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Q66914 (POLG_FCVUR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 Cat/United States/Urbana/1960) (FCV) [Reference proteome]
Taxonomic identifier292349 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Caliciviridae › Vesivirus ›
Virus hostFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]

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.

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.

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. Ref.7

Domain

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

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. Pro-Pol is first autocatalytically cleaved, then processes the whole polyprotein. Ref.2 Ref.3 Ref.6

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_0000341636
Chain1 – 4646Protein p5.6
PRO_0000036907
Chain47 – 331285Protein p32
PRO_0000036908
Chain332 – 685354NTPase
PRO_0000036909
Chain686 – 960275Protein p30
PRO_0000036910
Chain961 – 1071111Viral genome-linked protein
PRO_0000036911
Chain1072 – 1763692Protease-polymerase p76
PRO_0000036912

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
Site46 – 472Cleavage; by Pro-Pol
Site331 – 3322Cleavage; by Pro-Pol
Site685 – 6862Cleavage; by Pro-Pol
Site960 – 9612Cleavage; by Pro-Pol
Site1071 – 10722Cleavage; by Pro-Pol

Amino acid modifications

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

Experimental info

Mutagenesis461E → A: Complete loss of proteolytic processing between P5.6 and P32; Complete loss of infectious clone recovery. Ref.2
Mutagenesis3311E → A: Complete loss of infectious clone recovery. Ref.2
Mutagenesis6831E → A: Complete loss of infectious clone recovery. Ref.2
Mutagenesis6851E → A: Complete loss of infectious clone recovery. Ref.2
Mutagenesis9601E → A: Complete loss of infectious clone recovery. Ref.2
Mutagenesis10711E → A: Complete loss of infectious clone recovery. Ref.2
Mutagenesis11931C → G: Complete loss of proteolytic processing. Ref.3
Mutagenesis13451E → A: No effect on infectious clone recovery. Ref.2
Mutagenesis14191E → A: No effect on infectious clone recovery. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q66914 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7F105592DF0BF821

FASTA1,763194,911
        10         20         30         40         50         60 
MSQTLSFVLK THSVRKDFVH SVKRTLQRRR DLQYLYNKLS RPIRAEACPS CASYDVCPNC 

        70         80         90        100        110        120 
TSGSIPDDGS SKGQIPSWED VTKTSTYSLL LSEDTSDELH PDDLVNVAAH IRKALSTQSH 

       130        140        150        160        170        180 
PANVDMCKEQ LTSLLVMAEA MLPQRSRSTL PLHQKYVAAR LEWREKFFSK PLDFLLEKIG 

       190        200        210        220        230        240 
TSRDILQITA VWKIIIEKAC YCKSYGEHWF EAAKQKLREI KSYEHNTLKP LIGAFIDGLR 

       250        260        270        280        290        300 
LMTIDNPNPM GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDVI 

       310        320        330        340        350        360 
TSIITGFYDK IGKATKFYSQ IKALFTGFRS EDVANSFWYM AAAILCYLIT GLIPNNGRLS 

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

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

       490        500        510        520        530        540 
ILTGPPGCGK TTAALALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIVDEF DSSDKVDYAN 

       550        560        570        580        590        600 
FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSRRAGAF YRRVTIIDVA 

       610        620        630        640        650        660 
NPLAESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ HQSIKAPPPT 

       670        680        690        700        710        720 
FLNIDSLAQT MKQDFTLKNM AFEAENGHSE HRYGFVCQQG EVETVRRLLN AVRTRLNATF 

       730        740        750        760        770        780 
TVCVGSEASS SIGCTAHVLT PDEPFNGKKY VVSRCNEASL SALEGNCVQS ALGVCMSTKD 

       790        800        810        820        830        840 
LTHLCHFIRG KIVNDSVRLD ELPANQHVVT VNSVFDLAWA LRRHLTLAGQ FQAIRAAYDV 

       850        860        870        880        890        900 
LTAPDKVPAM LRHWMDETSF SDEHVVTQFV TPGGIVILES CGGARIWALG HNVIRAGGVT 

       910        920        930        940        950        960 
ATPTGGCIRF MGLSAQTMPW SEIFRELFSL LGRIWSSIKV STLVLTALGM YASRFRPKSE 

       970        980        990       1000       1010       1020 
AKGKTKSKVG PYRGRGVALT DDEYDEWREH NATRKLDLSV EDFLMLRHRA ALGADDADAV 

      1030       1040       1050       1060       1070       1080 
KFRSWWNSRS RLADDYEDVT VIGKGGVKHE KIRTNTLRAV DRGYDVSFAE ESGPGTKFHK 

      1090       1100       1110       1120       1130       1140 
NAIGSVTDVC GEHKGYCVHM GHGVYATVAH VAKGDSFFLG ERIFDLKTNG EFCCFRSTKI 

      1150       1160       1170       1180       1190       1200 
LPSAAPFFPG KPTRDPWGSP VATEWKPKPY TTTSGKIVGC FATTSTETHP GDCGLPYIDD 

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

      1270       1280       1290       1300       1310       1320 
RIIPKGTRLH VSPAHTEDFE ECSHQPASLG SGDPRCPKSL TAIVVDSLKP YCDKVEGPPH 

      1330       1340       1350       1360       1370       1380 
DILHRVQKML IDHLSGFVPV NISSETSMLS AFHKLNHDTS CGPYLGGRKK DHMTNGEPDK 

      1390       1400       1410       1420       1430       1440 
PLLDLLSAKW KLATQGIALP HEYTIGLKDE LRPVEKVAEG KRRMIWGCDV GVATVCAAAF 

      1450       1460       1470       1480       1490       1500 
KGVSDAITAN HQYGPVQVGI NMDSPSVEAL HQRIKSAAKV YAVDYSKWDS TQSPRVSAAS 

      1510       1520       1530       1540       1550       1560 
IDILRYFSDR SPIVDSAANT LKSPPIAIFN GVAVKVSSGL PSGMPLTSVI NSLNHCLYVG 

      1570       1580       1590       1600       1610       1620 
CAILQSLEAR GVPVTWNLFS TFDMMTYGDD GVYMFPMMFA SVSDQIFANL SAYGLKPTRV 

      1630       1640       1650       1660       1670       1680 
DKSVGSIEPI DPESVVFLKR TITRTPQGIR GLLDRSSIIR QFYYIKGENS DDWKTPPKSI 

      1690       1700       1710       1720       1730       1740 
DPTSRGQQLW NACLYASQHG VEFYNKIYKL AQKAVEYEEL HLEPPTYHSA LEHYNNQFNG 

      1750       1760 
VEARSDQIDS SGMTALHCDV FEV

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References

[1]"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].
[2]"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.
[3]"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.
[4]"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.
[5]"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.
[6]"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.
[7]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L40021 Genomic RNA. Translation: AAA79323.1.
RefSeqNP_783196.1. NC_001481.2.

3D structure databases

ProteinModelPortalQ66914.
ModBaseSearch...

Protein family/group databases

MEROPSC24.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.22.66. 8732.

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
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. Pept_Ser_Cys. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_FCVUR
AccessionPrimary (citable) accession number: Q66914
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents