Q8JN60 (POLG_BECNB) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 57. History...
Names and origin
|Protein names||Recommended name:|
Cleaved into the following 7 chains:
|Organism||Bovine enteric calicivirus NB (isolate Bovine/United States/Nebraska/1980) (BEC-NB) [Complete proteome]|
|Taxonomic identifier||190239 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Nebovirus ›|
|Virus host||Bos taurus (Bovine) [TaxID: 9913]|
|Sequence length||2210 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
NTPase presumably plays a role in replication By similarity.
Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation By similarity.
3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved By similarity.
RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs By similarity.
Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. Attaches virion to target cells inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm By similarity.
NTP + H2O = NDP + phosphate.
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Specific enzymatic cleavages by its own cysteine protease yield mature proteins. The protease cleaves itself from the nascent polyprotein autocatalytically By similarity.
VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.
Contains 1 peptidase C24 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 – 2210||2210||Genome polyprotein||PRO_0000341628|
|Chain||1 – 302||302||Protein p34||PRO_0000341629|
|Chain||303 – 645||343||NTPase||PRO_0000341630|
|Chain||646 – 925||280||Protein p30||PRO_0000341631|
|Chain||926 – 990||65||Viral genome-linked protein||PRO_0000341632|
|Chain||991 – 1174||184||3C-like protease||PRO_0000341633|
|Chain||1175 – 1659||485||RNA-directed RNA polymerase||PRO_0000341634|
|Chain||1660 – 2210||551||Capsid protein||PRO_0000341635|
|Domain||426 – 585||160||SF3 helicase|
|Domain||1010 – 1109||100||Peptidase C24|
|Domain||1379 – 1501||123||RdRp catalytic|
|Nucleotide binding||456 – 463||8||ATP Potential|
|Active site||1025||1||For 3CLpro activity By similarity|
|Active site||1103||1||For 3CLpro activity Potential|
|Site||302 – 303||2||Cleavage; by 3CLpro Potential|
|Site||645 – 646||2||Cleavage; by 3CLpro Potential|
|Site||925 – 926||2||Cleavage; by 3CLpro Potential|
|Site||990 – 991||2||Cleavage; by 3CLpro Potential|
|Site||1174 – 1175||2||Cleavage; by 3CLpro Potential|
|Site||1659 – 1660||2||Cleavage; by 3CLpro Potential|
Amino acid modifications
|Modified residue||940||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|AY082891 Genomic RNA. Translation: AAL99277.1.|
|RefSeq||NP_663315.1. NC_004064.1. |
3D structure databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|InterPro||IPR004005. Calicivirus_coat. |
|Pfam||PF00915. Calici_coat. 1 hit. |
PF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
|PRINTS||PR00916. 2CENDOPTASE. |
|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: Q8JN60|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|