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Genome polyprotein [Cleaved into: Protein p34; NTPase (EC 3.6.1.15) (p37); Protein p30; Viral genome-linked protein (VPg) (p8); 3C-like protease (3CLpro) (EC 3.4.22.66) (p20); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (p53); Capsid protein (VP1)]

 POLG_BECN1              Reviewed;        2210 AA.
Q288N7;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 1.
23-MAY-2018, entry version 68.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein p34;
Contains:
RecName: Full=NTPase;
EC=3.6.1.15;
AltName: Full=p37;
Contains:
RecName: Full=Protein p30;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
AltName: Full=p8;
Contains:
RecName: Full=3C-like protease;
Short=3CLpro;
EC=3.4.22.66;
AltName: Full=p20;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=p53;
Contains:
RecName: Full=Capsid protein;
AltName: Full=VP1;
ORFNames=ORF1;
Bovine enteric calicivirus Newbury agent-1 (isolate
Bovine/UK/Newbury1/1976) (BEC).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Nebovirus.
NCBI_TaxID=331642;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16574184; DOI=10.1016/j.virol.2006.02.027;
Oliver S.L., Asobayire E., Dastjerdi A.M., Bridger J.C.;
"Genomic characterization of the unclassified bovine enteric virus
Newbury agent-1 (Newbury1) endorses a new genus in the family
Caliciviridae.";
Virology 350:240-250(2006).
-!- FUNCTION: NTPase presumably plays a role in replication.
{ECO:0000250}.
-!- FUNCTION: Viral genome-linked protein is covalently linked to the
5'-end of the positive-strand, negative-strand genomic RNAs and
subgenomic RNA. Acts as a genome-linked replication primer. May
recruit ribosome to viral RNA thereby promoting viral proteins
translation (By similarity). {ECO:0000250}.
-!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp
is first released by autocleavage, then all other proteins are
cleaved. {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
antigenomic RNA by recognizing replications specific signals.
Transcribes also a subgenomic mRNA by initiating RNA synthesis
internally on antigenomic RNA. This sgRNA codes for structural
proteins. Catalyzes the covalent attachment VPg with viral RNAs
(By similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- FUNCTION: Capsid protein self-assembles to form an icosahedral
capsid with a T=3 symmetry, about 35 nm in diameter, and
consisting of 180 capsid proteins. A smaller form of capsid with a
diameter of 23 nm might be capsid proteins assembled as
icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins
and genomic or subgenomic RNA. Attaches virion to target cells
inducing endocytosis of the viral particle. Acidification of the
endosome induces conformational change of capsid protein thereby
injecting virus genomic RNA into host cytoplasm (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Endopeptidase with a preference for cleavage
when the P1 position is occupied by Glu-|-Xaa and the P1' position
is occupied by Gly-|-Yaa.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion. Host cytoplasm
{ECO:0000250}.
-!- PTM: Specific enzymatic cleavages by its own cysteine protease
yield mature proteins. The protease cleaves itself from the
nascent polyprotein autocatalytically (By similarity).
{ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
attached to the 5'-end of the polyadenylated genomic and
subgenomic RNAs. This uridylylated form acts as a nucleotide-
peptide primer for the polymerase (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; DQ013304; AAY60849.1; -; Genomic_RNA.
RefSeq; YP_529550.1; NC_007916.1.
SMR; Q288N7; -.
PRIDE; Q288N7; -.
GeneID; 5130542; -.
KEGG; vg:5130542; -.
OrthoDB; VOG0900006M; -.
Proteomes; UP000000668; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
CDD; cd00205; rhv_like; 1.
Gene3D; 2.60.120.20; -; 1.
InterPro; IPR004005; Calicivirus_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000317; Peptidase_C24.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
Pfam; PF00915; Calici_coat; 1.
Pfam; PF03510; Peptidase_C24; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00916; 2CENDOPTASE.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
ATP-binding; Capsid protein; Complete proteome;
Covalent protein-RNA linkage; Helicase; Host cytoplasm; Hydrolase;
Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
Reference proteome; RNA-directed RNA polymerase; Thiol protease;
Transferase; Viral RNA replication; Virion.
CHAIN 1 2210 Genome polyprotein.
/FTId=PRO_0000402448.
CHAIN 1 302 Protein p34. {ECO:0000250}.
/FTId=PRO_0000402449.
CHAIN 303 645 NTPase. {ECO:0000250}.
/FTId=PRO_0000402450.
CHAIN 646 925 Protein p30. {ECO:0000250}.
/FTId=PRO_0000402451.
CHAIN 926 990 Viral genome-linked protein.
{ECO:0000250}.
/FTId=PRO_0000402452.
CHAIN 991 1174 3C-like protease. {ECO:0000250}.
/FTId=PRO_0000402453.
CHAIN 1175 1659 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000402454.
CHAIN 1660 2210 Capsid protein. {ECO:0000250}.
/FTId=PRO_0000402455.
DOMAIN 426 585 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1010 1109 Peptidase C24.
DOMAIN 1379 1501 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 456 463 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
COMPBIAS 971 974 Poly-Asp.
COMPBIAS 1686 1692 Poly-Ala.
ACT_SITE 1025 1025 For 3CLpro activity. {ECO:0000250}.
ACT_SITE 1103 1103 For 3CLpro activity. {ECO:0000255}.
SITE 302 303 Cleavage; by 3CLpro. {ECO:0000255}.
SITE 645 646 Cleavage; by 3CLpro. {ECO:0000255}.
SITE 925 926 Cleavage; by 3CLpro. {ECO:0000255}.
SITE 990 991 Cleavage; by 3CLpro. {ECO:0000255}.
SITE 1174 1175 Cleavage; by 3CLpro. {ECO:0000255}.
SITE 1659 1660 Cleavage; by 3CLpro. {ECO:0000255}.
MOD_RES 940 940 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
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


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