POLG_FCVUR
ID POLG_FCVUR Reviewed; 1763 AA.
AC Q66914;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Protein p5.6;
DE Contains:
DE RecName: Full=Protein p32;
DE Contains:
DE RecName: Full=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=p39;
DE Contains:
DE RecName: Full=Protein p30;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE AltName: Full=p13;
DE Contains:
DE RecName: Full=Protease-polymerase p76;
DE Short=Pro-Pol;
DE EC=2.7.7.48;
DE EC=3.4.22.66;
GN ORFNames=ORF1;
OS Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Vesivirus.
OX NCBI_TaxID=292349;
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7618275; DOI=10.1006/viro.1995.1354;
RA Sosnovtsev S.V., Green K.Y.;
RT "RNA transcripts derived from a cloned full-length copy of the feline
RT calicivirus genome do not require VpG for infectivity.";
RL Virology 210:383-390(1995).
RN [2]
RP PROTEIN SEQUENCE OF 686-695, PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND
RP MUTAGENESIS OF GLU-46; GLU-331; GLU-683; GLU-685; GLU-960; GLU-1071;
RP GLU-1345 AND GLU-1419.
RX PubMed=12072506; DOI=10.1128/jvi.76.14.7060-7072.2002;
RA Sosnovtsev S.V., Garfield M., Green K.Y.;
RT "Processing map and essential cleavage sites of the nonstructural
RT polyprotein encoded by ORF1 of the feline calicivirus genome.";
RL J. Virol. 76:7060-7072(2002).
RN [3]
RP PROTEIN SEQUENCE OF 961-969 AND 1072-1080, PROTEOLYTIC PROCESSING OF
RP POLYPROTEIN, AND MUTAGENESIS OF CYS-1193.
RX PubMed=10400760; DOI=10.1128/jvi.73.8.6626-6633.1999;
RA Sosnovtseva S.A., Sosnovtsev S.V., Green K.Y.;
RT "Mapping of the feline calicivirus proteinase responsible for autocatalytic
RT processing of the nonstructural polyprotein and identification of a stable
RT proteinase-polymerase precursor protein.";
RL J. Virol. 73:6626-6633(1999).
RN [4]
RP PROTEIN SEQUENCE OF 961-980.
RX PubMed=11062050; DOI=10.1006/viro.2000.0579;
RA Sosnovtsev S.V., Green K.Y.;
RT "Identification and genomic mapping of the ORF3 and VPg proteins in feline
RT calicivirus virions.";
RL Virology 277:193-203(2000).
RN [5]
RP FUNCTION OF PROTEASE-POLYMERASE P76.
RX PubMed=15254188; DOI=10.1128/jvi.78.15.8172-8182.2004;
RA Kuyumcu-Martinez M., Belliot G., Sosnovtsev S.V., Chang K.O., Green K.Y.,
RA Lloyd R.E.;
RT "Calicivirus 3C-like proteinase inhibits cellular translation by cleavage
RT of poly(A)-binding protein.";
RL J. Virol. 78:8172-8182(2004).
RN [6]
RP FUNCTION OF PROTEASE-POLYMERASE P76.
RX PubMed=15105529; DOI=10.1099/vir.0.19564-0;
RA Willcocks M.M., Carter M.J., Roberts L.O.;
RT "Cleavage of eukaryotic initiation factor eIF4G and inhibition of host-cell
RT protein synthesis during feline calicivirus infection.";
RL J. Gen. Virol. 85:1125-1130(2004).
RN [7]
RP INTERACTION WITH NTPASE (PROTEIN P32), INTERACTION WITH PROTEIN P30
RP (PROTEIN P32), INTERACTION WITH PROTEASE-POLYMERASE P76 (PROTEIN P32),
RP INTERACTION WITH PROTEASE-POLYMERASE P76 (VIRAL GENOME-LINKED PROTEIN),
RP INTERACTION WITH CAPSID PROTEIN VP1 (VIRAL GENOME-LINKED PROTEIN),
RP INTERACTION WITH VIRAL GENOME-LINKED PROTEIN (PROTEASE-POLYMERASE P76),
RP INTERACTION WITH PROTEIN P32 (PROTEASE-POLYMERASE P76), INTERACTION WITH
RP CAPSID PROTEIN VP1 (PROTEASE-POLYMERASE P76), SUBUNIT (PROTEIN P32), AND
RP SUBUNIT (PROTEASE-POLYMERASE P76).
RX PubMed=16432023; DOI=10.1099/vir.0.81456-0;
RA Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.;
RT "Analysis of protein-protein interactions in the feline calicivirus
RT replication complex.";
RL J. Gen. Virol. 87:363-368(2006).
CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC similarities with helicases, does not seem to display any helicase
CC activity.
CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC to viral RNA thereby promoting viral proteins translation (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15105529,
CC ECO:0000269|PubMed:15254188}.
CC -!- FUNCTION: Protease-polymerase p76 processes the polyprotein: Pro-Pol is
CC first released by autocleavage, then all other proteins are cleaved.
CC Cleaves host translation initiation factor eIF4G1, eIF4G2 and PABP1
CC thereby inducing a shutdown of host protein synthesis. This shutdown
CC may not prevent viral mRNA from being translated since viral Vpg
CC replaces the cap. May cleave host polyadenylate-binding protein thereby
CC inhibiting cellular translation. It is also an RNA-directed RNA
CC polymerase which replicates genomic and antigenomic viral RNA by
CC recognizing specific signals. Transcribes also a subgenomic mRNA by
CC initiating RNA synthesis internally on antigenomic RNA. This sgRNA
CC codes for structural proteins. Catalyzes the covalent attachment VPg
CC with viral RNAs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with a preference for cleavage when the P1
CC position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01242};
CC -!- SUBUNIT: Protein p32: Homodimer. Interacts with NTPase, protein p30 and
CC protease-polymerase p76. {ECO:0000269|PubMed:16432023}.
CC -!- SUBUNIT: [Viral genome-linked protein]: Interacts with capsid protein
CC VP1 and protease-polymerase p76. {ECO:0000269|PubMed:16432023}.
CC -!- SUBUNIT: [Protease-polymerase p76]: Homooligomer. Interacts with Vpg,
CC protein p32 and may interact with capsid protein VP1.
CC {ECO:0000269|PubMed:16432023}.
CC -!- DOMAIN: Protease-polymerase is composed of two domains displaying two
CC different catalytic activity. These activities may act independently.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. Pro-
CC Pol is first autocatalytically cleaved, then processes the whole
CC polyprotein. {ECO:0000269|PubMed:10400760,
CC ECO:0000269|PubMed:12072506}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
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DR EMBL; L40021; AAA79323.1; -; Genomic_RNA.
DR RefSeq; NP_783196.1; NC_001481.2.
DR SMR; Q66914; -.
DR MEROPS; C24.002; -.
DR PRIDE; Q66914; -.
DR GeneID; 1502252; -.
DR KEGG; vg:1502252; -.
DR BRENDA; 3.4.22.66; 8732.
DR BRENDA; 3.4.23.B4; 8732.
DR Proteomes; UP000001098; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000317; Peptidase_C24.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF03510; Peptidase_C24; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00916; 2CENDOPTASE.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51894; CV_3CL_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Covalent protein-RNA linkage; Direct protein sequencing;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus;
KW Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Reference proteome; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Viral RNA replication.
FT CHAIN 1..1763
FT /note="Genome polyprotein"
FT /id="PRO_0000341636"
FT CHAIN 1..46
FT /note="Protein p5.6"
FT /id="PRO_0000036907"
FT CHAIN 47..331
FT /note="Protein p32"
FT /id="PRO_0000036908"
FT CHAIN 332..685
FT /note="NTPase"
FT /id="PRO_0000036909"
FT CHAIN 686..960
FT /note="Protein p30"
FT /id="PRO_0000036910"
FT CHAIN 961..1071
FT /note="Viral genome-linked protein"
FT /id="PRO_0000036911"
FT CHAIN 1072..1763
FT /note="Protease-polymerase p76"
FT /id="PRO_0000036912"
FT DOMAIN 458..614
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1073..1229
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1478..1603
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1110
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1131
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1193
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT BINDING 484..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 46..47
FT /note="Cleavage; by Pro-Pol"
FT SITE 331..332
FT /note="Cleavage; by Pro-Pol"
FT SITE 685..686
FT /note="Cleavage; by Pro-Pol"
FT SITE 960..961
FT /note="Cleavage; by Pro-Pol"
FT SITE 1071..1072
FT /note="Cleavage; by Pro-Pol"
FT MOD_RES 984
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT MUTAGEN 46
FT /note="E->A: Complete loss of proteolytic processing
FT between P5.6 and P32; Complete loss of infectious clone
FT recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
FT MUTAGEN 331
FT /note="E->A: Complete loss of infectious clone recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
FT MUTAGEN 683
FT /note="E->A: Complete loss of infectious clone recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
FT MUTAGEN 685
FT /note="E->A: Complete loss of infectious clone recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
FT MUTAGEN 960
FT /note="E->A: Complete loss of infectious clone recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
FT MUTAGEN 1071
FT /note="E->A: Complete loss of infectious clone recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
FT MUTAGEN 1193
FT /note="C->G: Complete loss of proteolytic processing."
FT /evidence="ECO:0000269|PubMed:10400760"
FT MUTAGEN 1345
FT /note="E->A: No effect on infectious clone recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
FT MUTAGEN 1419
FT /note="E->A: No effect on infectious clone recovery."
FT /evidence="ECO:0000269|PubMed:12072506"
SQ SEQUENCE 1763 AA; 194911 MW; 7F105592DF0BF821 CRC64;
MSQTLSFVLK THSVRKDFVH SVKRTLQRRR DLQYLYNKLS RPIRAEACPS CASYDVCPNC
TSGSIPDDGS SKGQIPSWED VTKTSTYSLL LSEDTSDELH PDDLVNVAAH IRKALSTQSH
PANVDMCKEQ LTSLLVMAEA MLPQRSRSTL PLHQKYVAAR LEWREKFFSK PLDFLLEKIG
TSRDILQITA VWKIIIEKAC YCKSYGEHWF EAAKQKLREI KSYEHNTLKP LIGAFIDGLR
LMTIDNPNPM GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDVI
TSIITGFYDK IGKATKFYSQ IKALFTGFRS EDVANSFWYM AAAILCYLIT GLIPNNGRLS
KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA RTVAISELNN PTTTSDTDSV
ERLLELAKIL HEEIKIHTLN PIMQSYNPIL RNLMSTLDGV ITSCNKRKAI AKKRPVPVCY
ILTGPPGCGK TTAALALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIVDEF DSSDKVDYAN
FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSRRAGAF YRRVTIIDVA
NPLAESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ HQSIKAPPPT
FLNIDSLAQT MKQDFTLKNM AFEAENGHSE HRYGFVCQQG EVETVRRLLN AVRTRLNATF
TVCVGSEASS SIGCTAHVLT PDEPFNGKKY VVSRCNEASL SALEGNCVQS ALGVCMSTKD
LTHLCHFIRG KIVNDSVRLD ELPANQHVVT VNSVFDLAWA LRRHLTLAGQ FQAIRAAYDV
LTAPDKVPAM LRHWMDETSF SDEHVVTQFV TPGGIVILES CGGARIWALG HNVIRAGGVT
ATPTGGCIRF MGLSAQTMPW SEIFRELFSL LGRIWSSIKV STLVLTALGM YASRFRPKSE
AKGKTKSKVG PYRGRGVALT DDEYDEWREH NATRKLDLSV EDFLMLRHRA ALGADDADAV
KFRSWWNSRS RLADDYEDVT VIGKGGVKHE KIRTNTLRAV DRGYDVSFAE ESGPGTKFHK
NAIGSVTDVC GEHKGYCVHM GHGVYATVAH VAKGDSFFLG ERIFDLKTNG EFCCFRSTKI
LPSAAPFFPG KPTRDPWGSP VATEWKPKPY TTTSGKIVGC FATTSTETHP GDCGLPYIDD
NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK GLICKQLDEI
RIIPKGTRLH VSPAHTEDFE ECSHQPASLG SGDPRCPKSL TAIVVDSLKP YCDKVEGPPH
DILHRVQKML IDHLSGFVPV NISSETSMLS AFHKLNHDTS CGPYLGGRKK DHMTNGEPDK
PLLDLLSAKW KLATQGIALP HEYTIGLKDE LRPVEKVAEG KRRMIWGCDV GVATVCAAAF
KGVSDAITAN HQYGPVQVGI NMDSPSVEAL HQRIKSAAKV YAVDYSKWDS TQSPRVSAAS
IDILRYFSDR SPIVDSAANT LKSPPIAIFN GVAVKVSSGL PSGMPLTSVI NSLNHCLYVG
CAILQSLEAR GVPVTWNLFS TFDMMTYGDD GVYMFPMMFA SVSDQIFANL SAYGLKPTRV
DKSVGSIEPI DPESVVFLKR TITRTPQGIR GLLDRSSIIR QFYYIKGENS DDWKTPPKSI
DPTSRGQQLW NACLYASQHG VEFYNKIYKL AQKAVEYEEL HLEPPTYHSA LEHYNNQFNG
VEARSDQIDS SGMTALHCDV FEV
