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Protein

Genome polyprotein

Gene
N/A
Organism
Theiler's murine encephalomyelitis virus (strain DA) (TMEV)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei1678For protease 3C activitySequence analysis1
Active sitei1710For protease 3C activitySequence analysis1
Active sitei1791For protease 3C activitySequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3 – 14Sequence analysisAdd BLAST12
Nucleotide bindingi1310 – 1317ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

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 virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000000283 Componenti: Genome

Subcellular locationi

Protein 2A :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3B :
RNA-directed RNA polymerase 3D-POL :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1560CytoplasmicSequence analysisAdd BLAST1560
Intramembranei1561 – 1579Sequence analysisAdd BLAST19
Topological domaini1580 – 2301CytoplasmicSequence analysisAdd BLAST722

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000401801 – 76Leader proteinAdd BLAST76
ChainiPRO_000031097177 – 414Protein VP0Sequence analysisAdd BLAST338
ChainiPRO_000004018177 – 147Protein VP4Sequence analysisAdd BLAST71
ChainiPRO_0000040182148 – 414Protein VP2Sequence analysisAdd BLAST267
ChainiPRO_0000040183415 – 646Protein VP3Sequence analysisAdd BLAST232
ChainiPRO_0000040184647 – 920Protein VP1Sequence analysisAdd BLAST274
ChainiPRO_0000040185921 – 1053Protein 2ASequence analysisAdd BLAST133
ChainiPRO_00000401861054 – 1189Protein 2BSequence analysisAdd BLAST136
ChainiPRO_00000401871190 – 1515Protein 2CSequence analysisAdd BLAST326
ChainiPRO_00000401881516 – 1603Protein 3ASequence analysisAdd BLAST88
ChainiPRO_00000401891604 – 1623Protein 3BSequence analysisAdd BLAST20
ChainiPRO_00000401901624 – 1840Protease 3CSequence analysisAdd BLAST217
ChainiPRO_00000401911841 – 2301RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi77N-myristoyl glycine; by hostBy similarity1
Modified residuei1606O-(5'-phospho-RNA)-tyrosineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei147 – 148CleavageSequence analysis2
Sitei414 – 415Cleavage; by protease 3CSequence analysis2
Sitei646 – 647Cleavage; by protease 3CSequence analysis2
Sitei920 – 921Cleavage; by protease 3CSequence analysis2
Sitei1053 – 1054Cleavage; by ribosomal skipSequence analysis2
Sitei1189 – 1190Cleavage; by protease 3CSequence analysis2
Sitei1515 – 1516Cleavage; by protease 3CSequence analysis2
Sitei1603 – 1604Cleavage; by protease 3CSequence analysis2
Sitei1623 – 1624Cleavage; by protease 3CSequence analysis2
Sitei1840 – 1841Cleavage; by protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Structurei

Secondary structure

12301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi90 – 92Combined sources3
Helixi103 – 106Combined sources4
Beta strandi162 – 166Combined sources5
Beta strandi169 – 175Combined sources7
Beta strandi179 – 181Combined sources3
Helixi182 – 184Combined sources3
Helixi204 – 206Combined sources3
Beta strandi210 – 217Combined sources8
Beta strandi226 – 231Combined sources6
Helixi233 – 235Combined sources3
Helixi238 – 240Combined sources3
Helixi241 – 247Combined sources7
Beta strandi250 – 262Combined sources13
Beta strandi270 – 279Combined sources10
Turni289 – 291Combined sources3
Beta strandi292 – 295Combined sources4
Beta strandi316 – 318Combined sources3
Helixi330 – 335Combined sources6
Beta strandi336 – 342Combined sources7
Turni343 – 345Combined sources3
Beta strandi347 – 353Combined sources7
Beta strandi358 – 362Combined sources5
Helixi364 – 366Combined sources3
Beta strandi370 – 381Combined sources12
Beta strandi390 – 406Combined sources17
Turni423 – 426Combined sources4
Beta strandi438 – 440Combined sources3
Helixi458 – 463Combined sources6
Beta strandi477 – 486Combined sources10
Beta strandi492 – 497Combined sources6
Turni503 – 506Combined sources4
Helixi508 – 513Combined sources6
Beta strandi516 – 521Combined sources6
Beta strandi523 – 529Combined sources7
Beta strandi536 – 544Combined sources9
Beta strandi546 – 548Combined sources3
Helixi554 – 557Combined sources4
Beta strandi560 – 566Combined sources7
Beta strandi568 – 570Combined sources3
Beta strandi572 – 577Combined sources6
Beta strandi582 – 584Combined sources3
Beta strandi586 – 589Combined sources4
Beta strandi601 – 611Combined sources11
Beta strandi618 – 628Combined sources11
Beta strandi633 – 637Combined sources5
Helixi651 – 653Combined sources3
Turni661 – 664Combined sources4
Helixi679 – 683Combined sources5
Beta strandi687 – 692Combined sources6
Beta strandi710 – 715Combined sources6
Beta strandi721 – 723Combined sources3
Beta strandi744 – 749Combined sources6
Beta strandi751 – 755Combined sources5
Helixi758 – 762Combined sources5
Beta strandi766 – 779Combined sources14
Beta strandi786 – 792Combined sources7
Helixi810 – 812Combined sources3
Beta strandi813 – 816Combined sources4
Beta strandi818 – 823Combined sources6
Beta strandi828 – 833Combined sources6
Beta strandi838 – 845Combined sources8
Beta strandi869 – 875Combined sources7
Beta strandi878 – 892Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TMEX-ray2.801647-920[»]
2148-414[»]
3415-650[»]
477-147[»]
1TMFX-ray3.50490-130[»]
ProteinModelPortaliP13899.
SMRiP13899.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13899.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1281 – 1446SF3 helicasePROSITE-ProRule annotationAdd BLAST166
Domaini2069 – 2187RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 46AcidicAdd BLAST17
Regioni60 – 73TheiloAdd BLAST14

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)DescriptionActionsGraphical viewLength
Zinc fingeri3 – 14Sequence analysisAdd BLAST12

Keywords - Domaini

Zinc-finger

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M20301 Genomic RNA. Translation: AAA47928.1.
PIRiA31228. GNNYTN.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TMEX-ray2.801647-920[»]
2148-414[»]
3415-650[»]
477-147[»]
1TMFX-ray3.50490-130[»]
ProteinModelPortaliP13899.
SMRiP13899.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP13899.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 155 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.