POLG_BECN1
ID POLG_BECN1 Reviewed; 2210 AA.
AC Q288N7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Newbury agent-1 (isolate
OS Bovine/UK/Newbury1/1976) (BEC).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Nebovirus.
OX NCBI_TaxID=331642;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16574184; DOI=10.1016/j.virol.2006.02.027;
RA Oliver S.L., Asobayire E., Dastjerdi A.M., Bridger J.C.;
RT "Genomic characterization of the unclassified bovine enteric virus Newbury
RT agent-1 (Newbury1) endorses a new genus in the family Caliciviridae.";
RL Virology 350:240-250(2006).
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; DQ013304; AAY60849.1; -; Genomic_RNA.
DR RefSeq; YP_529550.1; NC_007916.1.
DR SMR; Q288N7; -.
DR GeneID; 5130542; -.
DR KEGG; vg:5130542; -.
DR Proteomes; UP000000668; 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; Reference proteome; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2210
FT /note="Genome polyprotein"
FT /id="PRO_0000402448"
FT CHAIN 1..302
FT /note="Protein p34"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402449"
FT CHAIN 303..645
FT /note="NTPase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402450"
FT CHAIN 646..925
FT /note="Protein p30"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402451"
FT CHAIN 926..990
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402452"
FT CHAIN 991..1174
FT /note="3C-like protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402453"
FT CHAIN 1175..1659
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402454"
FT CHAIN 1660..2210
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402455"
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..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..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; 239021 MW; F05AF2411FE610DE CRC64;
MAPVVSRDRH RHKIPKPHQP APPHRCTVWC PEDCGWYVGR CSCPKSCQRE GWDDFFVADK
VKPPSYVASK TSVADVVDWL LEEDPATDGP SEFDLTQFFQ AYTDKSHQIH RDYAPDQLAQ
ALDMAYILSV DPPDIKLPEY EATRFTHDTS YKGKLPRWLR VYGFKSRELA KKAITNIKGG
AHWAKGLFKQ AWDTLPGWSE VEAYFKAFFA GIITGVEDAL SKSPSSVWTS LKLTPLLYIW
RNINECSDIP VILGAFWATL ELYNIPSKVY DLVSTALGPM VQDLARRVIN IIKGDGNGPK
QEGGRPSFSI PGVLLATFLS AIILGSMPSD GIIKKVLRGC ATAAGLVGGF NAVKSIITTV
QGASACKDVK KLASQLMCVT TMAATVSTRG ERQVLASMLN DLNESVRERL VDPAFAALVP
QLSAMSSKIM ELSTINAAAL SAARKRVPAK IVVLCGPPGH GKSVAAHKLA KMLNPNEPSI
WNPFSDHHDE YTAEDVVIID ETPAEPGQWV EDLIAMGSNS PFVPNYDRVE NKTRCFDSKY
VLITTNHNPL INPTHSRAAA LARRLTWVYV NSPDVADFLR QHPGVAPPAT LFKADCSHLN
FDIHPYNSIG TTAVVGHNGT TPLPRAKRTS LEGLCKHIKD LPDREGPPDG VPERMVLVAP
DKGTARFVEA VINTYHNSGL VAQPAAWDTT PQKYQLAVTW QGSTSSVVGQ RWDCNPQTPF
VAPHFTRNMF KRVLGTEVPE YHLLAYACRI TSSSLGDKSL PVPNPTVVIN DPSPTRLALA
LMRHLKNPIA SGLRVVWDLF RGCATGPKRL FTWALSQEWN PMPVTTAFTF PAGTVILHTA
GGVRVVVLPP GPQFGLTEVT HLADHSGQDD PVVPDMFGQT WTELLWRLLK VIGTFLANYG
VAIAGLTLSI AAFKTANKST RNDRQGWLSG SGVALSDEEY DEWMKYSKKK GKKINADEFL
QLRHRAAMGN DDDDARDYRS FYTAYQLGRE GNNCEDLPLH PAVGPTTGGG YYVHIGNGVG
ITLKHVASGE DVIKELGNDL VKIRARHHKM GDPAMVVGEG APVKFVTGHL VVDARNESVV
FDQTRLSVVR VKVPGLETQR GYCGLPYVNS AGHVVGLHQG SYGVGDKVFT PITDAPAASP
DTIMWRGLEC TRSDIVTHLP HGTKYSISPG MREEAHKCTH QPASLGRNDP RCNQTQVAMV
VKALTPYTSA PAIEKLDPCM VAAITEVRTA IQSLTPKGGF RPLTFAAAWQ SLDLSTSAGA
LAPGKTKRDL CDPDTGMPAG KYREMLLAAW SRAGTGTPLD HTYIVALKDE LRPVEKVAEG
KRRLIWGADA RVALIASAAL TPVANALKTV TNLLPIQVGV DPSSANCVSS WVGRLQRHDH
CLELDYSKWD STMSPVIINI AIDILCNTCG SDSLRMAVAQ TLKSRPTALV EGVSVPTKSG
LPSGMPFTSQ INSIVHWILW SATVRKCSLP LHIGSVNELA PFLTYGDDGL YTIPSHLTKS
IDEIISTLKG YGLSPTAPDK GANVEIKRTS FTYLSGPVFL KRRIVLTPGG HRALLDLTSL
ARQPVWVNGP RRSVWNHEAQ PIEIDAETRT IQLQNVLIEL AWHQPQDFDH VLALVVKSAE
ASGLTIPRYS QEEARAIYDG RYYGIQHVSL PNNSDLIREG NMSDNKSTPE QQHESSRAMD
AGATGAAAAA PAPPVAAAPA SGLVGALVAE PQSGPSAEQW RTAYTLFGTV SWNANAGPGT
ILTVGRLGPG MNPYTQHIAA MYGGWAGGMD IRITIAGSGF IGGTLAVAAI PPGVDPESVN
VLRMPHVLID ARGGVPLEVT LEDIRTSLYH PMGDTNTASL VIAVMTGLIN PLGTDTLSVT
VQLETRPGRD WVFFSLLPPT AGVASADPSQ LLTRVALATS PEVRFGTGVL GILGLPSNPS
VNRVYDVQSR TRGWSFPIPS SSVFMGDARN VEHNRRVMVQ SSAPNNPLSD VFPDGFPDFV
PQSDTEPDGG AVIAGQVLPH PGDNDNFWRL TPVVRGNTTA AINTIPERFN QVYFINLADE
EAVSAATEEL RFNGIQGIFG QRTNARAVQV MQGYVPRAEH IIRPAGFAGV GPQGPNVPIG
FAGTMPNFNA TASGADDLVP VWGPTLVHTA SLLAGTTYEL AENSMYVFSV STSTSTFELG
MLANGTWLGP AQLAGTGITW TEVLSVTYMG MRFAYNPLSG QGIGGESRRL
