POLG_SAFV
ID POLG_SAFV Reviewed; 2295 AA.
AC C0MHL9;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Leader protein;
DE Short=L;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=VP4-VP2;
DE Contains:
DE RecName: Full=Capsid protein VP4;
DE AltName: Full=P1A;
DE AltName: Full=Rho;
DE AltName: Full=Virion protein 4;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE AltName: Full=Beta;
DE AltName: Full=P1B;
DE AltName: Full=Virion protein 2;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=Gamma;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Alpha;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.4.13;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=VPg;
DE Short=P3B;
DE AltName: Full=Protein 3B;
DE Contains:
DE RecName: Full=Protease 3C;
DE Short=P3C;
DE EC=3.4.22.28 {ECO:0000250|UniProtKB:P12296};
DE AltName: Full=Picornain 3C;
DE AltName: Full=p22;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=RdRp;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE AltName: Full=3D polymerase;
DE Short=3Dpol;
DE AltName: Full=Protein 3D;
DE Short=3D;
OS Saffold virus (SafV) (Human TMEV-like virus-Saffold).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Cardiovirus.
OX NCBI_TaxID=434309;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SafV-3 NL2007;
RX PubMed=19412527; DOI=10.1371/journal.ppat.1000416;
RA Zoll J., Erkens-Hulshof S., Lanke K., Verduyn-Lunel F., Melchers W.J.G.,
RA Schoondermark-van de Ven E., Roivainen M., Galama J.M.D.,
RA van Kuppeveld F.J.M.;
RT "Saffold virus, a human Theiler's-like cardiovirus, is ubiquitous and
RT causes infection early in life.";
RL PLoS Pathog. 5:E1000416-E1000416(2009).
RN [2]
RP INTERACTION WITH THE LEADER PROTEIN (PROTEIN 2A), INTERACTION WITH PROTEIN
RP 2A (LEADER PROTEIN), AND FUNCTION (PROTEIN 2A).
RX PubMed=25210192; DOI=10.1128/jvi.02148-14;
RA Petty R.V., Basta H.A., Bacot-Davis V.R., Brown B.A., Palmenberg A.C.;
RT "Binding interactions between the encephalomyocarditis virus leader and
RT protein 2A.";
RL J. Virol. 88:13503-13509(2014).
RN [3]
RP FUNCTION (LEADER PROTEIN).
RC STRAIN=SafV-2;
RX PubMed=26115166; DOI=10.1016/j.virol.2015.06.004;
RA Ciomperlik J.J., Basta H.A., Palmenberg A.C.;
RT "Three cardiovirus leader proteins equivalently inhibit four different
RT nucleocytoplasmic trafficking pathways.";
RL Virology 484:194-202(2015).
RN [4] {ECO:0007744|PDB:5A8F, ECO:0007744|PDB:5CFC, ECO:0007744|PDB:5CFD}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 647-898; 415-646 AND 154-411,
RP FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), FUNCTION
RP (CAPSID PROTEIN VP3), FUNCTION (CAPSID PROTEIN VP4), SUBCELLULAR LOCATION
RP (CAPSID PROTEIN VP1), SUBCELLULAR LOCATION (CAPSID PROTEIN VP2),
RP SUBCELLULAR LOCATION (CAPSID PROTEIN VP3), AND DISULFIDE BOND.
RC STRAIN=SafV-3;
RX PubMed=27279624; DOI=10.1128/jvi.00746-16;
RA Mullapudi E., Novacek J., Palkova L., Kulich P., Lindberg A.M.,
RA van Kuppeveld F.J., Plevka P.;
RT "Structure and Genome Release Mechanism of the Human Cardiovirus Saffold
RT Virus 3.";
RL J. Virol. 90:7628-7639(2016).
CC -!- FUNCTION: [Leader protein]: Forms a complex with host RAN and probably
CC binds to exportins carrying activated MAPK in order to mediate the
CC hyperphosphorylation of host Phe/Gly containing nuclear pore proteins
CC (Nups) resulting in cessation of active nucleocytoplasmic transport
CC (Probable). Proteins with NLS signals fail to import, cellular mRNAs
CC fail to export, and some proteins small enough for diffusion are not
CC retained anymore (efflux) (By similarity). The resulting inhibition of
CC cellular protein synthesis serves to ensure maximal viral gene
CC expression and to evade host immune response (By similarity).
CC {ECO:0000250|UniProtKB:Q66765, ECO:0000305|PubMed:26115166}.
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000269|PubMed:27279624}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000269|PubMed:27279624}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000269|PubMed:27279624}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (PubMed:27279624). After binding to the host receptor, the capsid
CC undergoes conformational changes (By similarity). Capsid protein VP4 is
CC released, capsid protein VP1 N-terminus is externalized, and together,
CC they shape a pore in the host membrane through which the viral genome
CC is translocated into the host cell cytoplasm. After genome has been
CC released, the channel shrinks (By similarity).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:27279624}.
CC -!- FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of
CC immature procapsids. {ECO:0000250|UniProtKB:P08617}.
CC -!- FUNCTION: [Protein 2A]: Involved in host translation shutoff by
CC inhibiting cap-dependent mRNA translation (By similarity). Nuclear
CC localization is required for this function (By similarity). The
CC resulting inhibition of cellular protein synthesis serves to ensure
CC maximal viral gene expression and to evade host immune response (By
CC similarity). Inhibits the phosphorylation of the leader protein
CC (PubMed:25210192). {ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:25210192}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and causes an
CC increase in membrane permeability. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes (By similarity). It displays
CC RNA-binding, nucleotide binding and NTPase activities (By similarity).
CC {ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P08545}.
CC -!- FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic
CC domain. {ECO:0000250}.
CC -!- FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the
CC polymerase for the initiation of RNA chains.
CC {ECO:0000250|UniProtKB:P03304}.
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 cooperatively bind to the
CC protease. Cleaves host PABP1, this cleavage is important for viral
CC replication (By similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and
CC antigenomic RNAs by recognizing replications specific signals (By
CC similarity). Performs VPg uridylylation (By similarity).
CC {ECO:0000250|UniProtKB:P12296}.
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:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000305};
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:0000255|PROSITE-ProRule:PRU01222};
CC -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (By similarity).
CC Interacts with the leader protein (PubMed:25210192).
CC {ECO:0000250|UniProtKB:P13899, ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:25210192}.
CC -!- SUBUNIT: [Leader protein]: Interacts with host RAN; the complex L-RAN
CC recruits cellular kinases responsible for the L-induced
CC nucleocytoplasmic trafficking inhibition (By similarity). The complex
CC L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS
CC (By similarity). Interacts with the protein 2A (PubMed:25210192).
CC Interacts with host RNASEL; this interaction prevents RNASEL activation
CC by its substrate 2'-5' oligoadenylates (By similarity).
CC {ECO:0000250|UniProtKB:P13899, ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:25210192}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000269|PubMed:27279624}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000269|PubMed:27279624}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000269|PubMed:27279624}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2A]: Host nucleus, host nucleolus
CC {ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are probably
CC autophagosome-like vesicles. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are probably
CC autophagosome-like vesicles. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; 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 probably autophagosome-like vesicles.
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC 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 probably autophagosome-like vesicles. {ECO:0000305}.
CC -!- DOMAIN: [Leader protein]: The Theilo and zinc-finger regions may both
CC play a role in the inhibition of host nucleocytoplasmic trafficking and
CC IRF-3 dimerization antagonism by the L protein.
CC {ECO:0000250|UniProtKB:P13899}.
CC -!- PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC protease in vivo yield a variety of precursors and mature proteins (By
CC similarity). The polyprotein seems to be cotranslationally cleaved at
CC the 2A/2B junction by a ribosomal skip from one codon to the next
CC without formation of a peptide bond (By similarity). This process would
CC release the P1-2A peptide from the translational complex (By
CC similarity). {ECO:0000250|UniProtKB:P03304}.
CC -!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
CC are rendered infectious following cleavage of VP0 into VP4 and VP2.
CC This maturation seems to be an autocatalytic event triggered by the
CC presence of RNA in the capsid and is followed by a conformational
CC change of the particle. {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [VPg]: 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. {ECO:0000250|UniProtKB:P12296}.
CC -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250|UniProtKB:Q66282}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
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DR EMBL; FM207487; CAR62533.1; -; Genomic_RNA.
DR PDB; 5A8F; EM; 10.60 A; A=680-898, C=154-411.
DR PDB; 5CFC; X-ray; 2.50 A; A=647-898, C=154-411.
DR PDB; 5CFD; X-ray; 2.50 A; A=647-898, B=415-646, C=154-411.
DR PDBsum; 5A8F; -.
DR PDBsum; 5CFC; -.
DR PDBsum; 5CFD; -.
DR SMR; C0MHL9; -.
DR Proteomes; UP000174252; Genome.
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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039707; P:pore formation by virus in membrane of 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:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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 CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 4.10.90.10; -; 1.
DR InterPro; IPR015031; Capsid_VP4_Picornavir.
DR InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
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; 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 Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 2.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF08935; VP4_2; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
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; ATP-binding; Capsid protein; Coiled coil;
KW Covalent protein-RNA linkage; Disulfide bond; Helicase; Host cytoplasm;
KW Host cytoplasmic vesicle; Host membrane; Host nucleus;
KW Host-virus interaction; Hydrolase; Ion channel; Ion transport; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW RNA-directed RNA polymerase; T=pseudo3 icosahedral capsid protein;
KW Thiol protease; Transferase; Transport; Viral attachment to host cell;
KW Viral ion channel; Viral RNA replication; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..2295
FT /note="Genome polyprotein"
FT /id="PRO_0000446206"
FT CHAIN 1..71
FT /note="Leader protein"
FT /id="PRO_0000446207"
FT CHAIN 72..414
FT /note="Capsid protein VP0"
FT /id="PRO_0000446208"
FT CHAIN 72..143
FT /note="Capsid protein VP4"
FT /id="PRO_0000446209"
FT CHAIN 144..414
FT /note="Capsid protein VP2"
FT /id="PRO_0000446210"
FT CHAIN 415..646
FT /note="Capsid protein VP3"
FT /id="PRO_0000446211"
FT CHAIN 647..917
FT /note="Capsid protein VP1"
FT /id="PRO_0000446212"
FT CHAIN 918..1050
FT /note="Protein 2A"
FT /id="PRO_0000446213"
FT CHAIN 1051..1186
FT /note="Protein 2B"
FT /id="PRO_0000446214"
FT CHAIN 1187..1511
FT /note="Protein 2C"
FT /id="PRO_0000446215"
FT CHAIN 1512..1597
FT /note="Protein 3A"
FT /id="PRO_0000446216"
FT CHAIN 1598..1617
FT /note="VPg"
FT /id="PRO_0000446217"
FT CHAIN 1618..1834
FT /note="Protease 3C"
FT /id="PRO_0000446218"
FT CHAIN 1835..2295
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000446219"
FT DOMAIN 1278..1443
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1628..1821
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2063..2181
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 3..14
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT REGION 30..46
FT /note="Acidic"
FT /evidence="ECO:0000305"
FT REGION 55..68
FT /note="Theilo"
FT /evidence="ECO:0000250|UniProtKB:P13899"
FT REGION 69..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1042
FT /note="Host EIF4E binding"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT ACT_SITE 1672
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1706
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1785
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2069
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2167
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1307..1314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 143..144
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 414..415
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 646..647
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 917..918
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1050..1051
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1186..1187
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1511..1512
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1597..1598
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1617..1618
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1834..1835
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT MOD_RES 1600
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 72
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q66282"
FT DISULFID 501..503
FT /evidence="ECO:0000269|PubMed:27279624"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5CFC"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:5CFC"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:5CFC"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 370..381
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 390..406
FT /evidence="ECO:0007829|PDB:5CFC"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:5CFD"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:5CFD"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5CFD"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 536..544
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:5CFD"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:5CFD"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 601..611
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 620..628
FT /evidence="ECO:0007829|PDB:5CFD"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:5CFD"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:5CFC"
FT TURN 661..664
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 679..683
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 687..694
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 738..743
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 754..758
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 762..779
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 782..788
FT /evidence="ECO:0007829|PDB:5CFC"
FT HELIX 806..808
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 809..812
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 814..819
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 824..830
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 835..842
FT /evidence="ECO:0007829|PDB:5CFC"
FT STRAND 866..889
FT /evidence="ECO:0007829|PDB:5CFC"
SQ SEQUENCE 2295 AA; 257300 MW; 508AA51941DD7718 CRC64;
MACKHGYPLL CPLCTALDIT PDGSFTLLFD NEWYPTDLLT VNLDDDVFYP LDTNMDWTDL
PLIQDIVMEP QGNSNSSDKN NSQSSGNEGV IINNYYSNQY QNSIDLSANA NGVGKENSKP
QGQLMNILGS AADAFKNIAP LLMDQNTEEM TNLSDRVSSD TAGNTATNTQ STVGRLFGFG
QRHKGKHPAS CADTATDKVL AAERYYTIKL ASWTKTQESF DHIRVPLPHA LAGENGGVFS
STLRRHYLCK CGWRIQVQCN ASQFHAGSLL VFMAPEFDTS NHSTEVEPRA DTAFKVDANW
QKHAQILTGH AYVNTTTKVN VPLALNHQNF WQWTTYPHQI LNLRTNTTCD LEVPYVNVCP
TSSWTQHANW TLVIAVLTPL QYSQGSATTI EITASIQPVK PVFNGLRHTV VNPQSPFPVT
VREHAGTFFS TTPDTTVPVY GNTISTPFDY MCGEFTDLLS LCKIPTFLGN LDSNKKRIPY
FSATNSTPAT PLVTYQVTLS CSCMANSMLA AVARNFNQYR GSLNYLFVFT GSAMTKGKFL
ISYTPPGAGE PKTLDQAMQA TYAIWDLGLN SSYNFTVPFI SPTHYRQTSY NTPTITSVDG
WLTVWQLTPL TYPLGVPNDS HILTLVSGGD DFTLRMPVTF TKYVPQGVDN AEKGKVSDDN
ASTDFVAEPV KLPENQTRVS FVYDRSTLSS VLQSTSDVSS KFTPSTAKNL QNSILLTPLP
SDIVNNSVLP EQERWISFAS PTTQKPPYKT KQDWNFIMFS PFTYYKCDLE VTLSKNDRET
ISSVVRYVPC GAPSDLSDQT MPQTPSLADT RDPHMWVVGQ GTTNQISFVI PYTSPLSVLP
SVWFNGFSNF DNSSRFGVAP NADFGRLLLQ GQGTFSVHYR YKKMRVFCPR PTVFIPWPNP
QDTKIKSVRP TPTLELQNPI SIYRVDLFIN FSDEIIQFTY KVHGRTVCQY EIPGFGLSRS
GRLLVCMGEK PCQLPISTPK CFYHIVFTGS RNSFGVSIYK ARYRPWKQPL HDELHDYGFS
TFTDFFKAVR DYHASYYKQR LQHDIETNPG PVQSVFQLQG GVLTKSQAPM SGLQSMLLRA
IGIEADCTEF TRAVNLITDL CNTWESAKTT LSSPEFWTKM VMRIVKMFAA SVLYLHNPDL
TTTVCLSLMA GIDILTNDSV FNWLSTKLSK FFHTPAPPIV PLLQQQSPIR EANDSFNLAK
NIEWAIKTIK RIVEWITSWF KQEETSPQAK LDKMLTDFPE HCNSILAMRN GRKAYTDCAS
AFKYFEQLYN LAVQCKRIPL ATLCEKFKNK HDHAVARPEP VVVVLRGNAG QGKSVTSQII
AQAVSKLSFG RQSVYSLPPD SDYLDGYENQ YSVIMDDLGQ NPDGEDFKVF CQMVSSTNFL
PNMAHLEKKG TPFTSNFIIA TTNLPKFRPV TVAHYPAVDR RITFDLTVEA GDECVTHNGM
LDVEKAFEEI PGKPQLDCFN TDCRLLHKRG VRFVCNRTKN IYNLQQVVKM VKSTIDNKVE
NLKKMNTLVA QSPGNDMDYV LTCLRQTNAA LQDQIDELQE AFNQAQERQN FLSDWLKVSA
IVFASIASLS AVCKLVSRFK NLVCPAPVQI QLSEGEQAAY SGGKKGEKQT LQVLDVQGGG
KIVAQAGNPV MDYEVNIAKN MVNPITFFYA DKAQVTQSCL LIKGHLFVVN RHVAETDWCA
FELKGTRHER DSVQMRSVNK SGMEVDLTFV KVVKGPLFKD NSKKFCSKDD DFPARNETVT
GIMNTGVPFV FTGKFLIGNQ PVNTTTGACF NHCIHYRATT HRGWCGSALI CHVNGKKAVY
AMHSAGGGGM AAATIITQEM IEAAEKALDC LTPQGAIVEI GIDTVVHVPR KTKLRRTVAH
PCFQPKFEPA VLSRYDPRTT KDVDQVAFSK HTTNLEELPS VFSMVAREYA TRVFTTIGKE
NKILTPEQAI LGLPGMDPME KDTSPGLPYT QQGLKRAQLV NFEQGTMVQN LKEAHTKLTE
GNYEDILYQS FLKDEIRPIE KIHEAKTRIV DVPPFHHCIW GRQLLGRFAS RFQTNPGLDL
GSAIGTDPDT DWTAFAFQLL QYKYVYDVDY SNFDASHSTA MFEVLIENFF TTENGFDERI
GDYLRSLAVS RHAFEERRVL VRGGLPSGCA ATSMLNTIIN NIVIRAALHL TYSNFEFDDI
KVLSYGDDLL IATNYQINFN LVKQRLAPFN YKITPANKTV EFPEISNLYE VTFLKRKFVR
YNSCLFKPQM DTENLKAMVS YCRPGTLKEK LNSIALLAVH SGKSVYDEIF DPFRRIGIII
PEHGTMLYRW LNLFR
