POLG_BECNB
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 03-AUG-2022, entry version 88.
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.
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}.
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DR EMBL; AY082891; AAL99277.1; -; Genomic_RNA.
DR RefSeq; NP_663315.1; NC_004064.1.
DR SMR; Q8JN60; -.
DR PRIDE; 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: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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00915; Calici_coat; 1.
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 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 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
