ID POLG_EC11G Reviewed; 2195 AA. AC P29813; Q66785; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 24-JUN-2015, entry version 139. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=P3; DE Contains: DE RecName: Full=Protein 3AB; DE Contains: DE RecName: Full=P2; DE Contains: DE RecName: Full=P1; DE Contains: DE RecName: Full=Capsid protein VP0; DE AltName: Full=VP4-VP2; DE Contains: DE RecName: Full=Capsid protein VP4; DE AltName: Full=P1A; DE AltName: Full=Virion protein 4; DE Contains: DE RecName: Full=Capsid protein VP2; DE AltName: Full=P1B; DE AltName: Full=Virion protein 2; DE Contains: DE RecName: Full=Capsid protein VP3; DE AltName: Full=P1C; DE AltName: Full=Virion protein 3; DE Contains: DE RecName: Full=Capsid protein VP1; DE AltName: Full=P1D; DE AltName: Full=Virion protein 1; DE Contains: DE RecName: Full=Protease 2A; DE Short=P2A; DE EC=3.4.22.29; DE AltName: Full=Picornain 2A; DE AltName: Full=Protein 2A; DE Contains: DE RecName: Full=Protein 2B; DE Short=P2B; DE Contains: DE RecName: Full=Protein 2C; DE Short=P2C; DE EC=3.6.1.15; DE Contains: DE RecName: Full=Protein 3A; DE Short=P3A; DE Contains: DE RecName: Full=Viral protein genome-linked; DE Short=VPg; DE AltName: Full=Protein 3B; DE Short=P3B; DE Contains: DE RecName: Full=Protein 3CD; DE EC=3.4.22.28; DE Contains: DE RecName: Full=Protease 3C; DE Short=P3C; DE EC=3.4.22.28; DE Contains: DE RecName: Full=RNA-directed RNA polymerase; DE Short=RdRp; DE EC=2.7.7.48; DE AltName: Full=3D polymerase; DE Short=3Dpol; DE AltName: Full=Protein 3D; DE Short=3D; OS Echovirus 11 (strain Gregory). OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Picornavirales; Picornaviridae; Enterovirus; Enterovirus B. OX NCBI_TaxID=31705; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=7762294; DOI=10.1016/0168-1702(94)00104-K; RA Dahllund L., Nissinen L., Pulli T., Hyttinen V.P., Stanway G., RA Hyypiae T.; RT "The genome of echovirus 11."; RL Virus Res. 35:215-222(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 822-2195. RX PubMed=2170575; RA Auvinen P., Hyypiae T.; RT "Echoviruses include genetically distinct serotypes."; RL J. Gen. Virol. 71:2133-2139(1990). RN [3] RP INTERACTION WITH HOST CD55. RX PubMed=7517044; DOI=10.1073/pnas.91.13.6245; RA Bergelson J.M., Chan M., Solomon K.R., St John N.F., Lin H., RA Finberg R.W.; RT "Decay-accelerating factor (CD55), a glycosylphosphatidylinositol- RT anchored complement regulatory protein, is a receptor for several RT echoviruses."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6245-6248(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-859. RC STRAIN=Isolate clinical EV11-207; RX PubMed=12097583; DOI=10.1128/JVI.76.15.7694-7704.2002; RA Stuart A.D., McKee T.A., Williams P.A., Harley C., Shen S., RA Stuart D.I., Brown T.D., Lea S.M.; RT "Determination of the structure of a decay accelerating factor-binding RT clinical isolate of echovirus 11 allows mapping of mutants with RT altered receptor requirements for infection."; RL J. Virol. 76:7694-7704(2002). CC -!- FUNCTION: Capsid protein VP1: Forms an icosahedral capsid of CC pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid CC is 300 Angstroms in diameter, composed of 60 copies of each capsid CC protein and enclosing the viral positive strand RNA genome. Capsid CC protein VP1 mainly forms the vertices of the capsid. Capsid CC protein VP1 interacts with host CD55 to provide virion attachment CC to target host cells. This attachment induces virion CC internalization. Tyrosine kinases are probably involved in the CC entry process. After binding to its receptor, the capsid undergoes CC conformational changes. Capsid protein VP1 N-terminus (that CC contains an amphipathic alpha-helix) and capsid protein VP4 are CC externalized. Together, they shape a pore in the host membrane CC through which viral genome is translocated to host cell cytoplasm. CC After genome has been released, the channel shrinks (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: Capsid protein VP2: Forms an icosahedral capsid of CC pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid CC is 300 Angstroms in diameter, composed of 60 copies of each capsid CC protein and enclosing the viral positive strand RNA genome (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: Capsid protein VP3: Forms an icosahedral capsid of CC pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid CC is 300 Angstroms in diameter, composed of 60 copies of each capsid CC protein and enclosing the viral positive strand RNA genome (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: Capsid protein VP4: Lies on the inner surface of the CC capsid shell. After binding to the host receptor, the capsid CC undergoes conformational changes. Capsid protein VP4 is released, CC Capsid protein VP1 N-terminus is externalized, and together, they CC shape a pore in the host membrane through which the viral genome CC is translocated into the host cell cytoplasm. After genome has CC been released, the channel shrinks (By similarity). {ECO:0000250}. CC -!- FUNCTION: Capsid protein VP0: Component of immature procapsids, CC which is cleaved into capsid proteins VP4 and VP2 after CC maturation. Allows the capsid to remain inactive before the CC maturation step (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protein 2A: Cysteine protease that cleaves viral CC polyprotein and specific host proteins. It is responsible for the CC cleavage between the P1 and P2 regions, first cleavage occurring CC in the polyprotein. Cleaves also the host translation initiation CC factor EIF4G1, in order to shut down the capped cellular mRNA CC translation. Inhibits the host nucleus-cytoplasm protein and RNA CC trafficking by cleaving host members of the nuclear pores (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: Protein 2B: Plays an essential role in the virus CC replication cycle by acting as a viroporin. Creates a pore in the CC host reticulum endoplasmic and as a consequence releases Ca2+ in CC the cytoplasm of infected cell. In turn, high levels of CC cyctoplasmic calcium may trigger membrane trafficking and CC transport of viral ER-associated proteins to viroplasms, sites of CC viral genome replication (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protein 2C: Induces and associates with structural CC rearrangements of intracellular membranes. Displays RNA-binding, CC nucleotide binding and NTPase activities. May play a role in CC virion morphogenesis and viral RNA encapsidation by interacting CC with the capsid protein VP3 (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protein 3AB: Localizes the viral replication complex to CC the surface of membranous vesicles. Together with protein 3CD CC binds the Cis-Active RNA Element (CRE) which is involved in RNA CC synthesis initiation. Acts as a cofactor to stimulate the activity CC of 3D polymerase, maybe through a nucleid acid chaperone activity CC (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protein 3A: Localizes the viral replication complex to CC the surface of membranous vesicles. It inhibits host cell CC endoplasmic reticulum-to-Golgi apparatus transport and causes the CC dissassembly of the Golgi complex, possibly through GBF1 CC interaction. This would result in depletion of MHC, trail CC receptors and IFN receptors at the host cell surface (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: Viral protein genome-linked: acts as a primer for viral CC RNA replication and remains covalently bound to viral genomic RNA. CC VPg is uridylylated prior to priming replication into VPg-pUpU. CC The oriI viral genomic sequence may act as a template for this. CC The VPg-pUpU is then used as primer on the genomic RNA poly(A) by CC the RNA-dependent RNA polymerase to replicate the viral genome. CC VPg may be removed in the cytoplasm by an unknown enzyme termed CC "unlinkase". VPg is not cleaved off virion genomes because CC replicated genomic RNA are encapsidated at the site of replication CC (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protein 3CD: Is involved in the viral replication CC complex and viral polypeptide maturation. It exhibits protease CC activity with a specificity and catalytic efficiency that is CC different from protease 3C. Protein 3CD lacks polymerase activity. CC The 3C domain in the context of protein 3CD may have an RNA CC binding activity (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protease 3C: cleaves host DDX58/RIG-I and thus CC contributes to the inhibition of type I interferon production. CC Cleaves also host PABPC1 (By similarity). {ECO:0000250}. CC -!- FUNCTION: RNA-directed RNA polymerase: Replicates the viral CC genomic RNA on the surface of intracellular membranes. May form CC linear arrays of subunits that propagate along a strong head-to- CC tail interaction called interface-I. Covalently attaches UMP to a CC tyrosine of VPg, which is used to prime RNA synthesis. The CC positive stranded RNA genome is first replicated at virus induced CC membranous vesicles, creating a dsRNA genomic replication form. CC This dsRNA is then used as template to synthesize positive CC stranded RNA genomes. ss(+)RNA genomes are either translated, CC replicated or encapsidated (By similarity). {ECO:0000255|PROSITE- CC ProRule:PRU00539}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the CC picornavirus polyprotein. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the CC poliovirus polyprotein. In other picornavirus reactions Glu may be CC substituted for Gln, and Ser or Thr for Gly. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- ENZYME REGULATION: RNA-directed RNA polymerase: replication or CC transcription is subject to high level of random mutations by the CC nucleotide analog ribavirin. CC -!- SUBUNIT: Capsid protein VP1: Interacts with capsid protein VP0, CC and capsid protein VP3 to form heterotrimeric protomers. Five CC protomers subsequently associate to form pentamers which serve as CC building blocks for the capsid. Interacts with capsid protein VP4 CC in the mature capsid (By similarity). Interact with host CD55. CC Capsid protein VP0: interacts with capsid protein VP1 and capsid CC protein VP3 to form heterotrimeric protomers. Five protomers CC subsequently associate to form pentamers which serve as building CC blocks for the capsid. Capsid protein VP2: Interacts with capsid CC protein VP1 and capsid protein VP3 in the mature capsid (By CC similarity). Capsid protein VP3: interacts with capsid protein VP0 CC and capsid protein VP1 to form heterotrimeric protomers. Five CC protomers subsequently associate to form pentamers which serve as CC building blocks for the capsid. Interacts with capsid protein VP4 CC in the mature capsid (By similarity). Capsid protein VP4: CC Interacts with capsid protein VP1 and capsid protein VP3 (By CC similarity). Protein 2C: interacts with capsid protein VP3; this CC interaction may be important for virion morphogenesis (By CC similarity). Protein 3AB: interacts with protein 3CD (By CC similarity). Viral protein genome-linked: interacts with RNA- CC directed RNA polymerase (By similarity). Protein 3CD: interacts CC with protein 3AB and with RNA-directed RNA polymerase. RNA- CC directed RNA polymerase: interacts with viral protein genome- CC linked and with protein 3CD (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein VP0: Virion {ECO:0000250}. CC Host cytoplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein VP4: Virion {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion {ECO:0000250}. CC Host cytoplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion {ECO:0000250}. CC Host cytoplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein VP1: Virion {ECO:0000250}. CC Host cytoplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; CC Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the CC surface of intracellular membrane vesicles that are induced after CC virus infection as the site for viral RNA replication. These CC vesicles are derived from the endoplasmic reticulum. CC -!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; CC Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the CC surface of intracellular membrane vesicles that are induced after CC virus infection as the site for viral RNA replication. These CC vesicles are derived from the endoplasmic reticulum. CC -!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; CC Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the CC surface of intracellular membrane vesicles that are induced after CC virus infection as the site for viral RNA replication. These CC vesicles are derived from the endoplasmic reticulum. CC -!- SUBCELLULAR LOCATION: Protein 3AB: Host cytoplasmic vesicle CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; CC Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the CC surface of intracellular membrane vesicles that are induced after CC virus infection as the site for viral RNA replication. These CC vesicles are derived from the endoplasmic reticulum. CC -!- SUBCELLULAR LOCATION: Viral protein genome-linked: Virion CC {ECO:0000250}. Host cytoplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Protein 3CD: Host cytoplasmic vesicle CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; CC Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the CC surface of intracellular membrane vesicles that are induced after CC virus infection as the site for viral RNA replication. These CC vesicles are derived from the endoplasmic reticulum. CC -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host CC cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. CC Note=Probably localizes to the surface of intracellular membrane CC vesicles that are induced after virus infection as the site for CC viral RNA replication. These vesicles are derived from the CC endoplasmic reticulum. CC -!- PTM: Specific enzymatic cleavages in vivo by the viral proteases CC yield a variety of precursors and mature proteins. Polyprotein CC processing intermediates such as VP0 which is a VP4-VP2 precursor CC are produced. During virion maturation, non-infectious particles CC are rendered infectious following cleavage of VP0. This maturation CC cleavage is followed by a conformational change of the particle CC (By similarity). {ECO:0000250}. CC -!- PTM: VPg is uridylylated by the polymerase and is covalently CC linked to the 5'-end of genomic RNA. This uridylylated form acts CC as a nucleotide-peptide primer for the polymerase (By similarity). CC {ECO:0000250}. CC -!- PTM: Myristoylation of VP4 is required during RNA encapsidation CC and formation of the mature virus particle. {ECO:0000250}. CC -!- PTM: Capsid protein VP0: Myristoylation is required for the CC formation of pentamers during virus assembly. Further assembly of CC 12 pentamers and a molecule of genomic RNA generates the provirion CC (By similarity). {ECO:0000250}. CC -!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo by CC the viral proteases yield processing intermediates and the mature CC proteins. {ECO:0000250}. CC -!- PTM: Capsid protein VP0: During virion maturation, immature CC virions are rendered infectious following cleavage of VP0 into VP4 CC and VP2. This maturation seems to be an autocatalytic event CC triggered by the presence of RNA in the capsid and it is followed CC by a conformational change infectious virion (By similarity). CC {ECO:0000250}. CC -!- PTM: Viral protein genome-linked: VPg is uridylylated by the CC polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer CC for the genomic RNA replication (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 peptidase C3 domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU00539}. CC -!- SIMILARITY: Contains 1 SF3 helicase domain. {ECO:0000255|PROSITE- CC ProRule:PRU00551}. CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral CC capsid structure; CC URL="http://viperdb.scripps.edu/info_page.php?VDB=1h8t"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X80059; CAA56365.1; -; Genomic_RNA. DR EMBL; D10582; BAA01439.1; -; Genomic_RNA. DR PIR; A36642; GNNYEC. DR PDB; 2C8I; EM; 14.00 A; A=570-857, B=79-328, C=332-569, D=2-69. DR PDBsum; 2C8I; -. DR ProteinModelPortal; P29813; -. DR SMR; P29813; 2-69, 79-330, 332-858, 862-1011, 1551-2195. DR MEROPS; N08.001; -. DR PRIDE; P29813; -. DR EvolutionaryTrace; P29813; -. DR Proteomes; UP000002684; Chromosome. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0039618; C:T=pseudo3 icosahedral 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:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW. DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW. DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; ISS:UniProtKB. DR GO; GO:0039544; P:suppression by virus of host RIG-I activity by RIG-I proteolysis; ISS:UniProtKB. DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.20; -; 3. DR Gene3D; 4.10.80.10; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014838; P3A. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009003; Trypsin-like_Pept_dom. DR InterPro; IPR029053; Viral_coat. DR Pfam; PF08727; P3A; 1. DR Pfam; PF00548; Peptidase_C3; 1. DR Pfam; PF02226; Pico_P1A; 1. DR Pfam; PF00947; Pico_P2A; 1. DR Pfam; PF01552; Pico_P2B; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00073; Rhv; 3. DR Pfam; PF00910; RNA_helicase; 1. DR ProDom; PD001306; Peptidase_C3; 1. DR ProDom; PD649346; Pico_P2B; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50494; SSF50494; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF89043; SSF89043; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activation of host autophagy by virus; ATP-binding; KW Capsid protein; Complete proteome; Covalent protein-RNA linkage; KW DNA replication; Eukaryotic host gene expression shutoff by virus; KW Eukaryotic host translation shutoff by virus; Helicase; KW Host cytoplasm; Host cytoplasmic vesicle; KW Host gene expression shutoff by virus; Host membrane; KW Host mRNA suppression by virus; Host-virus interaction; Hydrolase; KW Inhibition of host innate immune response by virus; KW Inhibition of host mRNA nuclear export by virus; KW Inhibition of host RIG-I by virus; KW Inhibition of host RLR pathway by virus; Ion channel; Ion transport; KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; KW Nucleotidyltransferase; Phosphoprotein; KW Pore-mediated penetration of viral genome into host cell; Protease; KW Repeat; RNA-binding; RNA-directed RNA polymerase; KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase; KW Transport; Viral attachment to host cell; Viral immunoevasion; KW Viral ion channel; Viral penetration into host cytoplasm; KW Viral RNA replication; Virion; Virus endocytosis by host; KW Virus entry into host cell. FT INIT_MET 1 1 Removed; by host. {ECO:0000250}. FT CHAIN 2 2195 Genome polyprotein. {ECO:0000250}. FT /FTId=PRO_0000426431. FT CHAIN 2 850 P1. {ECO:0000250}. FT /FTId=PRO_0000426432. FT CHAIN 2 331 Capsid protein VP0. {ECO:0000255}. FT /FTId=PRO_0000426433. FT CHAIN 2 69 Capsid protein VP4. {ECO:0000255}. FT /FTId=PRO_0000426434. FT CHAIN 70 331 Capsid protein VP2. {ECO:0000255}. FT /FTId=PRO_0000426435. FT CHAIN 332 567 Capsid protein VP3. {ECO:0000255}. FT /FTId=PRO_0000426436. FT CHAIN 567 861 Capsid protein VP1. {ECO:0000255}. FT /FTId=PRO_0000426437. FT CHAIN 862 1439 P2. {ECO:0000250}. FT /FTId=PRO_0000426438. FT CHAIN 862 1011 Protease 2A. {ECO:0000255}. FT /FTId=PRO_0000426439. FT CHAIN 1012 1110 Protein 2B. {ECO:0000255}. FT /FTId=PRO_0000039708. FT CHAIN 1111 1439 Protein 2C. {ECO:0000255}. FT /FTId=PRO_0000039709. FT CHAIN 1440 2195 P3. {ECO:0000250}. FT /FTId=PRO_0000426440. FT CHAIN 1440 1550 Protein 3AB. {ECO:0000255}. FT /FTId=PRO_0000426441. FT CHAIN 1440 1528 Protein 3A. {ECO:0000255}. FT /FTId=PRO_0000039710. FT CHAIN 1529 1550 Viral protein genome-linked. FT {ECO:0000255}. FT /FTId=PRO_0000426442. FT CHAIN 1551 2195 Protein 3CD. {ECO:0000255}. FT /FTId=PRO_0000426443. FT CHAIN 1551 1732 Protease 3C. {ECO:0000255}. FT /FTId=PRO_0000426444. FT CHAIN 1733 2195 RNA-directed RNA polymerase. FT {ECO:0000250}. FT /FTId=PRO_0000426445. FT TOPO_DOM 2 1505 Cytoplasmic. {ECO:0000255}. FT INTRAMEM 1506 1521 {ECO:0000255}. FT TOPO_DOM 1522 2195 Cytoplasmic. {ECO:0000255}. FT DOMAIN 1215 1371 SF3 helicase. {ECO:0000255|PROSITE- FT ProRule:PRU00551}. FT DOMAIN 1551 1716 Peptidase C3. FT DOMAIN 1960 2076 RdRp catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU00539}. FT REGION 567 583 Amphipatic alpha-helix. {ECO:0000255}. FT REGION 1440 1463 Disordered. {ECO:0000250}. FT ACT_SITE 882 882 For Protease 2A activity. {ECO:0000250}. FT ACT_SITE 900 900 For Protease 2A activity. {ECO:0000250}. FT ACT_SITE 971 971 For Protease 2A activity. {ECO:0000250}. FT ACT_SITE 1590 1590 For Protease 3C activity. {ECO:0000255}. FT ACT_SITE 1621 1621 For Protease 3C activity. {ECO:0000255}. FT ACT_SITE 1697 1697 For Protease 3C activity. {ECO:0000250}. FT ACT_SITE 2062 2062 For RdRp activity. {ECO:0000250}. FT SITE 69 70 Cleavage; by autolysis. {ECO:0000255}. FT SITE 331 332 Cleavage; by Protease 3C. {ECO:0000255}. FT SITE 861 862 Cleavage; by Protease 2A. {ECO:0000255}. FT SITE 1011 1012 Cleavage; by Protease 3C. {ECO:0000255}. FT SITE 1439 1440 Cleavage; by Protease 3C. {ECO:0000255}. FT SITE 1528 1529 Cleavage; by Protease 3C. {ECO:0000255}. FT SITE 1550 1551 Cleavage; by Protease 3C. {ECO:0000255}. FT SITE 1733 1734 Cleavage; by Protease 3C. {ECO:0000255}. FT MOD_RES 1531 1531 O-(5'-phospho-RNA)-tyrosine. FT {ECO:0000250}. FT LIPID 2 2 N-myristoyl glycine; by host. FT {ECO:0000250}. FT CONFLICT 823 827 RLCQY -> SYANT (in Ref. 2; BAA01439). FT {ECO:0000305}. FT STRAND 4 7 FT STRAND 25 29 FT HELIX 36 38 FT HELIX 50 52 FT STRAND 57 59 FT STRAND 63 65 FT STRAND 83 87 FT STRAND 90 96 FT STRAND 100 102 FT TURN 113 115 FT HELIX 126 128 FT STRAND 138 140 FT STRAND 147 152 FT HELIX 159 167 FT STRAND 168 180 FT STRAND 188 197 FT STRAND 203 205 FT HELIX 212 215 FT STRAND 218 220 FT STRAND 225 227 FT STRAND 231 235 FT HELIX 239 241 FT TURN 242 244 FT HELIX 248 253 FT STRAND 254 260 FT TURN 261 263 FT STRAND 265 271 FT STRAND 276 278 FT TURN 282 284 FT STRAND 288 299 FT STRAND 308 324 FT TURN 339 342 FT STRAND 354 356 FT HELIX 374 378 FT HELIX 396 399 FT STRAND 401 407 FT STRAND 414 417 FT TURN 420 422 FT HELIX 424 427 FT HELIX 430 435 FT STRAND 438 442 FT STRAND 445 451 FT STRAND 458 466 FT STRAND 468 470 FT HELIX 476 479 FT STRAND 482 488 FT STRAND 490 492 FT STRAND 494 499 FT STRAND 504 506 FT STRAND 508 511 FT STRAND 520 530 FT STRAND 537 547 FT STRAND 552 556 FT STRAND 565 567 FT HELIX 603 605 FT HELIX 613 616 FT HELIX 629 631 FT HELIX 633 637 FT STRAND 641 651 FT STRAND 653 655 FT HELIX 656 658 FT STRAND 659 663 FT HELIX 670 676 FT STRAND 679 696 FT STRAND 710 716 FT HELIX 729 732 FT STRAND 734 736 FT STRAND 738 742 FT STRAND 749 752 FT STRAND 757 763 FT STRAND 767 770 FT HELIX 779 782 FT STRAND 787 794 FT STRAND 801 819 FT STRAND 854 856 SQ SEQUENCE 2195 AA; 245407 MW; 1CFC5DF288831AF0 CRC64; MGAQVSTQKT GAHETGLNAS GSSIIHYTNI NYYKDAASNS ANRQEFSQDP GKFTEPVKDI MVKSLPALNS PSAEECGYSD RVRSITLGNS TITTQESANV VVGYGRWPEY LKDNEATAED QPTQPDVATC RFYTLESVTW ERDSPGWWWK FPDALKDMGL FGQNMYYHYL GRAGYTLHVQ CNASKFHQGC LLVVCVPEAE MGCSQVDGTV NEHGLSEGET AKKFSSTSTN GTNTVQTIVT NAGMGVGVGN LTIYPHQWIN LRTNNCATIV MPYINNVPMD NMFRHHNFTL MIIPFVPLDY SSDSSTYVPI TVTVAPMCAE YNGLRLSTSL QGLPVMNTPG SNQFLTSDDF QSPSAMPQFD VTPELNIPGE VQNLMEIAEV DSVVPVNNVE GKLDTMEVYR IPVQSGNHQS DQVFGFQVQP GLDSVFKHTL LGEILNYFAH WSGSIKLTFV FCGSAMATGK FLLAYAPPGA NAPKNRKDAM LGTHIIWDVG LQSSCVLCVP WISQTHYRLV QQDEYTSAGN VTCWYQTGIV VPAGTPTSCS IMCFVSACND FSVRLLKDTP FIEQTALLQG DVVEAVENAV ARVADTIGSG PSNSQAVPAL TAVETGHTSQ VTPSDTMQTR HVKNYHSRSE SSIENFLSRS ACVYMGGYHT TNTDQTKLFA SWTISARRMV QMRRKLEIFT YVRFDVEVTF VITSKQDQGS RLGQDMPPLT HQIMYIPPGG PIPKSVTDYA WQTSTNPSIF WTEGNAPPRM SIPFISIGNA YSNFYDGWSH FSQNGVYGYN TLNHMGQIYV RHVNGSSPLP MTSTVRMYFK PKHVKAWVPR PPRLCQYKNA STVNFTPTNV TDKRTSINYI PETVKPDLSN YGAFGYQSGA VYVVNYRVVN RHLATHTDWQ NCVWEDYNRD LLISTTTAHG CDVIARCRCS TGVYYCQSKG KHYPVNFEGP GLVEVQESEY YPKRYQSHVL LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADVRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ NNGWLKKFTE MTNSCKGMEW ISIKIQKFIE WLKVKILPEV REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYASEAKR VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYTLPPD PDHFDGYKQQ AVVIVDDLCQ NPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSLFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSEKTCD EECCPVNFKR CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPIYREIKIS VAPETPPPPA IADLLKSVDS EAVREYCKEK GWLVPEVNST LQIEKHVSRA FICLQALTTF VSVAGIIYII YKLFAGFQGA YTGMPNQKPK VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT EYREFTMLGI YDRWAVLPRH AKPGPTILMN NQEVGVLDAK ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEANQA VLAINTSKFP NMYIPVGQVT DYGFLNLGGT PTKRMLMSNF PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPII NTPSKTKLEP SVFHQVFEGD KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA VDHYAGQLAT LDISTEPMRL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSRRTRD LTKLKECMDK YGLNLPMVTY VKDELRSADK VAKGKSRLIE ASSLNDSVAM RQTFGNLYRT FHLNPGIVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKLLLEKLG YTHKETNYID YLCNSHHLYR DKHYFERGGM PSGYSGTSMF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY GDDVIASYPW PIDASLLAET GKGYGLIMTP ADKGECFNEV TWTNVTFLKR YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF //