P36286 (POLG_SMSV1) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 90. History...
Names and origin
|Protein names||Recommended name:|
|Organism||San Miguel sea lion virus serotype 1 (SMSV-1) (SMSV serotype 1) [Complete proteome]|
|Taxonomic identifier||36406 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Vesivirus ›|
|Virus host||Otariidae (fur seals & sea lions) [TaxID: 9702]|
|Sequence length||1879 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 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 – 1879||1879||Genome polyprotein||PRO_0000342015|
|Chain||1 – 148||148||Protein p16||PRO_0000342016|
|Chain||149 – 435||287||Protein p32 By similarity||PRO_0000036928|
|Chain||436 – 791||356||NTPase By similarity||PRO_0000036929|
|Chain||792 – 1070||279||Protein p30 By similarity||PRO_0000036930|
|Chain||1071 – 1183||113||Viral genome-linked protein By similarity||PRO_0000036931|
|Chain||1184 – 1879||696||Protease-polymerase p76 By similarity||PRO_0000036932|
|Domain||564 – 720||157||SF3 helicase|
|Domain||1207 – 1311||105||Peptidase C24|
|Domain||1591 – 1716||126||RdRp catalytic|
|Nucleotide binding||590 – 597||8||ATP Potential|
|Active site||1222||1||For protease activity By similarity|
|Active site||1243||1||For protease activity By similarity|
|Active site||1305||1||For protease activity By similarity|
|Site||148 – 149||2||Cleavage; by Pro-Pol By similarity|
|Site||435 – 436||2||Cleavage; by Pro-Pol By similarity|
|Site||791 – 792||2||Cleavage; by Pro-Pol By similarity|
|Site||1070 – 1071||2||Cleavage; by Pro-Pol By similarity|
|Site||1183 – 1184||2||Cleavage; by Pro-Pol By similarity|
Amino acid modifications
|Modified residue||1093||1||O-(5'-phospho-RNA)-tyrosine By similarity|
|||Neill J.D., Seal B.S., Ridpath J.F.|
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION TO 724-726; 745; 765 AND 774.
|||"Genetic relatedness of the caliciviruses: San Miguel sea lion and vesicular exanthema of swine viruses constitute a single genotype within the Caliciviridae."|
Neill J.D., Meyer R.F., Seal B.S.
J. Virol. 69:4484-4488(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 724-1879.
|||"Nucleotide sequence of the capsid protein gene of two serotypes of San Miguel sea lion virus: identification of conserved and non-conserved amino acid sequences among calicivirus capsid proteins."|
Virus Res. 24:211-222(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1841-1879.
|U15301 Genomic RNA. Translation: AAA96501.2.|
M87481 Unassigned DNA. Translation: AAA16216.1.
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||SSF48371. SSF48371. 1 hit. |
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: P36286|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|