Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27409

- POLG_FCVF9

UniProt

P27409 - POLG_FCVF9

Protein

Genome polyprotein

Gene

ORF1

Organism
Feline calicivirus (strain F9) (FCV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity By similarity.By similarity
    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 By similarity.By similarity

    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-PolBy similarity
    Sitei331 – 3322Cleavage; by Pro-PolBy similarity
    Sitei685 – 6862Cleavage; by Pro-PolBy similarity
    Sitei960 – 9612Cleavage; by Pro-PolBy similarity
    Sitei1071 – 10722Cleavage; by Pro-PolBy similarity
    Active sitei1110 – 11101For protease activityBy similarity
    Active sitei1131 – 11311For protease activityBy similarity
    Active sitei1193 – 11931For protease activityBy similarity

    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

    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 F9) (FCV)
    Taxonomic identifieri11981 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeVesivirus
    Virus hostiFelidae (cat family) [TaxID: 9681]
    ProteomesiUP000008762: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17631763Genome polyproteinPRO_0000341997Add
    BLAST
    Chaini1 – 4646Protein p5.6By similarityPRO_0000036900Add
    BLAST
    Chaini47 – 331285Protein p32By similarityPRO_0000036901Add
    BLAST
    Chaini332 – 685354NTPaseBy similarityPRO_0000036902Add
    BLAST
    Chaini686 – 960275Protein p30By similarityPRO_0000036903Add
    BLAST
    Chaini961 – 1071111Viral genome-linked proteinBy similarityPRO_0000036904Add
    BLAST
    Chaini1072 – 1763692Protease-polymerase p76By similarityPRO_0000036905Add
    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 By similarity.By similarity
    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 By similarity.By similarity

    Structurei

    Secondary structure

    1
    1763
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi973 – 9764
    Helixi981 – 99313
    Helixi1000 – 101213
    Helixi1017 – 102913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M4HNMR-A970-1036[»]
    ProteinModelPortaliP27409.
    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 By similarity.By similarity

    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. 3 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. 4 hits.
    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.

    P27409-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTLSFVLK THSVRKDFVH SVKLTLARRR DLQYIYNKLS RTIRAEACPS     50
    CASYDVCPNC TSGDVPDDGS STMSIPSWED VTKSSTYSLL LSEDTSDELC 100
    PEDLVNVAAH IRKALSTQSH PANAEMCKEQ LTFLLVMAEA MLPQRSRASI 150
    PLHQQHTAAR LEWREKFFSK PLDFLLERVG VSKDILQTTA IWKIILEKAC 200
    YCKSYGEQWF TAAKQKLREM KNFESDTLKP LIGGFIDGLR FLTVDNPNPM 250
    GFLPKLIGLV KPLNLAMIID NHENTISGWI ITLTAIMELY NITECTIDII 300
    TSVITAFYDK IGKATKFYSC VKALFTGFRS EDVANSFWYM AAAILCYLIT 350
    GLIPNNGRFS KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA 400
    RTVALSELNN PTTTSDTDSV ERLLELAKIL HEEIKIHTLN PIMQSYNPIL 450
    RNLMSTLDGV ITSCNKRKAI ARKRQVPVCY ILTGPPGCGK TTAAQALAKK 500
    LSDQEPSVIN LDVDHHDTYT GNEVCIIDEF DSSDKVDYAN FVIGMVNSAP 550
    MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSKRAGAF YRRVTIIDVT 600
    NPFVESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ 650
    HQSMKAPPPT FLNIDSLAQT MKQDFLLKNM AFEAEDGCAE HRYGFVCQQE 700
    EVETVRRLLN AVRARMNATF TVCVGPETSH SIGCTAHVLT PNETFNGKKF 750
    VVSRCNEASL SALEGNCVKS ALGVCMSDKD LTHLCHFIKG KIVNDSVRLD 800
    ELPANQHVVT VNSVFDLAWA VRRHLTLAGQ FQAIRAAYDV LTVPDKIPAM 850
    LRHWMDETSF SDDHVVTQFV TPGGIVILES CGGARIWALG RNVIRAGGVT 900
    ATPTGGCVRL MGLSAPTMPW SEIFRELFSL LGRIWSSVKV SALVLTALGM 950
    YASRFRPKSE AKGKTKLKIG TYRGRGVALT DDEYDEWREH NASRKLDLSV 1000
    EDFLMLRHRA ALGADDNDAV KFRSWWNSRT KMANDYEDVT VIGKGGVKHE 1050
    KIRTNTLKAV DRGYDVSFAE ESGPGTKFHK NAIGSVTDVC GEHKGYCIHM 1100
    GHGVYASVAH VVKGDSFFLG ERIFDLKTNG EFCCFRSTKI LPSAAPFFSG 1150
    KPTRDPWGSP VATEWKPKMY TTTSGKILGC FATTSTETHP GDCGLPYIDD 1200
    NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK 1250
    GLICKQLDEI RIIPKGTRLH VSPAHTEDYQ ECSHQPASLG SGDPRCPKSL 1300
    TAIVVDSLKP YCENVEGPPH DVLHRVQKML IDHLSGFVPM NISSETSMLS 1350
    AFHKLNHDTS CGPYLGGRKK DHMANGEPDK QLLDLLSAKW KLATQGIALP 1400
    HEYTIGLKDE LRPVEKVSEG KRRMIWGCDV GVATVCAAAF KGVSDAITAN 1450
    HQYGPIQVGI NMDSPSVEAL FQRIKSAAKV FAVDYSKWDS TQSPRVSAAS 1500
    IDILRYFSDR SPIVDSASNT LKSPPVAIFN GVAVKVSSGL PSGMPLTSVI 1550
    NSLNHCLYVG CAILQSLEAK AIPVTWNLFS TFDIMTYGDD GVYMFPIMYA 1600
    SISDQIFGNL SSYGLKPTRV DKSVGAIEPI DPDSVVFLKR TITRTPQGIR 1650
    GLLDRSSIIR QFYYIKGENS DDWKSPPKHI DPTSRGQQLW NACLYASQHG 1700
    LEFFNKVYRL AERAVEYEEL HFEPPTYASA LDHYNSQFNG VEARSDQIDS 1750
    SGMTALHCDV FEV 1763
    Length:1,763
    Mass (Da):195,029
    Last modified:August 1, 1992 - v1
    Checksum:iBE3C34FD49F35D9B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86379 Genomic RNA. Translation: AAA79326.1.
    Z11536 Genomic RNA. Translation: CAA77635.1.
    PIRiA43382. RRWWF9.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86379 Genomic RNA. Translation: AAA79326.1 .
    Z11536 Genomic RNA. Translation: CAA77635.1 .
    PIRi A43382. RRWWF9.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M4H NMR - A 970-1036 [» ]
    ProteinModelPortali P27409.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.300. 3 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. 4 hits.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleotide sequence of a feline calicivirus."
      Carter M.J., Milton I.D., Meanger J., Bennett M., Gaskell R.M., Turner P.C.
      Virology 190:443-448(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Cloning and sequence determination of the feline calicivirus strain F9."
      Meanger J., Carter M.J., Gaskell R.M., Turner P.C.
      Biochem. Soc. Trans. 20:26S-26S(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Identification and sequence determination of the capsid protein gene of feline calicivirus."
      Carter M.J., Milton I.D., Turner P.C., Meanger J., Bennett M., Gaskell R.M.
      Arch. Virol. 122:223-235(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1098-1763.

    Entry informationi

    Entry nameiPOLG_FCVF9
    AccessioniPrimary (citable) accession number: P27409
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 102 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

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3