ID   B3VQP5_9ENTO            Unreviewed;      2209 AA.
AC   B3VQP5;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 119.
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};
DE   Flags: Precursor;
OS   Poliovirus 1.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus C.
OX   NCBI_TaxID=12080 {ECO:0000313|EMBL:ACF16830.1};
RN   [1] {ECO:0000313|EMBL:ACF16830.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A649 {ECO:0000313|EMBL:ACF16830.1};
RX   PubMed=18596089; DOI=10.1128/JVI.00468-08;
RA   Odoom J.K., Yunus Z., Dunn G., Minor P.D., Martin J.;
RT   "Changes in population dynamics during long-term evolution of sabin type 1
RT   poliovirus in an immunodeficient patient.";
RL   J. Virol. 82:9179-9190(2008).
RN   [2] {ECO:0007829|PDB:3OL6, ECO:0007829|PDB:3OL8}
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1749-2209 IN COMPLEX WITH
RP   MANGANESE AND ZINC.
RX   PubMed=21148772; DOI=10.1073/pnas.1007626107;
RA   Gong P., Peersen O.B.;
RT   "Structural basis for active site closure by the poliovirus RNA-dependent
RT   RNA polymerase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:22505-22510(2010).
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 Viral protein genome-linked and with protein
CC       3CD. {ECO:0000256|ARBA:ARBA00011236}.
CC   -!- SUBUNIT: Interacts with capsid protein VP1 and capsid protein VP3 in
CC       the mature capsid. {ECO:0000256|ARBA:ARBA00011188}.
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 3AB and with RNA-directed RNA
CC       polymerase. {ECO:0000256|ARBA:ARBA00011876}.
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}.
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DR   EMBL; EU794964; ACF16830.1; -; Genomic_RNA.
DR   PDB; 3OL6; X-ray; 2.50 A; A/E/I/M=1749-2209.
DR   PDB; 3OL8; X-ray; 2.75 A; A/E/I/M=1749-2209.
DR   PDB; 3OL9; X-ray; 2.25 A; A/E/I/M=1749-2209.
DR   PDB; 3OLA; X-ray; 2.55 A; A/E/I/M=1749-2209.
DR   PDB; 3OLB; X-ray; 2.41 A; A/E/I/M=1749-2209.
DR   PDBsum; 3OL6; -.
DR   PDBsum; 3OL8; -.
DR   PDBsum; 3OL9; -.
DR   PDBsum; 3OLA; -.
DR   PDBsum; 3OLB; -.
DR   SMR; B3VQP5; -.
DR   MEROPS; C03.001; -.
DR   EvolutionaryTrace; B3VQP5; -.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3OL6, ECO:0007829|PDB:3OL8};
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   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, ECO:0007829|PDB:3OL6};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0007829|PDB:3OL6};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1232..1388
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51218"
FT   DOMAIN          1566..1744
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000259|PROSITE:PS51874"
FT   DOMAIN          1975..2090
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   BINDING         1911
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0007829|PDB:3OLA"
FT   BINDING         1922
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0007829|PDB:3OLA"
FT   BINDING         1981
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OL8"
FT   BINDING         1981
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OL8"
FT   BINDING         1982
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OL8"
FT   BINDING         1984
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0007829|PDB:3OLA"
FT   BINDING         1986
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0007829|PDB:3OLA"
FT   BINDING         2018
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OL6, ECO:0007829|PDB:3OL8"
FT   BINDING         2020
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OL9, ECO:0007829|PDB:3OLB"
FT   BINDING         2020
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OLA"
FT   BINDING         2029
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OL9, ECO:0007829|PDB:3OLB"
FT   BINDING         2029
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OL6, ECO:0007829|PDB:3OL8"
FT   BINDING         2076
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OL8"
FT   BINDING         2076
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:3OL8"
FT   BINDING         2077
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3OL8"
SQ   SEQUENCE   2209 AA;  246506 MW;  600D35C305FA54F6 CRC64;
     MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFAQDP SKFTEPIKDV
     LIKTSPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEY LRDSEANPVD
     QPTEPDVAAC RFYTLDTVSW TKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
     CNASKFHQGA LGVFAVPEMC LAGDSNTTNI YTSYQNANPG ERGGTFTNTF TPDNNQESPA
     RKFCPVDYLF GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM AKHNNWGIAI
     LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG SNQYLTADNF
     QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA TKKNTMEMYR VRLSDKPHTD
     DPILCLSLSP ASDPRLSHTM LGEILNYYTH WAGSLKFTFL FCGSMMATGK LLVSYAPPGA
     DPPKKRKEAM LGTHVIWDIG LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV
     VPLSTPREMD ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA
     TSRDALPNTE ASGPAHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS RSESSIESFF
     ARGACVAILT VDNSASTKNN DKLFAVWKIT YKDTVQLRRK LEFFTYSRFD MEFTFVVTAN
     FTETNNGHAL NQVYQIMYVP PGAPVPGKWD DYTWQTSSNP SIFYTYGTAP ARISVPYVGI
     SNAYSHFYDG FSKIPLKDQS AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL
     KPKHIRVWCP RPPRAVAYYG PGVDYKDGTL TPLPTKDLTT YGFGHQNKAV YTAGYKICNY
     HLATQEDLQN AVNVMWDRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK YYPVSFVGPT
     FQYMEANDYY PARYQSHMLI GHGFASPGDC GGILRCNHGV IGIITAGGEG LVAFSDIRDL
     YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ IGDKITELTN MVTSTITEKL LKNLIKIISS
     LVIITRNYED TTTVLATLAL LGCDASPWQW LRKKACDILE IPYVIKQGDS WLKKFTEACN
     AAKGLEWVSN KISKFIDWLK EKIIPQARDK LEFVTKLKQL EMLENQISTI HQSCPSQEHQ
     EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV CLLVHGSPGT
     GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV IMDDLNQNPD GADMKLFCQM
     VSTVEFIPPM ASLEEKGILF TSNYVLASTN SSRISPPTVA HSDALARRFA FDMDIQVMNE
     YSRDGKLNMA MATEMCKNCH QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE
     RNRRSNIGNC MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV
     NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP NKKPNVPTIR
     TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA ILPTHASPGE SIVIDGKEVE
     ILDAKALEDQ AGTNLEITII TLKRNEKFRD IRPHIPTQIT ETNDGVLIVN TNKYPNMYVP
     VGAVTEQGYL NLGGRQTART LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK
     RSYFTQSQGE IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT
     DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY GTDGLEALDL
     STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL PLVTYVKDEL RSKTKVEQGK
     SRLIEASSLN DSVAMRMAFG NLYAAFHKNP GVITGSAVGC DPDLFWSKIP VLMEEKLFAF
     DYTGYDASLS PAWFEALKMV LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG
     TSIFNSMINN LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL
     TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR WTKDPRNTQD
     HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST LYRRWLDSF
//