Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-12081-00913
Entry Name
UniProt Accession
Theoretical PI
6.72
Molecular Weight
246540.16
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
RNA-directed RNA polymerase
Protein Synonyms/Alias
VP4-VP2; P1A; Virion protein 4; P1B; Virion protein 2; P1C; Virion protein 3; P1D; Virion protein 1; P2A; 3.4.22.29; Picornain 2A; Protein 2A; P2B; P2C; 3.6.1.15; P3A; VPg; Protein 3B; P3B; 3.4.22.28; P3C; 3.4.22.28; RdRp; 2.7.7.48; 3D polymerase; 3Dpol; Protein 3D; 3D;
Gene Name
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGAQVSSQK
[1][2][3]
N-Myristoylation
Organism
Poliovirus type 1 (strain Mahoney)
NCBI Taxa ID
12081
Reference
[1] Paul AV, Schultz A, Pincus SE, Oroszlan S, Wimmer E. Capsid protein VP4 ofpoliovirus is N-myristoylated. Proc Natl Acad Sci U S A. 1987 Nov;84(22):7827-31.[PMID:2825164]
[2] He Y, Bowman VD, Mueller S, Bator CM, Bella J, Peng X, Baker TS, Wimmer E,Kuhn RJ, Rossmann MG. Interaction of the poliovirus receptor with poliovirus.Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):79-84.[PMID:10618374]
[3] Moscufo N, Simons J, Chow M. Myristoylation is important at multiple stages inpoliovirus assembly. J Virol. 1991 May;65(5):2372-80.[PMID:1850017]
Functional Description
Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host epithelial cells. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells. Tyrosine kinases are probably involved in the entry process. Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins. Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha- helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).
Sequence Annotation
Topological domain: 2 1520 Cytoplasmic.
Topological domain: 1537 2209 Cytoplasmic.
Domain: 882 1031 Peptidase C3 1.
Domain: 1232 1388 SF3 helicase.
Domain: 1566 1731 Peptidase C3 2.
Domain: 1975 2090 RdRp catalytic.
Nucleotide-binding: 1256 1263 ATP.
Region: 580 600 Amphipatic alpha-helix.
Region: 1457 1479 Disordered.
Active site: 901 901 For Protease 2A activity.
Active site: 919 919 For Protease 2A activity.
Active site: 990 990 For Protease 2A activity.
Active site: 1605 1605 For Protease 3C activity.
Active site: 1636 1636 For Protease 3C activity.
Active site: 1712 1712 For Protease 3C activity.
Active site: 2076 2076 For RdRp activity.
Functional site: 25 25 Involved in the interaction with humanRTN3.
Functional site: 69 70 Cleavage; by autolysis.
Functional site: 341 342 Cleavage; by Protease 3C.
Functional site: 881 882 Cleavage; by Protease 2A.
Functional site: 1030 1031 Cleavage; by Protease 3C.
Functional site: 1127 1128 Cleavage; by Protease 3C.
Functional site: 1456 1457 Cleavage; by Protease 3C.
Functional site: 1543 1544 Cleavage; by Protease 3C.
Functional site: 1565 1566 Cleavage; by Protease 3C.
Functional site: 1748 1749 Cleavage; by Protease 3C.
Modified residue: 1546 1546 O-(5'-phospho-RNA)-tyrosine.
Modified residue: 1546 1546 O-UMP-tyrosine; transient.
Protein Length
2209 AA.
Protein Sequence
(Canonical)
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP SKFTEPIKDV  60
LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEY LRDSEANPVD  120
QPTEPDVAAC RFYTLDTVSW TKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ  180
CNASKFHQGA LGVFAVPEMC LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA  240
RRFCPVDYLL GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI  300
LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG SNQYLTADNF  360
QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA TKKNTMEMYR VRLSDKPHTD  420
DPILCLSLSP ASDPRLSHTM LGEILNYYTH WAGSLKFTFL FCGFMMATGK LLVSYAPPGA  480
DPPKKRKEAM LGTHVIWDIG LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV  540
VPLSTPREMD ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA  600
TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS RSESSIESFF  660
ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK LEFFTYSRFD MELTFVVTAN  720
FTETNNGHAL NQVYQIMYVP PGAPVPEKWD DYTWQTSSNP SIFYTYGTAP ARISVPYVGI  780
SNAYSHFYDG FSKVPLKDQS AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL  840
KPKHIRVWCP RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY  900
HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK YYPVSFVGPT  960
FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV IGIITAGGEG LVAFSDIRDL  1020
YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ ISDKITELTN MVTSTITEKL LKNLIKIISS  1080
LVIITRNYED TTTVLATLAL LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN  1140
AAKGLEWVSN KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ  1200
EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV CLLVHGSPGT  1260
GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV IMDDLNQNPD GADMKLFCQM  1320
VSTVEFIPPM ASLEEKGILF TSNYVLASTN SSRISPPTVA HSDALARRFA FDMDIQVMNE  1380
YSRDGKLNMA MATEMCKNCH QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE  1440
RNRRSNIGNC MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV  1500
NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP NKKPNVPTIR  1560
TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA ILPTHASPGE SIVIDGKEVE  1620
ILDAKALEDQ AGTNLEITII TLKRNEKFRD IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP  1680
VGAVTEQGYL NLGGRQTART LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK  1740
RSYFTQSQGE IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT  1800
DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY GTDGLEALDL  1860
STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL PLVTYVKDEL RSKTKVEQGK  1920
SRLIEASSLN DSVAMRMAFG NLYAAFHKNP GVITGSAVGC DPDLFWSKIP VLMEEKLFAF  1980
DYTGYDASLS PAWFEALKMV LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG  2040
TSIFNSMINN LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL  2100
TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR WTKDPRNTQD  2160
HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST LYRRWLDSF              2209
FASTA
(Canonical)
>LipidDB-12081-00913|P03300
MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFSQDPSKFTEPIKDV
LIKTAPMLNSPNIEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEYLRDSEANPVD
QPTEPDVAACRFYTLDTVSWTKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQ
CNASKFHQGALGVFAVPEMCLAGDSNTTTMHTSYQNANPGEKGGTFTGTFTPDNNQTSPA
RRFCPVDYLLGNGTLLGNAFVFPHQIINLRTNNCATLVLPYVNSLSIDSMVKHNNWGIAI
LPLAPLNFASESSPEIPITLTIAPMCCEFNGLRNITLPRLQGLPVMNTPGSNQYLTADNF
QSPCALPEFDVTPPIDIPGEVKNMMELAEIDTMIPFDLSATKKNTMEMYRVRLSDKPHTD
DPILCLSLSPASDPRLSHTMLGEILNYYTHWAGSLKFTFLFCGFMMATGKLLVSYAPPGA
DPPKKRKEAMLGTHVIWDIGLQSSCTMVVPWISNTTYRQTIDDSFTEGGYISVFYQTRIV
VPLSTPREMDILGFVSACNDFSVRLLRDTTHIEQKALAQGLGQMLESMIDNTVRETVGAA
TSRDALPNTEASGPTHSKEIPALTAVETGATNPLVPSDTVQTRHVVQHRSRSESSIESFF
ARGACVTIMTVDNPASTTNKDKLFAVWKITYKDTVQLRRKLEFFTYSRFDMELTFVVTAN
FTETNNGHALNQVYQIMYVPPGAPVPEKWDDYTWQTSSNPSIFYTYGTAPARISVPYVGI
SNAYSHFYDGFSKVPLKDQSAALGDSLYGAASLNDFGILAVRVVNDHNPTKVTSKIRVYL
KPKHIRVWCPRPPRAVAYYGPGVDYKDGTLTPLSTKDLTTYGFGHQNKAVYTAGYKICNY
HLATQDDLQNAVNVMWSRDLLVTESRAQGTDSIARCNCNAGVYYCESRRKYYPVSFVGPT
FQYMEANNYYPARYQSHMLIGHGFASPGDCGGILRCHHGVIGIITAGGEGLVAFSDIRDL
YAYEEEAMEQGITNYIESLGAAFGSGFTQQISDKITELTNMVTSTITEKLLKNLIKIISS
LVIITRNYEDTTTVLATLALLGCDASPWQWLRKKACDVLEIPYVIKQGDSWLKKFTEACN
AAKGLEWVSNKISKFIDWLKEKIIPQARDKLEFVTKLRQLEMLENQISTIHQSCPSQEHQ
EILFNNVRWLSIQSKRFAPLYAVEAKRIQKLEHTINNYIQFKSKHRIEPVCLLVHGSPGT
GKSVATNLIARAIAERENTSTYSLPPDPSHFDGYKQQGVVIMDDLNQNPDGADMKLFCQM
VSTVEFIPPMASLEEKGILFTSNYVLASTNSSRISPPTVAHSDALARRFAFDMDIQVMNE
YSRDGKLNMAMATEMCKNCHQPANFKRCCPLVCGKAIQLMDKSSRVRYSIDQITTMIINE
RNRRSNIGNCMEALFQGPLQYKDLKIDIKTSPPPECINDLLQAVDSQEVRDYCEKKGWIV
NITSQVQTERNINRAMTILQAVTTFAAVAGVVYVMYKLFAGHQGAYTGLPNKKPNVPTIR
TAKVQGPGFDYAVAMAKRNIVTATTSKGEFTMLGVHDNVAILPTHASPGESIVIDGKEVE
ILDAKALEDQAGTNLEITIITLKRNEKFRDIRPHIPTQITETNDGVLIVNTSKYPNMYVP
VGAVTEQGYLNLGGRQTARTLMYNFPTRAGQCGGVITCTGKVIGMHVGGNGSHGFAAALK
RSYFTQSQGEIQWMRPSKEVGYPIINAPSKTKLEPSAFHYVFEGVKEPAVLTKNDPRLKT
DFEEAIFSKYVGNKITEVDEYMKEAVDHYAGQLMSLDINTEQMCLEDAMYGTDGLEALDL
STSAGYPYVAMGKKKRDILNKQTRDTKEMQKLLDTYGINLPLVTYVKDELRSKTKVEQGK
SRLIEASSLNDSVAMRMAFGNLYAAFHKNPGVITGSAVGCDPDLFWSKIPVLMEEKLFAF
DYTGYDASLSPAWFEALKMVLEKIGFGDRVDYIDYLNHSHHLYKNKTYCVKGGMPSGCSG
TSIFNSMINNLIIRTLLLKTYKGIDLDHLKMIAYGDDVIASYPHEVDASLLAQSGKDYGL
TMTPADKSATFETVTWENVTFLKRFFRADEKYPFLIHPVMPMKEIHESIRWTKDPRNTQD
HVRSLCLLAWHNGEEEYNKFLAKIRSVPIGRALLLPEYSTLYRRWLDSF
Gene Ontology
GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-KW
GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0039618; C:T=pseudo3 icosahedral viral capsid; 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:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW
GO:0039520; P:induction by virus of host autophagy; IDA:UniProtKB
GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW
GO:0044694; P:pore-mediated entry of viral genome into 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:0039522; P:suppression by virus of host mRNA export from nucleus; IDA:UniProtKB
GO:0039544; P:suppression by virus of host RIG-I activity by RIG-I proteolysis; IDA:UniProtKB
GO:0039611; P:suppression by virus of host translation initiation factor activity; IDA:UniProtKB
GO:0006351; P:transcription, DNA-templated; IEA:InterPro
GO:0039694; P:viral RNA genome replication; IEA:InterPro
GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR003593; AAA+_ATPase
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir
InterPro; IPR014759; Helicase_SF3_ssRNA_vir
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR014838; P3A
InterPro; IPR000081; Peptidase_C3
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir
InterPro; IPR003138; Pico_P1A
InterPro; IPR002527; Pico_P2B
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; PF08727; P3A;
Pfam; PF00548; Peptidase_C3;
Pfam; PF02226; Pico_P1A;
Pfam; PF00947; Pico_P2A;
Pfam; PF01552; Pico_P2B;
Pfam; PF00680; RdRP_1;
Pfam; PF00073; Rhv;
Pfam; PF00910; RNA_helicase;
SMART
SMART; SM00382; AAA;
PROSITE
PROSITE; PS50507; RDRP_SSRNA_POS;
PROSITE; PS51218; SF3_HELICASE_2;
PRINTS