ID   POLG_FCVC6              Reviewed;        1762 AA.
AC   P27407;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
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 CFI/68 FIV) (FCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Vesivirus.
OX   NCBI_TaxID=11979;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Neill J.D.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 479-1762.
RX   PubMed=2077782; DOI=10.1016/0168-1702(90)90061-f;
RA   Neill J.D.;
RT   "Nucleotide sequence of a region of the feline calicivirus genome which
RT   encodes picornavirus-like RNA-dependent RNA polymerase, cysteine protease
RT   and 2C polypeptides.";
RL   Virus Res. 17:145-160(1990).
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; U13992; AAC13992.1; -; Genomic_RNA.
DR   EMBL; M32296; AAA42927.1; -; Genomic_RNA.
DR   PIR; A43488; A43488.
DR   PIR; T09245; T09245.
DR   SMR; P27407; -.
DR   MEROPS; C24.002; -.
DR   Proteomes; UP000008667; 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   3: Inferred from homology;
KW   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..1762
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000341990"
FT   CHAIN           1..46
FT                   /note="Protein p5.6"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036892"
FT   CHAIN           47..331
FT                   /note="Protein p32"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036893"
FT   CHAIN           332..684
FT                   /note="NTPase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036894"
FT   CHAIN           685..959
FT                   /note="Protein p30"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036895"
FT   CHAIN           960..1070
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036896"
FT   CHAIN           1071..1762
FT                   /note="Protease-polymerase p76"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036897"
FT   DOMAIN          458..614
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1072..1228
FT                   /note="Peptidase C24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   DOMAIN          1477..1602
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ACT_SITE        1109
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   ACT_SITE        1130
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   ACT_SITE        1192
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            684..685
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000250"
FT   SITE            959..960
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000250"
FT   SITE            1070..1071
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         983
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1762 AA;  195339 MW;  61C010202984AF40 CRC64;
     MSQTLSFVLK THNVRKDFVR SVKLTLARRR DLQYFYNKLS RSMRAEACPS CASYDVCPNC
     TSSDIPDDGS STELIPSWEE VTKTSTYSLL LSEDTSDELC PDDLANVAAH IRKAISTQSH
     PANSDMCKEQ LTSLLVMAEA MLPQRSRASI PLHQQHQAAR LEWREKFFSK PLDFLLERIG
     VSKDILQITA IWKIILEKAC YCKSYGEQWF TTAKQKLREM RSYESNTLKP LIGAFIDGLR
     FMTVDNPYPM GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDLM
     TSLITAFYDK IGKATKFYSH VKALFTGFRT EDVSNSFWYM AAAILCYLVT GLIPNNGRFL
     KIKCLLVRAT TLVSGIIATQ KLAAMFATWN SESIVNELSA RTVAISELNN PTTTSDTESV
     ERLLELAKIL HEEIKVHTLN PIMQSYNLIL RNLMSTLDGV ITCCNKRKAI ARKRQVPVCY
     ILTGPPGCGK TTAAQALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIIDEF DSSDKVDYAN
     FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSKRAGAF YRRVTYHDVA
     TLVESHKRAR PGTAVPRSCY KKNFSHLSLA KRGAECWCKE YVLDPKGLQH QSTKAPPPTF
     LNIDSLAQTM KQDFALKNMA FEAEVGCSEH RYGFVCQQSE VETVRRLLNA IRMRLNATFT
     VCVGLEASNS VGCTAHVLTP DEPFNGKRFV VSRCNEASLS ALEGNCVQTA LGVCMSNKDL
     THLCHFIKGK IVNDSVRLDE LPANQHVVTV NSVFDLAWAL RRHSTLTGQF QAIRAAYDVL
     HVPDKVPAML RHWMDETSFS DEHVVTQFIT PGGVVILESC GGARIWALGN NVIRAGGVTA
     IPTGGCVRLM GLSAQTMPWS EILSELFSLL GKIWSSVKVS TLILTALSMY ASRFRPKTEA
     KGKTKSKIGP YRGRGVALTD DEYDEWKEHN AARKLDLSVE DFLMLRHRAA LGADDTDAVK
     FRSWWNSRSR LADDFEDVTV IGKGGVKHEK IRTNTLRAVD RGYDVSFAEE SGPGAKFHKN
     AIGSVTDVCG EHKGYCVHMG HGVYASVAHV VKGDSFFLGE RIFDLKTNGE FCCFRSTKIL
     PSAAPFFSGR PTRDPWGSPV ATDWKPKPYS TTSGKIVGCF ATTSTETHPG DCGLPYIDDN
     GRVTGLHTGS GGPKTPSAKL VVPYVHIDMK TKSVTAQKYD VTKPDISYKG LVCKQLDEIR
     IIPKGTRLHV SPAHLEDFEE CSHQPASLGS GDPRCPKSLT AIVVDSLKPY CVVVNGPPHD
     ILHRVQKMLI DHLSGFVPMN ISSDTSMLSA FHKLNHDTSC GPYLGGRKKD HMVNGEPDKA
     LLDLLSSKWK LATQGIALPH EYTIGLKDEL RPIEKVQEGK RRMIWGCDVG VATVCAAAFK
     GVSDAITANH QYGPIQVGIN MDSPSVEALF QRIKSARKVF AVDYSKWDST QSPRVSAASI
     DILRYFSDRT PIVDSATNTL KSPPIAVFNG VAVKVSSGLP SGMPLTSVIN SLNHCLYVGC
     AILQSLEARN VPVTWNLFST FDMMTYGDDG VYMFPTMYAS ISDQIFANLS AYGLKPTRVD
     KSVGSIEPID PNSVVFLKRT ITRTPQGIRG LLDRSSILRQ FYYIKGENTD NWKEPPKTID
     PMSRGQQLWN ACLYASQHGI DFYNKVYKLA EKAVEYEGLH LEPPSYSTAL EHYNSQFNGV
     EARTDQIDTS GMAALHCDVF EV