Q66914 (POLG_FCVUR) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 84. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV) [Reference proteome]|
|Taxonomic identifier||292349 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Vesivirus ›|
|Virus host||Felis catus (Cat) (Felis silvestris catus) [TaxID: 9685]|
|Sequence length||1763 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.
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. Ref.7
Protease-polymerase is composed of two domains displaying two different catalytic activity. These activities may act independently.
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_0000341636|
|Chain||1 – 46||46||Protein p5.6||PRO_0000036907|
|Chain||47 – 331||285||Protein p32||PRO_0000036908|
|Chain||332 – 685||354||NTPase||PRO_0000036909|
|Chain||686 – 960||275||Protein p30||PRO_0000036910|
|Chain||961 – 1071||111||Viral genome-linked protein||PRO_0000036911|
|Chain||1072 – 1763||692||Protease-polymerase p76||PRO_0000036912|
|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|
|Site||46 – 47||2||Cleavage; by Pro-Pol|
|Site||331 – 332||2||Cleavage; by Pro-Pol|
|Site||685 – 686||2||Cleavage; by Pro-Pol|
|Site||960 – 961||2||Cleavage; by Pro-Pol|
|Site||1071 – 1072||2||Cleavage; by Pro-Pol|
Amino acid modifications
|Modified residue||984||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|Mutagenesis||46||1||E → A: Complete loss of proteolytic processing between P5.6 and P32; Complete loss of infectious clone recovery. Ref.2|
|Mutagenesis||331||1||E → A: Complete loss of infectious clone recovery. Ref.2|
|Mutagenesis||683||1||E → A: Complete loss of infectious clone recovery. Ref.2|
|Mutagenesis||685||1||E → A: Complete loss of infectious clone recovery. Ref.2|
|Mutagenesis||960||1||E → A: Complete loss of infectious clone recovery. Ref.2|
|Mutagenesis||1071||1||E → A: Complete loss of infectious clone recovery. Ref.2|
|Mutagenesis||1193||1||C → G: Complete loss of proteolytic processing. Ref.3|
|Mutagenesis||1345||1||E → A: No effect on infectious clone recovery. Ref.2|
|Mutagenesis||1419||1||E → A: No effect on infectious clone recovery. Ref.2|
|||"RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity."|
Sosnovtsev S.V., Green K.Y.
Virology 210:383-390(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome."|
Sosnovtsev S.V., Garfield M., Green K.Y.
J. Virol. 76:7060-7072(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 686-695, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF GLU-46; GLU-331; GLU-683; GLU-685; GLU-960; GLU-1071; GLU-1345 AND GLU-1419.
|||"Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein."|
Sosnovtseva S.A., Sosnovtsev S.V., Green K.Y.
J. Virol. 73:6626-6633(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 961-969 AND 1072-1080, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF CYS-1193.
|||"Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions."|
Sosnovtsev S.V., Green K.Y.
Virology 277:193-203(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 961-980.
|||"Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein."|
Kuyumcu-Martinez M., Belliot G., Sosnovtsev S.V., Chang K.O., Green K.Y., Lloyd R.E.
J. Virol. 78:8172-8182(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION OF CELLULAR TRANSLATION.
|||"Cleavage of eukaryotic initiation factor eIF4G and inhibition of host-cell protein synthesis during feline calicivirus infection."|
Willcocks M.M., Carter M.J., Roberts L.O.
J. Gen. Virol. 85:1125-1130(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY PROTEASE-POLYMERASE P76 OF HOST EIF4G.
|||"Analysis of protein-protein interactions in the feline calicivirus replication complex."|
Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.
J. Gen. Virol. 87:363-368(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION IN VIRAL REPLICATION COMPLEX.
|+||Additional computationally mapped references.|
|L40021 Genomic RNA. Translation: AAA79323.1.|
|RefSeq||NP_783196.1. NC_001481.2. |
3D structure databases
Protein family/group databases
Protocols and materials databases
Enzyme and pathway databases
|BRENDA||184.108.40.206. 8732. |
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: Q66914|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|