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P03304 (POLG_EMCV) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 13 chains:

  1. Leader protein
  2. Protein VP0
    Alternative name(s):
    VP4-VP2
  3. Protein VP4
    Alternative name(s):
    P1A
    Rho
    Virion protein 4
  4. Protein VP2
    Alternative name(s):
    Beta
    P1B
    Virion protein 2
  5. Protein VP3
    Alternative name(s):
    Gamma
    P1C
    Virion protein 3
  6. Protein VP1
    Alternative name(s):
    Alpha
    P1D
    Virion protein 1
  7. Protein 2A
    Short name=P2A
    Alternative name(s):
    G
  8. Protein 2B
    Short name=I
    Short name=P2B
  9. Protein 2C
    Short name=C
    Short name=P2C
    EC=3.6.1.15
  10. Protein 3A
    Short name=P3A
  11. Protein 3B
    Short name=P3B
    Alternative name(s):
    H
    VPg
  12. Protease 3C
    Short name=P3C
    EC=3.4.22.28
    Alternative name(s):
    Picornain 3C
    p22
  13. RNA-directed RNA polymerase 3D-POL
    Short name=E
    Short name=P3D-POL
    EC=2.7.7.48
OrganismEncephalomyocarditis virus [Complete proteome]
Taxonomic identifier12104 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length2290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

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. Ref.4

Protein VP0: VP0 precursor is a component of immature procapsids By similarity. Ref.4

Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.4

Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Ref.4

Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.4

Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. Cleaves host PABP1, this cleavage is important for viral replication. Ref.4

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.4

Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity. Ref.4

Catalytic activity

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.

Subunit structure

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. Ref.3

Subcellular location

Protein VP2: Virion. Host cytoplasm Potential.

Protein VP3: Virion. Host cytoplasm Potential.

Protein VP1: Virion. Host cytoplasm Potential.

Protein 2B: Host 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.

Protein 2C: Host 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.

Protein 3A: Host 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.

Protein 3B: Virion Potential.

Protease 3C: Host cytoplasm Potential.

RNA-directed RNA polymerase 3D-POL: Host 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.

Protein 2A: Host nucleus By similarity.

Post-translational modification

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.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 2 peptidase C3 domains.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Ontologies

Keywords
   Biological processEukaryotic 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
   Cellular componentCapsid protein
Host cytoplasm
Host cytoplasmic vesicle
Host membrane
Host nucleus
Membrane
Virion
   Coding sequence diversityRibosomal frameshifting
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionHelicase
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
Viral ion channel
   PTMCovalent protein-RNA linkage
Lipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host RIG-I activity by RIG-I proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

suppression by virus of host mRNA export from nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host translation

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

icosahedral viral capsid

Inferred from electronic annotation. Source: InterPro

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 21994459. Source: IntAct

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]
Isoform Genome polyprotein (identifier: P03304-1)

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.
Note: Produced by conventional translation.
Isoform 2B* (identifier: P0DJX7-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6767Leader protein
PRO_0000039780
Chain68 – 391324Protein VP0 Potential
PRO_0000310967
Chain68 – 13669Protein VP4 Potential
PRO_0000039781
Chain137 – 391255Protein VP2 Potential
PRO_0000039782
Chain392 – 622231Protein VP3 Potential
PRO_0000039783
Chain623 – 899277Protein VP1 Potential
PRO_0000039784
Chain900 – 1042143Protein 2A Potential
PRO_0000039785
Chain1043 – 1192150Protein 2B Potential
PRO_0000039786
Chain1193 – 1517325Protein 2C Potential
PRO_0000039787
Chain1518 – 160588Protein 3A Potential
PRO_0000039788
Chain1606 – 162520Protein 3B Potential
PRO_0000039789
Chain1626 – 1830205Protease 3C Potential
PRO_0000039790
Chain1831 – 2290460RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039791

Regions

Topological domain1 – 15621562Cytoplasmic Potential
Intramembrane1563 – 158119 Potential
Topological domain1582 – 2290709Cytoplasmic Potential
Domain1279 – 1445167SF3 helicase
Domain2059 – 2177119RdRp catalytic
Zinc finger10 – 2213 Potential
Nucleotide binding1311 – 13188ATP Potential
Region37 – 6125Acidic

Sites

Active site16711For protease 3C activity Potential
Active site17031For protease 3C activity Potential
Active site17841For protease 3C activity Potential
Site136 – 1372Cleavage Potential
Site391 – 3922Cleavage; by protease 3C Potential
Site622 – 6232Cleavage; by protease 3C Potential
Site899 – 9002Cleavage; by protease 3C Potential
Site1042 – 10432Cleavage; by ribosomal skip Potential
Site1192 – 11932Cleavage; by protease 3C Potential
Site1517 – 15182Cleavage; by protease 3C Potential
Site1605 – 16062Cleavage; by protease 3C Potential
Site1625 – 16262Cleavage; by protease 3C Potential
Site1830 – 18312Cleavage; by protease 3C Potential

Amino acid modifications

Modified residue16081O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation681N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict13371S → P in AAA43036. Ref.2
Sequence conflict13971F → L in AAA43036. Ref.2
Sequence conflict15181G → A in AAA43036. Ref.2
Sequence conflict15371Q → E in AAA43036. Ref.2
Sequence conflict15571N → S in AAA43036. Ref.2
Sequence conflict16121A → T in AAA43036. Ref.2
Sequence conflict17551L → V in AAA43036. Ref.2
Sequence conflict19161D → N in AAA43036. Ref.2
Sequence conflict1987 – 19882FL → IH in AAA43036. Ref.2
Sequence conflict20081V → I in AAA43036. Ref.2
Sequence conflict20491T → H in AAA43036. Ref.2
Sequence conflict21941T → K in AAA43036. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Genome polyprotein [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 26BC81BB7CF68CB5

FASTA2,290255,758
        10         20         30         40         50         60 
MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE DDVFDPELDM 

        70         80         90        100        110        120 
EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI DLSANAAGSD PPRLRSIFES 

       130        140        150        160        170        180 
LSGAVNAFSN MLPLLADQNT EEMENLSDRG LKTLPAIRSQ TPSQQWAVLS VMVPFMMESI 

       190        200        210        220        230        240 
RHHVLTLLQK RFWRWKGTTP SRLMIGHQHK SPLSTSAFPF LTSCPVKMVV SLVALRRHYL 

       250        260        270        280        290        300 
VKTGWRVQVQ CNASQFHAGG LLVFMAPEYP TLDAFAMDNR WSKDNLPNGT RTQTNKKGPF 

       310        320        330        340        350        360 
AMDHQNFWQW TLYPHQFLNL RTNTTVDLEV PYVNIAPTSS WTQHASWTLV IAVVAPLTYS 

       370        380        390        400        410        420 
TGASTSLDIT ASIQPVRPVF NGLRHETLSR QSPIPVTIRE HAGTWYSTLP DSTVPIYGKT 

       430        440        450        460        470        480 
PVAPSNYMVG EYKDFLEIAQ IPTFIGNKIP NAVPYIEASN TAVKTQPLAT YQVTLSCSCL 

       490        500        510        520        530        540 
ANTFLAALSR NFAQYRGSLV YTFVFTGTAM MKGKFLIAYT PPGAGKPTSR DQAMQATYAI 

       550        560        570        580        590        600 
WDLGLNSSYS FTVPFISPTH FRMVGTDQVN ITNADGWVTV WQLTPLTYPP GCPTSAKILT 

       610        620        630        640        650        660 
MVSAGKDFSL KMPISPAPWS PQGVENAEKG VTENTNATAD FVAQPVYLPE NQTKVAFFYN 

       670        680        690        700        710        720 
RSSPIGAFTV KSGSLESGFA PFSNGTCPNS VILTPGPQFD PAYDQLRPQR LTEIWGNGNE 

       730        740        750        760        770        780 
ETSKVFPLKS KQDYSFCLFS PFVYYKCDLE VTLSPHTSGN HGLLVRWCPT GTPTKPTTQV 

       790        800        810        820        830        840 
LHEVSSLSEG RTPQVYSAGP GISNQISFVV PYNSPLSVLS AVWYNGHKRF DNTGSLGIAP 

       850        860        870        880        890        900 
NSDFGTLFFA GTKPDIKFTV YLRYKNKRVF CPRPTVFFPW PTSGDKIDMT PRAGVLMLES 

       910        920        930        940        950        960 
PNALDISRTY PTLHVLIQFN HRGLEVRLFR HGHFWAETRA DVILRSKTKQ VSFLSNGNYP 

       970        980        990       1000       1010       1020 
SMDSRAPWNP WKNTYQAVLR AEPCRVTMDI YYKRVRPFRL PLVQKEWPVR EENVFGLYRI 

      1030       1040       1050       1060       1070       1080 
FNAHYAGYFA DLLIHDIETN PGPFMFRPRK QVFQTQGAAV SSMAQTLLPN DLASKAMGSA 

      1090       1100       1110       1120       1130       1140 
FTALLDANED AQKAMKIIKT LSSLSDAWEN VKETLNNPEF WKQLLSRCVQ LIAGMTIAVM 

      1150       1160       1170       1180       1190       1200 
HPDPLTLLCL GTLTAAEITS QTSLCEEIAA KFKTIFITPP PRFPTISLFQ QQSPLKQVND 

      1210       1220       1230       1240       1250       1260 
IFSLAKNLDW AVKTVEKVVD WFGTWIVQEE KEQTLDQLLQ RFPEHAKRIS DLRNGMAAYV 

      1270       1280       1290       1300       1310       1320 
ECKESFDFFE KLYNQAVKEK RTGIAAVCEK FRQKHDHATA RCEPVVIVLR GDAGQGKSLS 

      1330       1340       1350       1360       1370       1380 
SQVIAQAVSK TIFGRQSVYS LPPDSDFFDG YENQFAAIMD DLGQNPDGSD FTTFCQMVST 

      1390       1400       1410       1420       1430       1440 
TNFLPNMASL ERKGTPFTSQ LVVATTNLPE FRPVTIAHYP AVERRITFDY SVSAGPVCSK 

      1450       1460       1470       1480       1490       1500 
TEAGYKVLDV ERAFRPTGEA PLPCFQNNCL FLEKAGLQFR DNRTKEIISL VDVIERAVAR 

      1510       1520       1530       1540       1550       1560 
IERKKKVLTT VQTLVAQGPV DEVSFHSVVQ QLKARQQATD EQLEELQEAF AKVQERNSVF 

      1570       1580       1590       1600       1610       1620 
SDWLKISAML CAATLALSQV VKMAKAVKQM VKPDLVRVQL DEQEQGPYNE TARVKPKTLQ 

      1630       1640       1650       1660       1670       1680 
LLDIQGPNPV MDFEKYVAKH VTAPIGFVYP TGVSTQTCLL VRGRTLVVNR HMAESDWTSI 

      1690       1700       1710       1720       1730       1740 
VVRGVTHARS TVKILAIAKA GKETDVSFIR LSSGPLFRDN TSKFVKAGDV LPTGAAPVTG 

      1750       1760       1770       1780       1790       1800 
IMNTDIPMMY TGTFLKAGVS VPVETGQTFN HCIHYKANTR KGWCGSALLA DLGGSKKILG 

      1810       1820       1830       1840       1850       1860 
IHSAGSMGIA AASIVSQEMI RAVVNAFEPQ GALERLPDGP RIHVPRKTAL RPTVARQVFQ 

      1870       1880       1890       1900       1910       1920 
PAYAPAVLSK FDPRTEADVD EVAFSKHTSN QESLPPVFRM VAKEYANRVF TLLGKDNGRL 

      1930       1940       1950       1960       1970       1980 
TVKQALEGLE GMDPMDRNTS PGLPYTALGM RRTDVVDWES ATLIPFAAER LRKMNEGDFS 

      1990       2000       2010       2020       2030       2040 
EVVYQTFLKD ELRPIEKVQA AKTRIVDVPP FEHCILGRQL LGKFASKFQT QPGLELGSAI 

      2050       2060       2070       2080       2090       2100 
GCDPDVHWTA FGVAMQGFER VYDVDYSNFD STHSVAMFRL LAEEFFTPEN GFDPLTREYL 

      2110       2120       2130       2140       2150       2160 
ESLAISTHAF EEKRFLITGG LPSGCAATSM LNTIMNNIII RAGLYLTYKN FEFDDVKVLS 

      2170       2180       2190       2200       2210       2220 
YGDDLLVATN YQLDFDKVRA SLAKTGYKIT PANTTSTFPL NSTLEDVVFL KRKFKKEGPL 

      2230       2240       2250       2260       2270       2280 
YRPVMNREAL EAMLSYYRPG TLSEKLTSIT MLAVHSGKQE YDRLFAPFRE VGVVVPSFES 

      2290 
VEYRWRSLFW 

« Hide

Isoform 2B* [UniParc].

See P0DJX7.

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00463 Genomic RNA. Translation: CAA25152.1.
M54935 Genomic RNA. Translation: AAA43036.1.
PIRGNNYE. A03906.

3D structure databases

ProteinModelPortalP03304.
SMRP03304. Positions 1-32, 76-896.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP03304. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProIPR015031. 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]
PfamPF00548. 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]
PRINTSPR00918. CALICVIRUSNS.
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_EMCV
AccessionPrimary (citable) accession number: P03304
Secondary accession number(s): Q66764
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries