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P03304

- POLG_EMCV

UniProt

P03304 - POLG_EMCV

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Protein

Genome polyprotein

Gene
N/A
Organism
Encephalomyocarditis virus
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Leader protein: promotes host NUP62, NUP153, and NUP214 phosphorylation and induces cessation of active nucleocytoplasmic transport. Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response By similarity.1 Publication
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. The capsid interacts with host VCAM1 to provide virion attachment on murine vascular endothelial cells By similarity.1 Publication
Protein VP0: VP0 precursor is a component of immature procapsids By similarity.1 Publication
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity.1 Publication
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.1 Publication
Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity.1 Publication
Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. Cleaves host PABP1, this cleavage is important for viral replication.1 Publication
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.1 Publication
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity.1 Publication

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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
Sitei136 – 1372Cleavage Reviewed prediction
Sitei391 – 3922Cleavage; by protease 3C Reviewed prediction
Sitei622 – 6232Cleavage; by protease 3C Reviewed prediction
Sitei899 – 9002Cleavage; by protease 3C Reviewed prediction
Sitei1042 – 10432Cleavage; by ribosomal skip Reviewed prediction
Sitei1192 – 11932Cleavage; by protease 3C Reviewed prediction
Sitei1517 – 15182Cleavage; by protease 3C Reviewed prediction
Sitei1605 – 16062Cleavage; by protease 3C Reviewed prediction
Sitei1625 – 16262Cleavage; by protease 3C Reviewed prediction
Active sitei1671 – 16711For protease 3C activity Reviewed prediction
Active sitei1703 – 17031For protease 3C activity Reviewed prediction
Active sitei1784 – 17841For protease 3C activity Reviewed prediction
Sitei1830 – 18312Cleavage; by protease 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 2213 Reviewed predictionAdd
BLAST
Nucleotide bindingi1311 – 13188ATP Reviewed prediction

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. protein binding Source: IntAct
  6. RNA binding Source: UniProtKB-KW
  7. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  8. RNA helicase activity Source: InterPro
  9. 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 mRNA export from nucleus Source: UniProtKB-KW
  6. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  7. suppression by virus of host translation Source: UniProtKB-KW
  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 mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I 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
Rho
Virion protein 4
Alternative name(s):
Beta
P1B
Virion protein 2
Alternative name(s):
Gamma
P1C
Virion protein 3
Alternative name(s):
Alpha
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
G
Protein 2B
Short name:
I
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
C
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B
Short name:
P3B
Alternative name(s):
H
VPg
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
Picornain 3C
p22
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48)
Short name:
E
Short name:
P3D-POL
OrganismiEncephalomyocarditis virus
Taxonomic identifieri12104 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000008660: Genome

Subcellular locationi

Chain Protein VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B : Virion Reviewed prediction
Chain Protease 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 15621562Cytoplasmic Reviewed predictionAdd
BLAST
Intramembranei1563 – 158119 Reviewed predictionAdd
BLAST
Topological domaini1582 – 2290709Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. host cell nucleus Source: UniProtKB-SubCell
  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 – 6767Leader proteinPRO_0000039780Add
BLAST
Chaini68 – 391324Protein VP0 Reviewed predictionPRO_0000310967Add
BLAST
Chaini68 – 13669Protein VP4 Reviewed predictionPRO_0000039781Add
BLAST
Chaini137 – 391255Protein VP2 Reviewed predictionPRO_0000039782Add
BLAST
Chaini392 – 622231Protein VP3 Reviewed predictionPRO_0000039783Add
BLAST
Chaini623 – 899277Protein VP1 Reviewed predictionPRO_0000039784Add
BLAST
Chaini900 – 1042143Protein 2A Reviewed predictionPRO_0000039785Add
BLAST
Chaini1043 – 1192150Protein 2B Reviewed predictionPRO_0000039786Add
BLAST
Chaini1193 – 1517325Protein 2C Reviewed predictionPRO_0000039787Add
BLAST
Chaini1518 – 160588Protein 3A Reviewed predictionPRO_0000039788Add
BLAST
Chaini1606 – 162520Protein 3B Reviewed predictionPRO_0000039789Add
BLAST
Chaini1626 – 1830205Protease 3C Reviewed predictionPRO_0000039790Add
BLAST
Chaini1831 – 2290460RNA-directed RNA polymerase 3D-POL Reviewed predictionPRO_0000039791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi68 – 681N-myristoyl glycine; by host By similarity
Modified residuei1608 – 16081O-(5'-phospho-RNA)-tyrosine By 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.
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.
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Protease 3C interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication. Protein 2A interacts with host EIF4E By similarity.1 Publication

Protein-protein interaction databases

IntActiP03304. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP03304.
SMRiP03304. Positions 1-32, 76-896.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1279 – 1445167SF3 helicaseAdd
BLAST
Domaini2059 – 2177119RdRp catalyticAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 6125AcidicAdd
BLAST

Sequence similaritiesi

Contains 2 peptidase C3 domains.

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.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
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.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

Isoform Genome polyprotein (identifier: P03304-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE     50
DDVFDPELDM EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI 100
DLSANAAGSD PPRLRSIFES LSGAVNAFSN MLPLLADQNT EEMENLSDRG 150
LKTLPAIRSQ TPSQQWAVLS VMVPFMMESI RHHVLTLLQK RFWRWKGTTP 200
SRLMIGHQHK SPLSTSAFPF LTSCPVKMVV SLVALRRHYL VKTGWRVQVQ 250
CNASQFHAGG LLVFMAPEYP TLDAFAMDNR WSKDNLPNGT RTQTNKKGPF 300
AMDHQNFWQW TLYPHQFLNL RTNTTVDLEV PYVNIAPTSS WTQHASWTLV 350
IAVVAPLTYS TGASTSLDIT ASIQPVRPVF NGLRHETLSR QSPIPVTIRE 400
HAGTWYSTLP DSTVPIYGKT PVAPSNYMVG EYKDFLEIAQ IPTFIGNKIP 450
NAVPYIEASN TAVKTQPLAT YQVTLSCSCL ANTFLAALSR NFAQYRGSLV 500
YTFVFTGTAM MKGKFLIAYT PPGAGKPTSR DQAMQATYAI WDLGLNSSYS 550
FTVPFISPTH FRMVGTDQVN ITNADGWVTV WQLTPLTYPP GCPTSAKILT 600
MVSAGKDFSL KMPISPAPWS PQGVENAEKG VTENTNATAD FVAQPVYLPE 650
NQTKVAFFYN RSSPIGAFTV KSGSLESGFA PFSNGTCPNS VILTPGPQFD 700
PAYDQLRPQR LTEIWGNGNE ETSKVFPLKS KQDYSFCLFS PFVYYKCDLE 750
VTLSPHTSGN HGLLVRWCPT GTPTKPTTQV LHEVSSLSEG RTPQVYSAGP 800
GISNQISFVV PYNSPLSVLS AVWYNGHKRF DNTGSLGIAP NSDFGTLFFA 850
GTKPDIKFTV YLRYKNKRVF CPRPTVFFPW PTSGDKIDMT PRAGVLMLES 900
PNALDISRTY PTLHVLIQFN HRGLEVRLFR HGHFWAETRA DVILRSKTKQ 950
VSFLSNGNYP SMDSRAPWNP WKNTYQAVLR AEPCRVTMDI YYKRVRPFRL 1000
PLVQKEWPVR EENVFGLYRI FNAHYAGYFA DLLIHDIETN PGPFMFRPRK 1050
QVFQTQGAAV SSMAQTLLPN DLASKAMGSA FTALLDANED AQKAMKIIKT 1100
LSSLSDAWEN VKETLNNPEF WKQLLSRCVQ LIAGMTIAVM HPDPLTLLCL 1150
GTLTAAEITS QTSLCEEIAA KFKTIFITPP PRFPTISLFQ QQSPLKQVND 1200
IFSLAKNLDW AVKTVEKVVD WFGTWIVQEE KEQTLDQLLQ RFPEHAKRIS 1250
DLRNGMAAYV ECKESFDFFE KLYNQAVKEK RTGIAAVCEK FRQKHDHATA 1300
RCEPVVIVLR GDAGQGKSLS SQVIAQAVSK TIFGRQSVYS LPPDSDFFDG 1350
YENQFAAIMD DLGQNPDGSD FTTFCQMVST TNFLPNMASL ERKGTPFTSQ 1400
LVVATTNLPE FRPVTIAHYP AVERRITFDY SVSAGPVCSK TEAGYKVLDV 1450
ERAFRPTGEA PLPCFQNNCL FLEKAGLQFR DNRTKEIISL VDVIERAVAR 1500
IERKKKVLTT VQTLVAQGPV DEVSFHSVVQ QLKARQQATD EQLEELQEAF 1550
AKVQERNSVF SDWLKISAML CAATLALSQV VKMAKAVKQM VKPDLVRVQL 1600
DEQEQGPYNE TARVKPKTLQ LLDIQGPNPV MDFEKYVAKH VTAPIGFVYP 1650
TGVSTQTCLL VRGRTLVVNR HMAESDWTSI VVRGVTHARS TVKILAIAKA 1700
GKETDVSFIR LSSGPLFRDN TSKFVKAGDV LPTGAAPVTG IMNTDIPMMY 1750
TGTFLKAGVS VPVETGQTFN HCIHYKANTR KGWCGSALLA DLGGSKKILG 1800
IHSAGSMGIA AASIVSQEMI RAVVNAFEPQ GALERLPDGP RIHVPRKTAL 1850
RPTVARQVFQ PAYAPAVLSK FDPRTEADVD EVAFSKHTSN QESLPPVFRM 1900
VAKEYANRVF TLLGKDNGRL TVKQALEGLE GMDPMDRNTS PGLPYTALGM 1950
RRTDVVDWES ATLIPFAAER LRKMNEGDFS EVVYQTFLKD ELRPIEKVQA 2000
AKTRIVDVPP FEHCILGRQL LGKFASKFQT QPGLELGSAI GCDPDVHWTA 2050
FGVAMQGFER VYDVDYSNFD STHSVAMFRL LAEEFFTPEN GFDPLTREYL 2100
ESLAISTHAF EEKRFLITGG LPSGCAATSM LNTIMNNIII RAGLYLTYKN 2150
FEFDDVKVLS YGDDLLVATN YQLDFDKVRA SLAKTGYKIT PANTTSTFPL 2200
NSTLEDVVFL KRKFKKEGPL YRPVMNREAL EAMLSYYRPG TLSEKLTSIT 2250
MLAVHSGKQE YDRLFAPFRE VGVVVPSFES VEYRWRSLFW 2290

Note: Produced by conventional translation.

Length:2,290
Mass (Da):255,758
Last modified:July 21, 1986 - v1
Checksum:i26BC81BB7CF68CB5
GO
Isoform 2B* (identifier: P0DJX7-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P0DJX7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by -1 ribosomal frameshifting.

Length:128
Mass (Da):14,449
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1337 – 13371S → P in AAA43036. 1 Publication
Sequence conflicti1397 – 13971F → L in AAA43036. 1 Publication
Sequence conflicti1518 – 15181G → A in AAA43036. 1 Publication
Sequence conflicti1537 – 15371Q → E in AAA43036. 1 Publication
Sequence conflicti1557 – 15571N → S in AAA43036. 1 Publication
Sequence conflicti1612 – 16121A → T in AAA43036. 1 Publication
Sequence conflicti1755 – 17551L → V in AAA43036. 1 Publication
Sequence conflicti1916 – 19161D → N in AAA43036. 1 Publication
Sequence conflicti1987 – 19882FL → IH in AAA43036. 1 Publication
Sequence conflicti2008 – 20081V → I in AAA43036. 1 Publication
Sequence conflicti2049 – 20491T → H in AAA43036. 1 Publication
Sequence conflicti2194 – 21941T → K in AAA43036. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00463 Genomic RNA. Translation: CAA25152.1.
M54935 Genomic RNA. Translation: AAA43036.1.
PIRiA03906. GNNYE.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00463 Genomic RNA. Translation: CAA25152.1 .
M54935 Genomic RNA. Translation: AAA43036.1 .
PIRi A03906. GNNYE.

3D structure databases

ProteinModelPortali P03304.
SMRi P03304. Positions 1-32, 76-896.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03304. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
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.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view ]
PRINTSi PR00918. CALICVIRUSNS.
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region."
    Palmenberg A.C., Kirby E.M., Janda M.R., Drake N.L., Duke G.M., Potratz K.F., Collett M.S.
    Nucleic Acids Res. 12:2969-2985(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Nucleotide sequence of the 3'-terminus of encephalomyocarditis virus RNA."
    Petrov N.A., Chizhikov V.E., Blinov V.M., Karginov V.A., Mikryukov N.N., Gutorov V.V., Grishaev M.P., Beklemishev A.B., Vassilenko S.K.
    Bioorg. Khim. 10:274-279(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1337-2290.
  3. "TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus."
    Eldin P., Papon L., Oteiza A., Brocchi E., Lawson T.G., Mechti N.
    J. Gen. Virol. 90:536-545(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN TRIM22.
  4. "Site-specific cleavage of the host poly(A) binding protein by the encephalomyocarditis virus 3C proteinase stimulates viral replication."
    Kobayashi M., Arias C., Garabedian A., Palmenberg A.C., Mohr I.
    J. Virol. 86:10686-10694(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PROTEASE 3C.

Entry informationi

Entry nameiPOLG_EMCV
AccessioniPrimary (citable) accession number: P03304
Secondary accession number(s): Q66764
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi