Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-12112-00919
Entry Name
UniProt Accession
Theoretical PI
6.27
Molecular Weight
259319.25
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
QVQKKLKGAGQSSPA
[1]
N-Myristoylation
Organism
Foot-and-mouth disease virus (strain A10-61) (Aphthovirus A) (FMDV)
NCBI Taxa ID
12112
Reference
[1] Maurer-Stroh S, Eisenhaber B, Eisenhaber F. N-terminal N-myristoylation ofproteins: prediction of substrate proteins from amino acid sequence. J Mol Biol. 2002 Apr 5;317(4):541-57.[PMID:11955008]
Functional Description
The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription (By similarity).
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: 868 870 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: 725 726 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)
MNTTNCFIAL VYLIREIKTL FRSRTKGKME FTLHNGEKKT FYSRPNNHDN CWLNTILQLF  60
RYVDEPFFDW VYNSPENLTL DAIKQLENFT GLELHEGGPP ALVIWNIKHL LQTGIGTASR  120
PSEVCMVDGT DMCLADFHAG IFMKGQEHAV FACVTSDGWY AIDDEDFYPW TPDPSDVLVF  180
VPYDQEPLNG DWKTQVQKKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMSTQLG  240
DNTISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI  300
LTTRNGHTTS TTQSSVGVTY GYSTEEDHVA GPNTSGLETR VVQAERFFKK FLFDWTTDKP  360
FGYLTKLELP TDHHGVFGHL VDSYAYMRNG WDVEVSAVGN QFNGGCLLVA MVPEWKAFDT  420
REKYQLTLFP HQFISPRTNM TAHITVPYLG VNRYDQYKKH KPWTLVVMVL SPLTVSNTAA  480
PQIKVYANIA PTYVHVAGEL PSKEGIFPVA CADGYGGLVT TDPKTADPVY GKVYNPPKTN  540
YPGRFTNLLD VAEACPTFLR FDDGKPYVVT RADDTRLLAK FDVSLAAKHM SNTYLSGIAQ  600
YYTQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVETPPDT PEEAAHCIHA EWDTGLNSKF  660
TFSIPYVSAA DYAYTASDTA ETTNVQGWVC VYQITHGKAE NDTLLVSASA GKDFELRLPI  720
DPRTQTTTTG ESADPVTTTV ENYGGDTQVQ RRHHTDVGFI MDRFVKINSL SPTHVIDLMQ  780
THKHGIVGAL LRAATYYFSD LEIVVRHDGN LTWVPNGAPE AALSNTSNPT AYNKAPFTRL  840
ALPYTAPHRV LATVYDGTNK YSASDSRSGD LGSIAARVAT QLPASFNYGA IQAQAIHELL  900
VRMKRAELYC PRPLLAIKVT SQDRYKQKII APAKQLLNFD LLKLAGDVES NLGPFFFADV  960
RSNFSKLVDT INQMQEDMST KHGPDFNRLV SAFEELATGV KAIRTGLDEA KPWYKLIKLL  1020
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKS SDSLSSLFHV PAPAFSFGAP  1080
VLLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW  1140
IASEEKFVTM TDLVPGILEK QRDLNDPGKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA  1200
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP DPDHFDGYNQ  1260
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT  1320
PRTMVCPDAL NRRFHFDIDV SAKDGYKINN KLDIIKALED THTNPVAMFQ YDCALLNGMA  1380
VEMKRLQQDM FKPQPPLQNV YQLVQEVIER VELHEKVSSH PIFKQISIPS QKSVLYFLIE  1440
KGQHEAAIEF FEGMVHDSVK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM  1500
IRETRKRQKM VDDAVNEYIE RANITTDDKT LDEAEKNPLE TSGASTVGFR ERSLTGQKVR  1560
DDVSSEPAQP AEDQPQAEGP YSGPLERQKP LKVRAKLPQQ EGPYAGPMER QKPLKVKVKA  1620
PVVKEGPYEG PVKKPVALKV KARNLIVTES GAPPTDLQKM VMGNTKPVEL NLDGKTVAIC  1680
CATGVFGTAY LVPRHLFAEK YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALIVLH  1740
RGNCVRDITK HFRDTARMKK GTPVVGVVNN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL  1800
FAYKAATRAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLQK MKAHVDPEPH  1860
HEGLIVDTRD VEERVHVMRK TKLAPTVAYG VFNPEFGPAA LSNKDPRLNE GVVLDDVIFS  1920
KHKGDAKMTE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG  1980
LPWALQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFA CQTFLKDEIR PMEKVRAGKT  2040
RIVDVLPVEH ILYTKMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD  2100
VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK RITVEGGMPS  2160
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK  2220
SLGQTITPAD KSDKGFVLGQ SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG  2280
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA          2332
FASTA
(Canonical)
>LipidDB-12112-00919|P03306
MNTTNCFIALVYLIREIKTLFRSRTKGKMEFTLHNGEKKTFYSRPNNHDNCWLNTILQLF
RYVDEPFFDWVYNSPENLTLDAIKQLENFTGLELHEGGPPALVIWNIKHLLQTGIGTASR
PSEVCMVDGTDMCLADFHAGIFMKGQEHAVFACVTSDGWYAIDDEDFYPWTPDPSDVLVF
VPYDQEPLNGDWKTQVQKKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMSTQLG
DNTISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFTGLFGALLADKKTEETTLLEDRI
LTTRNGHTTSTTQSSVGVTYGYSTEEDHVAGPNTSGLETRVVQAERFFKKFLFDWTTDKP
FGYLTKLELPTDHHGVFGHLVDSYAYMRNGWDVEVSAVGNQFNGGCLLVAMVPEWKAFDT
REKYQLTLFPHQFISPRTNMTAHITVPYLGVNRYDQYKKHKPWTLVVMVLSPLTVSNTAA
PQIKVYANIAPTYVHVAGELPSKEGIFPVACADGYGGLVTTDPKTADPVYGKVYNPPKTN
YPGRFTNLLDVAEACPTFLRFDDGKPYVVTRADDTRLLAKFDVSLAAKHMSNTYLSGIAQ
YYTQYSGTINLHFMFTGSTDSKARYMVAYIPPGVETPPDTPEEAAHCIHAEWDTGLNSKF
TFSIPYVSAADYAYTASDTAETTNVQGWVCVYQITHGKAENDTLLVSASAGKDFELRLPI
DPRTQTTTTGESADPVTTTVENYGGDTQVQRRHHTDVGFIMDRFVKINSLSPTHVIDLMQ
THKHGIVGALLRAATYYFSDLEIVVRHDGNLTWVPNGAPEAALSNTSNPTAYNKAPFTRL
ALPYTAPHRVLATVYDGTNKYSASDSRSGDLGSIAARVATQLPASFNYGAIQAQAIHELL
VRMKRAELYCPRPLLAIKVTSQDRYKQKIIAPAKQLLNFDLLKLAGDVESNLGPFFFADV
RSNFSKLVDTINQMQEDMSTKHGPDFNRLVSAFEELATGVKAIRTGLDEAKPWYKLIKLL
SRLSCMAAVAARSKDPVLVAIMLADTGLEILDSTFVVKKSSDSLSSLFHVPAPAFSFGAP
VLLAGLVKVASSFFRSTPEDLERAEKQLKARDINDIFAILKNGEWLVKLILAIRDWIKAW
IASEEKFVTMTDLVPGILEKQRDLNDPGKYKEAKEWLDNARQACLKSGNVHIANLCKVVA
PAPSKSRPEPVVVCLRGKSGQGKSFLANVLAQAISTHFTGRIDSVWYCPPDPDHFDGYNQ
QTVVVMDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFT
PRTMVCPDALNRRFHFDIDVSAKDGYKINNKLDIIKALEDTHTNPVAMFQYDCALLNGMA
VEMKRLQQDMFKPQPPLQNVYQLVQEVIERVELHEKVSSHPIFKQISIPSQKSVLYFLIE
KGQHEAAIEFFEGMVHDSVKEELRPLIQQTSFVKRAFKRLKENFEIVALCLTLLANIVIM
IRETRKRQKMVDDAVNEYIERANITTDDKTLDEAEKNPLETSGASTVGFRERSLTGQKVR
DDVSSEPAQPAEDQPQAEGPYSGPLERQKPLKVRAKLPQQEGPYAGPMERQKPLKVKVKA
PVVKEGPYEGPVKKPVALKVKARNLIVTESGAPPTDLQKMVMGNTKPVELNLDGKTVAIC
CATGVFGTAYLVPRHLFAEKYDKIMLDGRAMTDSDYRVFEFEIKVKGQDMLSDAALIVLH
RGNCVRDITKHFRDTARMKKGTPVVGVVNNADVGRLIFSGEALTYKDIVVCMDGDTMPGL
FAYKAATRAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLQKMKAHVDPEPH
HEGLIVDTRDVEERVHVMRKTKLAPTVAYGVFNPEFGPAALSNKDPRLNEGVVLDDVIFS
KHKGDAKMTEEDKALFRRCAADYASRLHSVLGTANAPLSIYEAIKGVDGLDAMEPDTAPG
LPWALQGKRRGALIDFENGTVGPEVEAALKLMEKREYKFACQTFLKDEIRPMEKVRAGKT
RIVDVLPVEHILYTKMMIGRFCAQMHSNNGPQIGSAVGCNPDVDWQRFGTHFAQYRNVWD
VDYSAFDANHCSDAMNIMFEEVFRTDFGFHPNAEWILKTLVNTEHAYENKRITVEGGMPS
GCSATSIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEALKPHFK
SLGQTITPADKSDKGFVLGQSITDVTFLKRHFHMDYGTGFYKPVMASKTLEAILSFARRG
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; ISS: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; ISS: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;