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)

P08545

- POLG_TMEVG

UniProt

P08545 - POLG_TMEVG

Protein

Genome polyprotein

Gene
N/A
Organism
Theiler's murine encephalomyelitis virus (strain GDVII) (TMEV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Leader protein: promotes host NUP98 phosphorylation and blocks the export of host mRNA from the nucleus. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. The leader protein also inhibit host interferon regulatory factor 3 (IRF3) dimerization, thereby blocking the transcriptional activation of IFN genes 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 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. 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
    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
    Sitei147 – 1482CleavageSequence Analysis
    Sitei414 – 4152Cleavage; by protease 3CSequence Analysis
    Sitei646 – 6472Cleavage; by protease 3CSequence Analysis
    Sitei922 – 9232Cleavage; by protease 3CSequence Analysis
    Sitei1055 – 10562Cleavage; by ribosomal skipSequence Analysis
    Sitei1191 – 11922Cleavage; by protease 3CSequence Analysis
    Sitei1517 – 15182Cleavage; by protease 3CSequence Analysis
    Sitei1605 – 16062Cleavage; by protease 3CSequence Analysis
    Sitei1625 – 16262Cleavage; by protease 3CSequence Analysis
    Active sitei1680 – 16801For protease 3C activitySequence Analysis
    Active sitei1712 – 17121For protease 3C activitySequence Analysis
    Active sitei1793 – 17931For protease 3C activitySequence Analysis
    Sitei1842 – 18432Cleavage; by protease 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3 – 1412Sequence AnalysisAdd
    BLAST
    Nucleotide bindingi1312 – 13198ATPPROSITE-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

    Protein family/group databases

    MEROPSiC03.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 13 chains:
    Alternative name(s):
    VP4-VP2
    Alternative name(s):
    P1A
    Virion protein 4
    Alternative name(s):
    P1B
    Virion protein 2
    Alternative name(s):
    P1C
    Virion protein 3
    Alternative name(s):
    P1D
    Virion protein 1
    Protein 2A
    Short name:
    P2A
    Protein 2B
    Short name:
    P2B
    Protein 2C (EC:3.6.1.15)
    Short name:
    P2C
    Protein 3A
    Short name:
    P3A
    Protein 3B
    Short name:
    P3B
    Alternative name(s):
    VPg
    Protease 3C (EC:3.4.22.28)
    Short name:
    P3C
    Alternative name(s):
    Picornain 3C
    OrganismiTheiler's murine encephalomyelitis virus (strain GDVII) (TMEV)
    Taxonomic identifieri12127 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000008247: 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 – 7676Leader proteinPRO_0000040192Add
    BLAST
    Chaini77 – 414338Protein VP0Sequence AnalysisPRO_0000310972Add
    BLAST
    Chaini77 – 14771Protein VP4Sequence AnalysisPRO_0000040193Add
    BLAST
    Chaini148 – 414267Protein VP2Sequence AnalysisPRO_0000040194Add
    BLAST
    Chaini415 – 646232Protein VP3Sequence AnalysisPRO_0000040195Add
    BLAST
    Chaini647 – 922276Protein VP1Sequence AnalysisPRO_0000040196Add
    BLAST
    Chaini923 – 1055133Protein 2ASequence AnalysisPRO_0000040197Add
    BLAST
    Chaini1056 – 1191136Protein 2BSequence AnalysisPRO_0000040198Add
    BLAST
    Chaini1192 – 1517326Protein 2CSequence AnalysisPRO_0000040199Add
    BLAST
    Chaini1518 – 160588Protein 3ASequence AnalysisPRO_0000040200Add
    BLAST
    Chaini1606 – 162520Protein 3BSequence AnalysisPRO_0000040201Add
    BLAST
    Chaini1626 – 1842217Protease 3CSequence AnalysisPRO_0000040202Add
    BLAST
    Chaini1843 – 2303461RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000040203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi77 – 771N-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

    Structurei

    3D structure databases

    ProteinModelPortaliP08545.
    SMRiP08545. Positions 85-146, 148-922.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 15621562CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1582 – 2303722CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1283 – 1448166SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini2071 – 2189119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 4617AcidicAdd
    BLAST
    Regioni60 – 7314TheiloBy similarityAdd
    BLAST

    Domaini

    The Theilo and zinc-finger regions may both play a role in the inhibition of host mRNA export and IRF-3 dimerization antagonism by the L protein.By similarity

    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 fingeri3 – 1412Sequence 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.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR002527. Pico_P2B.
    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.
    [Graphical view]
    PRINTSiPR00918. CALICVIRUSNS.
    ProDomiPD649346. Pico_P2B. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF50494. SSF50494. 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.

    P08545-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACKHGYPDV CPICTAVDAT PDFEYLLMAD GEWFPTDLLC VDLDDDVFWP     50
    SDTSTQPQTM EWTDVPLVCD TVMEPQGNAS SSDKSNSQSS GNEGVIINNF 100
    YSNQYQNSID LSASGGNAGD APQNNGQLSS ILGGAANAFA TMAPLLMDQN 150
    TEEMENLSDR VASDKAGNSA TNTQSTVGRL CGYGKSHHGE HPTSCADAAT 200
    DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG GVFGATLRRH 250
    YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKSG TMEPSDPFTM 300
    DTTWRSPQSA PTGYRYDRQA GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD 350
    LEVPYVNVAP SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN 400
    PVFNGLRHET VLAQSPIPVT VREHQGCFYS TNPDTTVPIY GKTISTPSDY 450
    MCGEFSDLLE LCKLPTFLGN PSTDNKRYPY FSATNSVPAT SLVDYQVALS 500
    CSCTANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFR IAYTPPGAGK 550
    PTTRDQAMQA TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG 600
    WVTVWQLTPL TYPSGTPTHS DILTLVSAGD DFTLRMPISP TKWVPQGIDN 650
    AEKGKVSNDD ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET 700
    TFSYQENDFR LNCLLLTPLP SYCPDSSSGP VRTKAPVQWR WVRSGGANGA 750
    NFPLMTKQDY AFLCFSPFTY YKCDLEVTVS AMGAGTVSSV LRWAPTGAPA 800
    DVTDQLIGYT PSLGETRNPH MWIVGSGNSQ ISFVVPYNSP LSVLPAAWFN 850
    GWSDFGNTKD FGVAPTSDFG RIWIQGNSSA SVRIRYKKMK VFCPRPTLFF 900
    PWPTPTTTKI NADNPVPILE LENPASLYRI DLFITFTDEL ITFDYKVHGR 950
    PVLTFRIPGF GLTPAGRMLV CMGAKPAHSP FTSSKSLYHV IFTSTCNSFS 1000
    FTIYKGRYRS WKKPIHDELV DRGYTTFREF FKAVRGYHAD YYKQRLIHDV 1050
    EMNPGPVQSV FQPQGAVLTK SLAPQAGIQN ILLRLLGIEG DCSEVSKAIT 1100
    VVTDLVAAWE KAKTTLVSPE FWSELILKTT KFIAASVLYL HNPDFTTTVC 1150
    LSLMTGVDLL TNDSVFDWLK SKLSSFFRTP PPACPNVMQP QGPLREANEG 1200
    FTFAKNIEWA TKTIQSIVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI 1250
    MDMRNGRKAY CECTASFKYF DDLYNLAVTC KRIPLASLCE KFKNRHDHSV 1300
    TRPEPVVAVL RGAAGQGKSV TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD 1350
    GYENQFSVIM DDLGQNPDGE DFTVFCQMVS STNFLPNMAH LERKGTPFTS 1400
    SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK TPAGMLDIEK 1450
    AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTKTVYNL QQVVKMVNDT 1500
    ITRKTENVKK MNSLVAQSPP DWQHFENILT CLRQNNAALQ DQVDELQEAF 1550
    TQARERSDFL SDWLKVSAII FAGIVSLSAV IKLASKFKES IWPTPVRVEL 1600
    SEGEQAAYAG RARAQKQALQ VLDIQGGGKV LAQAGNPVMD FELFCAKNMV 1650
    SPITFYYPDK AEVTQSCLLL RAHLFVVNRH VAETEWTAFK LRDVRHERDT 1700
    VVMRSVNRSG AETDLTFVKV TKGPLFKDNV NKFCSNKDDF PARNDTVTGI 1750
    MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN 1800
    VNGKKAVYGM HSAGGGGLAA ATIITRELIE AAEKSMLALE PQGAIVDIST 1850
    GSVVHVPRKT KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT 1900
    TNMESLPPIF DIVCGEYANR VFTILGKDNG LLTVEQAVLG LSGMDPMEKD 1950
    TSPGLPYTQQ GLRRTDLLDF NTAKMTPQLD YAHSKLVLGV YDDVVYQSFL 2000
    KDEIRPLEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF QTKPGFELGS 2050
    AIGTDPDVDW TRYAAELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE 2100
    QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV 2150
    IIRAALYLTY SNFEFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK 2200
    ITPANKTTTF PLTSHLQDVT FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC 2250
    KPGTLKEKLM SIALLAVHSG PDIYDEIFLP FRNVGIVVPT YDSMLYRWLS 2300
    LFR 2303
    Length:2,303
    Mass (Da):256,344
    Last modified:January 1, 1990 - v2
    Checksum:i5D0FBE6E47F72A04
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1747 – 17504VTGI → CYRD in AAA47933. (PubMed:3023668)Curated
    Sequence conflicti1992 – 20009DDVVYQSFL → GRRCLPIIF in AAA47933. (PubMed:3023668)Curated
    Sequence conflicti2003 – 20031E → Q(PubMed:3023668)Curated
    Sequence conflicti2008 – 20081E → H in AAA47933. (PubMed:3023668)Curated
    Sequence conflicti2046 – 20461F → L in AAA47933. (PubMed:3023668)Curated
    Sequence conflicti2128 – 21347LIRGGLP → YSWGPA in AAA47933. (PubMed:3023668)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20562 Genomic RNA. Translation: AAA47929.1.
    M14703 Genomic RNA. Translation: AAA47933.1.
    PIRiA26100.
    A29193. GNNYTP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20562 Genomic RNA. Translation: AAA47929.1 .
    M14703 Genomic RNA. Translation: AAA47933.1 .
    PIRi A26100.
    A29193. GNNYTP.

    3D structure databases

    ProteinModelPortali P08545.
    SMRi P08545. Positions 85-146, 148-922.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.010.

    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.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR002527. Pico_P2B.
    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.
    [Graphical view ]
    PRINTSi PR00918. CALICVIRUSNS.
    ProDomi PD649346. Pico_P2B. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Insights into Theiler's virus neurovirulence based on a genomic comparison of the neurovirulent GDVII and less virulent BeAn strains."
      Pevear D.C., Borkowski J., Calenoff M., Oh C.K., Ostrawski B., Lipton H.L.
      Virology 165:1-12(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Theiler's virus genome is closely related to that of encephalomyocarditis virus, the prototype cardiovirus."
      Ozden S., Tangy F., Chamorro M., Brahic M.
      J. Virol. 60:1163-1165(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1704-2303.

    Entry informationi

    Entry nameiPOLG_TMEVG
    AccessioniPrimary (citable) accession number: P08545
    Secondary accession number(s): Q88593, Q88594
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Persistent strains of Theiler's virus (e.g. DA, TO, BeAn) cause persistent demyelinating disease whereas neurovirulent strains (such as GDVII) cause acute encephalitis.

    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