ID   POLG_BECNB              Reviewed;        2210 AA.
AC   Q8JN60;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Protein p34;
DE   Contains:
DE     RecName: Full=NTPase;
DE              EC=3.6.1.15;
DE     AltName: Full=p37;
DE   Contains:
DE     RecName: Full=Protein p30;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE     AltName: Full=p8;
DE   Contains:
DE     RecName: Full=3C-like protease;
DE              Short=3CLpro;
DE              EC=3.4.22.66;
DE     AltName: Full=p20;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              Short=RdRp;
DE              EC=2.7.7.48;
DE     AltName: Full=p53;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE     AltName: Full=VP1;
GN   ORFNames=ORF1;
OS   Bovine enteric calicivirus NB (isolate Bovine/United States/N ebraska/1980)
OS   (BEC-NB).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Nebovirus; Newbury 1 virus.
OX   NCBI_TaxID=2847999;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12239283; DOI=10.1128/jvi.76.20.10089-10098.2002;
RA   Smiley J.R., Chang K.O., Hayes J., Vinje J., Saif L.J.;
RT   "Characterization of an enteropathogenic bovine calicivirus representing a
RT   potentially new calicivirus genus.";
RL   J. Virol. 76:10089-10098(2002).
CC   -!- FUNCTION: NTPase presumably plays a role in replication. {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: 3C-like protease processes the polyprotein: 3CLpro-RdRp is
CC       first released by autocleavage, then all other proteins are cleaved.
CC       {ECO:0000250}.
CC   -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
CC       antigenomic RNA by recognizing replications specific signals.
CC       Transcribes also a subgenomic mRNA by initiating RNA synthesis
CC       internally on antigenomic RNA. This sgRNA codes for structural
CC       proteins. Catalyzes the covalent attachment VPg with viral RNAs (By
CC       similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC   -!- FUNCTION: Capsid protein self assembles to form an icosahedral capsid
CC       with a T=3 symmetry, about 35 nm in diameter, and consisting of 180
CC       capsid proteins. A smaller form of capsid with a diameter of 23 nm
CC       might be capsid proteins assembled as icosahedron with T=1 symmetry.
CC       The capsid encapsulate VP2 proteins and genomic or subgenomic RNA.
CC       Attaches virion to target cells inducing endocytosis of the viral
CC       particle. Acidification of the endosome induces conformational change
CC       of capsid protein thereby injecting virus genomic RNA into host
CC       cytoplasm (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   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion. Host cytoplasm
CC       {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages by its own cysteine protease yield
CC       mature proteins. The protease cleaves itself from the nascent
CC       polyprotein autocatalytically (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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY082891; AAL99277.1; -; Genomic_RNA.
DR   RefSeq; NP_663315.1; NC_004064.1.
DR   SMR; Q8JN60; -.
DR   GeneID; 951161; -.
DR   KEGG; vg:951161; -.
DR   Proteomes; UP000008174; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
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:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
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-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23192; Caliciviridae_RdRp; 1.
DR   Gene3D; 1.10.260.110; -; 1.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 6.10.140.320; -; 1.
DR   Gene3D; 6.10.250.3230; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR004005; Calicivirus_coat.
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   InterPro; IPR029053; Viral_coat.
DR   InterPro; IPR049434; VPg.
DR   Pfam; PF00915; Calici_coat; 1.
DR   Pfam; PF03510; Peptidase_C24; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   Pfam; PF20915; VPg; 1.
DR   PRINTS; PR00916; 2CENDOPTASE.
DR   PRINTS; PR00918; CALICVIRUSNS.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Capsid protein; Covalent protein-RNA linkage; Helicase;
KW   Host cytoplasm; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; RNA-directed RNA polymerase; Thiol protease;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..2210
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000341628"
FT   CHAIN           1..302
FT                   /note="Protein p34"
FT                   /id="PRO_0000341629"
FT   CHAIN           303..645
FT                   /note="NTPase"
FT                   /id="PRO_0000341630"
FT   CHAIN           646..925
FT                   /note="Protein p30"
FT                   /id="PRO_0000341631"
FT   CHAIN           926..990
FT                   /note="Viral genome-linked protein"
FT                   /id="PRO_0000341632"
FT   CHAIN           991..1174
FT                   /note="3C-like protease"
FT                   /id="PRO_0000341633"
FT   CHAIN           1175..1659
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000341634"
FT   CHAIN           1660..2210
FT                   /note="Capsid protein"
FT                   /id="PRO_0000341635"
FT   DOMAIN          426..585
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          991..1136
FT                   /note="Peptidase C24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   DOMAIN          1379..1501
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1656..1685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1656..1678
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1025
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   ACT_SITE        1039
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   ACT_SITE        1103
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   BINDING         456..463
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   SITE            302..303
FT                   /note="Cleavage; by 3CLpro"
FT                   /evidence="ECO:0000255"
FT   SITE            645..646
FT                   /note="Cleavage; by 3CLpro"
FT                   /evidence="ECO:0000255"
FT   SITE            925..926
FT                   /note="Cleavage; by 3CLpro"
FT                   /evidence="ECO:0000255"
FT   SITE            990..991
FT                   /note="Cleavage; by 3CLpro"
FT                   /evidence="ECO:0000255"
FT   SITE            1174..1175
FT                   /note="Cleavage; by 3CLpro"
FT                   /evidence="ECO:0000255"
FT   SITE            1659..1660
FT                   /note="Cleavage; by 3CLpro"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         940
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2210 AA;  238639 MW;  5D499C0C3188839E CRC64;
     MAPVVSRDQC KPKTPKPHRP APPHRCTTRC PEDCGWYVGR CSCPNVCQRE GWDDFFVADK
     VKPPSYVASK TSVADVVDWL LEEDPATDGP SEFDLTQFFQ AYTDKSHQIH RDYAPDQLAQ
     ALDMAYILSV DPPDIKLPEY EATRFTHDTS YKGKLPKWLR VYGIKSRELA KKAVTNIRGG
     AHWAKGLFKQ MWDSLPGWSE VEAYFKAFFA GIITGVEDAL SKSPSSVWTS LKLTPLLYIW
     RNINECSDIA VILGAFWATL ELYNIPSKVY DLVSTALGPM VQELARKVIN VVKGDGSGPK
     QEGGRPSFSI PGVLLATFLS AIILGSMPSD GLIKKILRGC ATAAGLVGGF NAVKSIITTV
     QGASACKDVK KLASQLMCVT TMAATVSTRG ERQVLASMLN DLNESVRERL VDPAYASLVP
     QLSAMSNKIV ELSTMNASAL SAARKRTPAK IIVLCGPPGH GKSVAAHKLA KMLNPNEPSI
     WNPFSDHHDE YTAEEVMVID ETPAEPGQWI EDLIAMGSNS PFVPNYDRVE NKTRCFDSKY
     VIITTNHNPL INPTHTRAAA LARRLTLVYV NSPDVADFLR QHPGVPPPAT LFKADCSHLH
     FDIHPYNSIG TTAIVGHNGT TPVPRAKRVS LEGLCKHVKE MPDREGPPDG VPERMVLVAP
     DKGTARFVEA VINTYHNSGL VAQPAAWDTT PQPYQLAVTW QGSNSTVTGQ RWDCNPQTPF
     VAPHFTRNMF KRVLGTEVPE YHLLAYACRI TSSSLGDKSL PVPNPTVVIN DPSPTRLALA
     LMRHLKNPIA SGLRVVWDLF RGCATGPKRL FTWALSQEWN PMPVTTAFTF PAGTVILHTA
     GGVRVVVLPP GPQFGLTEVA RLADHSGQDD PVVPDMFGAT WTELLWRLLK VIGTFLANYG
     VAIAGLTLSI AAFKTANKSA KNDRQGWLSG SGVALSDEEY DEWMKYSKKK GKKINADEFL
     QLRHRAAMGN DDDDARDYRS FYTAYQLGRE GNNCDDIPLH PAVGPTTGGG YYVHIGNGVG
     VTLKHVASGE DVIKELGNDL VKIRTKHHKV GDPAMVVGDG MPVKFVTGHL VVDTRSESVV
     FDQTRLNVIR VKVPGLETRR GYCGLPYVNS AGQVVGLHQG SYGVGDKVIT PITPEPTAPP
     DTIMWRGLEC ARSDIVTHLP HGTKYSVSPG MKEEATKCSH QPAPLGRNDP RCGQTQVAMV
     VKALSPYTGS PAVEKLDGCL VAAISEVRTA IQSLTPKGGF RPLTFAAAWQ SLDLSTSAGA
     LAPGKTKRDL CDPDTGMPTG KYKEELLRAW SRAGTGTALD HTYIVALKDE LRPVEKVAEG
     KRRLIWGADA RVALIASAAL SPIANALKTV TNLLPVQVGV DPSSASCVSA WVNRLNRHDH
     CLELDYSKWD STMSPVLINI AIDILCNTCA SDGLRVAVCQ TLKTRPTALV EGVAVPTKSG
     LPSGMPFTSQ INSIVHWILW SATVRKCSLP LNIGSVNELA PFLTYGDDGL YTIPSHLTKS
     IDEIVSTLKG YGLSPTAPDK GMNIEIKKTS FTYMSGPVFL KRRIVLTPGG HRALLDLTSL
     ARQPVWVNGP RRSVWDHEAQ PIEIDSEVRT IQLQNVLIES AWHQPQDFNQ VAALVYKSAE
     ASGITIPRYS LEEARAIYDG RFYGIQHVSM PCNSDLIREG NMSDNKSIPE QQHESSRAMD
     AGATGAAAAA PAPPVAAAPA SGLVGALVAE PQSGPSTEQW RTAYTLFGTV SWNANAGPGT
     ILTVGRLGPG MNPYTQHIAA MYGGWAGGMD IRITIAGSGF IGGTLAVAAI PPGVDPESVN
     VLRMPHVLID ARGGVPLEVT LEDIRTSLYH PMGDANTASL VIAVMTGLIN PLGTDTLSVT
     VQLETRPGRD WVFFSLLPPT AGVASADPSQ LLTRVALATS PEVRFGTGVL GILGLPSNPS
     VNRVYDVQSR TRGWSFPIPS SSVFMGDARN VEHTRRVMVQ SSAPNNPLSD VFPDGFPDFI
     PQSDTEPDGG AVIAGQVLPH PGDNDNFWRL TPVVRGNTTA AINTIPERFN QVYFINLADE
     EAVSAATEEL RFNGIQGIFG QRTTARAVQV MQGYVPRAEH IIRPAGFAGV GPQGPNVPIG
     FAGTMPNFNA TASGADDLVP VWGPTLVHTA SLLAGTTYEL AENSMYVFSV STSTSTFELG
     MLANGTWLGP AQLAGTGITW TEVLSVTYMG MRFAYNPLSG QGIGGESRRL
//