Q66765 (POLG_EMCVR) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 90. History...
Names and origin
|Protein names||Recommended name:|
Cleaved into the following 13 chains:
|Organism||Encephalomyocarditis virus (strain Rueckert) (EMCV) [Reference proteome]|
|Taxonomic identifier||650129 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Cardiovirus ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
Mus musculus (Mouse) [TaxID: 10090]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Sus scrofa (Pig) [TaxID: 9823]
|Sequence length||2292 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Leadear 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. Ref.2 Ref.3
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. The capsid interacts with host VCAM1 to provide virion attachment on murine vascular endothelial cells. Ref.2 Ref.3
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. Ref.2 Ref.3
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.
Protease 3C interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication By similarity. Protein 2A interacts with host EIF4E. Ref.3
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. Ref.3
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. Ref.3
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. Ref.3
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. Ref.3
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.
Belongs to the picornaviruses polyprotein family.
Contains 2 peptidase C3 domains.
Contains 1 RdRp catalytic domain.
Contains 1 SF3 helicase domain.
|This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]|
|Isoform Genome polyprotein (identifier: Q66765-1) |
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: P0DJX6-1) |
The sequence of this isoform can be found in the external entry P0DJX6.
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 key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 67||67||Leader protein By similarity||PRO_0000423146|
|Chain||68 – 393||326||Protein VP0 Potential||PRO_0000423147|
|Chain||68 – 137||70||Protein VP4 Potential||PRO_5000143569|
|Chain||138 – 393||256||Protein VP2 Potential||PRO_5000143570|
|Chain||394 – 624||231||Protein VP3 Potential||PRO_5000143571|
|Chain||625 – 901||277||Protein VP1 Potential||PRO_5000143572|
|Chain||902 – 1044||143||Protein 2A Potential||PRO_5000143573|
|Chain||1045 – 1194||150||Protein 2B Potential||PRO_5000143574|
|Chain||1195 – 1519||325||Protein 2C Potential||PRO_5000143575|
|Chain||1520 – 1607||88||Protein 3A Potential||PRO_5000143576|
|Chain||1608 – 1627||20||Protein 3B Potential||PRO_0000423148|
|Chain||1628 – 1832||205||Protease 3C Potential||PRO_5000143577|
|Chain||1833 – 2292||460||RNA-directed RNA polymerase 3D-POL Potential||PRO_5000143578|
|Topological domain||1 – 1564||1564||Cytoplasmic Potential|
|Intramembrane||1565 – 1583||19||Potential|
|Topological domain||1584 – 2292||709||Cytoplasmic Potential|
|Domain||1281 – 1447||167||SF3 helicase|
|Domain||2061 – 2179||119||RdRp catalytic|
|Zinc finger||10 – 22||13||Potential|
|Nucleotide binding||1313 – 1320||8||ATP Potential|
|Region||37 – 61||25||Acidic By similarity|
|Active site||1673||1||For protease 3C activity Potential|
|Active site||1705||1||For protease 3C activity Potential|
|Active site||1786||1||For protease 3C activity Potential|
|Site||137 – 138||2||Cleavage Potential|
|Site||393 – 394||2||Cleavage; by protease 3C Potential|
|Site||624 – 625||2||Cleavage; by protease 3C Potential|
|Site||901 – 902||2||Cleavage; by protease 3C Potential|
|Site||1044 – 1045||2||Cleavage; by ribosomal skip Potential|
|Site||1194 – 1195||2||Cleavage; by protease 3C Potential|
|Site||1519 – 1520||2||Cleavage; by protease 3C Potential|
|Site||1607 – 1608||2||Cleavage; by protease 3C Potential|
|Site||1627 – 1628||2||Cleavage; by protease 3C Potential|
|Site||1832 – 1833||2||Cleavage; by protease 3C Potential|
Amino acid modifications
|Modified residue||1610||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|Lipidation||68||1||N-myristoyl glycine; by host By similarity|
|||"Sequence and structural elements that contribute to efficient encephalomyocarditis virus RNA translation."|
Duke G.M., Hoffman M.A., Palmenberg A.C.
J. Virol. 66:1602-1602(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardioviruses."|
Porter F.W., Palmenberg A.C.
J. Virol. 83:1941-1951(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF LEADER PROTEIN.
|||"Mutational analysis of the EMCV 2A protein identifies a nuclear localization signal and an eIF4E binding site."|
Groppo R., Brown B.A., Palmenberg A.C.
Virology 410:257-267(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF PROTEIN 2A, SUBCELLULAR LOCATION OF PROTEIN 2A, INTERACTION OF PROTEIN 2A WITH HUMAN EIF4E.
|M81861 Genomic RNA. Translation: AAA43037.1.|
|RefSeq||NP_056777.1. NC_001479.1. |
3D structure databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|Gene3D||220.127.116.11. 1 hit. |
|InterPro||IPR015031. Capsid_VP4_Picornavir. |
|Pfam||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.
|PRINTS||PR00918. CALICVIRUSNS. |
|SUPFAM||SSF50494. SSF50494. 1 hit. |
|PROSITE||PS50507. RDRP_SSRNA_POS. 1 hit. |
PS51218. SF3_HELICASE_2. 1 hit.
|Accession||Primary (citable) accession number: Q66765|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|