Q8V736 (POLG_CACV4) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 67. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Canine calicivirus (strain 48) (CaCV)|
|Taxonomic identifier||292348 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae ›|
|Virus host||Canis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]|
|Sequence length||1929 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. Despite having similarities with helicases, does not seem to display any helicase activity 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.
Protease-polymerase processes the polyprotein: Pro-Pol is first released by autocleavage, then all other proteins are cleaved. Cleaves host translation initiation factor eIF4G1 and eIF4G2 thereby inducing a shutdown of host protein synthesis. This shutdown may not prevent viral mRNA from being translated since viral Vpg replaces the cap. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation. It is also a RNA-directed RNA polymerase which replicates genomic and antigenomic viral RNA by recognizing specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA encodes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs 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).
Protease-polymerase is composed of two domains displaying two different catalytic activity. These activities may act independently By similarity.
Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein 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 – 1929||1929||Genome polyprotein||PRO_0000341984|
|Chain||1 – 176||176||Protein p18||PRO_0000341985|
|Chain||177 – 468||292||Protein p32 By similarity||PRO_0000036886|
|Chain||469 – 825||357||NTPase By similarity||PRO_0000036887|
|Chain||826 – 1112||287||Protein p30 By similarity||PRO_0000036888|
|Chain||1113 – 1232||120||Viral genome-linked protein By similarity||PRO_0000036889|
|Chain||1233 – 1879||647||Protease-polymerase By similarity||PRO_0000036891|
|Domain||597 – 753||157||SF3 helicase|
|Domain||1256 – 1361||106||Peptidase C24|
|Domain||1643 – 1768||126||RdRp catalytic|
|Nucleotide binding||623 – 630||8||ATP Potential|
|Active site||1271||1||For protease activity By similarity|
|Active site||1292||1||For protease activity By similarity|
|Active site||1355||1||For protease activity By similarity|
|Site||176 – 177||2||Cleavage; by Pro-Pol By similarity|
|Site||468 – 469||2||Cleavage; by Pro-Pol By similarity|
|Site||825 – 826||2||Cleavage; by Pro-Pol By similarity|
|Site||1111 – 1112||2||Cleavage; by Pro-Pol By similarity|
|Site||1232 – 1233||2||Cleavage; by Pro-Pol By similarity|
Amino acid modifications
|Modified residue||1137||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|||"Complete nucleotide sequence, genome organization and phylogenic analysis of the canine calicivirus."|
Matsuura Y., Tohya Y., Nakamura K., Shimojima M., Roerink F., Mochizuki M., Takase K., Akashi H., Sugimura T.
Virus Genes 25:67-73(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Organization of the canine calicivirus genome from the RNA polymerase gene to the poly(A) tail."|
Roerink F., Hashimoto M., Tohya Y., Mochizuki M.
J. Gen. Virol. 80:929-935(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1571-1929.
|AB070225 Genomic RNA. Translation: BAB83601.1.|
AF053720 Genomic RNA. Translation: AAC16445.1.
|RefSeq||NP_777373.1. NC_004542.1. |
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR003593. AAA+_ATPase. |
|Pfam||PF03510. Peptidase_C24. 1 hit. |
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
|PRINTS||PR00916. 2CENDOPTASE. |
|SMART||SM00382. AAA. 1 hit. |
|SUPFAM||SSF50494. Pept_Ser_Cys. 1 hit. |
|PROSITE||PS50507. RDRP_SSRNA_POS. 1 hit. |
PS51218. SF3_HELICASE_2. 1 hit.
|Accession||Primary (citable) accession number: Q8V736|
Secondary accession number(s): O72119
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|