERRRG KKRMVVNYKA MNKATKGDAH 300
    NLPNKDELLT LVRGKKIYSS FDCKSGLWQV LLDKESQLLT AFTCPQGHYQ 350
    WNVVPFGLKQ APSIFPKTYA NSHSNQYSKY CCVYVDDILV FSNTGRKEHY 400
    IHVLNILRRC EKLGIILSKK KAQLFKEKIN FLGLEIDQGT HCPQNHILEH 450
    IHKFPDRIED KKQLQRFLGI LTYASDYIPK LASIRKPLQS KLKEDSTWTW 500
    NDTDSQYMAK IKKNLKSFPK LYHPEPNDKL VIETDASEEF WGGILKAIHN 550
    SHEYICRYAS GSFKAAERNY HSNEKELLAV IRVIKKFSIY LTPSRFLIRT 600
    DNKNFTHFVN INLKGDRKQG RLVRWQMWLS QYDFDVEHIA GTKNVFADFL 650
    QENTLTNYV 659
    Length:659
    Mass (Da):76,517
    Last modified:November 1, 1988 - v1
    Checksum:i25CC30475E38B3C6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04658 Genomic DNA. Translation: CAA28360.1.
    PIRiS00854.
    RefSeqiNP_612577.1. NC_003498.1.

    Genome annotation databases

    GeneIDi935429.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04658 Genomic DNA. Translation: CAA28360.1 .
    PIRi S00854.
    RefSeqi NP_612577.1. NC_003498.1.

    3D structure databases

    ProteinModelPortali P05400.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi A03.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 935429.

    Family and domain databases

    InterProi IPR000588. Pept_A3A.
    IPR000477. RT_dom.
    [Graphical view ]
    Pfami PF02160. Peptidase_A3. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00731. CAULIMOPTASE.
    PROSITEi PS50878. RT_POL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence of carnation etched ring virus DNA: comparison with cauliflower mosaic virus and retroviruses."
      Hull R., Sadler J., Longstaff M.
      EMBO J. 5:3083-3090(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiPOL_CERV
    AccessioniPrimary (citable) accession number: P05400
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 76 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

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3