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Protein

Genome polyprotein

Gene
N/A
Organism
Theiler's murine encephalomyelitis virus (strain BeAn 8386) (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 (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)DescriptionActionsGraphical viewLength
Active sitei1680For protease 3C activitySequence analysis1
Active sitei1793For protease 3C activitySequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3 – 14Sequence analysisAdd BLAST12
Nucleotide bindingi1312 – 1319ATPPROSITE-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 BeAn 8386) (TMEV)
Taxonomic identifieri12125 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000007538 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 – 1562CytoplasmicSequence analysisAdd BLAST1562
Intramembranei1563 – 1581Sequence analysisAdd BLAST19
Topological domaini1582 – 2303CytoplasmicSequence 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_00000401681 – 76Leader proteinAdd BLAST76
ChainiPRO_000031097077 – 414Protein VP0Sequence analysisAdd BLAST338
ChainiPRO_000004016977 – 147Protein VP4Sequence analysisAdd BLAST71
ChainiPRO_0000040170148 – 414Protein VP2Sequence analysisAdd BLAST267
ChainiPRO_0000040171415 – 646Protein VP3Sequence analysisAdd BLAST232
ChainiPRO_0000040172647 – 922Protein VP1Sequence analysisAdd BLAST276
ChainiPRO_0000040173923 – 1055Protein 2ASequence analysisAdd BLAST133
ChainiPRO_00000401741056 – 1191Protein 2BSequence analysisAdd BLAST136
ChainiPRO_00000401751192 – 1517Protein 2CSequence analysisAdd BLAST326
ChainiPRO_00000401761518 – 1605Protein 3ASequence analysisAdd BLAST88
ChainiPRO_00000401771606 – 1625Protein 3BSequence analysisAdd BLAST20
ChainiPRO_00000401781626 – 1842Protease 3CSequence analysisAdd BLAST217
ChainiPRO_00000401791843 – 2303RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi77N-myristoyl glycine; by hostBy similarity1
Disulfide bondi501 ↔ 503
Modified residuei1608O-(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
Sitei922 – 923Cleavage; by protease 3CSequence analysis2
Sitei1055 – 1056Cleavage; by ribosomal skipSequence analysis2
Sitei1191 – 1192Cleavage; by protease 3CSequence analysis2
Sitei1517 – 1518Cleavage; by protease 3CSequence analysis2
Sitei1605 – 1606Cleavage; by protease 3CSequence analysis2
Sitei1625 – 1626Cleavage; by protease 3CSequence analysis2
Sitei1842 – 1843Cleavage; by protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

Structurei

Secondary structure

12303
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi158 – 160Combined sources3
Beta strandi162 – 166Combined sources5
Beta strandi169 – 175Combined sources7
Beta strandi180 – 184Combined sources5
Helixi204 – 206Combined sources3
Beta strandi210 – 217Combined sources8
Beta strandi228 – 232Combined sources5
Beta strandi235 – 238Combined sources4
Helixi241 – 247Combined sources7
Beta strandi248 – 253Combined sources6
Beta strandi256 – 262Combined sources7
Beta strandi272 – 280Combined sources9
Beta strandi289 – 293Combined sources5
Turni330 – 334Combined sources5
Beta strandi335 – 341Combined sources7
Turni343 – 345Combined sources3
Beta strandi347 – 353Combined sources7
Beta strandi357 – 363Combined sources7
Turni364 – 366Combined sources3
Beta strandi369 – 378Combined sources10
Beta strandi390 – 400Combined sources11
Beta strandi403 – 406Combined sources4
Turni459 – 463Combined sources5
Beta strandi473 – 475Combined sources3
Beta strandi492 – 495Combined sources4
Beta strandi501 – 504Combined sources4
Helixi508 – 511Combined sources4
Beta strandi515 – 521Combined sources7
Beta strandi524 – 529Combined sources6
Beta strandi536 – 543Combined sources8
Beta strandi546 – 548Combined sources3
Helixi554 – 557Combined sources4
Beta strandi560 – 562Combined sources3
Beta strandi568 – 570Combined sources3
Beta strandi572 – 575Combined sources4
Beta strandi582 – 587Combined sources6
Beta strandi602 – 611Combined sources10
Beta strandi622 – 627Combined sources6
Beta strandi633 – 636Combined sources4
Beta strandi661 – 666Combined sources6
Turni680 – 684Combined sources5
Beta strandi698 – 700Combined sources3
Beta strandi712 – 714Combined sources3
Beta strandi717 – 719Combined sources3
Beta strandi727 – 729Combined sources3
Beta strandi732 – 734Combined sources3
Beta strandi747 – 749Combined sources3
Beta strandi751 – 753Combined sources3
Turni760 – 764Combined sources5
Beta strandi769 – 780Combined sources12
Beta strandi791 – 794Combined sources4
Beta strandi807 – 809Combined sources3
Beta strandi820 – 822Combined sources3
Beta strandi831 – 835Combined sources5
Beta strandi842 – 847Combined sources6
Beta strandi853 – 856Combined sources4
Beta strandi861 – 863Combined sources3
Beta strandi871 – 874Combined sources4
Beta strandi880 – 893Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TMFX-ray3.501647-922[»]
2148-414[»]
3415-646[»]
ProteinModelPortaliP08544.
SMRiP08544.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08544.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1283 – 1448SF3 helicasePROSITE-ProRule annotationAdd BLAST166
Domaini2071 – 2189RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi79 – 82Poly-Ser4
Compositional biasi1306 – 1309Poly-Val4
Compositional biasi1814 – 1817Poly-Gly4

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)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.

P08544-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACKHGYPDV CPICTAVDAT PGFEYLLMAD GEWYPTDLLC VDLDDDVFWP
60 70 80 90 100
SDTSNQSQTM DWTDVPLIRD IVMEPQGNSS SSDKSNSQSS GNEGVIINNF
110 120 130 140 150
YSNQYQNSID LSASGGNAGD APQTNGQLSN ILGGAANAFA TMAPLLLDQN
160 170 180 190 200
TEEMENLSDR VASDKAGNSA TNTQSTVGRL CGYGKSHHGE HPASCADTAT
210 220 230 240 250
DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG GVFGATLRRH
260 270 280 290 300
YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG TMEPSDPFTM
310 320 330 340 350
DTEWRSPQGA PTGYRYDSRT GFFATNHQNQ WQWTVYPHQI LNLRTNTTVD
360 370 380 390 400
LEVPYVNVAP SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN
410 420 430 440 450
PVFNGLRHET VIAQSPIPVT VREHKGCFYS TNPDTTVPIY GKTISTPSDY
460 470 480 490 500
MCGEFSDLLE LCKLPTFLGN PNTNNKRYPY FSATNSVPAT SMVDYQVALS
510 520 530 540 550
CSCMANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL IAYTPPGAGK
560 570 580 590 600
PTTRDQAMQS TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG
610 620 630 640 650
WVTVWKLTPL TYPSGTPTNS DILTLVSAGD DFTLRMPISP TKWVPQGVDN
660 670 680 690 700
AEKGKVSNDD ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET
710 720 730 740 750
TFNYQENDYR LNCLLLTPLP SFCPDSSSGP QKTKAPVQWR WVRSGGVNGA
760 770 780 790 800
NFPLMTKQDY AFLCFSPFTF YKCDLEVTVS ALGMTRVASV LRWAPTGAPA
810 820 830 840 850
DVTDQLIGYT PSLGETRNPH MWLVGAGNSQ VSFVVPYNSP LSVLPAAWFN
860 870 880 890 900
GWSDFGNTKD FGVAPNADFG RLWIQGNTSA SVRIRYKKMK VFCPRPTLFF
910 920 930 940 950
PWPTPTTTKI NADNPVPILE LENPAALYRI DLFITFTDEF ITFDYKVHGR
960 970 980 990 1000
PVLTFRIPGF GLTPAGRMLV CMGEQPAHGP FTSSRSLYHV IFTATCSSFS
1010 1020 1030 1040 1050
FSIYKGRYRS WKKPIHDELV DRGYTTFGEF FKAVRGYHAD YYRQRLIHDV
1060 1070 1080 1090 1100
ETNPGPVQSV FQPQGAVLTK SLAPQAGIQN LLLRLLGIDG DCSEVSKAIT
1110 1120 1130 1140 1150
VVTDLVAAWE KAKTTLVSPE FWSKLILKTT KFIAASVLYL HNPDFTTTVC
1160 1170 1180 1190 1200
LSLMTGVDLL TNDSVFDWLK QKLSSFFRTP PPACPNVMQP QGPLREANEG
1210 1220 1230 1240 1250
FTFAKNIEWA MKTIQSVVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI
1260 1270 1280 1290 1300
MDMRNGRKAY CECTASFKYF DELYNLAVTC KRIPLASLCE KFKNRHDHSV
1310 1320 1330 1340 1350
TRPEPVVVVL RGAAGQGKSV TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD
1360 1370 1380 1390 1400
GYENQFSVIM DDLGQNPDGE DFTVFCQMVS STNFLPNMAH LERKGTPFTS
1410 1420 1430 1440 1450
SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK TPAGMLDVEK
1460 1470 1480 1490 1500
AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTQTVYNL QQVVKMVNDT
1510 1520 1530 1540 1550
ITRKTENVKK MNSLVAQSPP DWEHFENILT CLRQNNAALQ DQLDELQEAF
1560 1570 1580 1590 1600
AQARERSDFL SDWLKVSAII FAGIASLSAV IKLASKFKES IWPTPVRVEL
1610 1620 1630 1640 1650
SEGEQAAYAG RARAQKQALQ VLDIQGGGKV LAQAGNPVMD FELFCAKNIV
1660 1670 1680 1690 1700
APITFYYPDK AEVTQSCLLL RAHLFVVNRH VAETDWTAFK LKDVRHERHT
1710 1720 1730 1740 1750
VALRSVNRSG AKTDLTFIKV TKGPLFKDNV NKFCSNKDDF PARNDTVTGI
1760 1770 1780 1790 1800
MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN
1810 1820 1830 1840 1850
VNGKKAVYGM HSAGGGGLAA ATIITKELIE AAEKSMLALE PQGAIVDIAT
1860 1870 1880 1890 1900
GSVVHVPRKT KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT
1910 1920 1930 1940 1950
TNMESLPPIF DVVCGEYANR VFTILGKENG LLTVEQAVLG LPGMDPMEKD
1960 1970 1980 1990 2000
TSPGLPYTQQ GLRRTDLLNF ITAKMTPQLD YAHSKLVIGV YDDVVYQSFL
2010 2020 2030 2040 2050
KDEIRPIEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF QTKPGLELGS
2060 2070 2080 2090 2100
AIGTDPDVDW TRYAVELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE
2110 2120 2130 2140 2150
QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV
2160 2170 2180 2190 2200
IIRAALYLTY SNFDFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK
2210 2220 2230 2240 2250
ITPANKTTTF PLTSHLQDVT FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC
2260 2270 2280 2290 2300
KPGTLKEKLM SIALLAVHSG PDIYDEIFLP FRNVGIVVPT YSSMLYRWLS

LFR
Length:2,303
Mass (Da):256,282
Last modified:August 1, 1988 - v1
Checksum:iE2C7737DFDBEB786
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M16020 Genomic RNA. Translation: AAA47930.1.
PIRiA29535. GNNYTM.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TMFX-ray3.501647-922[»]
2148-414[»]
3415-646[»]
ProteinModelPortaliP08544.
SMRiP08544.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP08544.

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_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: November 30, 2016
This is version 151 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.