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UniProtKB/Swiss-Prot entry P08545


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name POLG_TMEVG
Primary accession number P08545
Secondary accession numbers Q88593 Q88594
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 1, 1990 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 83)
Name and origin of the protein
Protein name Genome polyprotein
Synonyms None
Contains Protein VP0
     (VP4-VP2)
Protein VP4
     (Virion protein 4)
     (P1A)
Protein VP2
     (Virion protein 2)
     (P1B)
Protein VP3
     (Virion protein 3)
     (P1C)
Protein VP1
     (Virion protein 1)
     (P1D)
Protein 2A
     (P2A)
Protein 2B
     (P2B)
Protein 2C
     (P2C)
     (EC 3.6.1.15)
Protein 3A
     (P3A)
Protein 3B
     (P3B)
     (VPg)
Picornain 3C
     (EC 3.4.22.28)
     (Protease 3C)
     (P3C)
RNA-directed RNA polymerase 3D-POL
     (P3D-POL)
     (EC 2.7.7.48)
Gene name None
From
Theiler's murine encephalomyelitis virus (strain GDVII) (TMEV) [TaxID: 12127] 
Taxonomy Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; Picornaviridae; Cardiovirus.
Virus host Mus musculus (Mouse) [TaxID: 10090]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1016/0042-6822(88)90652-6; PubMed=2838951 [NCBI, ExPASy, EBI, Israel, Japan]
Pevear D.C., Borkowski J., Calenoff M., Oh C.K., Ostrawski B., Lipton H.L.;
"Insights into Theiler's virus neurovirulence based on a genomic comparison of the neurovirulent GDVII and less virulent BeAn strains.";
Virology 165:1-12(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1704-2303.
PubMed=3023668 [NCBI, ExPASy, EBI, Israel, Japan]
Ozden S., Tangy F., Chamorro M., Brahic M.;
"Theiler's virus genome is closely related to that of encephalomyocarditis virus, the prototype cardiovirus.";
J. Virol. 60:1163-1165(1986).
Comments
  • FUNCTION: 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).
  • FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
  • FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
  • FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
  • FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).
  • FUNCTION: Protein 3C is a 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 co-operatively to the protease (By similarity).
  • FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
  • CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • CATALYTIC ACTIVITY: 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.
  • CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
  • SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: Protein 2B: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). 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).
  • SUBCELLULAR LOCATION: Protein 2C: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). 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).
  • SUBCELLULAR LOCATION: Protein 3A: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). 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).
  • SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
  • SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
  • SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). 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).
  • PTM: 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).
  • PTM: VPg is covalently linked to the genomic RNA (By similarity).
  • PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
  • SIMILARITY: Belongs to the picornaviruses polyprotein family.
  • SIMILARITY: Contains 2 peptidase C3 domains [view classification].
  • SIMILARITY: Contains 1 RdRp catalytic domain.
  • SIMILARITY: Contains 1 SF3 helicase domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M20562; AAA47929.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14703; AAA47933.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26100; A26100.
A29193; GNNYTP.
3D structure databases
HSSP Q88571; 1TME. [HSSP ENTRY / PDB]
SMR P08545; 159-413, 415-646, 647-903.
ModBase P08545.
Protein family/group databases
MEROPS C03.010; -.
Ontologies
GO
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0018144; Biological process: RNA-protein covalent cross-linking (inferred from electronic annotation from UniProtKB-KW).
GO:0006410; Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR015031; Capsid_VP4_Picornavir.
IPR000605; Helicase_SF3_ssDNA/RNA_vir.
IPR014759; Helicase_SF3_ssRNA_vir.
IPR000199; Pept_C3_picorn.
IPR001676; Picornavirus_capsid.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.
Gene3D G3DSA:4.10.90.10; Capsid_VP4_Picornavir; 1.
Pfam PF08935; DUF1865; 1.
PF00548; Peptidase_C3; 1.
PF00680; RdRP_1; 1.
PF00073; Rhv; 2.
PF00910; RNA_helicase; 1.
Pfam graphical view of domain structure.
PROSITE PS50507; RDRP_SSRNA_POS; 1.
PS51218; SF3_HELICASE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P08545.
ProtoNet P08545.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Cytoplasm; Cytoplasmic vesicle; Helicase; Hydrolase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; RNA replication; RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; Virion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
PROPEP   1     76  76     Leader peptide. PRO_0000040192
CHAIN   77    414  338     Protein VP0 (Potential). PRO_0000310972
CHAIN   77    147  71     Protein VP4 (Potential). PRO_0000040193
CHAIN   148    414  267     Protein VP2 (Potential). PRO_0000040194
CHAIN   415    646  232     Protein VP3 (Potential). PRO_0000040195
CHAIN   647    922  276     Protein VP1 (Potential). PRO_0000040196
CHAIN   923   1055  133     Protein 2A (Potential). PRO_0000040197
CHAIN   1056   1191  136     Protein 2B (Potential). PRO_0000040198
CHAIN   1192   1517  326     Protein 2C (Potential). PRO_0000040199
CHAIN   1518   1605  88     Protein 3A (Potential). PRO_0000040200
CHAIN   1606   1625  20     Protein 3B (Potential). PRO_0000040201
CHAIN   1626   1842  217     Picornain 3C (Potential). PRO_0000040202
CHAIN   1843   2303  461     RNA-directed RNA polymerase 3D-POL (Potential). PRO_0000040203
TOPO_DOM   1   1562  1562     Cytoplasmic (Potential). 
TOPO_DOM   1563   1581  19     In membrane (Potential). 
TOPO_DOM   1582   2303  722     Cytoplasmic (Potential). 
DOMAIN   1283   1448  166     SF3 helicase. 
DOMAIN   2071   2189  119     RdRp catalytic. 
NP_BIND   1312   1319  8     ATP (Potential). 
ACT_SITE   1680   1680        For picornain 3C activity (Potential). 
ACT_SITE   1712   1712        For picornain 3C activity (Potential). 
ACT_SITE   1793   1793        For picornain 3C activity (Potential). 
SITE   147    148  2     Cleavage (Potential). 
SITE   414    415  2     Cleavage; by picornain 3C (Potential). 
SITE   646    647  2     Cleavage; by picornain 3C (Potential). 
SITE   922    923  2     Cleavage; by picornain 3C (Potential). 
SITE   1055   1056  2     Cleavage; by ribosomal skip (Potential). 
SITE   1191   1192  2     Cleavage; by picornain 3C (Potential). 
SITE   1517   1518  2     Cleavage; by picornain 3C (Potential). 
SITE   1605   1606  2     Cleavage; by picornain 3C (Potential). 
SITE   1625   1626  2     Cleavage; by picornain 3C (Potential). 
SITE   1842   1843  2     Cleavage; by picornain 3C (Potential). 
MOD_RES   1608   1608        O-(5'-phospho-RNA)-tyrosine (By similarity). 
LIPID   77     77        N-myristoyl glycine; by host (By similarity). 
CONFLICT   1747   1750        VTGI -> CYRD (in Ref. 2; AAA47933). 
CONFLICT   1992   2000        DDVVYQSFL -> GRRCLPIIF (in Ref. 2). 
CONFLICT   2003   2003        E -> Q (in Ref. 2). 
CONFLICT   2008   2008        E -> H (in Ref. 2; AAA47933). 
CONFLICT   2046   2046        F -> L (in Ref. 2; AAA47933). 
CONFLICT   2128   2134        LIRGGLP -> YSWGPA (in Ref. 2; AAA47933). 
Sequence information
Length: 2303 AA [This is the length of the unprocessed precursor] Molecular weight: 256344 Da [This is the MW of the unprocessed precursor] CRC64: 5D0FBE6E47F72A04 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MACKHGYPDV CPICTAVDAT PDFEYLLMAD GEWFPTDLLC VDLDDDVFWP SDTSTQPQTM 

        70         80         90        100        110        120 
EWTDVPLVCD TVMEPQGNAS SSDKSNSQSS GNEGVIINNF YSNQYQNSID LSASGGNAGD 

       130        140        150        160        170        180 
APQNNGQLSS ILGGAANAFA TMAPLLMDQN TEEMENLSDR VASDKAGNSA TNTQSTVGRL 

       190        200        210        220        230        240 
CGYGKSHHGE HPTSCADAAT DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG 

       250        260        270        280        290        300 
GVFGATLRRH YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKSG TMEPSDPFTM 

       310        320        330        340        350        360 
DTTWRSPQSA PTGYRYDRQA GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD LEVPYVNVAP 

       370        380        390        400        410        420 
SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN PVFNGLRHET VLAQSPIPVT 

       430        440        450        460        470        480 
VREHQGCFYS TNPDTTVPIY GKTISTPSDY MCGEFSDLLE LCKLPTFLGN PSTDNKRYPY 

       490        500        510        520        530        540 
FSATNSVPAT SLVDYQVALS CSCTANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFR 

       550        560        570        580        590        600 
IAYTPPGAGK PTTRDQAMQA TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG 

       610        620        630        640        650        660 
WVTVWQLTPL TYPSGTPTHS DILTLVSAGD DFTLRMPISP TKWVPQGIDN AEKGKVSNDD 

       670        680        690        700        710        720 
ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET TFSYQENDFR LNCLLLTPLP 

       730        740        750        760        770        780 
SYCPDSSSGP VRTKAPVQWR WVRSGGANGA NFPLMTKQDY AFLCFSPFTY YKCDLEVTVS 

       790        800        810        820        830        840 
AMGAGTVSSV LRWAPTGAPA DVTDQLIGYT PSLGETRNPH MWIVGSGNSQ ISFVVPYNSP 

       850        860        870        880        890        900 
LSVLPAAWFN GWSDFGNTKD FGVAPTSDFG RIWIQGNSSA SVRIRYKKMK VFCPRPTLFF 

       910        920        930        940        950        960 
PWPTPTTTKI NADNPVPILE LENPASLYRI DLFITFTDEL ITFDYKVHGR PVLTFRIPGF 

       970        980        990       1000       1010       1020 
GLTPAGRMLV CMGAKPAHSP FTSSKSLYHV IFTSTCNSFS FTIYKGRYRS WKKPIHDELV 

      1030       1040       1050       1060       1070       1080 
DRGYTTFREF FKAVRGYHAD YYKQRLIHDV EMNPGPVQSV FQPQGAVLTK SLAPQAGIQN 

      1090       1100       1110       1120       1130       1140 
ILLRLLGIEG DCSEVSKAIT VVTDLVAAWE KAKTTLVSPE FWSELILKTT KFIAASVLYL 

      1150       1160       1170       1180       1190       1200 
HNPDFTTTVC LSLMTGVDLL TNDSVFDWLK SKLSSFFRTP PPACPNVMQP QGPLREANEG 

      1210       1220       1230       1240       1250       1260 
FTFAKNIEWA TKTIQSIVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI MDMRNGRKAY 

      1270       1280       1290       1300       1310       1320 
CECTASFKYF DDLYNLAVTC KRIPLASLCE KFKNRHDHSV TRPEPVVAVL RGAAGQGKSV 

      1330       1340       1350       1360       1370       1380 
TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD GYENQFSVIM DDLGQNPDGE DFTVFCQMVS 

      1390       1400       1410       1420       1430       1440 
STNFLPNMAH LERKGTPFTS SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK 

      1450       1460       1470       1480       1490       1500 
TPAGMLDIEK AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTKTVYNL QQVVKMVNDT 

      1510       1520       1530       1540       1550       1560 
ITRKTENVKK MNSLVAQSPP DWQHFENILT CLRQNNAALQ DQVDELQEAF TQARERSDFL 

      1570       1580       1590       1600       1610       1620 
SDWLKVSAII FAGIVSLSAV IKLASKFKES IWPTPVRVEL SEGEQAAYAG RARAQKQALQ 

      1630       1640       1650       1660       1670       1680 
VLDIQGGGKV LAQAGNPVMD FELFCAKNMV SPITFYYPDK AEVTQSCLLL RAHLFVVNRH 

      1690       1700       1710       1720       1730       1740 
VAETEWTAFK LRDVRHERDT VVMRSVNRSG AETDLTFVKV TKGPLFKDNV NKFCSNKDDF 

      1750       1760       1770       1780       1790       1800 
PARNDTVTGI MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN 

      1810       1820       1830       1840       1850       1860 
VNGKKAVYGM HSAGGGGLAA ATIITRELIE AAEKSMLALE PQGAIVDIST GSVVHVPRKT 

      1870       1880       1890       1900       1910       1920 
KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT TNMESLPPIF DIVCGEYANR 

      1930       1940       1950       1960       1970       1980 
VFTILGKDNG LLTVEQAVLG LSGMDPMEKD TSPGLPYTQQ GLRRTDLLDF NTAKMTPQLD 

      1990       2000       2010       2020       2030       2040 
YAHSKLVLGV YDDVVYQSFL KDEIRPLEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF 

      2050       2060       2070       2080       2090       2100 
QTKPGFELGS AIGTDPDVDW TRYAAELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE 

      2110       2120       2130       2140       2150       2160 
QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV IIRAALYLTY 

      2170       2180       2190       2200       2210       2220 
SNFEFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK ITPANKTTTF PLTSHLQDVT 

      2230       2240       2250       2260       2270       2280 
FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC KPGTLKEKLM SIALLAVHSG PDIYDEIFLP 

      2290       2300 
FRNVGIVVPT YDSMLYRWLS LFR 

P08545 in FASTA format

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