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P03304

- POLG_EMCV

UniProt

P03304 - POLG_EMCV

Protein

Genome polyprotein

Gene
N/A
Organism
Encephalomyocarditis virus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Leader protein: promotes host NUP62, NUP153, and NUP214 phosphorylation and induces cessation of active nucleocytoplasmic transport. Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response By similarity.By similarity
    Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host VCAM1 to provide virion attachment on murine vascular endothelial cells By similarity.By similarity
    Protein VP0: VP0 precursor is a component of immature procapsids.By similarity
    Protein 2B: Affects membrane integrity and cause an increase in membrane permeability.By similarity
    Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.By similarity
    Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
    Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. Cleaves host PABP1, this cleavage is important for viral replication.1 Publication
    RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation
    Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity.By similarity

    Catalytic activityi

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
    NTP + H2O = NDP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei136 – 1372CleavageSequence Analysis
    Sitei391 – 3922Cleavage; by protease 3CSequence Analysis
    Sitei622 – 6232Cleavage; by protease 3CSequence Analysis
    Sitei899 – 9002Cleavage; by protease 3CSequence Analysis
    Sitei1042 – 10432Cleavage; by ribosomal skipSequence Analysis
    Sitei1192 – 11932Cleavage; by protease 3CSequence Analysis
    Sitei1517 – 15182Cleavage; by protease 3CSequence Analysis
    Sitei1605 – 16062Cleavage; by protease 3CSequence Analysis
    Sitei1625 – 16262Cleavage; by protease 3CSequence Analysis
    Active sitei1671 – 16711For protease 3C activitySequence Analysis
    Active sitei1703 – 17031For protease 3C activitySequence Analysis
    Active sitei1784 – 17841For protease 3C activitySequence Analysis
    Sitei1830 – 18312Cleavage; by protease 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri10 – 2213Sequence AnalysisAdd
    BLAST
    Nucleotide bindingi1311 – 13188ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. ion channel activity Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. RNA binding Source: UniProtKB-KW
    7. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    8. RNA helicase activity Source: InterPro
    9. structural molecule activity Source: InterPro

    GO - Biological processi

    1. induction by virus of host autophagy Source: UniProtKB
    2. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    3. protein oligomerization Source: UniProtKB-KW
    4. RNA-protein covalent cross-linking Source: UniProtKB-KW
    5. suppression by virus of host gene expression Source: UniProtKB-KW
    6. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
    7. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    8. transcription, DNA-templated Source: InterPro
    9. viral entry into host cell Source: UniProtKB-KW
    10. viral RNA genome replication Source: InterPro
    11. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

    Keywords - Biological processi

    Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 13 chains:
    Alternative name(s):
    VP4-VP2
    Alternative name(s):
    P1A
    Rho
    Virion protein 4
    Alternative name(s):
    Beta
    P1B
    Virion protein 2
    Alternative name(s):
    Gamma
    P1C
    Virion protein 3
    Alternative name(s):
    Alpha
    P1D
    Virion protein 1
    Protein 2A
    Short name:
    P2A
    Alternative name(s):
    G
    Protein 2B
    Short name:
    I
    Short name:
    P2B
    Protein 2C (EC:3.6.1.15)
    Short name:
    C
    Short name:
    P2C
    Protein 3A
    Short name:
    P3A
    Protein 3B
    Short name:
    P3B
    Alternative name(s):
    H
    VPg
    Protease 3C (EC:3.4.22.28)
    Short name:
    P3C
    Alternative name(s):
    Picornain 3C
    p22
    RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48)
    Short name:
    E
    Short name:
    P3D-POL
    OrganismiEncephalomyocarditis virus
    Taxonomic identifieri12104 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    Mus musculus (Mouse) [TaxID: 10090]
    Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000008660: Genome

    Subcellular locationi

    Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity

    GO - Cellular componenti

    1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. icosahedral viral capsid Source: InterPro
    4. integral to membrane of host cell Source: UniProtKB-KW
    5. membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6767Leader proteinPRO_0000039780Add
    BLAST
    Chaini68 – 391324Protein VP0Sequence AnalysisPRO_0000310967Add
    BLAST
    Chaini68 – 13669Protein VP4Sequence AnalysisPRO_0000039781Add
    BLAST
    Chaini137 – 391255Protein VP2Sequence AnalysisPRO_0000039782Add
    BLAST
    Chaini392 – 622231Protein VP3Sequence AnalysisPRO_0000039783Add
    BLAST
    Chaini623 – 899277Protein VP1Sequence AnalysisPRO_0000039784Add
    BLAST
    Chaini900 – 1042143Protein 2ASequence AnalysisPRO_0000039785Add
    BLAST
    Chaini1043 – 1192150Protein 2BSequence AnalysisPRO_0000039786Add
    BLAST
    Chaini1193 – 1517325Protein 2CSequence AnalysisPRO_0000039787Add
    BLAST
    Chaini1518 – 160588Protein 3ASequence AnalysisPRO_0000039788Add
    BLAST
    Chaini1606 – 162520Protein 3BSequence AnalysisPRO_0000039789Add
    BLAST
    Chaini1626 – 1830205Protease 3CSequence AnalysisPRO_0000039790Add
    BLAST
    Chaini1831 – 2290460RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi68 – 681N-myristoyl glycine; by hostBy similarity
    Modified residuei1608 – 16081O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex By similarity.By similarity
    VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity
    Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    Interactioni

    Subunit structurei

    Protease 3C interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication. Protein 2A interacts with host EIF4E By similarity.By similarity

    Protein-protein interaction databases

    IntActiP03304. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP03304.
    SMRiP03304. Positions 1-32, 76-896.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 15621562CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1582 – 2290709CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1563 – 158119Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1279 – 1445167SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini2059 – 2177119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 6125AcidicAdd
    BLAST

    Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated
    Contains 2 peptidase C3 domains.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri10 – 2213Sequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    4.10.90.10. 1 hit.
    InterProiIPR015031. Capsid_VP4_Picornavir.
    IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR021573. Leader_pept_picornaV.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF00548. Peptidase_C3. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    PF08935. VP4_2. 1 hit.
    PF11475. VP_N-CPKC. 1 hit.
    [Graphical view]
    PRINTSiPR00918. CALICVIRUSNS.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

    Isoform Genome polyprotein (identifier: P03304-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE     50
    DDVFDPELDM EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI 100
    DLSANAAGSD PPRLRSIFES LSGAVNAFSN MLPLLADQNT EEMENLSDRG 150
    LKTLPAIRSQ TPSQQWAVLS VMVPFMMESI RHHVLTLLQK RFWRWKGTTP 200
    SRLMIGHQHK SPLSTSAFPF LTSCPVKMVV SLVALRRHYL VKTGWRVQVQ 250
    CNASQFHAGG LLVFMAPEYP TLDAFAMDNR WSKDNLPNGT RTQTNKKGPF 300
    AMDHQNFWQW TLYPHQFLNL RTNTTVDLEV PYVNIAPTSS WTQHASWTLV 350
    IAVVAPLTYS TGASTSLDIT ASIQPVRPVF NGLRHETLSR QSPIPVTIRE 400
    HAGTWYSTLP DSTVPIYGKT PVAPSNYMVG EYKDFLEIAQ IPTFIGNKIP 450
    NAVPYIEASN TAVKTQPLAT YQVTLSCSCL ANTFLAALSR NFAQYRGSLV 500
    YTFVFTGTAM MKGKFLIAYT PPGAGKPTSR DQAMQATYAI WDLGLNSSYS 550
    FTVPFISPTH FRMVGTDQVN ITNADGWVTV WQLTPLTYPP GCPTSAKILT 600
    MVSAGKDFSL KMPISPAPWS PQGVENAEKG VTENTNATAD FVAQPVYLPE 650
    NQTKVAFFYN RSSPIGAFTV KSGSLESGFA PFSNGTCPNS VILTPGPQFD 700
    PAYDQLRPQR LTEIWGNGNE ETSKVFPLKS KQDYSFCLFS PFVYYKCDLE 750
    VTLSPHTSGN HGLLVRWCPT GTPTKPTTQV LHEVSSLSEG RTPQVYSAGP 800
    GISNQISFVV PYNSPLSVLS AVWYNGHKRF DNTGSLGIAP NSDFGTLFFA 850
    GTKPDIKFTV YLRYKNKRVF CPRPTVFFPW PTSGDKIDMT PRAGVLMLES 900
    PNALDISRTY PTLHVLIQFN HRGLEVRLFR HGHFWAETRA DVILRSKTKQ 950
    VSFLSNGNYP SMDSRAPWNP WKNTYQAVLR AEPCRVTMDI YYKRVRPFRL 1000
    PLVQKEWPVR EENVFGLYRI FNAHYAGYFA DLLIHDIETN PGPFMFRPRK 1050
    QVFQTQGAAV SSMAQTLLPN DLASKAMGSA FTALLDANED AQKAMKIIKT 1100
    LSSLSDAWEN VKETLNNPEF WKQLLSRCVQ LIAGMTIAVM HPDPLTLLCL 1150
    GTLTAAEITS QTSLCEEIAA KFKTIFITPP PRFPTISLFQ QQSPLKQVND 1200
    IFSLAKNLDW AVKTVEKVVD WFGTWIVQEE KEQTLDQLLQ RFPEHAKRIS 1250
    DLRNGMAAYV ECKESFDFFE KLYNQAVKEK RTGIAAVCEK FRQKHDHATA 1300
    RCEPVVIVLR GDAGQGKSLS SQVIAQAVSK TIFGRQSVYS LPPDSDFFDG 1350
    YENQFAAIMD DLGQNPDGSD FTTFCQMVST TNFLPNMASL ERKGTPFTSQ 1400
    LVVATTNLPE FRPVTIAHYP AVERRITFDY SVSAGPVCSK TEAGYKVLDV 1450
    ERAFRPTGEA PLPCFQNNCL FLEKAGLQFR DNRTKEIISL VDVIERAVAR 1500
    IERKKKVLTT VQTLVAQGPV DEVSFHSVVQ QLKARQQATD EQLEELQEAF 1550
    AKVQERNSVF SDWLKISAML CAATLALSQV VKMAKAVKQM VKPDLVRVQL 1600
    DEQEQGPYNE TARVKPKTLQ LLDIQGPNPV MDFEKYVAKH VTAPIGFVYP 1650
    TGVSTQTCLL VRGRTLVVNR HMAESDWTSI VVRGVTHARS TVKILAIAKA 1700
    GKETDVSFIR LSSGPLFRDN TSKFVKAGDV LPTGAAPVTG IMNTDIPMMY 1750
    TGTFLKAGVS VPVETGQTFN HCIHYKANTR KGWCGSALLA DLGGSKKILG 1800
    IHSAGSMGIA AASIVSQEMI RAVVNAFEPQ GALERLPDGP RIHVPRKTAL 1850
    RPTVARQVFQ PAYAPAVLSK FDPRTEADVD EVAFSKHTSN QESLPPVFRM 1900
    VAKEYANRVF TLLGKDNGRL TVKQALEGLE GMDPMDRNTS PGLPYTALGM 1950
    RRTDVVDWES ATLIPFAAER LRKMNEGDFS EVVYQTFLKD ELRPIEKVQA 2000
    AKTRIVDVPP FEHCILGRQL LGKFASKFQT QPGLELGSAI GCDPDVHWTA 2050
    FGVAMQGFER VYDVDYSNFD STHSVAMFRL LAEEFFTPEN GFDPLTREYL 2100
    ESLAISTHAF EEKRFLITGG LPSGCAATSM LNTIMNNIII RAGLYLTYKN 2150
    FEFDDVKVLS YGDDLLVATN YQLDFDKVRA SLAKTGYKIT PANTTSTFPL 2200
    NSTLEDVVFL KRKFKKEGPL YRPVMNREAL EAMLSYYRPG TLSEKLTSIT 2250
    MLAVHSGKQE YDRLFAPFRE VGVVVPSFES VEYRWRSLFW 2290

    Note: Produced by conventional translation.

    Length:2,290
    Mass (Da):255,758
    Last modified:July 21, 1986 - v1
    Checksum:i26BC81BB7CF68CB5
    GO
    Isoform 2B* (identifier: P0DJX7-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P0DJX7.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by -1 ribosomal frameshifting.

    Length:128
    Mass (Da):14,449
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1337 – 13371S → P in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1397 – 13971F → L in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1518 – 15181G → A in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1537 – 15371Q → E in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1557 – 15571N → S in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1612 – 16121A → T in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1755 – 17551L → V in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1916 – 19161D → N in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti1987 – 19882FL → IH in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti2008 – 20081V → I in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti2049 – 20491T → H in AAA43036. (PubMed:6091680)Curated
    Sequence conflicti2194 – 21941T → K in AAA43036. (PubMed:6091680)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00463 Genomic RNA. Translation: CAA25152.1.
    M54935 Genomic RNA. Translation: AAA43036.1.
    PIRiA03906. GNNYE.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00463 Genomic RNA. Translation: CAA25152.1 .
    M54935 Genomic RNA. Translation: AAA43036.1 .
    PIRi A03906. GNNYE.

    3D structure databases

    ProteinModelPortali P03304.
    SMRi P03304. Positions 1-32, 76-896.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03304. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    4.10.90.10. 1 hit.
    InterProi IPR015031. Capsid_VP4_Picornavir.
    IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR021573. Leader_pept_picornaV.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF00548. Peptidase_C3. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    PF08935. VP4_2. 1 hit.
    PF11475. VP_N-CPKC. 1 hit.
    [Graphical view ]
    PRINTSi PR00918. CALICVIRUSNS.
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region."
      Palmenberg A.C., Kirby E.M., Janda M.R., Drake N.L., Duke G.M., Potratz K.F., Collett M.S.
      Nucleic Acids Res. 12:2969-2985(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Nucleotide sequence of the 3'-terminus of encephalomyocarditis virus RNA."
      Petrov N.A., Chizhikov V.E., Blinov V.M., Karginov V.A., Mikryukov N.N., Gutorov V.V., Grishaev M.P., Beklemishev A.B., Vassilenko S.K.
      Bioorg. Khim. 10:274-279(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1337-2290.
    3. "TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus."
      Eldin P., Papon L., Oteiza A., Brocchi E., Lawson T.G., Mechti N.
      J. Gen. Virol. 90:536-545(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN TRIM22.
    4. "Site-specific cleavage of the host poly(A) binding protein by the encephalomyocarditis virus 3C proteinase stimulates viral replication."
      Kobayashi M., Arias C., Garabedian A., Palmenberg A.C., Mohr I.
      J. Virol. 86:10686-10694(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF PROTEASE 3C.

    Entry informationi

    Entry nameiPOLG_EMCV
    AccessioniPrimary (citable) accession number: P03304
    Secondary accession number(s): Q66764
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 127 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