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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).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
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 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 Source: UniProtKB-KW
  2. host cell nucleus Source: UniProtKB-KW
  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 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

        10         20         30         40         50
MACKHGYPDV CPICTAVDVT PGFEYLLLAD GEWFPTDLLC VDLDDDVFWP
60 70 80 90 100
SNSSNQSETM EWTDLPLVRD IVMEPQGNAS SSDKSNSQSS GNEGVIINNF
110 120 130 140 150
YSNQYQNSID LSASGGNAGD APQNNGQLSN ILGGAANAFA TMAPLLLDQN
160 170 180 190 200
TEEMENLSDR VASDKAGNSA TNTQSTVGRL CGYGEAHHGE HPASCADTAT
210 220 230 240 250
DKVLAAERYY TIDLASWTTT QEAFSHIRIP LPHVLAGEDG GVFGATLRRH
260 270 280 290 300
YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG DMEPTDPFTM
310 320 330 340 350
DTTWRAPQGA PTGYRYDSRT GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD
360 370 380 390 400
LEVPYVNIAP TSSWTQHANW TLVVAVFSPL QYASGSSSDV QITASIQPVN
410 420 430 440 450
PVFNGLRHET VIAQSPIAVT VREHKGCFYS TNPDTTVPIY GKTISTPNDY
460 470 480 490 500
MCGEFSDLLE LCKLPTFLGN PNSNNKRYPY FSATNSVPTT SLVDYQVALS
510 520 530 540 550
CSCMCNSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL IAYTPPGAGK
560 570 580 590 600
PTTRDQAMQA TYAIWDLGLN SSFVFTAPFI SPTHYRQTSY TSATIASVDG
610 620 630 640 650
WVTVWQLTPL TYPSGAPVNS DILTLVSAGD DFTLRMPISP TKWAPQGSDN
660 670 680 690 700
AEKGKVSNDD ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNIES
710 720 730 740 750
TFVYQENDLR LNCLLLTPLP SFCPDSTSGP VKTKAPVQWR WVRSGGTTNF
760 770 780 790 800
PLMTKQDYAF LCFSPFTYYK CDLEVTVSAL GTDTVASVLR WAPTGAPADV
810 820 830 840 850
TDQLIGYTPS LGETRNPHMW LVGAGNTQIS FVVPYNSPLS VLPAAWFNGW
860 870 880 890 900
SDFGNTKDFG VAPNADFGRL WIQGNTSASV RIRYKKMKVF CPRPTLFFPW
910 920 930 940 950
PVSTRSKINA DNPVPILELE NPAAFYRIDL FITFIDEFIT FDYKVHGRPV
960 970 980 990 1000
LTFRIPGFGL TPAGRMLVCM GEKPAHGPFT SSRSLYHVIF TATCSSFSFS
1010 1020 1030 1040 1050
IYKGRYRSWK KPIHDELVDR GYTTFGEFFR AVRAYHADYY KQRLIHDVEM
1060 1070 1080 1090 1100
NPGPVQSVFQ PQGAVLTKSL APQAGIQNLL LRLLGIDGDC SEVSKAITVV
1110 1120 1130 1140 1150
TDLFAAWERA KTTLVSPEFW SKLILKTTKF IAASVLYLHN PDFTTTVCLS
1160 1170 1180 1190 1200
LMTGVDLLTN DSVFDWLKNK LSSFFRTPPP VCPNVLQPQG PLREANEGFT
1210 1220 1230 1240 1250
FAKNIEWAMK TIQSIVNWLT SWFKQEEDHP QSKLDKFLME FPDHCRNIMD
1260 1270 1280 1290 1300
MRNGRKAYCE CTASFKYFDE LYNLAVTCKR IPLASLCEKF KNRHDHSVTR
1310 1320 1330 1340 1350
PEPVVVVLRG AAGQGKSVTS QIIAQSVSKM AFGRQSVYSM PPDSEYFDGY
1360 1370 1380 1390 1400
ENQFSVIMDD LGQNPDGEDF TVFCQMVSST NFLPNMAHLE RKGTPFTSSF
1410 1420 1430 1440 1450
IVATTNLPKF RPVTVAHYPA VDRRITFDFT VTAGPHCTTS NGMLDIEKAF
1460 1470 1480 1490 1500
DEIPGSKPQL ACFSADCPLL HKRGVMFTCN RTKAVYNLQQ VVKMVNDTIT
1510 1520 1530 1540 1550
RKTENVKKMN SLVAQSPPDW EHFENILTCL RQNNAALQDQ LDELQEAFAQ
1560 1570 1580 1590 1600
ARERSDFLSD WLKVSAIIFA GIASLSAVIK LASKFKESIW PSPVRVELSE
1610 1620 1630 1640 1650
GEQAAYAGRA RAQKQALQVL DIQGGGKVLA QAGNPVMDFE LFCAKNMVAP
1660 1670 1680 1690 1700
ITFYYPDKAE VTQSCLLLRA HLFVVNRHVA ETEWTAFKLK DVRHERDTVV
1710 1720 1730 1740 1750
TRSVNRSGAE TDLTFIKVTK GPLFKDNVNK FCSNKDDFPA RNDAVTGIMN
1760 1770 1780 1790 1800
TGLAFVYSGN FLIGNQPVNT TTGACFNHCL HYRAQTRRGW CGSAVICNVN
1810 1820 1830 1840 1850
GKKAVYGMHS AGGGGLAAAT IITRELIEAA EKSMLALEPQ GAIVDISTGS
1860 1870 1880 1890 1900
VVHVPRKTKL RRTVAHDVFQ PKFEPAVLSR YDPRTDKDVD VVAFSKHTTN
1910 1920 1930 1940 1950
MESLPPVFDI VCDEYANRVF TILGKDNGLL TVEQAVLGLP GMDPMEKDTS
1960 1970 1980 1990 2000
PGLPYTQQGL RRTDLLNFNT AKMTPQLDYA HSKLVLGVYD DVVYQSFLKD
2010 2020 2030 2040 2050
EIRPLEKIHE AKTRIVDVPP FAHCIWGRQL LGRFASKFQT KPGLELGSAI
2060 2070 2080 2090 2100
GTDPDVDWTP YAAELSGFNY VYDVDYSNFD ASHSTAMFEC LIKNFFTEQN
2110 2120 2130 2140 2150
GFDRRIAEYL RSLAVSRHAY EDRRVLIRGG LLSGCAATSM LNTIMNNVII
2160 2170 2180 2190 2200
RAALYLTYSN FEFDDIKVLS YGDDLLIGTN YQIDFNLVKE RLAPFGYKIT
2210 2220 2230 2240 2250
PANKTTTFPL TSHLQDVTFL KRRFVRFNSY LFRPQMDAVN LKAMVSYCKP
2260 2270 2280 2290 2300
GTLKEKLMSI ALLAVHSGPD IYDEIFLPFR NVGIVVPTYS SMLYRWLSLF

R
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 29, 2014
This is version 146 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