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Q9DUN3

- POLG_VESVA

UniProt

Q9DUN3 - POLG_VESVA

Protein

Genome polyprotein

Gene

ORF1

Organism
Vesicular exanthema of swine virus serotype A48 (isolate Swine/United States/A48/1948) (VESV)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 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 and eIF4G2 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
    Sitei148 – 1492Cleavage; by Pro-PolBy similarity
    Sitei435 – 4362Cleavage; by Pro-PolBy similarity
    Sitei791 – 7922Cleavage; by Pro-PolBy similarity
    Sitei1070 – 10712Cleavage; by Pro-PolBy similarity
    Sitei1183 – 11842Cleavage; by Pro-PolBy similarity
    Active sitei1222 – 12221For protease activityBy similarity
    Active sitei1243 – 12431For protease activityBy similarity
    Active sitei1305 – 13051For protease activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi590 – 5978ATPPROSITE-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. transcription, DNA-templated Source: InterPro
    3. viral RNA genome replication Source: InterPro

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    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
    OrganismiVesicular exanthema of swine virus serotype A48 (isolate Swine/United States/A48/1948) (VESV)
    Taxonomic identifieri85617 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeVesivirus
    Virus hostiSus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000007661: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18811881Genome polyproteinPRO_0000402456Add
    BLAST
    Chaini1 – 148148Protein p16By similarityPRO_0000402457Add
    BLAST
    Chaini149 – 435287Protein p32By similarityPRO_0000402458Add
    BLAST
    Chaini436 – 791356NTPaseBy similarityPRO_0000402459Add
    BLAST
    Chaini792 – 1070279Protein p30By similarityPRO_0000402460Add
    BLAST
    Chaini1071 – 1183113Viral genome-linked proteinBy similarityPRO_0000402461Add
    BLAST
    Chaini1184 – 1881698Protease-polymerase p76By similarityPRO_0000402462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1093 – 10931O-(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

    3D structure databases

    ProteinModelPortaliQ9DUN3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini564 – 720157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1207 – 1311105Peptidase C24Add
    BLAST
    Domaini1593 – 1718126RdRp 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. 6 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR016024. ARM-type_fold.
    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]
    SUPFAMiSSF48371. SSF48371. 3 hits.
    SSF50494. 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.

    Q9DUN3-1 [UniParc]FASTAAdd to Basket

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    MAQTLSKISN KENASSGLRP KRFKPHQPIP TWMVRCEPLD HDSRRGRDPV     50
    RASPQAKRVR TPTPYPRHLK PAASAVVRSG NNPSHLKPAS TDVVRSGPQP 100
    LCCEAKDGGV VRSCKTYNLK PAHESKAVAF SLPKTDGPTG NEPEFIAEAC 150
    PSCALYDTCP NCTSKVINDD GSTDGTIPSW DQIETTPAFL SLLSNTDEEM 200
    SADELTNLAA HLRKAFETGS HPANVDYSKD QLQGLLEMAE AAVPPARRQT 250
    LPFYQQRLEA RRTWREKIFN QPLEEINKIL TTSKDRFQRC AAWKVILEKA 300
    VLAKEYGEEA YAYAQQALKN INSFDVNLVL KMAAATFIDH IRMMTVDNPD 350
    LVSYIPKLIV KLKPLTLKMI IDNHENTKEG WLVTLTSLAE LYGMVEVAID 400
    FVPTVVGKLF DLLMKTTSKM YSMFKSVVLA TFTSESLDFT NPFWYAIAAI 450
    LCFLITGAIP HNGKMKIHKN ILSNATGIVA GIKAIQALAA MFSTWSNERL 500
    VNDLSSRTIA LTELNNPTIT ADIDAVINLQ RLAEVLRDEV KSHTLNPLMQ 550
    PYNPILRNLM SALDKVISCC TRRKAIATKR TAPVAVILTG PPGCGKTTAA 600
    FALAKRLSQQ KPSIISLDVD HHDTYTGNEV CIIDEFDSSD KVDYANFVVN 650
    MVNTNPMVLN CDLIENKGKT FTSKYVIMTS NTETPVKPTS RRAGAFYRRV 700
    MIVDVTNNAV DKWKSDNPGK AVPKWCFNKD FSHLSLSLRG TEPYSKEYVL 750
    DPTGRNHQSR RAPPPQQITL EQLAQKMVVQ HTTNTSEFVT QAGDVPVFGF 800
    VCQNNEIDTV YNLLAAVKAR YGANFNLYKG MVRTAHENSG CGAHVHVISR 850
    EDNFRGKAFT VNRSRLESVP HLEGDSFRRS LGVVMSDKDV TTMFYYIKGK 900
    VINDQVSLTE LPANQHVVTV HTVYDMAWAL RRHLKWSGQW QLIKAAYEIM 950
    CYPDTAACAL RNWMDSTDFS EEHVVTQFIA PGGTIILESC YGARMWATGQ 1000
    RLIRAGGLTE AGGPQGGVRF AGLGARNVPW SEILREFMTL ISHIWSQIKG 1050
    ATVVLTALTF YLKRFRPRVE AKGKNKNKGP RKNTGVALTD DEYNDWKQSK 1100
    AEKNLDLTVK DFLQLRHRAA MGADNTDAVK FRYWYSKKQK IYHDLENFPI 1150
    IGRGGLKREL IRKGPLRPRG NDFYDEPDDW YSEGVIDGVT HKNAIVSVDD 1200
    VDGMHKGYAI HIGHGVYISL KHVLTGNARI LSEEPKGITI SGELATFRLN 1250
    NILPTAVPVG TNKPIKDPWG NPVSTDWQFK NYNTTSGNIY GACGSSCSLT 1300
    RQGDCGLPYV DDHGVVVGLH AGSGGDKCPS RKLIVPYVKV DMRIRDTCTK 1350
    ESPTKTHKPT FSYRGLLGKE TGEPRTIMKG TRLHVSPAHV DDYEECTHQP 1400
    ASLGAGDPRC PISLTGIMVN NLQPYTEASP GPDTATLNRV SKMLTSHMEG 1450
    YVPKVHKTEE DSISAFYMLN HDTLCGPYIG ARKKDHVKDG VLDKNLLDLL 1500
    SSKWNRAKLG LALPHEYALG LKDELRPKDK VAVGKRRLIW GCDVGVSTVC 1550
    AAAFKRVSES IMANHALGFI QVGINMDGPA VEDLFKRLER PKHDRYCVDY 1600
    SKWDSTQPPK VTSQSIDILR HFTDKSPIVD SACATLKSNP IGIFNGVAFK 1650
    VAGGLPSGMP LTSIINSLNH CLMVGSAVVK ALEDSGVRVT WNIFDSMDLF 1700
    TYGDDGVYIV PPLISSVMPK VFANLRQFGL KPTRTDKSDA EITPIPADEP 1750
    VEFLKRTIVR TENGVRALLD RSSIIRQFYY IKAENTENWT VPPKRIDTPS 1800
    RGQQLYNACL YASQHGEEFY TSKIVPLIER AVKLEGLHIE VPEFHQAVAA 1850
    YNGYFNGTEG QPNQIAHASG GLGLSGEVFE N 1881
    Length:1,881
    Mass (Da):208,813
    Last modified:March 1, 2001 - v1
    Checksum:i6E487A72523AFE4F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76874 Genomic RNA. Translation: AAG13641.1.
    RefSeqiNP_066255.1. NC_002551.1.

    Genome annotation databases

    GeneIDi911834.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76874 Genomic RNA. Translation: AAG13641.1 .
    RefSeqi NP_066255.1. NC_002551.1.

    3D structure databases

    ProteinModelPortali Q9DUN3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 911834.

    Family and domain databases

    Gene3Di 3.40.50.300. 6 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR016024. ARM-type_fold.
    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 SSF48371. SSF48371. 3 hits.
    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. "The capsid protein of vesicular exanthema of swine virus serotype A48: relationship to the capsid protein of other animal caliciviruses."
      Neill J.D., Meyer R.F., Seal B.S.
      Virus Res. 54:39-50(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Complete nucleotide sequence of the genomic RNA of vesicular exanthema of swine virus A48."
      Neill J.D., Seal B.S., Ridpath J.F.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_VESVA
    AccessioniPrimary (citable) accession number: Q9DUN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 70 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