Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-73482-00916
Entry Name
UniProt Accession
Theoretical PI
6.27
Molecular Weight
258926.56
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
RNA-directed RNA polymerase 3D-POL
Protein Synonyms/Alias
Lpro; 3.4.22.46; VP4-VP2; P1A; Virion protein 4; P1B; Virion protein 2; P1C; Virion protein 3; P1D; Virion protein 1; P2A; P52; P2B; P2C; 3.6.1.15; P3A; P3B-1; Genome-linked protein VPg1; P3B-2; Genome-linked protein VPg2; P3B-3; Genome-linked protein VPg3; 3.4.22.28; Protease 3C; P3C; Protease P20B; P3D-POL; 2.7.7.48; P56A;
Gene Name
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
202
Canonical
KVQRKLKGAGQSSPA
[1]
N-Myristoylation
Organism
Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/196 serotype O) (FMDV)
NCBI Taxa ID
73482
Reference
[1] Belsham GJ, Abrams CC, King AM, Roosien J, Vlak JM. Myristoylation offoot-and-mouth disease virus capsid protein precursors is independent of otherviral proteins and occurs in both mammalian and insect cells. J Gen Virol. 1991Mar;72 ( Pt 3):747-51.[PMID:1848606]
Functional Description
The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.Protein VP0: VP0 precursor is a component of immature procapsids.
Sequence Annotation
Topological domain: 1 1480 Cytoplasmic.
Topological domain: 1502 2332 Cytoplasmic.
Domain: 1 201 Peptidase C28.
Domain: 1189 1353 SF3 helicase.
Domain: 1652 1836 Peptidase C3.
Domain: 2096 2214 RdRp catalytic.
Nucleotide-binding: 1217 1224 ATP.
Motif: 869 871 Cell attachment site.
Active site: 51 51 For leader protease activity.
Active site: 148 148 For leader protease activity.
Active site: 163 163 For leader protease activity.
Active site: 1695 1695 For picornain 3C activity.
Active site: 1722 1722 For picornain 3C activity.
Active site: 1812 1812 For picornain 3C activity.
Functional site: 201 202 Cleavage; by leader protease.
Functional site: 286 287 Cleavage.
Functional site: 504 505 Cleavage; by picornain 3C.
Functional site: 724 725 Cleavage; by picornain 3C.
Functional site: 935 936 Cleavage; by picornain 3C.
Functional site: 953 954 Cleavage; by ribosomal skip.
Functional site: 1107 1108 Cleavage; by picornain 3C.
Functional site: 1425 1426 Cleavage; by picornain 3C.
Functional site: 1578 1579 Cleavage; by picornain 3C.
Functional site: 1601 1602 Cleavage; by picornain 3C.
Functional site: 1625 1626 Cleavage; by picornain 3C.
Functional site: 1649 1650 Cleavage; by picornain 3C.
Functional site: 1862 1863 Cleavage; by picornain 3C.
Modified residue: 1581 1581 O-(5'-phospho-RNA)-tyrosine.
Modified residue: 1604 1604 O-(5'-phospho-RNA)-tyrosine.
Modified residue: 1628 1628 O-(5'-phospho-RNA)-tyrosine.
Protein Length
2332 AA.
Protein Sequence
(Canonical)
MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN CWLNAILQLF  60
RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP ALVIWNIKHL LHTGIGTASR  120
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF  180
VPYDQEPLNG EWKAKVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG  240
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI  300
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT HLFDWVTSDS  360
FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN QFNGGCLLVA MVPELYSIQK  420
RELYQLTLFP HQFINPRTNM TAHITVPFVG VNRYDQYKVH KPWTLVVMVV APLTVNTEGA  480
PQIKVYANIA PTNVHVAGEF PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ  540
LPGRFTNLLD VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ  600
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE WDTGLNSKFT  660
FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG DALVVLASAG KDFELRLPVD  720
ARAETTSAGE SADPVTTTVE NYGGETQIQR RQHTDVSFIM DRFVKVTPQN QINILDLMQI  780
PSHTLVGALL RASTYYFSDL EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA  840
LPYTAPHRVL ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL  900
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES NPGPFFFSDV  960
RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV KAIRTGLDEA KPWYKLIKLL  1020
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP  1080
VLLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW  1140
IASEEKFVTM TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA  1200
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP DPDHFDGYNQ  1260
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT  1320
PRTMVCPDAL NRRFHFDIDV SAKDGYKINS KLDIIKALED THANPVAMFQ YDCALLNGMA  1380
VEMKRMQQDM FKPQPPLQNV YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE  1440
KGQHEAAIEF FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM  1500
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR ERTLPGQKAC  1560
DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ EGPYAGPMER QKPLKVKAKA  1620
PVVKEGPYEG PVKKPVALKV KAKNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC  1680
CATGVFGTAY LVPRHLFAEK YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH  1740
RGNRVRDITK HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL  1800
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK MKAHIDPEPH  1860
HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA LSNKDPRLNE GVVLDEVIFS  1920
KHKGDTKMSE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG  1980
LPWALQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT  2040
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD  2100
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK RITVGGGMPS  2160
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK  2220
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG  2280
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA          2332
FASTA
(Canonical)
>LipidDB-73482-00916|P03305
MNTTDCFIALVQAIREIKALFLSRTTGKMELTLYNGEKKTFYSRPNNHDNCWLNAILQLF
RYVEEPFFDWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIKHLLHTGIGTASR
PSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVF
VPYDQEPLNGEWKAKVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLG
DNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRI
LTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVVQAERFFKTHLFDWVTSDS
FGRCHLLELPTDHKGVYGSLTDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELYSIQK
RELYQLTLFPHQFINPRTNMTAHITVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNTEGA
PQIKVYANIAPTNVHVAGEFPSKEGIFPVACSDGYGGLVTTDPKTADPVYGKVFNPPRNQ
LPGRFTNLLDVAEACPTFLRFEGGVPYVTTKTDSDRVLAQFDMSLAAKQMSNTFLAGLAQ
YYTQYSGTINLHFMFTGPTDAKARYMVAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFT
FSIPYLSAADYAYTASGVAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFELRLPVD
ARAETTSAGESADPVTTTVENYGGETQIQRRQHTDVSFIMDRFVKVTPQNQINILDLMQI
PSHTLVGALLRASTYYFSDLEIAVKHEGDLTWVPNGAPEKALDNTTNPTAYHKAPLTRLA
LPYTAPHRVLATVYNGECRYNRNAVPNLRGDLQVLAQKVARTLPTSFNYGAIKATRVTEL
LYRMKRAETYCPRPLLAIHPTEARHKQKIVAPVKQTLNFDLLKLAGDVESNPGPFFFSDV
RSNFSKLVETINQMQEDMSTKHGPDFNRLVSAFEELAIGVKAIRTGLDEAKPWYKLIKLL
SRLSCMAAVAARSKDPVLVAIMLADTGLEILDSTFVVKKISDSLSSLFHVPAPVFSFGAP
VLLAGLVKVASSFFRSTPEDLERAEKQLKARDINDIFAILKNGEWLVKLILAIRDWIKAW
IASEEKFVTMTDLVPGILEKQRDLNDPSKYKEAKEWLDNARQACLKSGNVHIANLCKVVA
PAPSKSRPEPVVVCLRGKSGQGKSFLANVLAQAISTHFTGRIDSVWYCPPDPDHFDGYNQ
QTVVVMDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFT
PRTMVCPDALNRRFHFDIDVSAKDGYKINSKLDIIKALEDTHANPVAMFQYDCALLNGMA
VEMKRMQQDMFKPQPPLQNVYQLVQEVIDRVELHEKVSSHPIFKQISIPSQKSVLYFLIE
KGQHEAAIEFFEGMVHDSIKEELRPLIQQTSFVKRAFKRLKENFEIVALCLTLLANIVIM
IRETRKRQKMVDDAVNEYIEKANITTDDKTLDEAEKSPLETSGASTVGFRERTLPGQKAC
DDVNSEPAQPVEEQPQAEGPYAGPLERQKPLKVRAKLPQQEGPYAGPMERQKPLKVKAKA
PVVKEGPYEGPVKKPVALKVKAKNLIVTESGAPPTDLQKMVMGNTKPVELILDGKTVAIC
CATGVFGTAYLVPRHLFAEKYDKIMVDGRAMTDSDYRVFEFEIKVKGQDMLSDAALMVLH
RGNRVRDITKHFRDTARMKKGTPVVGVINNADVGRLIFSGEALTYKDIVVCMDGDTMPGL
FAYRAATKAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLLKMKAHIDPEPH
HEGLIVDTRDVEERVHVMRKTKLAPTVAHGVFNPEFGPAALSNKDPRLNEGVVLDEVIFS
KHKGDTKMSEEDKALFRRCAADYASRLHSVLGTANAPLSIYEAIKGVDGLDAMEPDTAPG
LPWALQGKRRGALIDFENGTVGPEVEAALKLMEKREYKFVCQTFLKDEIRPLEKVRAGKT
RIVDVLPVEHILYTRMMIGRFCAQMHSNNGPQIGSAVGCNPDVDWQRFGTHFAQYRNVWD
VDYSAFDANHCSDAMNIMFEEVFRTEFGFHPNAEWILKTLVNTEHAYENKRITVGGGMPS
GCSATSIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEALKPHFK
SLGQTITPADKSDKGFVLGHSITDVTFLKRHFHMDYGTGFYKPVMASKTLEAILSFARRG
TIQEKLISVAGLAVHSGPDEYRRLFEPFQGLFEIPSYRSLYLRWVNAVCGDA
Gene Ontology
GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-KW
GO:0019030; C:icosahedral viral capsid; IEA:InterPro
GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro
GO:0005216; F:ion channel activity; IEA:UniProtKB-KW
GO:0003723; F:RNA binding; IEA:UniProtKB-KW
GO:0003724; F:RNA helicase activity; IEA:InterPro
GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW
GO:0005198; F:structural molecule activity; IEA:InterPro
GO:0075512; P:clathrin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW
GO:0039520; P:induction by virus of host autophagy; IDA:UniProtKB
GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW
GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW
GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW
GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW
GO:0039544; P:suppression by virus of host RIG-I activity by RIG-I proteolysis; ISS:UniProtKB
GO:0039611; P:suppression by virus of host translation initiation factor activity; IDA:UniProtKB
GO:0006351; P:transcription, DNA-templated; IEA:InterPro
GO:0019082; P:viral protein processing; IEA:InterPro
GO:0039694; P:viral RNA genome replication; IEA:InterPro
GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR015031; Capsid_VP4_Picornavir
InterPro; IPR004080; FMDV_VP1_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; IPR008739; Peptidase_C28
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir
InterPro; IPR001676; Picornavirus_capsid
InterPro; IPR001205; RNA-dir_pol_C
InterPro; IPR007094; RNA-dir_pol_PSvirus
InterPro; IPR009003; Trypsin-like_Pept_dom
InterPro; IPR029053; Viral_coat
Pfam
Pfam; PF05408; Peptidase_C28;
Pfam; PF00548; Peptidase_C3;
Pfam; PF00680; RdRP_1;
Pfam; PF00073; Rhv;
Pfam; PF00910; RNA_helicase;
Pfam; PF08935; VP4_2;
SMART
PROSITE
PROSITE; PS50507; RDRP_SSRNA_POS;
PROSITE; PS51218; SF3_HELICASE_2;
PRINTS
PRINTS; PR00918; CALICVIRUSNS;
PRINTS; PR01542; FMDVP1COAT;