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O91466

- CATV_GVCPM

UniProt

O91466 - CATV_GVCPM

Protein

Viral cathepsin

Gene

VCATH

Organism
Cydia pomonella granulosis virus (isolate Mexico/1963) (CpGV) (Cydia pomonella granulovirus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system By similarity.By similarity

    Catalytic activityi

    Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei148 – 1481By similarity
    Active sitei280 – 2801By similarity
    Active sitei300 – 3001By similarity

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Protein family/group databases

    MEROPSiC01.047.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Viral cathepsin (EC:3.4.22.50)
    Short name:
    V-cath
    Alternative name(s):
    Cysteine proteinase
    Short name:
    CP
    Gene namesi
    Name:VCATH
    Synonyms:ORF8R
    OrganismiCydia pomonella granulosis virus (isolate Mexico/1963) (CpGV) (Cydia pomonella granulovirus)
    Taxonomic identifieri654905 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageBaculoviridaeBetabaculovirus
    Virus hostiCydia pomonella (Codling moth) [TaxID: 82600]
    ProteomesiUP000009249: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 124104Activation peptideSequence AnalysisPRO_0000322218Add
    BLAST
    Chaini125 – 333209Viral cathepsinPRO_0000050588Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi145 ↔ 186By similarity
    Glycosylationi170 – 1701N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi179 ↔ 219By similarity
    Disulfide bondi272 ↔ 321By similarity

    Post-translational modificationi

    Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliO91466.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O91466-1 [UniParc]FASTAAdd to Basket

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    MTKLLNFVIL ASVLTVTAHA LTYDLNNSDE LFKNFAIKYN KTYVSDEERA    50
    IKLENFKNNL KMINEKNMAS KYAVFDINEY SDLNKNALLR RTTGFRLGLK 100
    KNPSAFTMTE CSVVVIKDEP QALLPETLDW RDKHGVTPVK NQMECGSCWA 150
    FSTIANIESL YNIKYDKALN LSEQHLVNCD NINNGCAGGL MHWALESILQ 200
    EGGVVSAENE PYYGFDGVCK KSPFELSISG SRRYVLQNEN KLRELLVVNG 250
    PISVAIDVSD LINYKAGIAD ICENNEGLNH AVLLVGYGVK NDVPYWILKN 300
    SWGAEWGEEG YFRVQRDKNS CGMMNEYASS AIL 333
    Length:333
    Mass (Da):37,434
    Last modified:November 1, 1998 - v1
    Checksum:iF531CC9AC34FFF5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53466 Genomic DNA. Translation: AAK70678.1.
    RefSeqiNP_148795.1. NC_002816.1.

    Genome annotation databases

    GeneIDi921370.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53466 Genomic DNA. Translation: AAK70678.1 .
    RefSeqi NP_148795.1. NC_002816.1.

    3D structure databases

    ProteinModelPortali O91466.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C01.047.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 921370.

    Family and domain databases

    InterProi IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of the Cydia pomonella granulovirus cathepsin and chitinase genes."
      Kang W., Tristem M., Maeda S., Crook N.E., O'Reilly D.R.
      J. Gen. Virol. 79:2283-2292(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Mexican 1.
    2. "The complete sequence of the Cydia pomonella granulovirus genome."
      Luque T., Finch R., Crook N., O'Reilly D.R., Winstanley D.
      J. Gen. Virol. 82:2531-2547(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Mexican 1.

    Entry informationi

    Entry nameiCATV_GVCPM
    AccessioniPrimary (citable) accession number: O91466
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 69 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, Reference 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