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P13899

- POLG_TMEVD

UniProt

P13899 - POLG_TMEVD

Protein

Genome polyprotein

Gene
N/A
Organism
Theiler's murine encephalomyelitis virus (strain DA) (TMEV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    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.2 Publications
    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
    Sitei920 – 9212Cleavage; by protease 3CSequence Analysis
    Sitei1053 – 10542Cleavage; by ribosomal skipSequence Analysis
    Sitei1189 – 11902Cleavage; by protease 3CSequence Analysis
    Sitei1515 – 15162Cleavage; by protease 3CSequence Analysis
    Sitei1603 – 16042Cleavage; by protease 3CSequence Analysis
    Sitei1623 – 16242Cleavage; by protease 3CSequence Analysis
    Active sitei1678 – 16781For protease 3C activitySequence Analysis
    Active sitei1710 – 17101For protease 3C activitySequence Analysis
    Active sitei1791 – 17911For protease 3C activitySequence Analysis
    Sitei1840 – 18412Cleavage; by protease 3CSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri3 – 1412Sequence AnalysisAdd
    BLAST
    Nucleotide bindingi1310 – 13178ATPPROSITE-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 IRF3 activity Source: UniProtKB-KW
    6. suppression by virus of host mRNA export from nucleus Source: UniProtKB
    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-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 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
    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 DA) (TMEV)
    Taxonomic identifieri12126 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000000283: 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_0000040180Add
    BLAST
    Chaini77 – 414338Protein VP0Sequence AnalysisPRO_0000310971Add
    BLAST
    Chaini77 – 14771Protein VP4Sequence AnalysisPRO_0000040181Add
    BLAST
    Chaini148 – 414267Protein VP2Sequence AnalysisPRO_0000040182Add
    BLAST
    Chaini415 – 646232Protein VP3Sequence AnalysisPRO_0000040183Add
    BLAST
    Chaini647 – 920274Protein VP1Sequence AnalysisPRO_0000040184Add
    BLAST
    Chaini921 – 1053133Protein 2ASequence AnalysisPRO_0000040185Add
    BLAST
    Chaini1054 – 1189136Protein 2BSequence AnalysisPRO_0000040186Add
    BLAST
    Chaini1190 – 1515326Protein 2CSequence AnalysisPRO_0000040187Add
    BLAST
    Chaini1516 – 160388Protein 3ASequence AnalysisPRO_0000040188Add
    BLAST
    Chaini1604 – 162320Protein 3BSequence AnalysisPRO_0000040189Add
    BLAST
    Chaini1624 – 1840217Protease 3CSequence AnalysisPRO_0000040190Add
    BLAST
    Chaini1841 – 2301461RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000040191Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi77 – 771N-myristoyl glycine; by hostBy similarity
    Modified residuei1606 – 16061O-(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

    Secondary structure

    1
    2301
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi90 – 923
    Helixi103 – 1064
    Beta strandi162 – 1665
    Beta strandi169 – 1757
    Beta strandi179 – 1813
    Helixi182 – 1843
    Helixi204 – 2063
    Beta strandi210 – 2178
    Beta strandi226 – 2316
    Helixi233 – 2353
    Helixi238 – 2403
    Helixi241 – 2477
    Beta strandi250 – 26213
    Beta strandi270 – 27910
    Turni289 – 2913
    Beta strandi292 – 2954
    Beta strandi316 – 3183
    Helixi330 – 3356
    Beta strandi336 – 3427
    Turni343 – 3453
    Beta strandi347 – 3537
    Beta strandi358 – 3625
    Helixi364 – 3663
    Beta strandi370 – 38112
    Beta strandi390 – 40617
    Turni423 – 4264
    Beta strandi438 – 4403
    Helixi458 – 4636
    Beta strandi477 – 48610
    Beta strandi492 – 4976
    Turni503 – 5064
    Helixi508 – 5136
    Beta strandi516 – 5216
    Beta strandi523 – 5297
    Beta strandi536 – 5449
    Beta strandi546 – 5483
    Helixi554 – 5574
    Beta strandi560 – 5667
    Beta strandi568 – 5703
    Beta strandi572 – 5776
    Beta strandi582 – 5843
    Beta strandi586 – 5894
    Beta strandi601 – 61111
    Beta strandi618 – 62811
    Beta strandi633 – 6375
    Helixi651 – 6533
    Turni661 – 6644
    Helixi679 – 6835
    Beta strandi687 – 6926
    Beta strandi710 – 7156
    Beta strandi721 – 7233
    Beta strandi744 – 7496
    Beta strandi751 – 7555
    Helixi758 – 7625
    Beta strandi766 – 77914
    Beta strandi786 – 7927
    Helixi810 – 8123
    Beta strandi813 – 8164
    Beta strandi818 – 8236
    Beta strandi828 – 8336
    Beta strandi838 – 8458
    Beta strandi869 – 8757
    Beta strandi878 – 89215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TMEX-ray2.801647-920[»]
    2148-414[»]
    3415-650[»]
    477-147[»]
    1TMFX-ray3.50490-130[»]
    ProteinModelPortaliP13899.
    SMRiP13899. Positions 85-146, 159-413, 415-902.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13899.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 15601560CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1580 – 2301722CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1561 – 157919Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1281 – 1446166SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini2069 – 2187119RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 4617AcidicAdd
    BLAST
    Regioni60 – 7314TheiloAdd
    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.

    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.

    P13899-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACKHGYPDV CPICTAVDVT PGFEYLLLAD GEWFPTDLLC VDLDDDVFWP     50
    SNSSNQSETM EWTDLPLVRD IVMEPQGNAS SSDKSNSQSS GNEGVIINNF 100
    YSNQYQNSID LSASGGNAGD APQNNGQLSN ILGGAANAFA TMAPLLLDQN 150
    TEEMENLSDR VASDKAGNSA TNTQSTVGRL CGYGEAHHGE HPASCADTAT 200
    DKVLAAERYY TIDLASWTTT QEAFSHIRIP LPHVLAGEDG GVFGATLRRH 250
    YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG DMEPTDPFTM 300
    DTTWRAPQGA PTGYRYDSRT GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD 350
    LEVPYVNIAP TSSWTQHANW TLVVAVFSPL QYASGSSSDV QITASIQPVN 400
    PVFNGLRHET VIAQSPIAVT VREHKGCFYS TNPDTTVPIY GKTISTPNDY 450
    MCGEFSDLLE LCKLPTFLGN PNSNNKRYPY FSATNSVPTT SLVDYQVALS 500
    CSCMCNSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL IAYTPPGAGK 550
    PTTRDQAMQA TYAIWDLGLN SSFVFTAPFI SPTHYRQTSY TSATIASVDG 600
    WVTVWQLTPL TYPSGAPVNS DILTLVSAGD DFTLRMPISP TKWAPQGSDN 650
    AEKGKVSNDD ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNIES 700
    TFVYQENDLR LNCLLLTPLP SFCPDSTSGP VKTKAPVQWR WVRSGGTTNF 750
    PLMTKQDYAF LCFSPFTYYK CDLEVTVSAL GTDTVASVLR WAPTGAPADV 800
    TDQLIGYTPS LGETRNPHMW LVGAGNTQIS FVVPYNSPLS VLPAAWFNGW 850
    SDFGNTKDFG VAPNADFGRL WIQGNTSASV RIRYKKMKVF CPRPTLFFPW 900
    PVSTRSKINA DNPVPILELE NPAAFYRIDL FITFIDEFIT FDYKVHGRPV 950
    LTFRIPGFGL TPAGRMLVCM GEKPAHGPFT SSRSLYHVIF TATCSSFSFS 1000
    IYKGRYRSWK KPIHDELVDR GYTTFGEFFR AVRAYHADYY KQRLIHDVEM 1050
    NPGPVQSVFQ PQGAVLTKSL APQAGIQNLL LRLLGIDGDC SEVSKAITVV 1100
    TDLFAAWERA KTTLVSPEFW SKLILKTTKF IAASVLYLHN PDFTTTVCLS 1150
    LMTGVDLLTN DSVFDWLKNK LSSFFRTPPP VCPNVLQPQG PLREANEGFT 1200
    FAKNIEWAMK TIQSIVNWLT SWFKQEEDHP QSKLDKFLME FPDHCRNIMD 1250
    MRNGRKAYCE CTASFKYFDE LYNLAVTCKR IPLASLCEKF KNRHDHSVTR 1300
    PEPVVVVLRG AAGQGKSVTS QIIAQSVSKM AFGRQSVYSM PPDSEYFDGY 1350
    ENQFSVIMDD LGQNPDGEDF TVFCQMVSST NFLPNMAHLE RKGTPFTSSF 1400
    IVATTNLPKF RPVTVAHYPA VDRRITFDFT VTAGPHCTTS NGMLDIEKAF 1450
    DEIPGSKPQL ACFSADCPLL HKRGVMFTCN RTKAVYNLQQ VVKMVNDTIT 1500
    RKTENVKKMN SLVAQSPPDW EHFENILTCL RQNNAALQDQ LDELQEAFAQ 1550
    ARERSDFLSD WLKVSAIIFA GIASLSAVIK LASKFKESIW PSPVRVELSE 1600
    GEQAAYAGRA RAQKQALQVL DIQGGGKVLA QAGNPVMDFE LFCAKNMVAP 1650
    ITFYYPDKAE VTQSCLLLRA HLFVVNRHVA ETEWTAFKLK DVRHERDTVV 1700
    TRSVNRSGAE TDLTFIKVTK GPLFKDNVNK FCSNKDDFPA RNDAVTGIMN 1750
    TGLAFVYSGN FLIGNQPVNT TTGACFNHCL HYRAQTRRGW CGSAVICNVN 1800
    GKKAVYGMHS AGGGGLAAAT IITRELIEAA EKSMLALEPQ GAIVDISTGS 1850
    VVHVPRKTKL RRTVAHDVFQ PKFEPAVLSR YDPRTDKDVD VVAFSKHTTN 1900
    MESLPPVFDI VCDEYANRVF TILGKDNGLL TVEQAVLGLP GMDPMEKDTS 1950
    PGLPYTQQGL RRTDLLNFNT AKMTPQLDYA HSKLVLGVYD DVVYQSFLKD 2000
    EIRPLEKIHE AKTRIVDVPP FAHCIWGRQL LGRFASKFQT KPGLELGSAI 2050
    GTDPDVDWTP YAAELSGFNY VYDVDYSNFD ASHSTAMFEC LIKNFFTEQN 2100
    GFDRRIAEYL RSLAVSRHAY EDRRVLIRGG LLSGCAATSM LNTIMNNVII 2150
    RAALYLTYSN FEFDDIKVLS YGDDLLIGTN YQIDFNLVKE RLAPFGYKIT 2200
    PANKTTTFPL TSHLQDVTFL KRRFVRFNSY LFRPQMDAVN LKAMVSYCKP 2250
    GTLKEKLMSI ALLAVHSGPD IYDEIFLPFR NVGIVVPTYS SMLYRWLSLF 2300
    R 2301
    Length:2,301
    Mass (Da):256,161
    Last modified:January 1, 1990 - v1
    Checksum:i0B6095DF153DBFDF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20301 Genomic RNA. Translation: AAA47928.1.
    PIRiA31228. GNNYTN.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20301 Genomic RNA. Translation: AAA47928.1 .
    PIRi A31228. GNNYTN.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TME X-ray 2.80 1 647-920 [» ]
    2 148-414 [» ]
    3 415-650 [» ]
    4 77-147 [» ]
    1TMF X-ray 3.50 4 90-130 [» ]
    ProteinModelPortali P13899.
    SMRi P13899. Positions 85-146, 159-413, 415-902.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P13899.

    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. "Molecular cloning and sequence determination of DA strain of Theiler's murine encephalomyelitis viruses."
      Ohara Y., Stein S., Fu J., Stillman L., Klaman L., Roos R.P.
      Virology 164:245-255(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Alternative translation initiation site in the DA strain of Theiler's murine encephalomyelitis virus."
      Kong W.P., Roos R.P.
      J. Virol. 65:3395-3399(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE INITIATION.
    3. "Inhibition of mRNA export and dimerization of interferon regulatory factor 3 by Theiler's virus leader protein."
      Ricour C., Delhaye S., Hato S.V., Olenyik T.D., Michel B., van Kuppeveld F.J., Gustin K.E., Michiels T.
      J. Gen. Virol. 90:177-186(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE LEADER PROTEIN.
    4. "Random mutagenesis defines a domain of Theiler's virus leader protein that is essential for antagonism of nucleocytoplasmic trafficking and cytokine gene expression."
      Ricour C., Borghese F., Sorgeloos F., Hato S.V., van Kuppeveld F.J., Michiels T.
      J. Virol. 83:11223-11232(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE LEADER PROTEIN.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiPOLG_TMEVD
    AccessioniPrimary (citable) accession number: P13899
    Secondary accession number(s): Q88564
    , Q88565, Q88566, Q88567, Q88568, Q88569, Q88570, Q88571, Q88572, Q88573, Q88574, Q89580
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 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

    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