ID Q8V398_9ENTO Unreviewed; 2179 AA.
AC Q8V398;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 2.
DT 27-MAR-2024, entry version 142.
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 Enterovirus J.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus.
OX NCBI_TaxID=1330521 {ECO:0000313|EMBL:AAL68560.2, ECO:0000313|Proteomes:UP000326389};
RN [1] {ECO:0000313|EMBL:AAL68560.2, ECO:0000313|Proteomes:UP000326389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N125 {ECO:0000313|EMBL:AAL68560.2,
RC ECO:0000313|Proteomes:UP000326389};
RX PubMed=11773400;
RA Oberste M.S., Maher K., Pallansch M.A.;
RT "Molecular phylogeny and proposed classification of the simian
RT picornaviruses.";
RL J. Virol. 76:1244-1251(2002).
RN [2] {ECO:0000313|EMBL:AAL68560.2, ECO:0000313|Proteomes:UP000326389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N125 {ECO:0000313|EMBL:AAL68560.2,
RC ECO:0000313|Proteomes:UP000326389};
RX PubMed=18024906; DOI=10.1099/vir.0.83124-0;
RA Oberste M.S., Maher K., Pallansch M.A.;
RT "Complete genome sequences for nine simian enteroviruses.";
RL J. Gen. Virol. 88:3360-3372(2007).
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: 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 + H(+) + phosphate; 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=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); 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. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBUNIT: Interacts with RNA-directed RNA polymerase.
CC {ECO:0000256|ARBA:ARBA00011124}.
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: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. 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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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; AF414372; AAL68560.2; -; Genomic_RNA.
DR MEROPS; C03.011; -.
DR Proteomes; UP000326389; Genome.
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: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:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
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:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus 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:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd23213; Enterovirus_RdRp; 1.
DR CDD; cd00205; rhv_like; 3.
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; 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; 3.
DR Pfam; PF00910; RNA_helicase; 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 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 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 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|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}; Virion {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 1201..1359
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1535..1713
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 1944..2060
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2179 AA; 241674 MW; 87D11999F1C88063 CRC64;
MGAQISTQKS GSHETGTYAT GGSTINYTNI NYYKDSYAAS ASRQDFSQDP AKFTKPVVDA
LTEAAVPLKS PSAEACGYSD RVLQLTLGNS TITTQEAANI VVGYGKWPEH LKPIDANSID
APTKPDVAVN RFYTLKAKKW EKNSSGWMWK LPDCLNDTGV FGQNCWYHFL YRGGWAVHVQ
CNASKFHQGA LLVFLAPDFT RGAPTTTTTG TIPNVSYSDT MPGEDGTTFR NPLFLDNGTM
LQQATVFPHQ WINLRTNNSA TIIVPYINNI PADSPVRHNN WTLCVVPVVP LDYSDGATTV
VPVTVTLAPM CCEFDGLRNA VSQGLPVKAT PGSYQFLTTS DDCSEGLLPN FHSTPEIFIP
GQVNNLLELV QIETMMTINN VAAQSAGVER ISIPVSVQSD VDAQIAAFAV NPGGDGVFQS
TYLGQICRYF NNWSGSIEIT FMFCGSFMAT GKILIAYTPP GGSAPTDRKS AMLGTHIIWD
FGLQSSATLV IPWISNTCMR NVASLAYQDT YFAGGFVTMW YQTNFVVPAG APTTARIIAL
CAAKGDFCLR LLKDSTDITQ SAVLQNSPEA AIEGIINATV HNITPQNISS TEGSIGSAAP
ALQAAETGAT STATPEGMIE TRSVINRQHI AESSVESFYS RAGLVGIVQL QGTQSSTFTT
WVIDTMGFVQ QRRKLELFTY MRFDAEFTML VCADEEINPY NIQYMYVPPG SGVPSDHDSY
LWQSGTNPSI YVKSTDPPAQ FSIPFMSTCA AYAWFYDGYP RAYGNDAAQL NKSYGMLPAN
QFGTFCMRLL GSALKTNLTV RIYMRPKHVK CWAPRPFRML PYVEKNRPSY HTPPVDPIKN
RTNITTTGAF GQQSGSVYVG NYKITNLHLA NEFDKDNQVW SCYERDLIVS TTTAHGCDTI
ARCNCNTGVY FCKSTNKHYP VSFQGPGLTF IEANEYYPAR YQSHVLLAVG HAQPGDCGGI
LRCEHGVIGI VTAGGEGLVA FADLRDLLWL EDDAMEQGVS DYVQRLGSAF GAGFTNEIAE
KTQHIKEMLI GQDSVLEKCL KALIKIVSAM VILIRNHEDL ITVTATLALI GCSASPWQWL
KSKVCSYFQI PMVQKQADGW MKKFTEATNA AKGLEWLANK ISKFIDWVKS KIVPQVKEKL
EFLSKLKQLP LLESQIATIE HSAPSQEAQE TLHGNVQYLA HYCRKFAPLY AAEAKRVYHL
EKRMNNYMRF KTKSRIEPVC LLIHGSPGAG KSVVSSLVGR AIAEKMNSSV YSLPPDPDHF
DGYKQQAVVI MDDLCQNPDG KDVSLLCQMV STVDFIPPMA SLEEKGILYT SPFMIASTNH
GSISAPTISD SRALARRFFL DVDIFIHDEY KTETGKLNMP AACMHCNSCD PANFKRCCPI
ICGKALMFSD RRTSVRYTTD MLVSEMFREY SHRNSIGNVL EALFQGPPVY KELKISVAEE
VPPPPAIADL LKSVDSEEVR HYCESKGWII PATETNVERH INRAMTILQA VSTFVAVAGC
VFVVYKLFAG FQGAYTGLPF TKPKVPTIRQ AKVQGPNFEF AVAMMKRNSC IAKTGQGEFT
MLGIWDKWAV LPRHAKPGDS IIVDDKEVPV EDAKELVDSE GVNLELTLIK LRRNEKFRDI
RGFLPNEPGE IGDAVLAINT SRFPNMFIPV GKVTEYGFLN LSGTPTHRVL MYNFPTKSGQ
CGGVLMATGK VLGIHVGGNG HQGFAATLLR SYFNEEQGQI EWIETNKESG YPIINAPTKT
KLEPSVFHDI FEGKKEPAVL NPRDPRLKTD FEEAIFSKYV GNVNAHVDEY MKEAVDHYAG
QLLTLDINIE PLCLEDAVYG TDGLEALDLT TSAGYPYVTL GIKKRDILSK KTRDLSKLRE
CMDKYGLNLP MVTYVKDELR SREKVEQGKS RLIEASSLND SVAMRQTFGN LYRTFHNNPG
VMTGSAVGCN PDTFWSKIPV MLDGELFAFD YTGYDASLSP VWFAALKLVL EKLGYTSDET
KYIDYLCNSY HLYKNKHYFV RGGMPSGCSG TSIFNSMINN IIIRTLLLKT YKNIDLDKFR
MIAYGDDVIA SYPYPIDAGL LAKAGKEYGL TMTPADKSAT FNDVTWENVT FLKRYFRADE
QFNFLVHPVM PMKEIHESIR WTKDAKNTQE HVRSLCELAW HNGEEAYNEF LNKIRSVPVG
RCLLLPAYST LRRKWLDSF
//
