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P13899

- POLG_TMEVD

UniProt

P13899 - POLG_TMEVD

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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

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.2 Publications
Protein VP0: VP0 precursor is a component of immature procapsids By similarity.2 Publications
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity.2 Publications
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.2 Publications
Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity.2 Publications
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.2 Publications
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.2 Publications
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity.2 Publications

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
Sitei920 – 9212Cleavage; by protease 3C Reviewed prediction
Sitei1053 – 10542Cleavage; by ribosomal skip Reviewed prediction
Sitei1189 – 11902Cleavage; by protease 3C Reviewed prediction
Sitei1515 – 15162Cleavage; by protease 3C Reviewed prediction
Sitei1603 – 16042Cleavage; by protease 3C Reviewed prediction
Sitei1623 – 16242Cleavage; by protease 3C Reviewed prediction
Active sitei1678 – 16781For protease 3C activity Reviewed prediction
Active sitei1710 – 17101For protease 3C activity Reviewed prediction
Active sitei1791 – 17911For protease 3C activity Reviewed prediction
Sitei1840 – 18412Cleavage; by protease 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri3 – 1412 Reviewed prediction
Add
BLAST
Nucleotide bindingi1310 – 13178ATP 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 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 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 – 15601560Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1561 – 157919 Reviewed prediction
Add
BLAST
Topological domaini1580 – 2301722Cytoplasmic 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_0000040180Add
BLAST
Chaini77 – 414338Protein VP0 Reviewed prediction
PRO_0000310971Add
BLAST
Chaini77 – 14771Protein VP4 Reviewed prediction
PRO_0000040181Add
BLAST
Chaini148 – 414267Protein VP2 Reviewed prediction
PRO_0000040182Add
BLAST
Chaini415 – 646232Protein VP3 Reviewed prediction
PRO_0000040183Add
BLAST
Chaini647 – 920274Protein VP1 Reviewed prediction
PRO_0000040184Add
BLAST
Chaini921 – 1053133Protein 2A Reviewed prediction
PRO_0000040185Add
BLAST
Chaini1054 – 1189136Protein 2B Reviewed prediction
PRO_0000040186Add
BLAST
Chaini1190 – 1515326Protein 2C Reviewed prediction
PRO_0000040187Add
BLAST
Chaini1516 – 160388Protein 3A Reviewed prediction
PRO_0000040188Add
BLAST
Chaini1604 – 162320Protein 3B Reviewed prediction
PRO_0000040189Add
BLAST
Chaini1624 – 1840217Protease 3C Reviewed prediction
PRO_0000040190Add
BLAST
Chaini1841 – 2301461RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000040191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi77 – 771N-myristoyl glycine; by host By similarity
Modified residuei1606 – 16061O-(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, Lipoprotein, Myristate, Phosphoprotein

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP13899.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1281 – 1446166SF3 helicase
Add
BLAST
Domaini2069 – 2187119RdRp catalytic
Add
BLAST

Region

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

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.

P13899-1 [UniParc]FASTAAdd to Basket

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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: July 9, 2014
This is version 144 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