|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3033278 [NCBI, ExPASy, EBI, Israel, Japan]
Pevear D.C.,
Calenoff M.,
Rozhon E.,
Lipton H.L.;
"Analysis of the complete nucleotide sequence of the picornavirus Theiler's murine encephalomyelitis virus indicates that it is closely related to cardioviruses.";
J. Virol. 61:1507-1516(1987).
|
[2]
|
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 148-922.
PubMed=1312722 [NCBI, ExPASy, EBI, Israel, Japan]
Luo M.,
He C.,
Toth K.S.,
Zhang C.X.,
Lipton H.L.;
"Three-dimensional structure of Theiler murine encephalomyelitis virus (BeAn strain).";
Proc. Natl. Acad. Sci. U.S.A. 89:2409-2413(1992).
|
|
|
|
- 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.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1tmf";.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 2303 AA [This is the length of the unprocessed precursor] |
Molecular weight: 256282 Da [This is the MW of the unprocessed precursor] |
CRC64: E2C7737DFDBEB786 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MACKHGYPDV CPICTAVDAT PGFEYLLMAD GEWYPTDLLC VDLDDDVFWP SDTSNQSQTM
70 80 90 100 110 120
DWTDVPLIRD IVMEPQGNSS SSDKSNSQSS GNEGVIINNF YSNQYQNSID LSASGGNAGD
130 140 150 160 170 180
APQTNGQLSN ILGGAANAFA TMAPLLLDQN TEEMENLSDR VASDKAGNSA TNTQSTVGRL
190 200 210 220 230 240
CGYGKSHHGE HPASCADTAT DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG
250 260 270 280 290 300
GVFGATLRRH YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG TMEPSDPFTM
310 320 330 340 350 360
DTEWRSPQGA PTGYRYDSRT GFFATNHQNQ WQWTVYPHQI LNLRTNTTVD LEVPYVNVAP
370 380 390 400 410 420
SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN PVFNGLRHET VIAQSPIPVT
430 440 450 460 470 480
VREHKGCFYS TNPDTTVPIY GKTISTPSDY MCGEFSDLLE LCKLPTFLGN PNTNNKRYPY
490 500 510 520 530 540
FSATNSVPAT SMVDYQVALS CSCMANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL
550 560 570 580 590 600
IAYTPPGAGK PTTRDQAMQS TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG
610 620 630 640 650 660
WVTVWKLTPL TYPSGTPTNS DILTLVSAGD DFTLRMPISP TKWVPQGVDN AEKGKVSNDD
670 680 690 700 710 720
ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET TFNYQENDYR LNCLLLTPLP
730 740 750 760 770 780
SFCPDSSSGP QKTKAPVQWR WVRSGGVNGA NFPLMTKQDY AFLCFSPFTF YKCDLEVTVS
790 800 810 820 830 840
ALGMTRVASV LRWAPTGAPA DVTDQLIGYT PSLGETRNPH MWLVGAGNSQ VSFVVPYNSP
850 860 870 880 890 900
LSVLPAAWFN GWSDFGNTKD FGVAPNADFG RLWIQGNTSA SVRIRYKKMK VFCPRPTLFF
910 920 930 940 950 960
PWPTPTTTKI NADNPVPILE LENPAALYRI DLFITFTDEF ITFDYKVHGR PVLTFRIPGF
970 980 990 1000 1010 1020
GLTPAGRMLV CMGEQPAHGP FTSSRSLYHV IFTATCSSFS FSIYKGRYRS WKKPIHDELV
1030 1040 1050 1060 1070 1080
DRGYTTFGEF FKAVRGYHAD YYRQRLIHDV ETNPGPVQSV FQPQGAVLTK SLAPQAGIQN
1090 1100 1110 1120 1130 1140
LLLRLLGIDG DCSEVSKAIT VVTDLVAAWE KAKTTLVSPE FWSKLILKTT KFIAASVLYL
1150 1160 1170 1180 1190 1200
HNPDFTTTVC LSLMTGVDLL TNDSVFDWLK QKLSSFFRTP PPACPNVMQP QGPLREANEG
1210 1220 1230 1240 1250 1260
FTFAKNIEWA MKTIQSVVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI MDMRNGRKAY
1270 1280 1290 1300 1310 1320
CECTASFKYF DELYNLAVTC KRIPLASLCE KFKNRHDHSV TRPEPVVVVL 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
TPAGMLDVEK AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTQTVYNL QQVVKMVNDT
1510 1520 1530 1540 1550 1560
ITRKTENVKK MNSLVAQSPP DWEHFENILT CLRQNNAALQ DQLDELQEAF AQARERSDFL
1570 1580 1590 1600 1610 1620
SDWLKVSAII FAGIASLSAV IKLASKFKES IWPTPVRVEL SEGEQAAYAG RARAQKQALQ
1630 1640 1650 1660 1670 1680
VLDIQGGGKV LAQAGNPVMD FELFCAKNIV APITFYYPDK AEVTQSCLLL RAHLFVVNRH
1690 1700 1710 1720 1730 1740
VAETDWTAFK LKDVRHERHT VALRSVNRSG AKTDLTFIKV TKGPLFKDNV NKFCSNKDDF
1750 1760 1770 1780 1790 1800
PARNDTVTGI MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN
1810 1820 1830 1840 1850 1860
VNGKKAVYGM HSAGGGGLAA ATIITKELIE AAEKSMLALE PQGAIVDIAT GSVVHVPRKT
1870 1880 1890 1900 1910 1920
KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT TNMESLPPIF DVVCGEYANR
1930 1940 1950 1960 1970 1980
VFTILGKENG LLTVEQAVLG LPGMDPMEKD TSPGLPYTQQ GLRRTDLLNF ITAKMTPQLD
1990 2000 2010 2020 2030 2040
YAHSKLVIGV YDDVVYQSFL KDEIRPIEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF
2050 2060 2070 2080 2090 2100
QTKPGLELGS AIGTDPDVDW TRYAVELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE
2110 2120 2130 2140 2150 2160
QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV IIRAALYLTY
2170 2180 2190 2200 2210 2220
SNFDFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK ITPANKTTTF PLTSHLQDVT
2230 2240 2250 2260 2270 2280
FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC KPGTLKEKLM SIALLAVHSG PDIYDEIFLP
2290 2300
FRNVGIVVPT YSSMLYRWLS LFR
|
P08544 in FASTA format |
|
ExPASy Home page
