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Q66765

- POLG_EMCVR

UniProt

Q66765 - POLG_EMCVR

Protein

Genome polyprotein

Gene
N/A
Organism
Encephalomyocarditis virus (strain Rueckert) (EMCV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Leadear 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.
    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 By similarity. The capsid interacts with host VCAM1 to provide virion attachment on murine vascular endothelial cells.By similarity
    Protein VP0: Protein VP0: VP0 precursor is a component of immature procapsids.By similarity
    Protein 2A: involved in host translation shutoff. Nuclear localization is required for this function.
    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. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease By similarity.By similarity
    RNA-directed RNA polymerase 3D-POL: replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation

    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
    Sitei137 – 1382CleavageSequence Analysis
    Sitei393 – 3942Cleavage; by protease 3CSequence Analysis
    Sitei624 – 6252Cleavage; by protease 3CSequence Analysis
    Sitei901 – 9022Cleavage; by protease 3CSequence Analysis
    Sitei1044 – 10452Cleavage; by ribosomal skipSequence Analysis
    Sitei1194 – 11952Cleavage; by protease 3CSequence Analysis
    Sitei1519 – 15202Cleavage; by protease 3CSequence Analysis
    Sitei1607 – 16082Cleavage; by protease 3CSequence Analysis
    Sitei1627 – 16282Cleavage; by protease 3CSequence Analysis
    Active sitei1673 – 16731For protease 3C activitySequence Analysis
    Active sitei1705 – 17051For protease 3C activitySequence Analysis
    Active sitei1786 – 17861For protease 3C activitySequence Analysis
    Sitei1832 – 18332Cleavage; by protease 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri10 – 2213Sequence AnalysisAdd
    BLAST
    Nucleotide bindingi1313 – 13208ATPPROSITE-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. RNA binding Source: UniProtKB-KW
    6. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    7. RNA helicase activity Source: InterPro
    8. 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 (strain Rueckert) (EMCV)
    Taxonomic identifieri650129 [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]
    ProteomesiUP000002319: 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 proteinBy similarityPRO_0000423146Add
    BLAST
    Chaini68 – 393326Protein VP0Sequence AnalysisPRO_0000423147Add
    BLAST
    Chaini68 – 13770Protein VP4Sequence AnalysisPRO_5000143569Add
    BLAST
    Chaini138 – 393256Protein VP2Sequence AnalysisPRO_5000143570Add
    BLAST
    Chaini394 – 624231Protein VP3Sequence AnalysisPRO_5000143571Add
    BLAST
    Chaini625 – 901277Protein VP1Sequence AnalysisPRO_5000143572Add
    BLAST
    Chaini902 – 1044143Protein 2ASequence AnalysisPRO_5000143573Add
    BLAST
    Chaini1045 – 1194150Protein 2BSequence AnalysisPRO_5000143574Add
    BLAST
    Chaini1195 – 1519325Protein 2CSequence AnalysisPRO_5000143575Add
    BLAST
    Chaini1520 – 160788Protein 3ASequence AnalysisPRO_5000143576Add
    BLAST
    Chaini1608 – 162720Protein 3BSequence AnalysisPRO_0000423148Add
    BLAST
    Chaini1628 – 1832205Protease 3CSequence AnalysisPRO_5000143577Add
    BLAST
    Chaini1833 – 2292460RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_5000143578Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi68 – 681N-myristoyl glycine; by hostBy similarity
    Modified residuei1610 – 16101O-(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 By similarity. Protein 2A interacts with host EIF4E.By similarity1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ66765.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 15641564CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1584 – 2292709CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1565 – 158319Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1281 – 1447167SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini2061 – 2179119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 6125AcidicBy similarityAdd
    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: Q66765-1) [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 PPRTYGQFSN LFSGAVNAFS NMLPLLADQN TEEMENLSDR 150
    VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE HPASCADTAS EKILAVERYY 200
    TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGAALRRH YLVKTGWRVQ 250
    VQCNASQFHA GGLLVFMAPE YPTLDAFAMD NRWSKDNLPN GTRTQTNKKG 300
    PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT 350
    LVIAVVAPLT YSTGASTSLD ITASIQPVRP VFNGLRHETL SRQSPIPVTI 400
    REHAGTWYST LPDSTVPIYG KTPVAPSNYM VGEYKDFLEI AQIPTFIGNK 450
    IPNAVPYIEA SNTAVKTQPL ATYQVTLSCS CLANTFLAAL SRNFAQYRGS 500
    LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY AIWDLGLNSS 550
    YSFTVPFISP THFRMVGTDQ VNITNADGWV TVWQLTPLTY PPGCPTSAKI 600
    LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTNAT ADFVAQPVYL 650
    PENQTKVAFF YNRSSPIGAF TVKSGSLESG FAPFSNGTCP NSVILTPGPQ 700
    FDPAYDQLRP QRLTEIWGNG NEETSKVFPL KSKQDYSFCL FSPFVYYKCD 750
    LEVTLSPHTS GNHGLLVRWC PTGTPTKPTT QVLHEVSSLS EGRTPQVYSA 800
    GPGISNQISF VVPYNSPLSV LSAVWYNGHK RFDNTGSLGI APNSDFGTLF 850
    FAGTKPDIKF TVYLRYKNKR VFCPRPTVFF PWPTSGDKID MTPRAGVLML 900
    ESPNALDISR TYPTLHVLIQ FNHRGLEVRL FRHGHFWAET RADVILRSKT 950
    KQVSFLSNGN YPSMDSRAPW NPWKNTYQAV LRAEPCRVTM DIYYKRVRPF 1000
    RLPLVQKEWP VREENVFGLY RIFNAHYAGY FADLLIHDIE TNPGPFMFRP 1050
    RKQVFQTQGA AVSSMAQTLL PNDLASKAMG SAFTALLDAN EDAQKAMKII 1100
    KTLSSLSDAW ENVKETLNNP EFWKQLLSRC VQLIAGMTIA VMHPDPLTLL 1150
    CLGTLTAAEI TSQTSLCEEI AAKFKTIFIT PPPRFPTISL FQQQSPLKQV 1200
    NDIFSLAKNL DWAVKTVEKV VDWFGTWIVQ EEKEQTLDQL LQRFPEHAKR 1250
    ISDLRNGMAA YVECKESFDF FEKLYNQAVK EKRTGIAAVC EKFRQKHDHA 1300
    TARCEPVVIV LRGDAGQGKS LSSQVIAQAV SKTIFGRQSV YSLPPDSDFF 1350
    DGYENQFAAI MDDLGQNPDG SDFTTFCQMV STTNFLPNMA SLERKGTPFT 1400
    SQLVVATTNL PEFRPVTIAH YPAVERRITF DYSVSAGPVC SKTEAGYKVL 1450
    DVERAFRPTG EAPLPCFQNN CLFLEKAGLQ FRDNRTKEII SLVDVIERAV 1500
    ARIERKKKVL TTVQTLVAQG PVDEVSFHSV VQQLKARQQA TDEQLEELQE 1550
    AFAKVQERNS VFSDWLKISA MLCAATLALS QVVKMAKAVK QMVKPDLVRV 1600
    QLDEQEQGPY NETARVKPKT LQLLDIQGPN PVMDFEKYVA KHVTAPIGFV 1650
    YPTGVSTQTC LLVRGRTLVV NRHMAESDWT SIVVRGVTHA RSTVKILAIA 1700
    KAGKETDVSF IRLSSGPLFR DNTSKFVKAG DVLPTGAAPV TGIMNTDIPM 1750
    MYTGTFLKAG VSVPVETGQT FNHCIHYKAN TRKGWCGSAL LADLGGSKKI 1800
    LGIHSAGSMG IAAASIVSQE MIRAVVNAFE PQGALERLPD GPRIHVPRKT 1850
    ALRPTVARQV FQPAYAPAVL SKFDPRTEAD VDEVAFSKHT SNQESLPPVF 1900
    RMVAKEYANR VFTLLGKDNG RLTVKQALEG LEGMDPMDRN TSPGLPYTAL 1950
    GMRRTDVVDW ESATLIPFAA ERLRKMNEGD FSEVVYQTFL KDELRPIEKV 2000
    QAAKTRIVDV PPFEHCILGR QLLGKFASKF QTQPGLELGS AIGCDPDVHW 2050
    TAFGVAMQGF ERVYDVDYSN FDSTHSVAMF RLLAEEFFTP ENGFDPLTRE 2100
    YLESLAISTH AFEEKRFLIT GGLPSGCAAT SMLNTIMNNI IIRAGLYLTY 2150
    KNFEFDDVKV LSYGDDLLVA TNYQLDFDKV RASLAKTGYK ITPANTTSTF 2200
    PLNSTLEDVV FLKRKFKKEG PLYRPVMNRE ALEAMLSYYR PGTLSEKLTS 2250
    ITMLAVHSGK QEYDRLFAPF REVGVVVPSF ESVEYRWRSL FW 2292

    Note: Produced by conventional translation.

    Length:2,292
    Mass (Da):255,459
    Last modified:November 1, 1996 - v1
    Checksum:i01C0537888CEFC94
    GO
    Isoform 2B* (identifier: P0DJX6-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P0DJX6.
    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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81861 Genomic RNA. Translation: AAA43037.1.
    RefSeqiNP_056777.1. NC_001479.1.

    Genome annotation databases

    GeneIDi1493923.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81861 Genomic RNA. Translation: AAA43037.1 .
    RefSeqi NP_056777.1. NC_001479.1.

    3D structure databases

    ProteinModelPortali Q66765.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1493923.

    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. "Sequence and structural elements that contribute to efficient encephalomyocarditis virus RNA translation."
      Duke G.M., Hoffman M.A., Palmenberg A.C.
      J. Virol. 66:1602-1609(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardioviruses."
      Porter F.W., Palmenberg A.C.
      J. Virol. 83:1941-1951(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF LEADER PROTEIN.
    3. "Mutational analysis of the EMCV 2A protein identifies a nuclear localization signal and an eIF4E binding site."
      Groppo R., Brown B.A., Palmenberg A.C.
      Virology 410:257-267(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF PROTEIN 2A, SUBCELLULAR LOCATION OF PROTEIN 2A, INTERACTION OF PROTEIN 2A WITH HUMAN EIF4E.

    Entry informationi

    Entry nameiPOLG_EMCVR
    AccessioniPrimary (citable) accession number: Q66765
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2013
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 96 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