P27407 (POLG_FCVC6) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 97. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Feline calicivirus (strain CFI/68 FIV) (FCV) [Complete proteome]|
|Taxonomic identifier||11979 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Vesivirus ›|
|Virus host||Felidae (cat family) [TaxID: 9681]|
|Sequence length||1762 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, eIF4G2 and PABP1 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 codes 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 – 1762||1762||Genome polyprotein||PRO_0000341990|
|Chain||1 – 46||46||Protein p5.6 By similarity||PRO_0000036892|
|Chain||47 – 331||285||Protein p32 By similarity||PRO_0000036893|
|Chain||332 – 684||353||NTPase By similarity||PRO_0000036894|
|Chain||685 – 959||275||Protein p30 By similarity||PRO_0000036895|
|Chain||960 – 1070||111||Viral genome-linked protein By similarity||PRO_0000036896|
|Chain||1071 – 1762||692||Protease-polymerase p76 By similarity||PRO_0000036897|
|Domain||458 – 614||157||SF3 helicase|
|Domain||1094 – 1198||105||Peptidase C24|
|Domain||1477 – 1602||126||RdRp catalytic|
|Nucleotide binding||484 – 491||8||ATP Potential|
|Active site||1109||1||For protease activity By similarity|
|Active site||1130||1||For protease activity By similarity|
|Active site||1192||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||684 – 685||2||Cleavage; by Pro-Pol By similarity|
|Site||959 – 960||2||Cleavage; by Pro-Pol By similarity|
|Site||1070 – 1071||2||Cleavage; by Pro-Pol By similarity|
Amino acid modifications
|Modified residue||983||1||O-(5'-phospho-RNA)-tyrosine By similarity|
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Nucleotide sequence of a region of the feline calicivirus genome which encodes picornavirus-like RNA-dependent RNA polymerase, cysteine protease and 2C polypeptides."|
Virus Res. 17:145-160(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 479-1762.
|U13992 Genomic RNA. Translation: AAC13992.1.|
M32296 Genomic RNA. Translation: AAA42927.1.
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. SSF50494. 1 hit. |
SSF52540. SSF52540. 4 hits.
|PROSITE||PS50507. RDRP_SSRNA_POS. 1 hit. |
PS51218. SF3_HELICASE_2. 1 hit.
|Accession||Primary (citable) accession number: P27407|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|