ID   Q66338_9ENTO            Unreviewed;      2185 AA.
AC   Q66338;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 163.
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   Coxsackievirus B3.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX   NCBI_TaxID=12072 {ECO:0000313|EMBL:AAB59927.1};
RN   [1] {ECO:0000313|EMBL:AAB59927.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3027968; DOI=10.1016/0042-6822(87)90435-1;
RA   Lindberg A.M., Staalhandske P.O.K., Pettersson U.;
RT   "Genome of coxsackievirus B3.";
RL   Virology 156:50-63(1987).
RN   [2] {ECO:0000313|EMBL:AAB59927.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2157045;
RA   Klump W.M., Bergmann I., Mueller B.C., Ameis D., Kandolf R.;
RT   "Complete nucleotide sequence of infectious Coxsackievirus B3 cDNA: two
RT   initial 5' uridine residues are regained during plus-strand RNA
RT   synthesis.";
RL   J. Virol. 64:1573-1583(1990).
RN   [3] {ECO:0000313|EMBL:AAB59927.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tracy S., Chapman N.M., Tu Z.;
RT   "Coxsackievirus-B3 from an infectious cDNA copy of the genome is
RT   cardiovirulent in mice.";
RL   Arch. Virol. 122:398-409(1992).
RN   [4] {ECO:0000313|EMBL:AAV34213.1, ECO:0000313|Proteomes:UP000161976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20 {ECO:0000313|EMBL:AAV34213.1};
RX   PubMed=1310000; DOI=10.1007/BF01317202;
RA   Tracy S., Chapman N.M., Tu Z.;
RT   "Coxsackievirus B3 from an infectious cDNA copy of the genome is
RT   cardiovirulent in mice.";
RL   Arch. Virol. 122:399-409(1992).
RN   [5] {ECO:0000313|EMBL:AAV34213.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=20 {ECO:0000313|EMBL:AAV34213.1};
RA   Tracy S., Chapman N.M., Tu Z.;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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 (By similarity). Following
CC       genome release from the infecting virion in the cytoplasm, the VPg-RNA
CC       linkage is probably removed by host TDP2 (By similarity). During the
CC       late stage of the replication cycle, host TDP2 is excluded from sites
CC       of viral RNA synthesis and encapsidation, allowing for the generation
CC       of progeny virions. {ECO:0000256|ARBA:ARBA00024846}.
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: Component of immature procapsids, which is cleaved into
CC       capsid proteins VP4 and VP2 after maturation (By similarity). Allows
CC       the capsid to remain inactive before the maturation step.
CC       {ECO:0000256|ARBA:ARBA00025202}.
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: Homohexamer; forms a hexameric ring structure with 6-fold
CC       symmetry characteristic of AAA+ ATPases (By similarity). Interacts (via
CC       N-terminus) with host RTN3 (via reticulon domain); this interaction is
CC       important for viral replication (By similarity). Interacts with capsid
CC       protein VP3; this interaction may be important for virion
CC       morphogenesis. {ECO:0000256|ARBA:ARBA00026015}.
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 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}. Virion
CC       {ECO:0000256|ARBA:ARBA00004328}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00008303, ECO:0000256|RuleBase:RU364118}.
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DR   EMBL; M88483; AAB59927.1; -; mRNA.
DR   EMBL; AY752946; AAV34213.1; -; Genomic_RNA.
DR   MEROPS; C03.011; -.
DR   SABIO-RK; Q66338; -.
DR   Proteomes; UP000110494; Genome.
DR   Proteomes; UP000161976; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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: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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; 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; 4.10.80.10; Picornavirus coat protein VP4; 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; IPR036988; Pico_P1A_sf.
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   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   2: Evidence at transcript level;
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   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 mRNA nuclear export by virus
KW   {ECO:0000256|ARBA:ARBA00023197, ECO:0000256|RuleBase:RU364118};
KW   Inhibition of host RIG-I by virus {ECO:0000256|ARBA:ARBA00023090};
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          1205..1361
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51218"
FT   DOMAIN          1541..1719
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000259|PROSITE:PS51874"
FT   DOMAIN          1950..2066
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
SQ   SEQUENCE   2185 AA;  243560 MW;  0E804BFF517F63A6 CRC64;
     MGAQVSTQKT GAHETRLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP GKFTEPVKDI
     MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGVWPDY LKDSEATAED
     QPTQPDVATC RFYTLDSVQW QKTSPGWWWK LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ
     CNASKFHQGC LLVVCVPEAE MGCATLDNTP SSAELLGGDS AKEFADKPVA SGSNKLVQRV
     VYNAGMGVGV GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL
     DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD FQSPSAMPQY
     DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY QIPVRSNEGS GTQVFGFPLQ
     PGYSSVFSRT LLGEILNYYT HWSGSIKLTF MFCGSAMATG KFLLAYSPPG AGAPTKRVDA
     MLGTHVVWDV GLQSSCVLCI PWISQTHYRF VASDEYTAGG FITCWYQTNI VVPADAQSSC
     YIMCFVSACN DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA
     LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYK NSGAKRYAEW
     VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ NQDAQILTHQ IMYVPPGGPV
     PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI PFLSIGNAYS NFYDGWSEFS RNGVYGINTL
     NNMGTLYARH VNAGSTGPIK STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFRPSGVTT
     TRQSITTMTN TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTTHG
     CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL LAAGFSEPGD
     CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME QGVKDYVEQL GNALGSGFTN
     QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP
     WRWLKQKVSQ YYGIPMAERQ NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV
     REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR
     VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYSLPPD
     PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSPFVLA
     STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSVKTCD DECCPVNFKK
     CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS
     VAPETPPPPA IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF
     VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM MKRNSSRVKT
     EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK ELVDKDGTNL ELTLLKLNRN
     EKFRDIRGFL AKEEVEVNEA VLAINTSKFP NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF
     PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI
     NTPSKTKLEP SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA
     VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTKD
     LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE ASSLNDSVAM RQTFGNLYKT
     FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKMLLEKLG
     YTHKETNYID YLCNSHHLYR DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI
     DLDQFRMIAY GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNVTFLKR
     YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI
     RSVPVGRCLT LPAFSTLRRK WLDSF
//