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P08544

- POLG_TMEVB

UniProt

P08544 - POLG_TMEVB

Protein

Genome polyprotein

Gene
N/A
Organism
Theiler's murine encephalomyelitis virus (strain BeAn 8386) (TMEV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      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 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 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 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 BeAn 8386) (TMEV)
    Taxonomic identifieri12125 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000007538: 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_0000040168Add
    BLAST
    Chaini77 – 414338Protein VP0Sequence AnalysisPRO_0000310970Add
    BLAST
    Chaini77 – 14771Protein VP4Sequence AnalysisPRO_0000040169Add
    BLAST
    Chaini148 – 414267Protein VP2Sequence AnalysisPRO_0000040170Add
    BLAST
    Chaini415 – 646232Protein VP3Sequence AnalysisPRO_0000040171Add
    BLAST
    Chaini647 – 922276Protein VP1Sequence AnalysisPRO_0000040172Add
    BLAST
    Chaini923 – 1055133Protein 2ASequence AnalysisPRO_0000040173Add
    BLAST
    Chaini1056 – 1191136Protein 2BSequence AnalysisPRO_0000040174Add
    BLAST
    Chaini1192 – 1517326Protein 2CSequence AnalysisPRO_0000040175Add
    BLAST
    Chaini1518 – 160588Protein 3ASequence AnalysisPRO_0000040176Add
    BLAST
    Chaini1606 – 162520Protein 3BSequence AnalysisPRO_0000040177Add
    BLAST
    Chaini1626 – 1842217Protease 3CSequence AnalysisPRO_0000040178Add
    BLAST
    Chaini1843 – 2303461RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000040179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi77 – 771N-myristoyl glycine; by hostBy similarity
    Disulfide bondi501 ↔ 503
    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, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

    Structurei

    Secondary structure

    1
    2303
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi158 – 1603
    Beta strandi162 – 1665
    Beta strandi169 – 1757
    Beta strandi180 – 1845
    Helixi204 – 2063
    Beta strandi210 – 2178
    Beta strandi228 – 2325
    Beta strandi235 – 2384
    Helixi241 – 2477
    Beta strandi248 – 2536
    Beta strandi256 – 2627
    Beta strandi272 – 2809
    Beta strandi289 – 2935
    Turni330 – 3345
    Beta strandi335 – 3417
    Turni343 – 3453
    Beta strandi347 – 3537
    Beta strandi357 – 3637
    Turni364 – 3663
    Beta strandi369 – 37810
    Beta strandi390 – 40011
    Beta strandi403 – 4064
    Turni459 – 4635
    Beta strandi473 – 4753
    Beta strandi492 – 4954
    Beta strandi501 – 5044
    Helixi508 – 5114
    Beta strandi515 – 5217
    Beta strandi524 – 5296
    Beta strandi536 – 5438
    Beta strandi546 – 5483
    Helixi554 – 5574
    Beta strandi560 – 5623
    Beta strandi568 – 5703
    Beta strandi572 – 5754
    Beta strandi582 – 5876
    Beta strandi602 – 61110
    Beta strandi622 – 6276
    Beta strandi633 – 6364
    Beta strandi661 – 6666
    Turni680 – 6845
    Beta strandi698 – 7003
    Beta strandi712 – 7143
    Beta strandi717 – 7193
    Beta strandi727 – 7293
    Beta strandi732 – 7343
    Beta strandi747 – 7493
    Beta strandi751 – 7533
    Turni760 – 7645
    Beta strandi769 – 78012
    Beta strandi791 – 7944
    Beta strandi807 – 8093
    Beta strandi820 – 8223
    Beta strandi831 – 8355
    Beta strandi842 – 8476
    Beta strandi853 – 8564
    Beta strandi861 – 8633
    Beta strandi871 – 8744
    Beta strandi880 – 89314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TMFX-ray3.501647-922[»]
    2148-414[»]
    3415-646[»]
    ProteinModelPortaliP08544.
    SMRiP08544. Positions 85-146, 148-922.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08544.

    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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi79 – 824Poly-Ser
    Compositional biasi1306 – 13094Poly-Val
    Compositional biasi1814 – 18174Poly-Gly

    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.

    P08544-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACKHGYPDV CPICTAVDAT PGFEYLLMAD GEWYPTDLLC VDLDDDVFWP     50
    SDTSNQSQTM DWTDVPLIRD IVMEPQGNSS SSDKSNSQSS GNEGVIINNF 100
    YSNQYQNSID LSASGGNAGD APQTNGQLSN ILGGAANAFA TMAPLLLDQN 150
    TEEMENLSDR VASDKAGNSA TNTQSTVGRL CGYGKSHHGE HPASCADTAT 200
    DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG GVFGATLRRH 250
    YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG TMEPSDPFTM 300
    DTEWRSPQGA PTGYRYDSRT GFFATNHQNQ WQWTVYPHQI LNLRTNTTVD 350
    LEVPYVNVAP SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN 400
    PVFNGLRHET VIAQSPIPVT VREHKGCFYS TNPDTTVPIY GKTISTPSDY 450
    MCGEFSDLLE LCKLPTFLGN PNTNNKRYPY FSATNSVPAT SMVDYQVALS 500
    CSCMANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL IAYTPPGAGK 550
    PTTRDQAMQS TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG 600
    WVTVWKLTPL TYPSGTPTNS DILTLVSAGD DFTLRMPISP TKWVPQGVDN 650
    AEKGKVSNDD ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET 700
    TFNYQENDYR LNCLLLTPLP SFCPDSSSGP QKTKAPVQWR WVRSGGVNGA 750
    NFPLMTKQDY AFLCFSPFTF YKCDLEVTVS ALGMTRVASV LRWAPTGAPA 800
    DVTDQLIGYT PSLGETRNPH MWLVGAGNSQ VSFVVPYNSP LSVLPAAWFN 850
    GWSDFGNTKD FGVAPNADFG RLWIQGNTSA SVRIRYKKMK VFCPRPTLFF 900
    PWPTPTTTKI NADNPVPILE LENPAALYRI DLFITFTDEF ITFDYKVHGR 950
    PVLTFRIPGF GLTPAGRMLV CMGEQPAHGP FTSSRSLYHV IFTATCSSFS 1000
    FSIYKGRYRS WKKPIHDELV DRGYTTFGEF FKAVRGYHAD YYRQRLIHDV 1050
    ETNPGPVQSV FQPQGAVLTK SLAPQAGIQN LLLRLLGIDG DCSEVSKAIT 1100
    VVTDLVAAWE KAKTTLVSPE FWSKLILKTT KFIAASVLYL HNPDFTTTVC 1150
    LSLMTGVDLL TNDSVFDWLK QKLSSFFRTP PPACPNVMQP QGPLREANEG 1200
    FTFAKNIEWA MKTIQSVVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI 1250
    MDMRNGRKAY CECTASFKYF DELYNLAVTC KRIPLASLCE KFKNRHDHSV 1300
    TRPEPVVVVL RGAAGQGKSV TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD 1350
    GYENQFSVIM DDLGQNPDGE DFTVFCQMVS STNFLPNMAH LERKGTPFTS 1400
    SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK TPAGMLDVEK 1450
    AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTQTVYNL QQVVKMVNDT 1500
    ITRKTENVKK MNSLVAQSPP DWEHFENILT CLRQNNAALQ DQLDELQEAF 1550
    AQARERSDFL SDWLKVSAII FAGIASLSAV IKLASKFKES IWPTPVRVEL 1600
    SEGEQAAYAG RARAQKQALQ VLDIQGGGKV LAQAGNPVMD FELFCAKNIV 1650
    APITFYYPDK AEVTQSCLLL RAHLFVVNRH VAETDWTAFK LKDVRHERHT 1700
    VALRSVNRSG AKTDLTFIKV TKGPLFKDNV NKFCSNKDDF PARNDTVTGI 1750
    MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN 1800
    VNGKKAVYGM HSAGGGGLAA ATIITKELIE AAEKSMLALE PQGAIVDIAT 1850
    GSVVHVPRKT KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT 1900
    TNMESLPPIF DVVCGEYANR VFTILGKENG LLTVEQAVLG LPGMDPMEKD 1950
    TSPGLPYTQQ GLRRTDLLNF ITAKMTPQLD YAHSKLVIGV YDDVVYQSFL 2000
    KDEIRPIEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF QTKPGLELGS 2050
    AIGTDPDVDW TRYAVELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE 2100
    QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV 2150
    IIRAALYLTY SNFDFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK 2200
    ITPANKTTTF PLTSHLQDVT FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC 2250
    KPGTLKEKLM SIALLAVHSG PDIYDEIFLP FRNVGIVVPT YSSMLYRWLS 2300
    LFR 2303
    Length:2,303
    Mass (Da):256,282
    Last modified:August 1, 1988 - v1
    Checksum:iE2C7737DFDBEB786
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16020 Genomic RNA. Translation: AAA47930.1.
    PIRiA29535. GNNYTM.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16020 Genomic RNA. Translation: AAA47930.1 .
    PIRi A29535. GNNYTM.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TMF X-ray 3.50 1 647-922 [» ]
    2 148-414 [» ]
    3 415-646 [» ]
    ProteinModelPortali P08544.
    SMRi P08544. Positions 85-146, 148-922.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P08544.

    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. "Analysis of the complete nucleotide sequence of the picornavirus Theiler's murine encephalomyelitis virus indicates that it is closely related to cardioviruses."
      Pevear D.C., Calenoff M., Rozhon E., Lipton H.L.
      J. Virol. 61:1507-1516(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Three-dimensional structure of Theiler murine encephalomyelitis virus (BeAn strain)."
      Luo M., He C., Toth K.S., Zhang C.X., Lipton H.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:2409-2413(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 148-922.

    Entry informationi

    Entry nameiPOLG_TMEVB
    AccessioniPrimary (citable) accession number: P08544
    Secondary accession number(s): Q88583
    , Q88584, Q88585, Q88586, Q88587, Q88588, Q88589, Q88590, Q88591, Q88592
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 141 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

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