Q6WQ42 (POLG_AEVL2) Reviewed, UniProtKB/Swiss-Prot
Last modified July 9, 2014. Version 75. History...
Names and origin
|Protein names||Recommended name:|
Cleaved into the following 12 chains:
|Organism||Avian encephalomyelitis virus (strain L2Z) (AEV) [Complete proteome]|
|Taxonomic identifier||475780 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Tremovirus ›|
|Virus host||Anas (ducks) [TaxID: 8835]|
Gallus gallus (Chicken) [TaxID: 9031]
Phasianidae [TaxID: 9005]
|Sequence length||2134 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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.
Protein VP0: VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, AEV VP4 may not be myristoylated By similarity.
Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability By similarity.
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.
Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity.
Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer By similarity.
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.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.
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.
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. May associate with membranes through a N-terminal amphipathic helix 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.
RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Interacts with membranes in a complex with viral protein 3AB. 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.
Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. 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 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.
Belongs to the picornaviridae polyprotein family.
Contains 1 peptidase C3 domain.
Contains 1 RdRp catalytic domain.
Contains 1 SF3 helicase domain.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 2134||2134||Genome polyprotein By similarity||PRO_0000310521|
|Chain||1 – 242||242||Protein VP0 Potential||PRO_0000310522|
|Chain||1 – 19||19||Protein VP4 Potential||PRO_0000310523|
|Chain||20 – 242||223||Protein VP2 Potential||PRO_0000310524|
|Chain||243 – 487||245||Protein VP3 Potential||PRO_0000310525|
|Chain||488 – 757||270||Protein VP1 Potential||PRO_0000310526|
|Chain||758 – 806||49||Protein 2A Potential||PRO_0000310527|
|Chain||807 – 1021||215||Protein 2B Potential||PRO_0000310528|
|Chain||1022 – 1347||326||Protein 2C Potential||PRO_0000310529|
|Chain||1348 – 1412||65||Protein 3A Potential||PRO_0000310530|
|Chain||1413 – 1433||21||Protein 3B Potential||PRO_0000310531|
|Chain||1434 – 1648||215||Protease 3C Potential||PRO_0000310532|
|Chain||1649 – 2134||486||RNA-directed RNA polymerase 3D-POL Potential||PRO_0000310533|
|Topological domain||1 – 1377||1377||Cytoplasmic Potential|
|Intramembrane||1378 – 1392||15||Potential|
|Topological domain||1393 – 2134||742||Cytoplasmic Potential|
|Domain||1127 – 1289||163||SF3 helicase|
|Domain||1433 – 1627||195||Peptidase C3|
|Domain||1880 – 2001||122||RdRp catalytic|
|Nucleotide binding||1153 – 1160||8||ATP Potential|
|Compositional bias||251 – 254||4||Poly-Ser|
|Active site||1477||1||For protease 3C activity By similarity|
|Active site||1515||1||For protease 3C activity By similarity|
|Active site||1603||1||For protease 3C activity By similarity|
|Site||19 – 20||2||Cleavage Potential|
|Site||242 – 243||2||Cleavage; by protease 3C Potential|
|Site||487 – 488||2||Cleavage; by protease 3C Potential|
|Site||757 – 758||2||Cleavage; by host Potential|
|Site||806 – 807||2||Cleavage; by protease 3C By similarity|
|Site||1021 – 1022||2||Cleavage; by protease 3C Potential|
|Site||1347 – 1348||2||Cleavage; by protease 3C Potential|
|Site||1412 – 1413||2||Cleavage; by protease 3C Potential|
|Site||1433 – 1434||2||Cleavage; by protease 3C Potential|
|Site||1648 – 1649||2||Cleavage; by protease 3C By similarity|
Amino acid modifications
|Modified residue||1415||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|AY275539 Genomic RNA. Translation: AAN09930.2.|
3D structure databases
Protocols and materials databases
Family and domain databases
|Gene3D||184.108.40.206. 3 hits. |
|InterPro||IPR000605. Helicase_SF3_ssDNA/RNA_vir. |
|Pfam||PF04970. LRAT. 1 hit. |
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
|SUPFAM||SSF50494. SSF50494. 1 hit. |
SSF52540. SSF52540. 1 hit.
|PROSITE||PS50507. RDRP_SSRNA_POS. 1 hit. |
PS51218. SF3_HELICASE_2. 1 hit.
|Accession||Primary (citable) accession number: Q6WQ42|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|