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Q8V736 (POLG_CACV4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 6 chains:

  1. Protein p18
  2. Protein p32
  3. NTPase
    EC=3.6.1.15
    Alternative name(s):
    p39
  4. Protein p30
  5. Viral genome-linked protein
    Alternative name(s):
    VPg
    p13
  6. Protease-polymerase
    Short name=Pro-Pol
    EC=2.7.7.48
    EC=3.4.22.66
Gene names
ORF Names:ORF1
OrganismCanine calicivirus (strain 48) (CaCV)
Taxonomic identifier292348 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageCaliciviridae
Virus hostCanis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]

Protein attributes

Sequence length1929 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 an 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.

Catalytic activity

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).

Domain

Protease-polymerase is composed of two domains displaying two different catalytic activity. These activities may act independently By similarity.

Post-translational modification

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.

Sequence similarities

Contains 1 peptidase C24 domain.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19291929Genome polyprotein
PRO_0000341984
Chain1 – 176176Protein p18
PRO_0000341985
Chain177 – 468292Protein p32 By similarity
PRO_0000036886
Chain469 – 825357NTPase By similarity
PRO_0000036887
Chain826 – 1112287Protein p30 By similarity
PRO_0000036888
Chain1113 – 1232120Viral genome-linked protein By similarity
PRO_0000036889
Chain1233 – 1879647Protease-polymerase By similarity
PRO_0000036891

Regions

Domain597 – 753157SF3 helicase
Domain1256 – 1361106Peptidase C24
Domain1643 – 1768126RdRp catalytic
Nucleotide binding623 – 6308ATP Potential

Sites

Active site12711For protease activity By similarity
Active site12921For protease activity By similarity
Active site13551For protease activity By similarity
Site176 – 1772Cleavage; by Pro-Pol By similarity
Site468 – 4692Cleavage; by Pro-Pol By similarity
Site825 – 8262Cleavage; by Pro-Pol By similarity
Site1111 – 11122Cleavage; by Pro-Pol By similarity
Site1232 – 12332Cleavage; by Pro-Pol By similarity

Amino acid modifications

Modified residue11371O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8V736 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 9F8A92FC0657A623

FASTA1,929214,806
        10         20         30         40         50         60 
MASAIALSSS TAQNKITLKS VASRLQQTDD PDIRVWSQSV GFHLQFSNWK CANAFCRFVT 

        70         80         90        100        110        120 
DAYNLTPYKE CARSITRQLT SLSNYLSAQT GVSVSGTQFL LSPSDVEVPV AKTGESVSDI 

       130        140        150        160        170        180 
MVPSYSVNGT SMEFDSMAQL AQALTTGFTF SVNDAQIGNA PAQTGESVSG TGFIAEACPS 

       190        200        210        220        230        240 
CALYDKCPNC TSELINDDGS SQSPGDIPHW THHKIASGIV NILSSDMSSM EDDDFANIAA 

       250        260        270        280        290        300 
HVKKALGTNS HPANNDMSKD QLNWLLNIAE ASLIRKADRT ALPMNAARIA ARRGWREKLF 

       310        320        330        340        350        360 
NEPADKLYTL LRKSKDSFQK SAIWGILFEK ASNAKHYTEI VFQDIVKLIK EECNPSNNFY 

       370        380        390        400        410        420 
FKVMAQSFLD HFRMLVIDNP DPVANLPKFI LKLKPLNLKM IIENHENTAE GWIVTLTAVA 

       430        440        450        460        470        480 
ELYGWLEFAV DLVPKIVSEL YDLLTSATQK CFSMVRELLT NLNILKAESF DFTNPFWYAL 

       490        500        510        520        530        540 
AALLSYFVTG FLPNNAKCSA IKQTLNGATT LVAGITAIQK LAAMFSAWSN ESVVDDLSTK 

       550        560        570        580        590        600 
VIGLTEADNP TVTQDIDAVT NLQIMAEQLK DQIKLKTLDP TFQPYLPVLR NLMSTTDSVI 

       610        620        630        640        650        660 
SHCAKRKALA TQRTAPVCII LTGPAGCGKT TLAYAIANRL SAQKPSVLNL NIDHHDAYTG 

       670        680        690        700        710        720 
NEVCIIDEFD SNPDSKFVEF VVEMVNTNPM LLNCDLIENK GKTFSSKYVI MTSNNETPVK 

       730        740        750        760        770        780 
PNSTRAPPFY RRVRIIDVTN PGVMSFKYEN PGQEVPSYLF SNDFNHLSMS MRGFGAFSKT 

       790        800        810        820        830        840 
RVIDPEGRKT CGLEGPPGQR VDVDDIVRYM QRMYRENQMN FKSEAGNNRL KTPRFAFVTQ 

       850        860        870        880        890        900 
RKHVDTVYKI LAAAKTTYNG YYSLTKDSFD VNEGHNIGSS VFVVGDDKEI PHNCKIFRCN 

       910        920        930        940        950        960 
HLAMFRHPEL AHIEGDNFRA ALGVTMSDQD VTLMFYHIRG KHIQDEVRLD ELPANHHIVT 

       970        980        990       1000       1010       1020 
VHSVYDMAWA LNRHLSLTGK WQALKAVYDL YMTPDILPAA LRHWMDNTKF SSDHVVTQFI 

      1030       1040       1050       1060       1070       1080 
VPGGTIILET CNGARMWATS RRLIRAGGIS NNNGPEGGFR FGSIAPRDIP WSEILREFLN 

      1090       1100       1110       1120       1130       1140 
LISLIWSRVK GATIVLTALL LYMKRYKPRS EAKGKTKGGR GAIRHGGKGI VLSDDEYDEW 

      1150       1160       1170       1180       1190       1200 
REFNMEKRMD MSVDEFLMLK HRAALGSDDT GAIQFRSWWT ARQMRESTGL DHDDVTVIGK 

      1210       1220       1230       1240       1250       1260 
GGVRHEVHRT EIMKAPKQKK KSFAWGEDMY AEGDGKIVNH VNAIVPVTGL CGEHIGYAVH 

      1270       1280       1290       1300       1310       1320 
IGHGKCISLK HVLKTGSYVF NQKPIDVTFD GELAHFQIQQ PPSSAAPVTF SSKPTRDPWG 

      1330       1340       1350       1360       1370       1380 
RSVSTEWKHD TYNTTAGKMY GSICWTATRT QPGDCGLPYV DRAGQVVGLH AGSGGDSAPG 

      1390       1400       1410       1420       1430       1440 
RKIVIPVTKF KLPSNTVLSN RFWKEEAPTI SYKGLTVQET GVNKAVLKGT NYHVSPAHVD 

      1450       1460       1470       1480       1490       1500 
DYQDCTHQPA NLGAQDERYP VSLTSIVINN LEPYKQPTQG PPTEVLNKAY NMLVQHYEPL 

      1510       1520       1530       1540       1550       1560 
IPKATTHLEM GDAFAALNVK TSCGPYITGR KKDHIDPETG KWDETLRNHI NARWSLATQG 

      1570       1580       1590       1600       1610       1620 
VPIPHEYQLG LKDELRPKDK IAVGKRRLIW GCDVGVAVVA ASAFKEVSSA IMAMSEFDFI 

      1630       1640       1650       1660       1670       1680 
QVGINMDGTA VETLYKRLYT PGTHRYCVDY SKWDSTQPPN VTRMSLELLR HFTDKSPVVD 

      1690       1700       1710       1720       1730       1740 
SAVATLSSPS IAVFGGVSFK TNGGLPSGMP LTSILNSLNH CLLVGSAIIQ VLESKGVDVN 

      1750       1760       1770       1780       1790       1800 
WNIYDTIDLF TYGDDGVYIV PNFVHSVMPE VFSCLSSYGL KPTRTDKSSA PITEIPLSEP 

      1810       1820       1830       1840       1850       1860 
IEFLKRQFVR NQFGVRALLD RSSLIRQFYY IKGKNTMEWT KPPEQIDLTS RTAQLQVVML 

      1870       1880       1890       1900       1910       1920 
YASQHGREFY KKCLDYYQLA MEYEGIKLDA PTYDEALAKY NANFNGVEDC DLLPAGYDEH 


RLDKIVFEN 

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References

[1]"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].
[2]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB070225 Genomic RNA. Translation: BAB83601.1.
AF053720 Genomic RNA. Translation: AAC16445.1.
RefSeqNP_777373.1. NC_004542.1.

3D structure databases

ProteinModelPortalQ8V736.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956316.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR003593. AAA+_ATPase.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR000317. Peptidase_C24.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF03510. Peptidase_C24. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
PRINTSPR00916. 2CENDOPTASE.
PR00918. CALICVIRUSNS.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_CACV4
AccessionPrimary (citable) accession number: Q8V736
Secondary accession number(s): O72119
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries