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P27409 (POLG_FCVF9) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 6 chains:

  1. Protein p5.6
  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 p76
    Short name=Pro-Pol
    EC=2.7.7.48
    EC=3.4.22.66
Gene names
ORF Names:ORF1
OrganismFeline calicivirus (strain F9) (FCV) [Complete proteome]
Taxonomic identifier11981 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageCaliciviridaeVesivirus
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length1763 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 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 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).

Subunit structure

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.

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 – 17631763Genome polyprotein
PRO_0000341997
Chain1 – 4646Protein p5.6 By similarity
PRO_0000036900
Chain47 – 331285Protein p32 By similarity
PRO_0000036901
Chain332 – 685354NTPase By similarity
PRO_0000036902
Chain686 – 960275Protein p30 By similarity
PRO_0000036903
Chain961 – 1071111Viral genome-linked protein By similarity
PRO_0000036904
Chain1072 – 1763692Protease-polymerase p76 By similarity
PRO_0000036905

Regions

Domain458 – 614157SF3 helicase
Domain1095 – 1199105Peptidase C24
Domain1478 – 1603126RdRp catalytic
Nucleotide binding484 – 4918ATP Potential

Sites

Active site11101For protease activity By similarity
Active site11311For protease activity By similarity
Active site11931For protease activity By similarity
Site46 – 472Cleavage; by Pro-Pol By similarity
Site331 – 3322Cleavage; by Pro-Pol By similarity
Site685 – 6862Cleavage; by Pro-Pol By similarity
Site960 – 9612Cleavage; by Pro-Pol By similarity
Site1071 – 10722Cleavage; by Pro-Pol By similarity

Amino acid modifications

Modified residue9841O-(5'-phospho-RNA)-tyrosine By similarity

Secondary structure

......... 1763
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27409 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: BE3C34FD49F35D9B

FASTA1,763195,029
        10         20         30         40         50         60 
MSQTLSFVLK THSVRKDFVH SVKLTLARRR DLQYIYNKLS RTIRAEACPS CASYDVCPNC 

        70         80         90        100        110        120 
TSGDVPDDGS STMSIPSWED VTKSSTYSLL LSEDTSDELC PEDLVNVAAH IRKALSTQSH 

       130        140        150        160        170        180 
PANAEMCKEQ LTFLLVMAEA MLPQRSRASI PLHQQHTAAR LEWREKFFSK PLDFLLERVG 

       190        200        210        220        230        240 
VSKDILQTTA IWKIILEKAC YCKSYGEQWF TAAKQKLREM KNFESDTLKP LIGGFIDGLR 

       250        260        270        280        290        300 
FLTVDNPNPM GFLPKLIGLV KPLNLAMIID NHENTISGWI ITLTAIMELY NITECTIDII 

       310        320        330        340        350        360 
TSVITAFYDK IGKATKFYSC VKALFTGFRS EDVANSFWYM AAAILCYLIT GLIPNNGRFS 

       370        380        390        400        410        420 
KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA RTVALSELNN PTTTSDTDSV 

       430        440        450        460        470        480 
ERLLELAKIL HEEIKIHTLN PIMQSYNPIL RNLMSTLDGV ITSCNKRKAI ARKRQVPVCY 

       490        500        510        520        530        540 
ILTGPPGCGK TTAAQALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIIDEF DSSDKVDYAN 

       550        560        570        580        590        600 
FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSKRAGAF YRRVTIIDVT 

       610        620        630        640        650        660 
NPFVESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ HQSMKAPPPT 

       670        680        690        700        710        720 
FLNIDSLAQT MKQDFLLKNM AFEAEDGCAE HRYGFVCQQE EVETVRRLLN AVRARMNATF 

       730        740        750        760        770        780 
TVCVGPETSH SIGCTAHVLT PNETFNGKKF VVSRCNEASL SALEGNCVKS ALGVCMSDKD 

       790        800        810        820        830        840 
LTHLCHFIKG KIVNDSVRLD ELPANQHVVT VNSVFDLAWA VRRHLTLAGQ FQAIRAAYDV 

       850        860        870        880        890        900 
LTVPDKIPAM LRHWMDETSF SDDHVVTQFV TPGGIVILES CGGARIWALG RNVIRAGGVT 

       910        920        930        940        950        960 
ATPTGGCVRL MGLSAPTMPW SEIFRELFSL LGRIWSSVKV SALVLTALGM YASRFRPKSE 

       970        980        990       1000       1010       1020 
AKGKTKLKIG TYRGRGVALT DDEYDEWREH NASRKLDLSV EDFLMLRHRA ALGADDNDAV 

      1030       1040       1050       1060       1070       1080 
KFRSWWNSRT KMANDYEDVT VIGKGGVKHE KIRTNTLKAV DRGYDVSFAE ESGPGTKFHK 

      1090       1100       1110       1120       1130       1140 
NAIGSVTDVC GEHKGYCIHM GHGVYASVAH VVKGDSFFLG ERIFDLKTNG EFCCFRSTKI 

      1150       1160       1170       1180       1190       1200 
LPSAAPFFSG KPTRDPWGSP VATEWKPKMY TTTSGKILGC FATTSTETHP GDCGLPYIDD 

      1210       1220       1230       1240       1250       1260 
NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK GLICKQLDEI 

      1270       1280       1290       1300       1310       1320 
RIIPKGTRLH VSPAHTEDYQ ECSHQPASLG SGDPRCPKSL TAIVVDSLKP YCENVEGPPH 

      1330       1340       1350       1360       1370       1380 
DVLHRVQKML IDHLSGFVPM NISSETSMLS AFHKLNHDTS CGPYLGGRKK DHMANGEPDK 

      1390       1400       1410       1420       1430       1440 
QLLDLLSAKW KLATQGIALP HEYTIGLKDE LRPVEKVSEG KRRMIWGCDV GVATVCAAAF 

      1450       1460       1470       1480       1490       1500 
KGVSDAITAN HQYGPIQVGI NMDSPSVEAL FQRIKSAAKV FAVDYSKWDS TQSPRVSAAS 

      1510       1520       1530       1540       1550       1560 
IDILRYFSDR SPIVDSASNT LKSPPVAIFN GVAVKVSSGL PSGMPLTSVI NSLNHCLYVG 

      1570       1580       1590       1600       1610       1620 
CAILQSLEAK AIPVTWNLFS TFDIMTYGDD GVYMFPIMYA SISDQIFGNL SSYGLKPTRV 

      1630       1640       1650       1660       1670       1680 
DKSVGAIEPI DPDSVVFLKR TITRTPQGIR GLLDRSSIIR QFYYIKGENS DDWKSPPKHI 

      1690       1700       1710       1720       1730       1740 
DPTSRGQQLW NACLYASQHG LEFFNKVYRL AERAVEYEEL HFEPPTYASA LDHYNSQFNG 

      1750       1760 
VEARSDQIDS SGMTALHCDV FEV 

« Hide

References

[1]"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].
[2]"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].
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86379 Genomic RNA. Translation: AAA79326.1.
Z11536 Genomic RNA. Translation: CAA77635.1.
PIRRRWWF9. A43382.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M4HNMR-A970-1036[»]
ProteinModelPortalP27409.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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. 4 hits.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_FCVF9
AccessionPrimary (citable) accession number: P27409
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: March 19, 2014
This is version 98 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references