ID   POLG_HPE2W              Reviewed;        2179 AA.
AC   O73556;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein VP0;
DE     AltName: Full=P1AB;
DE     AltName: Full=Virion protein 0;
DE   Contains:
DE     RecName: Full=Capsid protein VP3;
DE     AltName: Full=P1C;
DE     AltName: Full=Virion protein 3;
DE   Contains:
DE     RecName: Full=Capsid protein VP1;
DE     AltName: Full=P1D;
DE     AltName: Full=Virion protein 1;
DE   Contains:
DE     RecName: Full=Protein 2A H-NC {ECO:0000303|PubMed:34315275};
DE              Short=P2A;
DE     AltName: Full=Protein 2A;
DE   Contains:
DE     RecName: Full=Protein 2B;
DE              Short=P2B;
DE   Contains:
DE     RecName: Full=Protein 2C;
DE              Short=P2C;
DE              EC=3.6.1.15 {ECO:0000250|UniProtKB:P03300};
DE   Contains:
DE     RecName: Full=Protein 3A;
DE              Short=P3A;
DE   Contains:
DE     RecName: Full=Viral protein genome-linked;
DE              Short=VPg;
DE     AltName: Full=Protein 3B;
DE              Short=P3B;
DE   Contains:
DE     RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE              Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE              EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE     AltName: Full=Picornain 3C;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE              Short=P3D-POL;
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
OS   Human parechovirus 2 (strain Williamson) (HPeV-2) (Echovirus 23).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Paavivirinae; Parechovirus; Parechovirus A.
OX   NCBI_TaxID=122962;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9820139; DOI=10.1099/0022-1317-79-11-2641;
RA   Ghazi F., Hughes P.J., Hyypiae T., Stanway G.;
RT   "Molecular analysis of human parechovirus type 2 (formerly echovirus 23).";
RL   J. Gen. Virol. 79:2641-2650(1998).
RN   [2]
RP   REVIEW.
RX   PubMed=34315275; DOI=10.1098/rsob.210008;
RA   Domanska A., Guryanov S., Butcher S.J.;
RT   "A comparative analysis of parechovirus protein structures with other
RT   picornaviruses.";
RL   Open Biol. 11:210008-210008(2021).
CC   -!- FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry together with capsid proteins VP1 and VP3 (By similarity).
CC       The capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC       capsid protein and enclosing the viral positive strand RNA genome (By
CC       similarity). Capsid proteins interact with host alpha-V/beta-3 integrin
CC       heterodimer to provide virion attachment target cell (By similarity).
CC       This attachment induces virion internalization predominantly through
CC       clathrin-mediated endocytosis (By similarity). Binds packaging signals
CC       present in the viral RNA (By similarity).
CC       {ECO:0000250|UniProtKB:Q66578, ECO:0000250|UniProtKB:Q8JV21}.
CC   -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry together with capsid proteins VP0 and VP1 (By similarity).
CC       The capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC       capsid protein and enclosing the viral positive strand RNA genome (By
CC       similarity). Capsid proteins interact with host alpha-V/beta-3 integrin
CC       heterodimer to provide virion attachment target cell (By similarity).
CC       This attachment induces virion internalization predominantly through
CC       clathrin-mediated endocytosis (By similarity). Binds packaging signals
CC       present in the viral RNA (By similarity).
CC       {ECO:0000250|UniProtKB:Q66578, ECO:0000250|UniProtKB:Q8JV21}.
CC   -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry together with capsid proteins VP0 and VP3 (By similarity).
CC       The capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC       capsid protein and enclosing the viral positive strand RNA genome (By
CC       similarity). Capsid proteins interact with host alpha-V/beta-3 integrin
CC       heterodimer to provide virion attachment target cell (By similarity).
CC       This attachment induces virion internalization predominantly through
CC       clathrin-mediated endocytosis (By similarity). Binds packaging signals
CC       present in the viral RNA (By similarity).
CC       {ECO:0000250|UniProtKB:Q66578, ECO:0000250|UniProtKB:Q8JV21}.
CC   -!- FUNCTION: [Protein 2A H-NC]: Is not a protease.
CC       {ECO:0000303|PubMed:34315275}.
CC   -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC       replication cycle by acting as a viroporin. Creates a pore in the host
CC       reticulum endoplasmic and as a consequence releases Ca2+ in the
CC       cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
CC       may trigger membrane trafficking and transport of viral ER-associated
CC       proteins to viroplasms, sites of viral genome replication.
CC       {ECO:0000250|UniProtKB:P03300}.
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:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protein 3A]: Localizes the viral replication complex to the
CC       surface of membranous vesicles (By similarity). It inhibits host cell
CC       endoplasmic reticulum-to-Golgi apparatus transport and causes the
CC       disassembly of the Golgi complex, possibly through GBF1 interaction (By
CC       similarity). This would result in depletion of MHC, trail receptors and
CC       IFN receptors at the host cell surface (By similarity). Plays an
CC       essential role in viral RNA replication by recruiting ACBD3 and PI4KB
CC       at the viral replication sites, thereby allowing the formation of the
CC       rearranged membranous structures where viral replication takes place
CC       (By similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:Q9YLG5}.
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 VPg-pUpU
CC       is then used as primer on the genomic RNA poly(A) by the RNA-dependent
CC       RNA polymerase to replicate the viral genome. Following genome release
CC       from the infecting virion in the cytoplasm, the VPg-RNA linkage is
CC       probably removed by host TDP2. During the late stage of the replication
CC       cycle, host TDP2 is excluded from sites of viral RNA synthesis and
CC       encapsidation, allowing for the generation of progeny virions.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC       proteins from the precursor polyprotein (By similarity). In addition to
CC       its proteolytic activity, it binds to viral RNA, and thus influences
CC       viral genome replication. RNA and substrate bind cooperatively to the
CC       protease (By similarity). {ECO:0000250|UniProtKB:P03304,
CC       ECO:0000250|UniProtKB:P12296}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase 3D-POL]: Replicates the viral
CC       genomic RNA on the surface of intracellular membranes. Covalently
CC       attaches UMP to a tyrosine of VPg, which is used to prime RNA
CC       synthesis. The positive stranded RNA genome is first replicated at
CC       virus induced membranous vesicles, creating a dsRNA genomic replication
CC       form. This dsRNA is then used as template to synthesize positive
CC       stranded RNA genomes. ss(+)RNA genomes are either translated,
CC       replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase 3D-POL]:
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:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY: [Protein 2C]:
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:0000250|UniProtKB:P03300};
CC   -!- CATALYTIC ACTIVITY: [Protease 3C]:
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:0000255|PROSITE-ProRule:PRU01222};
CC   -!- COFACTOR: [RNA-directed RNA polymerase 3D-POL]:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P03300};
CC       Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
CC       center. The magnesium ions are not prebound but only present for
CC       catalysis. {ECO:0000250|UniProtKB:P03300};
CC   -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 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. {ECO:0000250|UniProtKB:P03300}.
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. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
CC       capsid protein VP1 to form heterotrimeric protomers. Five protomers
CC       subsequently associate to form pentamers which serve as building blocks
CC       for the capsid. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 2C]: Homohexamer; forms a hexameric ring structure
CC       with 6-fold symmetry characteristic of AAA+ ATPases.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
CC       ACBD3 (By similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:Q66578}.
CC   -!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
CC       polymerase. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase 3D-POL]: Interacts with Viral
CC       protein genome-linked. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host
CC       cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC       {ECO:0000250|UniProtKB:Q66578}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2A H-NC]: Host cytoplasm
CC       {ECO:0000250|UniProtKB:Q66578}. Host nucleus, host nucleolus
CC       {ECO:0000250|UniProtKB:Q66578}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q66578}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q66578}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q66578}. Note=Probably localizes to the surface
CC       of intracellular membrane vesicles that are induced after virus
CC       infection as the site for viral RNA replication. These vesicles are
CC       derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q66578}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q66578}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q66578}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q66578}. Note=Probably localizes to the surface
CC       of intracellular membrane vesicles that are induced after virus
CC       infection as the site for viral RNA replication. These vesicles are
CC       derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q66578}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q66578}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q66578}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q66578}. Note=Probably localizes to the surface
CC       of intracellular membrane vesicles that are induced after virus
CC       infection as the site for viral RNA replication. These vesicles are
CC       derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q66578}.
CC   -!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host
CC       cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC       to the surface of intracellular membrane vesicles that are induced
CC       after virus infection as the site for viral RNA replication. These
CC       vesicles are derived from the endoplasmic reticulum (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: [Capsid protein VP0]: The N-terminus mediates the interactions
CC       among pentamers (By similarity). In order to facilitate delivery of the
CC       virus genome into the cytoplasm, the N-termini of VP0s have to be
CC       released from contacts between pentamers and exposed at the particle
CC       surface, resulting in capsid disruption (By similarity).
CC       {ECO:0000250|UniProtKB:Q66578}.
CC   -!- DOMAIN: [Capsid protein VP3]: The N-terminus binds RNA.
CC       {ECO:0000250|UniProtKB:Q8JV21}.
CC   -!- DOMAIN: [Protein 2A H-NC]: Contains a H-NC box.
CC       {ECO:0000303|PubMed:34315275}.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC       the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC       peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages yield mature proteins (By
CC       similarity). All cleavages are catalyzed by P3C (By similarity).
CC       {ECO:0000250|UniProtKB:Q8JV21}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ005695; CAA06679.1; -; Genomic_RNA.
DR   SMR; O73556; -.
DR   IntAct; O73556; 1.
DR   Proteomes; UP000000670; Segment.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA: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:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; 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; cd23217; Parechovirus_RdRp; 1.
DR   CDD; cd00205; rhv_like; 2.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR007053; LRAT_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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   InterPro; IPR009419; VPP_parechovir_P3A.
DR   InterPro; IPR009407; VPP_parechovir_P3B.
DR   Pfam; PF06344; Parecho_VpG; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF06363; Picorna_P3A; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 1.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   PRINTS; PR00918; CALICVIRUSNS.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51934; LRAT; 1.
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   ATP-binding; Capsid protein; Covalent protein-RNA linkage; Helicase;
KW   Host cytoplasm; Host cytoplasmic vesicle; Host membrane; Host nucleus;
KW   Host-virus interaction; Hydrolase; Ion channel; Ion transport; Lipoprotein;
KW   Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW   RNA-binding; RNA-directed RNA polymerase;
KW   T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW   Transport; Viral attachment to host cell; Viral ion channel;
KW   Viral RNA replication; Virion; Virus entry into host cell.
FT   CHAIN           1..289
FT                   /note="Capsid protein VP0"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039750"
FT   CHAIN           290..542
FT                   /note="Capsid protein VP3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039751"
FT   CHAIN           543..775
FT                   /note="Capsid protein VP1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039752"
FT   CHAIN           776..922
FT                   /note="Protein 2A H-NC"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039753"
FT   CHAIN           923..1044
FT                   /note="Protein 2B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039754"
FT   CHAIN           1045..1373
FT                   /note="Protein 2C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039755"
FT   CHAIN           1374..1490
FT                   /note="Protein 3A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039756"
FT   CHAIN           1491..1510
FT                   /note="Viral protein genome-linked"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039757"
FT   CHAIN           1511..1710
FT                   /note="Protease 3C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039758"
FT   CHAIN           1711..2179
FT                   /note="RNA-directed RNA polymerase 3D-POL"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039759"
FT   DOMAIN          786..881
FT                   /note="LRAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   DOMAIN          1156..1317
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1517..1707
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1944..2058
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   MOTIF           763..765
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        796
FT                   /note="For protein 2A H-NC"
FT                   /evidence="ECO:0000250|UniProtKB:P53816"
FT   ACT_SITE        865
FT                   /note="For protein 2A H-NC; Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P53816"
FT   ACT_SITE        1557
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1595
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1669
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1896
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   BINDING         1184..1191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   BINDING         1950
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1950
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         2044
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         2044
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   SITE            289..290
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            542..543
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            772..773
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            922..923
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            1044..1045
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            1373..1374
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            1490..1491
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            1516..1517
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   SITE            1710..1711
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:Q66578"
FT   MOD_RES         1493
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
SQ   SEQUENCE   2179 AA;  245874 MW;  96803C0BB8856664 CRC64;
     METIKSIADM ATGVTKTIDA TINSVNEIIT NTDNASGGDI LTKVADDASN ILGPNCYATT
     SEPENKDVVQ ATTTVNTTNL TQHPSAPTLP FTPDFSNVDT FHSMAYDTTT GSKNPNKLVR
     LTTHAWASTL QRGHQIDHVN LPVDFWDEQR KPAYGHAKYF AAVRCGFHFQ VQVNVNQGTA
     GSALVVYEPK PVVDYDKDLE FGAFTNLPHV LMNLAETTQA DLCIPYVADT NYVKTDSSDL
     GQLKVYVWTP LSIPSGSSNQ VDVTILGSLL QLDFQNPRVY GQNVDIYDTA PSKPIPLRKT
     KYLTMSTKYK WTRNKVDIAE GPGSMNMANV LSTTAAQSVA LVGERAFYDP RTAGSKSRFD
     DLVKISQLFS VMADSTTPSA NHGIDQKGYF KWSANSDPQA IVHRNLVHLN LFPNLKVFEN
     SYSYFRGSLI IRLSVYASTF NRGRLNGFFP NSSTDETSEI DNAIYTICDI GSDNSFEITI
     PYSFSTWMRK THGKPIGLFQ IEVLNRLTYN YSSPNEVYCI VQGKMGQDAK FFCPTGSLVT
     FQNSWGSQMD LTDPLCIEDS VEDCKQTITP TELGLTSAQD DGPLGNDKPN YFLNFKSMNV
     DIFTVSHTKV DNIFGRAWFA HVHDFTNDGL WRQGLEFPKE GHGALSLLFA YFTGELNIHV
     LFLSDRGFLR VGHTYDTETN RTNFLSSSGI ITVPAGEQMT LSVPSYSNKP LRTVRSSNAL
     GYLLCKPLLT GTSSGRIEIF LSLRCPNFFF PLPAPKPATR KYRGDLATWS DQSPYGRQGK
     KQLMKLAYLD RGFYKHYGIV VGDDVYQLDS DDIFKTALTG KAKFTKTRLT PDWVVEEECE
     LDYFRIKYLE SSVNSEHIFS VDNNCETIAK DIFGSHSLSQ HQQIGLIGTI LLTAGLMSTI
     KTPVNPTTIK EFFNHAIEGD EQGLSLLVQK CTTFFSSAAT ELLDNDLVKF IIKILVRILC
     YMVLYCHKPN ILTTACLSTL LVMDVTSSSV LSPSCKALMQ CLMDGDVKKL AEVVAESMSN
     TDDDEIKEQI CDTVKYTKQI LSNQGPFKGF NEISTAFRHI DWWIQTLLKI KDMVLSVFKP
     SVEKRAVEWL ERNKEHVCSI LDYASDIIVK SKDQTKMKTQ EFYQRYNDCL SKFKPIMAMC
     FRSCHNSISN TVYRLFQELA RIPNRMATQN DLIRVEPIGI WIQGEPGQGK SFLTHTLSKQ
     LQKTCGLQGI YTNPTASEFM DGYDNQDIHL IDDLGQTRKE RDIEMLCNCI SSDPDIVPMA
     HLEEKGKFYT SKLVIATTNK PDFSSTVLLD SGALRRRFPY IMHIRAAKHY SKSGKLNVSQ
     AMPHMSTGEC WEVSKNGRDW ETLKLKELID KITVDYKERI ANYNTWKKQL EDQTLDDLDD
     AVSYIKHNYP DAIPYIDEYL NIEMSTLIEQ MEAFIEPKPS VFKCFASRVG DKIKEASREV
     VKWFSDKLKS MLNFVERNKA WLTVVSAVTS AIGILLLVTK IFKKEESKDE RAYNPTLPVA
     KPKGTFPVSQ REFKNEAPYD GQLEHIISQM AYITGSTTGH ITHCAGYQHD EIILHGHSIK
     YLEQEEELTL HYKNKVFPIE QPSVTQVTLG GKPMDLAIVK CKLPFRFKKN SKYYTNKIGT
     ESMLIWMTEQ GIITKEVQRV HHSGGIKTRE GTESTKTISY TVKSCKGMCG GLLISKVEGN
     FKILGMHIAG NGEMGVAIPF NFLKNDMSDQ GIVTEVTPIQ PMYINTKSQI HKSPVYGAVE
     VKMGPAVLSK SDTRLEEPVD CLVKKSASKY RVNKFQVNNE LWQGVKACVK SKFREIFGVN
     GIVDMKTAIL GTSHVNSMDL STSAGYSFVK SGYKKKDLIC LEPFSVSPML EKLVQEKFHN
     LLKGNQITTI FNTCLKDELR KLDKIATGKT RCIEACEIDY CIVYRMIMME IYDKIYQTPC
     YYSGLAVGIN PYRDWHFMIN ALNDYNYEMD YSQYDGSLSS MLLWEAVQVL AYCHDSPDLV
     MQLHKPVIDS DHVVFNERWL IHGGMPSGSP CTTVLNSLCN LMMCIYTTNL ISPGIDCLPI
     VYGDDVILSL DKEIEPERLQ SIMAESFGAE VTGSRKDEPP SLKPRMEVEF LKRKPGYFPE
     STFIVGKLDT ENMIQHLMWM KNFSTFKQQL QSYLMELCLH GKDTYQHYVK ILNPYLKEWN
     IPVDDYEVVI GKLVPMVFD
//