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Q66914

- POLG_FCVUR

UniProt

Q66914 - POLG_FCVUR

Protein

Genome polyprotein

Gene

ORF1

Organism
Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.
    Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation By similarity.By similarity
    Protease-polymerase p76 processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved. Cleaves host translation initiation factor eIF4G1, eIF4G2 and PABP1 thereby inducing a shutdown of host protein synthesis. This shutdown may not prevent viral mRNA from being translated since viral Vpg replaces the cap. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation. It is also an RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs.

    Catalytic activityi

    NTP + H2O = NDP + phosphate.
    Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei46 – 472Cleavage; by Pro-Pol
    Sitei331 – 3322Cleavage; by Pro-Pol
    Sitei685 – 6862Cleavage; by Pro-Pol
    Sitei960 – 9612Cleavage; by Pro-Pol
    Sitei1071 – 10722Cleavage; by Pro-Pol
    Active sitei1110 – 11101For protease activityBy similarity
    Active sitei1131 – 11311For protease activityBy similarity
    Active sitei1193 – 11931For protease activity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi484 – 4918ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. RNA binding Source: InterPro
    4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    5. RNA helicase activity Source: InterPro

    GO - Biological processi

    1. RNA-protein covalent cross-linking Source: UniProtKB-KW
    2. suppression by virus of host gene expression Source: UniProtKB-KW
    3. transcription, DNA-templated Source: InterPro
    4. viral RNA genome replication Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

    Keywords - Biological processi

    Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Viral RNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.4.22.66. 8732.

    Protein family/group databases

    MEROPSiC24.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 6 chains:
    Alternative name(s):
    p39
    Alternative name(s):
    VPg
    p13
    Protease-polymerase p76 (EC:2.7.7.48, EC:3.4.22.66)
    Short name:
    Pro-Pol
    Gene namesi
    ORF Names:ORF1
    OrganismiFeline calicivirus (strain Cat/United States/Urbana/1960) (FCV)
    Taxonomic identifieri292349 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeVesivirus
    Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
    ProteomesiUP000001098: Genome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461E → A: Complete loss of proteolytic processing between P5.6 and P32; Complete loss of infectious clone recovery. 1 Publication
    Mutagenesisi331 – 3311E → A: Complete loss of infectious clone recovery. 1 Publication
    Mutagenesisi683 – 6831E → A: Complete loss of infectious clone recovery. 1 Publication
    Mutagenesisi685 – 6851E → A: Complete loss of infectious clone recovery. 1 Publication
    Mutagenesisi960 – 9601E → A: Complete loss of infectious clone recovery. 1 Publication
    Mutagenesisi1071 – 10711E → A: Complete loss of infectious clone recovery. 1 Publication
    Mutagenesisi1193 – 11931C → G: Complete loss of proteolytic processing. 1 Publication
    Mutagenesisi1345 – 13451E → A: No effect on infectious clone recovery. 1 Publication
    Mutagenesisi1419 – 14191E → A: No effect on infectious clone recovery. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17631763Genome polyproteinPRO_0000341636Add
    BLAST
    Chaini1 – 4646Protein p5.6PRO_0000036907Add
    BLAST
    Chaini47 – 331285Protein p32PRO_0000036908Add
    BLAST
    Chaini332 – 685354NTPasePRO_0000036909Add
    BLAST
    Chaini686 – 960275Protein p30PRO_0000036910Add
    BLAST
    Chaini961 – 1071111Viral genome-linked proteinPRO_0000036911Add
    BLAST
    Chaini1072 – 1763692Protease-polymerase p76PRO_0000036912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei984 – 9841O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein.2 Publications
    VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Phosphoprotein

    Interactioni

    Subunit structurei

    Protein p32: homodimer, interacts with NTPase, protein p30 and Pro-Pol. Viral genome-linked protein interacts with capsid protein and Pro-Pol. Protease-polymerase p76: Homooligomers, interacts with Vpg, protein p32 and may interact with capsid protein.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ66914.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini458 – 614157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1095 – 1199105Peptidase C24Add
    BLAST
    Domaini1478 – 1603126RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Protease-polymerase is composed of two domains displaying two different catalytic activity. These activities may act independently.

    Sequence similaritiesi

    Contains 1 peptidase C24 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.40.50.300. 4 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR000317. Peptidase_C24.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF03510. Peptidase_C24. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view]
    PRINTSiPR00916. 2CENDOPTASE.
    PR00918. CALICVIRUSNS.
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q66914-1 [UniParc]FASTAAdd to Basket

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    MSQTLSFVLK THSVRKDFVH SVKRTLQRRR DLQYLYNKLS RPIRAEACPS     50
    CASYDVCPNC TSGSIPDDGS SKGQIPSWED VTKTSTYSLL LSEDTSDELH 100
    PDDLVNVAAH IRKALSTQSH PANVDMCKEQ LTSLLVMAEA MLPQRSRSTL 150
    PLHQKYVAAR LEWREKFFSK PLDFLLEKIG TSRDILQITA VWKIIIEKAC 200
    YCKSYGEHWF EAAKQKLREI KSYEHNTLKP LIGAFIDGLR LMTIDNPNPM 250
    GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDVI 300
    TSIITGFYDK IGKATKFYSQ IKALFTGFRS EDVANSFWYM AAAILCYLIT 350
    GLIPNNGRLS KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA 400
    RTVAISELNN PTTTSDTDSV ERLLELAKIL HEEIKIHTLN PIMQSYNPIL 450
    RNLMSTLDGV ITSCNKRKAI AKKRPVPVCY ILTGPPGCGK TTAALALAKK 500
    LSDQEPSVIN LDVDHHDTYT GNEVCIVDEF DSSDKVDYAN FVIGMVNSAP 550
    MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSRRAGAF YRRVTIIDVA 600
    NPLAESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ 650
    HQSIKAPPPT FLNIDSLAQT MKQDFTLKNM AFEAENGHSE HRYGFVCQQG 700
    EVETVRRLLN AVRTRLNATF TVCVGSEASS SIGCTAHVLT PDEPFNGKKY 750
    VVSRCNEASL SALEGNCVQS ALGVCMSTKD LTHLCHFIRG KIVNDSVRLD 800
    ELPANQHVVT VNSVFDLAWA LRRHLTLAGQ FQAIRAAYDV LTAPDKVPAM 850
    LRHWMDETSF SDEHVVTQFV TPGGIVILES CGGARIWALG HNVIRAGGVT 900
    ATPTGGCIRF MGLSAQTMPW SEIFRELFSL LGRIWSSIKV STLVLTALGM 950
    YASRFRPKSE AKGKTKSKVG PYRGRGVALT DDEYDEWREH NATRKLDLSV 1000
    EDFLMLRHRA ALGADDADAV KFRSWWNSRS RLADDYEDVT VIGKGGVKHE 1050
    KIRTNTLRAV DRGYDVSFAE ESGPGTKFHK NAIGSVTDVC GEHKGYCVHM 1100
    GHGVYATVAH VAKGDSFFLG ERIFDLKTNG EFCCFRSTKI LPSAAPFFPG 1150
    KPTRDPWGSP VATEWKPKPY TTTSGKIVGC FATTSTETHP GDCGLPYIDD 1200
    NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK 1250
    GLICKQLDEI RIIPKGTRLH VSPAHTEDFE ECSHQPASLG SGDPRCPKSL 1300
    TAIVVDSLKP YCDKVEGPPH DILHRVQKML IDHLSGFVPV NISSETSMLS 1350
    AFHKLNHDTS CGPYLGGRKK DHMTNGEPDK PLLDLLSAKW KLATQGIALP 1400
    HEYTIGLKDE LRPVEKVAEG KRRMIWGCDV GVATVCAAAF KGVSDAITAN 1450
    HQYGPVQVGI NMDSPSVEAL HQRIKSAAKV YAVDYSKWDS TQSPRVSAAS 1500
    IDILRYFSDR SPIVDSAANT LKSPPIAIFN GVAVKVSSGL PSGMPLTSVI 1550
    NSLNHCLYVG CAILQSLEAR GVPVTWNLFS TFDMMTYGDD GVYMFPMMFA 1600
    SVSDQIFANL SAYGLKPTRV DKSVGSIEPI DPESVVFLKR TITRTPQGIR 1650
    GLLDRSSIIR QFYYIKGENS DDWKTPPKSI DPTSRGQQLW NACLYASQHG 1700
    VEFYNKIYKL AQKAVEYEEL HLEPPTYHSA LEHYNNQFNG VEARSDQIDS 1750
    SGMTALHCDV FEV 1763
    Length:1,763
    Mass (Da):194,911
    Last modified:November 1, 1996 - v1
    Checksum:i7F105592DF0BF821
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40021 Genomic RNA. Translation: AAA79323.1.
    RefSeqiNP_783196.1. NC_001481.2.

    Genome annotation databases

    GeneIDi1502252.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40021 Genomic RNA. Translation: AAA79323.1 .
    RefSeqi NP_783196.1. NC_001481.2.

    3D structure databases

    ProteinModelPortali Q66914.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C24.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1502252.

    Enzyme and pathway databases

    BRENDAi 3.4.22.66. 8732.

    Family and domain databases

    Gene3Di 3.40.50.300. 4 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR000317. Peptidase_C24.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF03510. Peptidase_C24. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view ]
    PRINTSi PR00916. 2CENDOPTASE.
    PR00918. CALICVIRUSNS.
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity."
      Sosnovtsev S.V., Green K.Y.
      Virology 210:383-390(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome."
      Sosnovtsev S.V., Garfield M., Green K.Y.
      J. Virol. 76:7060-7072(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 686-695, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF GLU-46; GLU-331; GLU-683; GLU-685; GLU-960; GLU-1071; GLU-1345 AND GLU-1419.
    3. "Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein."
      Sosnovtseva S.A., Sosnovtsev S.V., Green K.Y.
      J. Virol. 73:6626-6633(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 961-969 AND 1072-1080, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF CYS-1193.
    4. "Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions."
      Sosnovtsev S.V., Green K.Y.
      Virology 277:193-203(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 961-980.
    5. "Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein."
      Kuyumcu-Martinez M., Belliot G., Sosnovtsev S.V., Chang K.O., Green K.Y., Lloyd R.E.
      J. Virol. 78:8172-8182(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF PROTEASE-POLYMERASE P76.
    6. "Cleavage of eukaryotic initiation factor eIF4G and inhibition of host-cell protein synthesis during feline calicivirus infection."
      Willcocks M.M., Carter M.J., Roberts L.O.
      J. Gen. Virol. 85:1125-1130(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF PROTEASE-POLYMERASE P76.
    7. "Analysis of protein-protein interactions in the feline calicivirus replication complex."
      Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.
      J. Gen. Virol. 87:363-368(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION IN VIRAL REPLICATION COMPLEX.

    Entry informationi

    Entry nameiPOLG_FCVUR
    AccessioniPrimary (citable) accession number: Q66914
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 9, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 94 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, Direct protein sequencing, 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