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P08544

- POLG_TMEVB

UniProt

P08544 - POLG_TMEVB

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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

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.
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.
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.
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.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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 – 1482Cleavage Reviewed prediction
Sitei414 – 4152Cleavage; by protease 3C Reviewed prediction
Sitei646 – 6472Cleavage; by protease 3C Reviewed prediction
Sitei922 – 9232Cleavage; by protease 3C Reviewed prediction
Sitei1055 – 10562Cleavage; by ribosomal skip Reviewed prediction
Sitei1191 – 11922Cleavage; by protease 3C Reviewed prediction
Sitei1517 – 15182Cleavage; by protease 3C Reviewed prediction
Sitei1605 – 16062Cleavage; by protease 3C Reviewed prediction
Sitei1625 – 16262Cleavage; by protease 3C Reviewed prediction
Active sitei1680 – 16801For protease 3C activity Reviewed prediction
Active sitei1793 – 17931For protease 3C activity Reviewed prediction
Sitei1842 – 18432Cleavage; by protease 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri3 – 1412 Reviewed prediction
Add
BLAST
Nucleotide bindingi1312 – 13198ATP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. induction by virus of host autophagy Source: UniProtKB
  3. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  4. protein oligomerization Source: UniProtKB-KW
  5. suppression by virus of host IRF3 activity Source: UniProtKB-KW
  6. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  7. suppression by virus of host mRNA export from nucleus Source: UniProtKB
  8. suppression by virus of host translation Source: UniProtKB-KW
  9. transcription, DNA-templated Source: InterPro
  10. viral RNA genome replication Source: InterPro
  11. viral entry into host cell Source: UniProtKB-KW
  12. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

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 VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B : Virion Reviewed prediction
Chain Protease 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 15621562Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1563 – 158119 Reviewed prediction
Add
BLAST
Topological domaini1582 – 2303722Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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 protein
PRO_0000040168Add
BLAST
Chaini77 – 414338Protein VP0 Reviewed prediction
PRO_0000310970Add
BLAST
Chaini77 – 14771Protein VP4 Reviewed prediction
PRO_0000040169Add
BLAST
Chaini148 – 414267Protein VP2 Reviewed prediction
PRO_0000040170Add
BLAST
Chaini415 – 646232Protein VP3 Reviewed prediction
PRO_0000040171Add
BLAST
Chaini647 – 922276Protein VP1 Reviewed prediction
PRO_0000040172Add
BLAST
Chaini923 – 1055133Protein 2A Reviewed prediction
PRO_0000040173Add
BLAST
Chaini1056 – 1191136Protein 2B Reviewed prediction
PRO_0000040174Add
BLAST
Chaini1192 – 1517326Protein 2C Reviewed prediction
PRO_0000040175Add
BLAST
Chaini1518 – 160588Protein 3A Reviewed prediction
PRO_0000040176Add
BLAST
Chaini1606 – 162520Protein 3B Reviewed prediction
PRO_0000040177Add
BLAST
Chaini1626 – 1842217Protease 3C Reviewed prediction
PRO_0000040178Add
BLAST
Chaini1843 – 2303461RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000040179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi77 – 771N-myristoyl glycine; by host By similarity
Disulfide bondi501 ↔ 503
Modified residuei1608 – 16081O-(5'-phospho-RNA)-tyrosine By 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.
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.
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

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.

Miscellaneous databases

EvolutionaryTraceiP08544.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1283 – 1448166SF3 helicase
Add
BLAST
Domaini2071 – 2189119RdRp catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 4617Acidic
Add
BLAST
Regioni60 – 7314Theilo By similarity
Add
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

Contains 2 peptidase C3 domains.

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

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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: July 9, 2014
This is version 140 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

Similar proteinsi