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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).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)LengthDescriptionGraphical viewFeature identifierActions
Sitei147 – 1482CleavageSequence Analysis
Sitei414 – 4152Cleavage; by protease 3CSequence Analysis
Sitei646 – 6472Cleavage; by protease 3CSequence Analysis
Sitei922 – 9232Cleavage; by protease 3CSequence Analysis
Sitei1055 – 10562Cleavage; by ribosomal skipSequence Analysis
Sitei1191 – 11922Cleavage; by protease 3CSequence Analysis
Sitei1517 – 15182Cleavage; by protease 3CSequence Analysis
Sitei1605 – 16062Cleavage; by protease 3CSequence Analysis
Sitei1625 – 16262Cleavage; by protease 3CSequence Analysis
Active sitei1680 – 16801For protease 3C activitySequence Analysis
Active sitei1793 – 17931For protease 3C activitySequence Analysis
Sitei1842 – 18432Cleavage; by protease 3CSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri3 – 1412Sequence AnalysisAdd
BLAST
Nucleotide bindingi1312 – 13198ATPPROSITE-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 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 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 15621562CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1563 – 158119Sequence AnalysisAdd
BLAST
Topological domaini1582 – 2303722CytoplasmicSequence AnalysisAdd
BLAST

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_0000040168Add
BLAST
Chaini77 – 414338Protein VP0Sequence AnalysisPRO_0000310970Add
BLAST
Chaini77 – 14771Protein VP4Sequence AnalysisPRO_0000040169Add
BLAST
Chaini148 – 414267Protein VP2Sequence AnalysisPRO_0000040170Add
BLAST
Chaini415 – 646232Protein VP3Sequence AnalysisPRO_0000040171Add
BLAST
Chaini647 – 922276Protein VP1Sequence AnalysisPRO_0000040172Add
BLAST
Chaini923 – 1055133Protein 2ASequence AnalysisPRO_0000040173Add
BLAST
Chaini1056 – 1191136Protein 2BSequence AnalysisPRO_0000040174Add
BLAST
Chaini1192 – 1517326Protein 2CSequence AnalysisPRO_0000040175Add
BLAST
Chaini1518 – 160588Protein 3ASequence AnalysisPRO_0000040176Add
BLAST
Chaini1606 – 162520Protein 3BSequence AnalysisPRO_0000040177Add
BLAST
Chaini1626 – 1842217Protease 3CSequence AnalysisPRO_0000040178Add
BLAST
Chaini1843 – 2303461RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000040179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi77 – 771N-myristoyl glycine; by hostBy similarity
Disulfide bondi501 ↔ 503
Modified residuei1608 – 16081O-(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, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

Structurei

Secondary structure

1
2303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi158 – 1603Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi169 – 1757Combined sources
Beta strandi180 – 1845Combined sources
Helixi204 – 2063Combined sources
Beta strandi210 – 2178Combined sources
Beta strandi228 – 2325Combined sources
Beta strandi235 – 2384Combined sources
Helixi241 – 2477Combined sources
Beta strandi248 – 2536Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi272 – 2809Combined sources
Beta strandi289 – 2935Combined sources
Turni330 – 3345Combined sources
Beta strandi335 – 3417Combined sources
Turni343 – 3453Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi357 – 3637Combined sources
Turni364 – 3663Combined sources
Beta strandi369 – 37810Combined sources
Beta strandi390 – 40011Combined sources
Beta strandi403 – 4064Combined sources
Turni459 – 4635Combined sources
Beta strandi473 – 4753Combined sources
Beta strandi492 – 4954Combined sources
Beta strandi501 – 5044Combined sources
Helixi508 – 5114Combined sources
Beta strandi515 – 5217Combined sources
Beta strandi524 – 5296Combined sources
Beta strandi536 – 5438Combined sources
Beta strandi546 – 5483Combined sources
Helixi554 – 5574Combined sources
Beta strandi560 – 5623Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi572 – 5754Combined sources
Beta strandi582 – 5876Combined sources
Beta strandi602 – 61110Combined sources
Beta strandi622 – 6276Combined sources
Beta strandi633 – 6364Combined sources
Beta strandi661 – 6666Combined sources
Turni680 – 6845Combined sources
Beta strandi698 – 7003Combined sources
Beta strandi712 – 7143Combined sources
Beta strandi717 – 7193Combined sources
Beta strandi727 – 7293Combined sources
Beta strandi732 – 7343Combined sources
Beta strandi747 – 7493Combined sources
Beta strandi751 – 7533Combined sources
Turni760 – 7645Combined sources
Beta strandi769 – 78012Combined sources
Beta strandi791 – 7944Combined sources
Beta strandi807 – 8093Combined sources
Beta strandi820 – 8223Combined sources
Beta strandi831 – 8355Combined sources
Beta strandi842 – 8476Combined sources
Beta strandi853 – 8564Combined sources
Beta strandi861 – 8633Combined sources
Beta strandi871 – 8744Combined sources
Beta strandi880 – 89314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMFX-ray3.501647-922[»]
2148-414[»]
3415-646[»]
ProteinModelPortaliP08544.
SMRiP08544. Positions 85-146, 148-922.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08544.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1283 – 1448166SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini2071 – 2189119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 4617AcidicAdd
BLAST
Regioni60 – 7314TheiloBy similarityAdd
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

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.

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 .
PIRi A29535. GNNYTM.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 143 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