ID   POLG_FCVF9              Reviewed;        1763 AA.
AC   P27409;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 129.
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 F9) (FCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Vesivirus.
OX   NCBI_TaxID=11981;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1529544; DOI=10.1016/0042-6822(92)91231-i;
RA   Carter M.J., Milton I.D., Meanger J., Bennett M., Gaskell R.M.,
RA   Turner P.C.;
RT   "The complete nucleotide sequence of a feline calicivirus.";
RL   Virology 190:443-448(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1633955; DOI=10.1042/bst020026s;
RA   Meanger J., Carter M.J., Gaskell R.M., Turner P.C.;
RT   "Cloning and sequence determination of the feline calicivirus strain F9.";
RL   Biochem. Soc. Trans. 20:26S-26S(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1098-1763.
RX   PubMed=1731695; DOI=10.1007/bf01317185;
RA   Carter M.J., Milton I.D., Turner P.C., Meanger J., Bennett M.,
RA   Gaskell R.M.;
RT   "Identification and sequence determination of the capsid protein gene of
RT   feline calicivirus.";
RL   Arch. Virol. 122:223-235(1992).
RN   [4] {ECO:0007744|PDB:2M4H}
RP   STRUCTURE BY NMR OF 969-1039.
RX   PubMed=23487472; DOI=10.1128/jvi.03151-12;
RA   Leen E.N., Kwok K.Y., Birtley J.R., Simpson P.J., Subba-Reddy C.V.,
RA   Chaudhry Y., Sosnovtsev S.V., Green K.Y., Prater S.N., Tong M., Young J.C.,
RA   Chung L.M., Marchant J., Roberts L.O., Kao C.C., Matthews S.,
RA   Goodfellow I.G., Curry S.;
RT   "Structures of the compact helical core domains of feline calicivirus and
RT   murine norovirus VPg proteins.";
RL   J. Virol. 87:5318-5330(2013).
CC   -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC       similarities with helicases, does not seem to display any helicase
CC       activity (By similarity). {ECO:0000250}.
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}.
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 (By similarity). {ECO:0000250}.
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 (By similarity). Interacts with
CC       NTPase, protein p30 and protease-polymerase p76 (By similarity).
CC       {ECO:0000250|UniProtKB:Q66914}.
CC   -!- SUBUNIT: [Viral genome-linked protein]: Interacts with capsid protein
CC       VP1 and protease-polymerase p76 (By similarity).
CC       {ECO:0000250|UniProtKB:Q66914}.
CC   -!- SUBUNIT: [Protease-polymerase p76]: Homooligomer (By similarity).
CC       Interacts with Vpg, protein p32 and may interact with capsid protein
CC       VP1 (By similarity). {ECO:0000250|UniProtKB:Q66914}.
CC   -!- DOMAIN: Protease-polymerase is composed of two domains displaying two
CC       different catalytic activity. These activities may act independently
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. Pro-
CC       Pol is first autocatalytically cleaved, then processes the whole
CC       polyprotein (By similarity). {ECO:0000250}.
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; M86379; AAA79326.1; -; Genomic_RNA.
DR   EMBL; Z11536; CAA77635.1; -; Genomic_RNA.
DR   PIR; A43382; RRWWF9.
DR   PDB; 2M4H; NMR; -; A=969-1039.
DR   PDBsum; 2M4H; -.
DR   BMRB; P27409; -.
DR   SMR; P27409; -.
DR   MEROPS; C24.002; -.
DR   PRIDE; P27409; -.
DR   BRENDA; 3.4.22.66; 8732.
DR   Proteomes; UP000008762; 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; 2.
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   3D-structure; ATP-binding; Covalent protein-RNA linkage;
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   RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1763
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000341997"
FT   CHAIN           1..46
FT                   /note="Protein p5.6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036900"
FT   CHAIN           47..331
FT                   /note="Protein p32"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036901"
FT   CHAIN           332..685
FT                   /note="NTPase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036902"
FT   CHAIN           686..960
FT                   /note="Protein p30"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036903"
FT   CHAIN           961..1071
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036904"
FT   CHAIN           1072..1763
FT                   /note="Protease-polymerase p76"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036905"
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                   /evidence="ECO:0000250"
FT   SITE            331..332
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000250"
FT   SITE            685..686
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000250"
FT   SITE            960..961
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000250"
FT   SITE            1071..1072
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         984
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
FT   STRAND          973..976
FT                   /evidence="ECO:0007829|PDB:2M4H"
FT   HELIX           981..993
FT                   /evidence="ECO:0007829|PDB:2M4H"
FT   HELIX           1000..1012
FT                   /evidence="ECO:0007829|PDB:2M4H"
FT   HELIX           1017..1029
FT                   /evidence="ECO:0007829|PDB:2M4H"
SQ   SEQUENCE   1763 AA;  195029 MW;  BE3C34FD49F35D9B CRC64;
     MSQTLSFVLK THSVRKDFVH SVKLTLARRR DLQYIYNKLS RTIRAEACPS CASYDVCPNC
     TSGDVPDDGS STMSIPSWED VTKSSTYSLL LSEDTSDELC PEDLVNVAAH IRKALSTQSH
     PANAEMCKEQ LTFLLVMAEA MLPQRSRASI PLHQQHTAAR LEWREKFFSK PLDFLLERVG
     VSKDILQTTA IWKIILEKAC YCKSYGEQWF TAAKQKLREM KNFESDTLKP LIGGFIDGLR
     FLTVDNPNPM GFLPKLIGLV KPLNLAMIID NHENTISGWI ITLTAIMELY NITECTIDII
     TSVITAFYDK IGKATKFYSC VKALFTGFRS EDVANSFWYM AAAILCYLIT GLIPNNGRFS
     KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA RTVALSELNN PTTTSDTDSV
     ERLLELAKIL HEEIKIHTLN PIMQSYNPIL RNLMSTLDGV ITSCNKRKAI ARKRQVPVCY
     ILTGPPGCGK TTAAQALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIIDEF DSSDKVDYAN
     FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSKRAGAF YRRVTIIDVT
     NPFVESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ HQSMKAPPPT
     FLNIDSLAQT MKQDFLLKNM AFEAEDGCAE HRYGFVCQQE EVETVRRLLN AVRARMNATF
     TVCVGPETSH SIGCTAHVLT PNETFNGKKF VVSRCNEASL SALEGNCVKS ALGVCMSDKD
     LTHLCHFIKG KIVNDSVRLD ELPANQHVVT VNSVFDLAWA VRRHLTLAGQ FQAIRAAYDV
     LTVPDKIPAM LRHWMDETSF SDDHVVTQFV TPGGIVILES CGGARIWALG RNVIRAGGVT
     ATPTGGCVRL MGLSAPTMPW SEIFRELFSL LGRIWSSVKV SALVLTALGM YASRFRPKSE
     AKGKTKLKIG TYRGRGVALT DDEYDEWREH NASRKLDLSV EDFLMLRHRA ALGADDNDAV
     KFRSWWNSRT KMANDYEDVT VIGKGGVKHE KIRTNTLKAV DRGYDVSFAE ESGPGTKFHK
     NAIGSVTDVC GEHKGYCIHM GHGVYASVAH VVKGDSFFLG ERIFDLKTNG EFCCFRSTKI
     LPSAAPFFSG KPTRDPWGSP VATEWKPKMY TTTSGKILGC FATTSTETHP GDCGLPYIDD
     NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK GLICKQLDEI
     RIIPKGTRLH VSPAHTEDYQ ECSHQPASLG SGDPRCPKSL TAIVVDSLKP YCENVEGPPH
     DVLHRVQKML IDHLSGFVPM NISSETSMLS AFHKLNHDTS CGPYLGGRKK DHMANGEPDK
     QLLDLLSAKW KLATQGIALP HEYTIGLKDE LRPVEKVSEG KRRMIWGCDV GVATVCAAAF
     KGVSDAITAN HQYGPIQVGI NMDSPSVEAL FQRIKSAAKV FAVDYSKWDS TQSPRVSAAS
     IDILRYFSDR SPIVDSASNT LKSPPVAIFN GVAVKVSSGL PSGMPLTSVI NSLNHCLYVG
     CAILQSLEAK AIPVTWNLFS TFDIMTYGDD GVYMFPIMYA SISDQIFGNL SSYGLKPTRV
     DKSVGAIEPI DPDSVVFLKR TITRTPQGIR GLLDRSSIIR QFYYIKGENS DDWKSPPKHI
     DPTSRGQQLW NACLYASQHG LEFFNKVYRL AERAVEYEEL HFEPPTYASA LDHYNSQFNG
     VEARSDQIDS SGMTALHCDV FEV