P27409 (POLG_FCVF9) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 91. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Feline calicivirus (strain F9) (FCV) [Complete proteome]|
|Taxonomic identifier||11981 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Vesivirus ›|
|Virus host||Felidae (cat family) [TaxID: 9681]|
|Sequence length||1763 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 p76 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).
Protein p32: homodimer, interacts with NTPase, protein p30 and Pro-Pol. Viral genome-linked protein interacts with capsid protein and Pro-Pol. Protease-polymerase p76: Homooligomers, interacts with Vpg, protein p32 and may interact with capsid protein By similarity.
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 – 1763||1763||Genome polyprotein||PRO_0000341997|
|Chain||1 – 46||46||Protein p5.6 By similarity||PRO_0000036900|
|Chain||47 – 331||285||Protein p32 By similarity||PRO_0000036901|
|Chain||332 – 685||354||NTPase By similarity||PRO_0000036902|
|Chain||686 – 960||275||Protein p30 By similarity||PRO_0000036903|
|Chain||961 – 1071||111||Viral genome-linked protein By similarity||PRO_0000036904|
|Chain||1072 – 1763||692||Protease-polymerase p76 By similarity||PRO_0000036905|
|Domain||458 – 614||157||SF3 helicase|
|Domain||1095 – 1199||105||Peptidase C24|
|Domain||1478 – 1603||126||RdRp catalytic|
|Nucleotide binding||484 – 491||8||ATP Potential|
|Active site||1110||1||For protease activity By similarity|
|Active site||1131||1||For protease activity By similarity|
|Active site||1193||1||For protease activity By similarity|
|Site||46 – 47||2||Cleavage; by Pro-Pol By similarity|
|Site||331 – 332||2||Cleavage; by Pro-Pol By similarity|
|Site||685 – 686||2||Cleavage; by Pro-Pol By similarity|
|Site||960 – 961||2||Cleavage; by Pro-Pol By similarity|
|Site||1071 – 1072||2||Cleavage; by Pro-Pol By similarity|
Amino acid modifications
|Modified residue||984||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|||"The complete nucleotide sequence of a feline calicivirus."|
Carter M.J., Milton I.D., Meanger J., Bennett M., Gaskell R.M., Turner P.C.
Virology 190:443-448(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Cloning and sequence determination of the feline calicivirus strain F9."|
Meanger J., Carter M.J., Gaskell R.M., Turner P.C.
Biochem. Soc. Trans. 20:26S-26S(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Identification and sequence determination of the capsid protein gene of feline calicivirus."|
Carter M.J., Milton I.D., Turner P.C., Meanger J., Bennett M., Gaskell R.M.
Arch. Virol. 122:223-235(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1098-1763.
|M86379 Genomic RNA. Translation: AAA79326.1.|
Z11536 Genomic RNA. Translation: CAA77635.1.
|PIR||RRWWF9. A43382. |
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: P27409|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|