ID A0A023ZSL9_HE71 Unreviewed; 2193 AA. AC A0A023ZSL9; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 27-NOV-2024, entry version 65. DE RecName: Full=Genome polyprotein {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P3 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3AB {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=P1 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP0 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=VP4-VP2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP4 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1A {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 4 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP2 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1B {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 2 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP3 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1C {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 3 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Capsid protein VP1 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=P1D {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Virion protein 1 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protease 2A {ECO:0000256|RuleBase:RU364118}; DE Short=P2A {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.29 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Picornain 2A {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 2A {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 2B {ECO:0000256|RuleBase:RU364118}; DE Short=P2B {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 2C {ECO:0000256|RuleBase:RU364118}; DE Short=P2C {ECO:0000256|RuleBase:RU364118}; DE EC=3.6.1.15 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3A {ECO:0000256|RuleBase:RU364118}; DE Short=P3A {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Viral protein genome-linked {ECO:0000256|RuleBase:RU364118}; DE Short=VPg {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 3B {ECO:0000256|RuleBase:RU364118}; DE Short=P3B {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protein 3CD {ECO:0000256|RuleBase:RU364118}; DE EC=3.4.22.28 {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=Protease 3C {ECO:0000256|RuleBase:RU364118}; DE Short=P3C {ECO:0000256|RuleBase:RU364118}; DE Contains: DE RecName: Full=RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU364118}; DE Short=RdRp {ECO:0000256|RuleBase:RU364118}; DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=3D polymerase {ECO:0000256|RuleBase:RU364118}; DE Short=3Dpol {ECO:0000256|RuleBase:RU364118}; DE AltName: Full=Protein 3D {ECO:0000256|RuleBase:RU364118}; DE Short=3D {ECO:0000256|RuleBase:RU364118}; OS Human enterovirus 71 (EV71) (EV-71). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus A. OX NCBI_TaxID=39054 {ECO:0000313|EMBL:AHY81310.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:AHY81310.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M538-TW12 {ECO:0000313|EMBL:AHY81310.1}; RA Huang S.-W., Cheng H.-L., Hsieh H.-Y., Chang C.-L., Tsai H.-P., Kuo P.-H., RA Wang S.-M., Liu C.-C., Su I.-J., Wang J.-R.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AHY81310.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M538-TW12 {ECO:0000313|EMBL:AHY81310.1}; RX PubMed=24766641; DOI=10.1186/1423-0127-21-33; RA Huang S.W., Cheng H.L., Hsieh H.Y., Chang C.L., Tsai H.P., Kuo P.H., RA Wang S.M., Liu C.C., Su I.J., Wang J.R.; RT "Mutations in the non-structural protein region contribute to intra- RT genotypic evolution of enterovirus 71."; RL J. Biomed. Sci. 21:33-33(2014). CC -!- FUNCTION: Acts as a primer for viral RNA replication and remains CC covalently bound to viral genomic RNA. VPg is uridylylated prior to CC priming replication into VPg-pUpU. The oriI viral genomic sequence may CC act as a template for this. The VPg-pUpU is then used as primer on the CC genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate CC the viral genome. Following genome release from the infecting virion in CC the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2. CC During the late stage of the replication cycle, host TDP2 is excluded CC from sites of viral RNA synthesis and encapsidation, allowing for the CC generation of progeny virions. {ECO:0000256|ARBA:ARBA00045467}. CC -!- FUNCTION: Capsid protein VP0: Component of immature procapsids, which CC is cleaved into capsid proteins VP4 and VP2 after maturation. Allows CC the capsid to remain inactive before the maturation step. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. Capsid protein VP1 mainly forms CC the vertices of the capsid. Capsid protein VP1 interacts with host cell CC receptor to provide virion attachment to target host cells. This CC attachment induces virion internalization. Tyrosine kinases are CC probably involved in the entry process. After binding to its receptor, CC the capsid undergoes conformational changes. Capsid protein VP1 N- CC terminus (that contains an amphipathic alpha-helix) and capsid protein CC VP4 are 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. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 CC symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms CC in diameter, composed of 60 copies of each capsid protein and enclosing CC the viral positive strand RNA genome. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Capsid protein VP4: Lies on the inner surface of the capsid CC shell. After binding to the host receptor, the capsid undergoes CC conformational changes. Capsid protein VP4 is released, Capsid protein CC VP1 N-terminus is externalized, and together, they shape a pore in the CC host membrane through which the viral genome is translocated into the CC host cell cytoplasm. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Cysteine protease that cleaves viral polyprotein and specific CC host proteins. It is responsible for the autocatalytic cleavage between CC the P1 and P2 regions, which is the first cleavage occurring in the CC polyprotein. Cleaves also the host translation initiation factor CC EIF4G1, in order to shut down the capped cellular mRNA translation. CC Inhibits the host nucleus-cytoplasm protein and RNA trafficking by CC cleaving host members of the nuclear pores. Counteracts stress granule CC formation probably by antagonizing its assembly or promoting its CC dissassembly. Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting CC the type-I IFN production and the establishment of the antiviral state. CC Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN CC production and the establishment of the antiviral state. CC {ECO:0000256|ARBA:ARBA00045143}. CC -!- FUNCTION: Localizes the viral replication complex to the surface of CC membranous vesicles. It inhibits host cell endoplasmic reticulum-to- CC Golgi apparatus transport and causes the disassembly of the Golgi CC complex, possibly through GBF1 interaction. This would result in CC depletion of MHC, trail receptors and IFN receptors at the host cell CC surface. Plays an essential role in viral RNA replication by recruiting CC ACBD3 and PI4KB at the viral replication sites, thereby allowing the CC formation of the rearranged membranous structures where viral CC replication takes place. {ECO:0000256|ARBA:ARBA00045482}. CC -!- FUNCTION: Protease 2A: Cysteine protease that cleaves viral polyprotein CC and specific host proteins. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protease 3C: Major viral protease that mediates proteolytic CC processing of the polyprotein. Cleaves host EIF5B, contributing to host CC translation shutoff. Cleaves also host PABPC1, contributing to host CC translation shutoff. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 2B: Plays an essential role in the virus replication CC cycle by acting as a viroporin. Creates a pore in the host reticulum CC endoplasmic and as a consequence releases Ca2+ in the cytoplasm of CC infected cell. In turn, high levels of cytoplasmic calcium may trigger CC membrane trafficking and transport of viral ER-associated proteins to CC viroplasms, sites of viral genome replication. CC {ECO:0000256|RuleBase:RU364118}. 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 virion CC morphogenesis and viral RNA encapsidation by interacting with the CC capsid protein VP3. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3A: Localizes the viral replication complex to the CC surface of membranous vesicles. It inhibits host cell endoplasmic CC reticulum-to-Golgi apparatus transport and causes the disassembly of CC the Golgi complex, possibly through GBF1 interaction. This would result CC in depletion of MHC, trail receptors and IFN receptors at the host cell CC surface. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3AB: Localizes the viral replication complex to the CC surface of membranous vesicles. Together with protein 3CD binds the CC Cis-Active RNA Element (CRE) which is involved in RNA synthesis CC initiation. Acts as a cofactor to stimulate the activity of 3D CC polymerase, maybe through a nucleid acid chaperone activity. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Protein 3CD: Involved in the viral replication complex and CC viral polypeptide maturation. It exhibits protease activity with a CC specificity and catalytic efficiency that is different from protease CC 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the CC 5'UTR of the viral genome. {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: RNA-directed RNA polymerase: Replicates the viral genomic RNA CC on the surface of intracellular membranes. May form linear arrays of CC subunits that propagate along a strong head-to-tail interaction called CC interface-I. Covalently attaches UMP to a tyrosine of VPg, which is CC used to prime RNA synthesis. The positive stranded RNA genome is first CC replicated at virus induced membranous vesicles, creating a dsRNA CC genomic replication form. This dsRNA is then used as template to CC synthesize positive stranded RNA genomes. ss(+)RNA genomes are either CC translated, replicated or encapsidated. CC {ECO:0000256|RuleBase:RU364118}. CC -!- FUNCTION: Viral protein genome-linked: acts as a primer for viral RNA CC replication and remains covalently bound to viral genomic RNA. VPg is CC uridylylated prior to priming replication into VPg-pUpU. The oriI viral CC genomic sequence may act as a template for this. The VPg-pUpU is then CC used as primer on the genomic RNA poly(A) by the RNA-dependent RNA CC polymerase to replicate the viral genome. CC {ECO:0000256|RuleBase:RU364118}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus CC polyprotein. In other picornavirus reactions Glu may be substituted CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; CC Evidence={ECO:0000256|RuleBase:RU364118}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus CC polyprotein.; EC=3.4.22.29; Evidence={ECO:0000256|ARBA:ARBA00024513, CC ECO:0000256|RuleBase:RU364118}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC diphosphate + phosphate + H(+); Xref=Rhea:RHEA:23680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CC Evidence={ECO:0000256|ARBA:ARBA00001491, CC ECO:0000256|RuleBase:RU364118}; CC -!- CATALYTIC ACTIVITY: CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + CC diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000256|RuleBase:RU364118}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBUNIT: Capsid protein VP1: Interacts with capsid protein VP0, and CC capsid protein VP3 to form heterotrimeric protomers. Five protomers CC subsequently associate to form pentamers which serve as building blocks CC for the capsid. Interacts with capsid protein VP2, capsid protein VP3 CC and capsid protein VP4 following cleavage of capsid protein VP0. CC {ECO:0000256|RuleBase:RU364118}. CC -!- SUBUNIT: Homodimer. Interacts with host GBF1. Interacts (via GOLD CC domain) with host ACBD3 (via GOLD domain); this interaction allows the CC formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 CC stoichiometry, which will stimulate the recruitment of host PI4KB in CC order to synthesize PI4P at the viral RNA replication sites. CC {ECO:0000256|ARBA:ARBA00046425}. CC -!- SUBUNIT: Homohexamer; forms a hexameric ring structure with 6-fold CC symmetry characteristic of AAA+ ATPases. Interacts (via N-terminus) CC with host RTN3 (via reticulon domain); this interaction is important CC for viral replication. Interacts with capsid protein VP3; this CC interaction may be important for virion morphogenesis. CC {ECO:0000256|ARBA:ARBA00046779}. CC -!- SUBUNIT: Interacts with RNA-directed RNA polymerase. CC {ECO:0000256|ARBA:ARBA00011124}. CC -!- SUBUNIT: Interacts with capsid protein VP0 and capsid protein VP1 to CC form heterotrimeric protomers. Five protomers subsequently associate to CC form pentamers which serve as building blocks for the capsid. Interacts CC with capsid protein VP4 in the mature capsid. Interacts with protein CC 2C; this interaction may be important for virion morphogenesis. CC {ECO:0000256|ARBA:ARBA00046709}. CC -!- SUBUNIT: Interacts with capsid protein VP1 and capsid protein VP3 to CC form heterotrimeric protomers. {ECO:0000256|ARBA:ARBA00011474}. CC -!- SUBUNIT: Interacts with protein 3CD. {ECO:0000256|ARBA:ARBA00011647}. CC -!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane CC {ECO:0000256|ARBA:ARBA00004295}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004295}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004295}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Virion CC {ECO:0000256|ARBA:ARBA00004328}. CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC {ECO:0000256|ARBA:ARBA00008303, ECO:0000256|RuleBase:RU364118}. 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; KF974790; AHY81310.1; -; Genomic_RNA. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. 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:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0015267; F:channel activity; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; 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-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. 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; IEA:UniProtKB-KW. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW. DR GO; GO:0044694; P:symbiont genome entry into host cell via pore formation in plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0039554; P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity; IEA:UniProtKB-KW. DR GO; GO:0039522; P:symbiont-mediated suppression of host mRNA export from nucleus; IEA:UniProtKB-KW. 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 GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW. DR CDD; cd23213; Enterovirus_RdRp; 1. DR CDD; cd00205; rhv_like; 3. DR FunFam; 1.20.960.20:FF:000001; Genome polyprotein; 1. DR FunFam; 2.40.10.10:FF:000018; Genome polyprotein; 1. DR FunFam; 2.40.10.10:FF:000020; Genome polyprotein; 1. DR FunFam; 2.40.10.10:FF:000022; Genome polyprotein; 1. DR FunFam; 2.60.120.20:FF:000001; Genome polyprotein; 1. DR FunFam; 2.60.120.20:FF:000002; Genome polyprotein; 1. DR FunFam; 2.60.120.20:FF:000003; Genome polyprotein; 1. DR FunFam; 3.30.70.270:FF:000008; Genome polyprotein; 1. DR FunFam; 4.10.880.10:FF:000001; Genome polyprotein; 1. DR FunFam; 4.10.880.10:FF:000002; Genome polyprotein; 1. DR Gene3D; 1.20.960.20; -; 1. DR Gene3D; 2.60.120.20; -; 3. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 6.10.20.20; Poliovirus 3A protein-like; 1. DR Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 2. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR043502; DNA/RNA_pol_sf. 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; IPR036203; P3A_soluble_dom. DR InterPro; IPR044067; PCV_3C_PRO. DR InterPro; IPR000081; Peptidase_C3. DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR003138; Pico_P1A. DR InterPro; IPR002527; Pico_P2B. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR033703; Rhv-like. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. 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; 2. DR Pfam; PF22663; Rhv_5; 1. DR Pfam; PF00910; RNA_helicase; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2. DR SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2. DR PROSITE; PS51874; PCV_3C_PRO; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 3: Inferred from homology; KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050, KW ECO:0000256|RuleBase:RU364118}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364118}; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813}; KW Capsid protein {ECO:0000256|ARBA:ARBA00022561, KW ECO:0000256|RuleBase:RU364118}; KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520, KW ECO:0000256|RuleBase:RU364118}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW Eukaryotic host gene expression shutoff by virus KW {ECO:0000256|ARBA:ARBA00023247, ECO:0000256|RuleBase:RU364118}; KW Eukaryotic host translation shutoff by virus KW {ECO:0000256|ARBA:ARBA00022809, ECO:0000256|RuleBase:RU364118}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364118}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, KW ECO:0000256|RuleBase:RU364118}; KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488, KW ECO:0000256|RuleBase:RU364118}; KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995, KW ECO:0000256|RuleBase:RU364118}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, KW ECO:0000256|RuleBase:RU364118}; KW Host mRNA suppression by virus {ECO:0000256|ARBA:ARBA00022557, KW ECO:0000256|RuleBase:RU364118}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, KW ECO:0000256|RuleBase:RU364118}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364118}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632, ECO:0000256|RuleBase:RU364118}; KW Inhibition of host MDA5 by virus {ECO:0000256|ARBA:ARBA00023260}; KW Inhibition of host mRNA nuclear export by virus KW {ECO:0000256|ARBA:ARBA00023197, ECO:0000256|RuleBase:RU364118}; KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482, KW ECO:0000256|RuleBase:RU364118}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU364118}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU364118}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU364118}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364118}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Myristate {ECO:0000256|ARBA:ARBA00022707, ECO:0000256|RuleBase:RU364118}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU364118}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|RuleBase:RU364118}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Pore-mediated penetration of viral genome into host cell KW {ECO:0000256|ARBA:ARBA00023255, ECO:0000256|RuleBase:RU364118}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364118}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU364118}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU364118}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484, KW ECO:0000256|RuleBase:RU364118}; KW T=pseudo3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022706, KW ECO:0000256|RuleBase:RU364118}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364118}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364118}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804, KW ECO:0000256|RuleBase:RU364118}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, KW ECO:0000256|RuleBase:RU364118}; KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039, KW ECO:0000256|RuleBase:RU364118}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595, KW ECO:0000256|RuleBase:RU364118}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953, KW ECO:0000256|RuleBase:RU364118}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU364118}; KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890, KW ECO:0000256|RuleBase:RU364118}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296, KW ECO:0000256|RuleBase:RU364118}; Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 1216..1374 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51218" FT DOMAIN 1549..1727 FT /note="Peptidase C3" FT /evidence="ECO:0000259|PROSITE:PS51874" FT DOMAIN 1958..2073 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2193 AA; 242794 MW; E7415653EFAD6125 CRC64; MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKDSYAAT AGKQSLKQDP DKFANPVKDI FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI IVGYGEWPSY CSDDDATAVD KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK FPDVLTETGV FGQNAQFHYL YRSGFCIHVQ CNASKFHQGA LLVAILPEYV IGTVAGGTGT EDSHPPYKQT QPGADGFELQ HPYVLDAGIP ISQLTICPHQ WINLRTNNCA TIIVPYMNTL PFDSALNHCN FGLLVVPISP LDFDQGATPV IPITITLAPM CSEFAGLRQA VTQGFPTEPK PGTNQFLTTD DGVSAPILPN FHPTPCIHIP GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA GKGELCAVFR ADPGRDGPWQ STMLGQLCGY YTQWSGSLEV TFMFTGSFMA TGKMLIAYTP PGGPLPKDRA TAMLGTHVIW DFGLQSSVTL VIPWISNTHY RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYIIAL AAAQKNFTMK LCKDTSHILQ TASIQGDRVA DVIESSIGDS VSRALTQALP APTGQNTQVS SHRLDTGEVP ALQAAEIGAS SNTSDESMIE TRCVLNSHST AETTLDSFFS RAGLVGEIDL PLEGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF TFVACTPTGQ VVPQLLQYMF VPPGAPKPDS RESLAWQTAT NPSVFVKLTD PPAQVSVPFM SPASAYQWFY DGYPTFGEHK QEKDLEYGAC PNNMMGTFSV RTVGSSKSKY PLVVRIYMRM KHVRAWIPRP MRNQNYLFKA NPNYAGNSIK PTGTSRTAIT TLGKFGQQSG AIYVGNFRVV NRHLATHNDW ANLVWEDSSR DLLVSSTTAQ GCDTIARCDC QTGVYYCNSK RKHYPVSFSK PSLIYVDASE YYPARYQSHL MLAVGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR DLLWLDEEAM EQGVSDYIKG LGDAFGTGFT DAVSREVEAL RNHLIGSDGA VEKILKNLIK LISALVIVIR SDYDMVTLTA TLALIGCHGS PWAWIKAKTA SILGIPIAQK QSASWLKKFN DMASAAKGLE WISNKISKFI DWLREKIVPA AREKAEFLTN LKQLPLLENQ ITNLEQSAAS QEDLEAMFGN VSYLAHFCRK FQPLYATEAK RVYVLEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT GIIARAIADK YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL FCQMVSTVDF IPPMASLEEK GVSFTSKFVI ASTNASNIIV PTVSDSDAIR RRFYMDCDIE VTDSYKTELG RLDAGRAAKL CSENNTANFK RCSPLVCGKA IQLRDRKSKV RYSVDTVVSE LIREYNSRSA IGNTIEALFQ GPPKFRPIRI SLEEKPAPDA ISDLLASVDS EEVRQYCREQ GWIIPETPTN VERHLNRAVL VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQVLKKP VLRTATVQGP SLDFALSLLR RNIRQVQTDQ GHFTMLGVRD RLAVLPRHAQ PGKTIWVEHK LVNVLDAIEL VDEQGVNLEL TLVTLDTNEK FRDVTKFIPE TISGASDATL VINTEHMPSM FVPVGDVVQY GFLNLSGKPT HRTMMYNFPT KAGQCGGVVT SVGKIVGIHI GGNGRQGFCA GLKRSYFAST QGEIQWVKPN KETGRLNING PTHTKLEPSV FHDVFEGNKE PAVLTSKDPR LEVDFEQALF SKYVGNVLHE PDEYVTQAAL HYANQLKQLD INTSKMSMEE ACYGTENLEA IDLCTSAGYP YSALGIRKRD ILNPVTRDVS KMKLYMDKYG LDLPYSTYVK DELRSLDKIK KGKSRLIEAS SLNDSVYLRM TFGHLYEVFH ANPGTVTGSA VGCNPDVFWS KLPILLPGAL FAFDYSGYDA SLSPVWFRAL EIVLREIGYP EEAVSLIEGI NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRTL LIKTFKGIDL DELNMVAYGD DVLASYPFPI DCLELAKTGK EYGLTMTPAD KSPCFNEVTW ENATFLKRGF LPDYQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC LLAWHNGKDE YEKFVSTIRS VPVGKALAIP NFENLRRNWL ELF //