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POLN_EEEV8
ID   POLN_EEEV8              Reviewed;        2474 AA.
AC   Q306W8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Polyprotein P1234;
DE            Short=P1234;
DE   AltName: Full=Non-structural polyprotein;
DE   Contains:
DE     RecName: Full=Polyprotein P123';
DE              Short=P123';
DE   Contains:
DE     RecName: Full=Polyprotein P123;
DE              Short=P123;
DE   Contains:
DE     RecName: Full=mRNA-capping enzyme nsP1;
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:P36328};
DE              EC=2.7.7.- {ECO:0000250|UniProtKB:P36328};
DE     AltName: Full=Non-structural protein 1;
DE   Contains:
DE     RecName: Full=Protease nsP2;
DE              EC=3.1.3.33 {ECO:0000250|UniProtKB:P08411};
DE              EC=3.4.22.- {ECO:0000250|UniProtKB:P27282};
DE              EC=3.6.1.15 {ECO:0000250|UniProtKB:Q8JUX6};
DE              EC=3.6.4.13 {ECO:0000250|UniProtKB:Q8JUX6};
DE     AltName: Full=Non-structural protein 2;
DE              Short=nsP2;
DE   Contains:
DE     RecName: Full=Non-structural protein 3';
DE              Short=nsP3';
DE              EC=3.1.3.84 {ECO:0000250|UniProtKB:P27282};
DE   Contains:
DE     RecName: Full=Non-structural protein 3;
DE              Short=nsP3;
DE              EC=3.1.3.84 {ECO:0000250|UniProtKB:P27282};
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase nsP4;
DE              EC=2.7.7.19 {ECO:0000250|UniProtKB:P03317};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=Non-structural protein 4;
DE              Short=nsP4;
OS   Eastern equine encephalitis virus (strain PE-3.0815) (EEEV) (Eastern equine
OS   encephalomyelitis virus).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=374597;
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9126; Passeriformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Kondig J.P., Turell M.J., Lee J.S., O'Guinn M.L., Wasieloski L.P. Jr.;
RT   "Eastern equine encephalomyelitis virus strain.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral
CC       replicase, which is activated by cleavages carried out by the viral
CC       protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.
CC   -!- FUNCTION: [Polyprotein P123]: The early replication complex formed by
CC       the polyprotein P123 and nsP4 synthesizes the minus-strand RNAs
CC       (antigenome) (By similarity). Polyprotein P123 is a short-lived
CC       polyprotein that accumulates during early stage of infection
CC       (Probable). As soon P123 is cleaved into mature proteins, the plus-
CC       strand RNAs synthesis begins (By similarity).
CC       {ECO:0000250|UniProtKB:P03317, ECO:0000305}.
CC   -!- FUNCTION: [Polyprotein P123']: The early replication complex formed by
CC       the polyprotein P123' and nsP4 synthesizes minus-strand RNAs
CC       (antigenome) (Probable). Polyprotein P123' is a short-lived polyprotein
CC       that accumulates during early stage of infection (Probable). As soon
CC       P123' is cleaved into mature proteins, the plus-strand RNAs synthesis
CC       begins (Probable). {ECO:0000305}.
CC   -!- FUNCTION: [mRNA-capping enzyme nsP1]: Cytoplasmic capping enzyme that
CC       catalyzes two virus-specific reactions: methyltransferase and nsP1
CC       guanylyltransferase (By similarity). mRNA-capping is necessary since
CC       all viral RNAs are synthesized in the cytoplasm, and host capping
CC       enzymes are restricted to the nucleus (Probable). The enzymatic
CC       reaction involves a covalent link between 7-methyl-GMP and nsP1,
CC       whereas eukaryotic capping enzymes form a covalent complex only with
CC       GMP (Probable). NsP1 capping consists in the following reactions: GTP
CC       is first methylated into 7-methyl-GMP and then is covalently linked to
CC       nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is
CC       transferred to the mRNA to create the cap structure (By similarity).
CC       NsP1 is also needed for the initiation of the minus-strand RNAs
CC       synthesis (By similarity). Probably serves as a membrane anchor for the
CC       replication complex composed of nsP1-nsP4 (By similarity). Nsp1 is
CC       needed for the initiation of the minus-strand RNAs synthesis (By
CC       similarity). Palmitoylated nsP1 is remodeling host cell cytoskeleton,
CC       and induces filopodium-like structure formation at the surface of the
CC       host cell (By similarity). {ECO:0000250|UniProtKB:P03317,
CC       ECO:0000250|UniProtKB:P08411, ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q8JUX6, ECO:0000305}.
CC   -!- FUNCTION: [Protease nsP2]: Multifunctional protein whose N-terminus is
CC       part of the RNA polymerase complex and displays NTPase, RNA
CC       triphosphatase and helicase activities (By similarity). NTPase and RNA
CC       triphosphatase are involved in viral RNA capping and helicase keeps a
CC       check on the dsRNA replication intermediates (By similarity). The C-
CC       terminus harbors a protease that specifically cleaves the polyproteins
CC       and releases the mature proteins (By similarity). Required for the
CC       shutoff of minus-strand RNAs synthesis (By similarity). Inhibits host
CC       translation to ensure maximal viral gene expression and evade host
CC       immune response (By similarity). {ECO:0000250|UniProtKB:P03317,
CC       ECO:0000250|UniProtKB:P08411, ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q8JUX6}.
CC   -!- FUNCTION: [Non-structural protein 3]: Seems to be essential for minus-
CC       strand RNAs and subgenomic 26S mRNAs synthesis (By similarity).
CC       Displays mono-ADP-ribosylhydrolase activity (By similarity). ADP-
CC       ribosylation is a post-translational modification that controls various
CC       processes of the host cell and the virus probably needs to revert it
CC       for optimal viral replication (By similarity). Binds proteins of FXR
CC       and G3BP families and sequesters them into the viral RNA replication
CC       complexes thereby inhibiting the formation of host stress granules on
CC       viral mRNAs (By similarity). The nsp3-FXR and nsp3-G3BP complexes bind
CC       viral RNAs and probably orchestrate the assembly of viral replication
CC       complexes, thanks to the ability of G3BP and FXR family members to
CC       self-assemble and bind DNA (By similarity).
CC       {ECO:0000250|UniProtKB:P03317, ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q4QXJ8}.
CC   -!- FUNCTION: [Non-structural protein 3']: Seems to be essential for minus-
CC       strand RNAs and subgenomic 26S mRNAs synthesis (By similarity).
CC       Displays mono-ADP-ribosylhydrolase activity (Probable). ADP-
CC       ribosylation is a post-translational modification that controls various
CC       processes of the host cell and the virus probably needs to revert it
CC       for optimal viral replication (Probable). Binds proteins of FXR and
CC       G3BP families and sequesters them into the viral RNA replication
CC       complexes thereby inhibiting the formation of host stress granules on
CC       viral mRNAs (Probable). The nsp3'-FXR and nsp3-G3BP complexes bind
CC       viral RNAs and probably orchestrate the assembly of viral replication
CC       complexes, thanks to the ability of G3BP and FXR family members to
CC       self-assemble and bind DNA (Probable). {ECO:0000250|UniProtKB:P03317,
CC       ECO:0000305}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase nsP4]: RNA dependent RNA
CC       polymerase (By similarity). Replicates genomic and antigenomic RNA by
CC       recognizing replications specific signals. The early replication
CC       complex formed by the polyprotein P123 and nsP4 synthesizes minus-
CC       strand RNAs (By similarity). The late replication complex composed of
CC       fully processed nsP1-nsP4 is responsible for the production of genomic
CC       and subgenomic plus-strand RNAs (By similarity).
CC       {ECO:0000250|UniProtKB:P03317}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-
CC         L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133;
CC         Evidence={ECO:0000250|UniProtKB:P27282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[nsP1 protein]-L-histidine + N(7)-methyl-GTP = [nsP1 protein]-
CC         N(tele)-(N(7)-methylguanosine 5'-phospho)-L-histidine + diphosphate;
CC         Xref=Rhea:RHEA:54792, Rhea:RHEA-COMP:13994, Rhea:RHEA-COMP:13995,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:33019, ChEBI:CHEBI:87133,
CC         ChEBI:CHEBI:138334; Evidence={ECO:0000250|UniProtKB:P27282};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54793;
CC         Evidence={ECO:0000250|UniProtKB:P27282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[nsP1 protein]-N(tele)-(N(7)-methylguanosine 5'-phospho)-L-
CC         histidine + a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+)
CC         = [nsP1 protein]-L-histidine + a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(purine-ribonucleoside) in mRNA;
CC         Xref=Rhea:RHEA:54800, Rhea:RHEA-COMP:12925, Rhea:RHEA-COMP:13929,
CC         Rhea:RHEA-COMP:13994, Rhea:RHEA-COMP:13995, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:133968, ChEBI:CHEBI:138276,
CC         ChEBI:CHEBI:138334; Evidence={ECO:0000250|UniProtKB:P27282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a
CC         5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33;
CC         Evidence={ECO:0000250|UniProtKB:P08411};
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:0000250|UniProtKB:Q8JUX6};
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:0000250|UniProtKB:Q8JUX6};
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=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose
CC         + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA-
CC         COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967,
CC         ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:P27282};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429;
CC         Evidence={ECO:0000250|UniProtKB:P27282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose
CC         + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA-
CC         COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967,
CC         ChEBI:CHEBI:142540; Evidence={ECO:0000250|UniProtKB:P27282};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249;
CC         Evidence={ECO:0000250|UniProtKB:P27282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC         Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC         ChEBI:CHEBI:173115; EC=2.7.7.19;
CC         Evidence={ECO:0000250|UniProtKB:P03317};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-beta-D-ribose 1''-phosphate + H2O = ADP-D-ribose +
CC         phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84;
CC         Evidence={ECO:0000250|UniProtKB:P36328};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25030;
CC         Evidence={ECO:0000250|UniProtKB:P36328};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P03317};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P03317};
CC       Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis
CC       at 60% of the levels observed with Mg(2+).
CC       {ECO:0000250|UniProtKB:P03317};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P03317};
CC       Note=For nsP4 RNA-directed RNA polymerase activity.
CC       {ECO:0000250|UniProtKB:P03317};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P27282};
CC       Note=For nsP1 guanylylation. {ECO:0000250|UniProtKB:P27282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=For nsP2 RNA triphosphatase activity.
CC       {ECO:0000250|UniProtKB:Q8JUX6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=For nsP2 NTPase activity. {ECO:0000250|UniProtKB:Q8JUX6};
CC   -!- ACTIVITY REGULATION: [mRNA-capping enzyme nsP1]: Inhibited by
CC       sinefungin. {ECO:0000250|UniProtKB:P27282}.
CC   -!- SUBUNIT: [mRNA-capping enzyme nsP1]: Interacts with non-structural
CC       protein 3 (By similarity). Interacts with RNA-directed RNA polymerase
CC       nsP4 (By similarity). Interacts with protease nsP2 (By similarity).
CC       interacts with itself (By similarity). {ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q4QXJ8, ECO:0000250|UniProtKB:Q8JUX6}.
CC   -!- SUBUNIT: [Non-structural protein 3]: Interacts with mRNA-capping enzyme
CC       nsP1 (By similarity). Interacts with host DDX1 (By similarity).
CC       Interacts with host DDX3 (By similarity). Interacts (via C-terminus)
CC       with host FXR1; this interaction inhibits the formation of host stress
CC       granules on viral mRNAs and the nsp3-FXR1 complexes bind viral RNAs and
CC       probably orchestrate the assembly of viral replication complexes (By
CC       similarity). Interacts (via C-terminus) with host FXR2; this
CC       interaction inhibits the formation of host stress granules on viral
CC       mRNAs and the nsp3-FXR2 complexes bind viral RNAs and probably
CC       orchestrate the assembly of viral replication complexes (By
CC       similarity). Interacts (via C-terminus) with host FMR1; this
CC       interaction inhibits the formation of host stress granules on viral
CC       mRNAs and the nsp3-FMR1 complexes bind viral RNAs and probably
CC       orchestrate the assembly of viral replication complexes (By
CC       similarity). Interacts (via C-terminus) with host G3BP1; this
CC       interaction inhibits the formation of host stress granules on viral
CC       mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably
CC       orchestrate the assembly of viral replication complexes (By
CC       similarity). Interacts (via C-terminus) with host G3BP2; this
CC       interaction inhibits the formation of host stress granules on viral
CC       mRNAs and the nsp3-G3BP2 complexes bind viral RNAs and probably
CC       orchestrate the assembly of viral replication complexes (By
CC       similarity). {ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q4QXJ8, ECO:0000250|UniProtKB:Q8JUX6}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase nsP4]: Interacts with mRNA-
CC       capping enzyme nsP1 (By similarity). Interacts with protease nsP2 (By
CC       similarity). interacts with itself (By similarity).
CC       {ECO:0000250|UniProtKB:P27282, ECO:0000250|UniProtKB:Q4QXJ8,
CC       ECO:0000250|UniProtKB:Q8JUX6}.
CC   -!- SUBUNIT: [Protease nsP2]: Interacts with RNA-directed RNA polymerase
CC       nsP4 (By similarity). Interacts with mRNA-capping enzyme nsP1 (By
CC       similarity). Interacts with KPNA1/karyopherin-alpha1; this interaction
CC       probably allows the active transport of protease nsP2 into the host
CC       nucleus (By similarity). {ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q4QXJ8, ECO:0000250|UniProtKB:Q8JUX6}.
CC   -!- SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle
CC       membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC       Note=Part of cytoplasmic vesicles, which are probably formed at the
CC       plasma membrane and internalized leading to late endosomal/lysosomal
CC       spherules containing the replication complex. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Polyprotein P123']: Host cytoplasmic vesicle
CC       membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC       Note=Part of cytoplasmic vesicles, which are probably formed at the
CC       plasma membrane and internalized leading to late endosomal/lysosomal
CC       spherules containing the replication complex. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Polyprotein P123]: Host cytoplasmic vesicle
CC       membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC       Note=Part of cytoplasmic vesicles, which are probably formed at the
CC       plasma membrane and internalized leading to late endosomal/lysosomal
CC       spherules containing the replication complex. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [mRNA-capping enzyme nsP1]: Host cytoplasmic
CC       vesicle membrane {ECO:0000250|UniProtKB:P08411}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P08411}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P08411}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P08411}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P08411}. Host cell projection, host filopodium
CC       {ECO:0000250|UniProtKB:P08411}. Note=In the late phase of infection,
CC       the polyprotein is quickly cleaved before localization to cellular
CC       membranes. Then a fraction of nsP1 localizes to the inner surface of
CC       the plasma membrane and its filopodial extensions. Only the
CC       palmitoylated nsP1 localizes to the host filopodia (By similarity).
CC       NsP1 is also part of cytoplasmic vesicles, which are probably formed at
CC       the plasma membrane and internalized leading to late
CC       endosomal/lysosomal spherules containing the replication complex (By
CC       similarity). {ECO:0000250|UniProtKB:P08411}.
CC   -!- SUBCELLULAR LOCATION: [Protease nsP2]: Host cytoplasmic vesicle
CC       membrane {ECO:0000250|UniProtKB:P08411}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P08411}. Host nucleus
CC       {ECO:0000250|UniProtKB:P27282}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P27282}. Note=In the late phase of infection,
CC       the polyprotein is quickly cleaved before localization to cellular
CC       membranes. Then approximately half of nsP2 is found in the nucleus (By
CC       similarity). Shuttles between cytoplasm and nucleus (By similarity).
CC       NsP2 is also part of cytoplasmic vesicles, which are probably formed at
CC       the plasma membrane and internalized leading to late
CC       endosomal/lysosomal spherules containing the replication complex (By
CC       similarity). {ECO:0000250|UniProtKB:P08411,
CC       ECO:0000250|UniProtKB:P27282}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host cytoplasmic
CC       vesicle membrane {ECO:0000250|UniProtKB:P03317}; Peripheral membrane
CC       protein {ECO:0000305}. Note=In the late phase of infection, the
CC       polyprotein is quickly cleaved before localization to cellular
CC       membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By
CC       similarity). NsP3 is also part of cytoplasmic vesicles, which are
CC       probably formed at the plasma membrane and internalized leading to late
CC       endosomal/lysosomal spherules containing the replication complex (By
CC       similarity). {ECO:0000250|UniProtKB:P03317}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 3']: Host cytoplasmic
CC       vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000305}. Note=In the late phase of infection, the polyprotein is
CC       quickly cleaved before localization to cellular membranes. Then nsP3
CC       and nsP3' form aggregates in cytoplasm (By similarity). NsP3' is also
CC       part of cytoplasmic vesicles, which are probably formed at the plasma
CC       membrane and internalized leading to late endosomal/lysosomal spherules
CC       containing the replication complex (Probable).
CC       {ECO:0000250|UniProtKB:P03317, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase nsP4]: Host
CC       cytoplasmic vesicle membrane; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P08411}. Note=NsP4 is part of cytoplasmic
CC       vesicles, which are probably formed at the plasma membrane and
CC       internalized leading to late endosomal/lysosomal spherules containing
CC       the replication complex. {ECO:0000250|UniProtKB:P08411}.
CC   -!- DOMAIN: [Protease nsP2]: The N-terminus exhibits NTPase and RNA
CC       triphosphatase activities and is proposed to have helicase activity,
CC       whereas the C-terminus possesses protease activity (By similarity).
CC       Contains a nuclear localization signal and a nuclear export signal,
CC       these two motifs are probably involved in the shuttling between the
CC       cytoplasm and the nucleus of nsP2 (By similarity).
CC       {ECO:0000250|UniProtKB:P27282, ECO:0000250|UniProtKB:Q8JUX6}.
CC   -!- DOMAIN: [Non-structural protein 3]: In the N-terminus, the macro domain
CC       displays a mono-ADP-ribosylhydrolase activity (By similarity). The
CC       central part has a zinc-binding function (By similarity). The C-
CC       terminus contains two regions responsible for the formation of the
CC       nsP3/FXR and nsp3/G3BP complexes (By similarity).
CC       {ECO:0000250|UniProtKB:P03317, ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q4QXJ8}.
CC   -!- DOMAIN: [Non-structural protein 3']: In the N-terminus, the macro
CC       domain displays a mono-ADP-ribosylhydrolase activity (By similarity).
CC       The central part has a zinc-binding function (By similarity). The C-
CC       terminus contains two regions responsible for the formation of the
CC       nsP3'/FXR and nsp3'/G3BP complexes (By similarity).
CC       {ECO:0000250|UniProtKB:P03317, ECO:0000250|UniProtKB:P27282,
CC       ECO:0000250|UniProtKB:Q4QXJ8}.
CC   -!- PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield
CC       mature proteins (By similarity). The processing of the polyprotein is
CC       temporally regulated (By similarity). In early stages (1.7 hpi), P1234
CC       is first cleaved in trans through its nsP2 protease activity, releasing
CC       P123' and nsP4, which associate to form the early replication complex
CC       (By similarity). At the same time, P1234 is also cut at the nsP1/nsP2
CC       site early in infection but with lower efficiency (By similarity).
CC       After replication of the viral minus-strand RNAs (4 hpi), the
CC       polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very
CC       efficiently, preventing accumulation of P123' and P1234 and allowing
CC       the formation of the late replication complex (By similarity).
CC       NsP3'/nsP4 site is not cleaved anymore and P34 is produced rather than
CC       nsP4 (By similarity). {ECO:0000250|UniProtKB:P03317}.
CC   -!- PTM: [Polyprotein P123]: Specific enzymatic cleavages in vivo yield
CC       mature proteins (By similarity). The processing of the polyprotein is
CC       temporally regulated (By similarity). In early stages (1.7 hpi), P123
CC       is cleaved at the nsP1/nsP2 site with low efficiency (By similarity).
CC       After replication of the viral minus-strand RNAs (4 hpi), the
CC       polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very
CC       efficiently, preventing accumulation of P123 and allowing the formation
CC       of the late replication complex (By similarity).
CC       {ECO:0000250|UniProtKB:P03317}.
CC   -!- PTM: [Polyprotein P123']: Specific enzymatic cleavages in vivo yield
CC       mature proteins (By similarity). The processing of the polyprotein is
CC       temporally regulated (By similarity). In early stages (1.7 hpi), P123'
CC       is cleaved at the nsP1/nsP2 site with low efficiency (By similarity).
CC       After replication of the viral minus-strand RNAs (4 hpi), the
CC       polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very
CC       efficiently, preventing accumulation of P123' and allowing the
CC       formation of the late replication complex (By similarity).
CC       {ECO:0000250|UniProtKB:P03317}.
CC   -!- PTM: [mRNA-capping enzyme nsP1]: Palmitoylated by host
CC       palmitoyltransferases ZDHHC2 and ZDHHC19.
CC       {ECO:0000250|UniProtKB:P03317}.
CC   -!- PTM: [Non-structural protein 3]: Phosphorylated by host on serines and
CC       threonines. {ECO:0000250|UniProtKB:P08411}.
CC   -!- PTM: [Non-structural protein 3']: Phosphorylated by host on serines and
CC       threonines. {ECO:0000250|UniProtKB:P08411}.
CC   -!- PTM: [RNA-directed RNA polymerase nsP4]: Ubiquitinated; targets the
CC       protein for rapid degradation via the ubiquitin system (By similarity).
CC       Nsp4 is present in extremely low quantities due to low frequency of
CC       translation through the amber stop-codon and the degradation by the
CC       ubiquitin pathway (By similarity). {ECO:0000250|UniProtKB:P03317}.
CC   -!- MISCELLANEOUS: Viral replication produces dsRNA in the late phase of
CC       infection, resulting in a strong activation of host EIF2AK2/PKR,
CC       leading to almost complete phosphorylation of EIF2A (By similarity).
CC       This inactivates completely cellular translation initiation, resulting
CC       shutoff of host proteins synthesis (By similarity). However,
CC       phosphorylation of EIF2A is probably not the only mechanism responsible
CC       for the host translation shutoff (By similarity). The viral translation
CC       can still occur normally because it relies on a hairpin structure in
CC       the coding region of sgRNA and is EIF2A-, EIF2D-, EIF4G- EIF4A-
CC       independent (By similarity). {ECO:0000250|UniProtKB:P03317}.
CC   -!- MISCELLANEOUS: The genome codes for P123, but readthrough of a
CC       terminator codon UGA occurs between the codons for Asn-1856 and Arg-
CC       1858 giving rise to P1234 (Probable). P1234 is cleaved quickly by nsP2
CC       into P123' and nsP4 (By similarity). Further processing of p123' gives
CC       nsP1, nsP2 and nsP3' which is 6 amino acids longer than nsP3 since the
CC       cleavage site is after the readthrough (By similarity). This unusual
CC       molecular mechanism ensures that few nsP4 are produced compared to
CC       other non-structural proteins (By similarity). Mutant viruses with no
CC       alternative termination site grow significantly slower than wild-type
CC       virus (By similarity). The opal termination codon is frequently mutated
CC       to a sense codon on passage in cell culture (By similarity). The
CC       presence of the opal codon may be a requirement for viral maintenance
CC       in both vertebrate and invertebrate hosts and a selective advantage may
CC       be conferred in cell culture for the sense codon (By similarity).
CC       {ECO:0000250|UniProtKB:O90368, ECO:0000250|UniProtKB:P03317,
CC       ECO:0000305}.
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DR   EMBL; DQ241303; ABB45865.1; -; Genomic_RNA.
DR   MEROPS; C09.002; -.
DR   Proteomes; UP000008275; Genome.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044176; C:host cell filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
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:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   Gene3D; 3.40.220.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   Gene3D; 3.90.70.110; -; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR002620; Alphavirus_nsp2pro.
DR   InterPro; IPR044936; Alphavirus_nsp2pro_sf.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR044371; Macro_X_NSP3-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF01661; Macro; 1.
DR   Pfam; PF01707; Peptidase_C9; 1.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51154; MACRO; 1.
DR   PROSITE; PS51520; NSP2PRO; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host transcription shutoff by virus; GTP-binding; Helicase;
KW   Host cell membrane; Host cell projection; Host cytoplasm;
KW   Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW   Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host RNA polymerase II by virus; Lipoprotein; Membrane;
KW   Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Palmitate; Phosphoprotein; Protease; RNA suppression of termination;
KW   RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
KW   Thiol protease; Transferase; Ubl conjugation; Viral RNA replication; Zinc.
FT   CHAIN           1..2474
FT                   /note="Polyprotein P1234"
FT                   /id="PRO_0000308385"
FT   CHAIN           1..1866
FT                   /note="Polyprotein P123'"
FT                   /id="PRO_0000228753"
FT   CHAIN           1..1859
FT                   /note="Polyprotein P123"
FT                   /id="PRO_0000228754"
FT   CHAIN           1..533
FT                   /note="mRNA-capping enzyme nsP1"
FT                   /id="PRO_0000228755"
FT   CHAIN           534..1327
FT                   /note="Protease nsP2"
FT                   /id="PRO_0000228756"
FT   CHAIN           1328..1866
FT                   /note="Non-structural protein 3'"
FT                   /id="PRO_0000228757"
FT   CHAIN           1328..1859
FT                   /note="Non-structural protein 3"
FT                   /id="PRO_0000228758"
FT   CHAIN           1867..2474
FT                   /note="RNA-directed RNA polymerase nsP4"
FT                   /id="PRO_0000228759"
FT   DOMAIN          28..257
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          674..839
FT                   /note="(+)RNA virus helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          840..988
FT                   /note="(+)RNA virus helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          1001..1320
FT                   /note="Peptidase C9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00853"
FT   DOMAIN          1328..1486
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          2231..2346
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          242..261
FT                   /note="NsP1 membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P08411"
FT   REGION          1002..1021
FT                   /note="Nucleolus localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P08411"
FT   REGION          1773..1785
FT                   /note="Binding to host G3BP family members"
FT                   /evidence="ECO:0000250|UniProtKB:Q4QXJ8"
FT   REGION          1838..1854
FT                   /note="Binding to host FXR family members"
FT                   /evidence="ECO:0000250|UniProtKB:Q4QXJ8"
FT   MOTIF           1054..1063
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P27282"
FT   MOTIF           1177..1181
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P27282"
FT   ACT_SITE        1010
FT                   /note="For cysteine protease nsP2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00853"
FT   ACT_SITE        1079
FT                   /note="For cysteine protease nsP2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00853"
FT   BINDING         719..726
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   BINDING         1337
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:P36328"
FT   BINDING         1351
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
FT   BINDING         1359
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
FT   BINDING         1438
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:P36328"
FT   BINDING         1439
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:P36328"
FT   BINDING         1440
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
FT   BINDING         1589
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   BINDING         1591
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   BINDING         1614
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   BINDING         1632
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   SITE            37
FT                   /note="Involved in the phosphoramide link with 7-methyl-
FT                   GMP"
FT                   /evidence="ECO:0000250|UniProtKB:P27282"
FT   SITE            533..534
FT                   /note="Cleavage; by protease nsP2"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   SITE            1327..1328
FT                   /note="Cleavage; by protease nsP2"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   SITE            1866..1867
FT                   /note="Cleavage; by protease nsP2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
FT   LIPID           417
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
SQ   SEQUENCE   2474 AA;  276424 MW;  854E586BBCE980BD CRC64;
     MEKVHVDLDA DSPYVKLLQK CFPHFEIEAT QVTDNDHANA RAFSHLATKL IESEVDPDQV
     ILDIGSAPVR HTHSKHKYHC ICPMISAEDP DRLQRYADKL RKSDVTDRFI ASKAADLLTV
     MSTPDVETPS LCMHTDSTCR YHGTVAVYQD VYAVHAPTSI YHQALKGVRT IYWIGFDTTP
     FMYKNMAGAY PTYNTNWADE SVLEARNIGL CSSDLHEKRL GKISIMRKKK LQPTNKVVFS
     VGSTIYTEER ILLRSWHLPN VFHLKGKTSF TGRCNTIVSC DGYVVKKITI SPGIYGKVDN
     LASTLHREGF LSCKVTDTLR GERVSFPVCT YVPATLCDQM TGILATDVSV DDAQKLLVGL
     NQRIVVNGRT QRNTNTMQNY LLPVVAQAFS RWAREYRADL EDEKDLGVRE RSLVMGCCWA
     FKTHKITSIY KKPGTQTIKK VPAVFNSFVI PQFNSYGLNI GLRRRIKMLL EEKRKPAPII
     TEADVAHLKG MQEEAEAVAE AEAVRAALPP LLPEVERETI EADIDLIMQE AGAGSVETPR
     RHIKVTTYPG EETIGSYAVL SPQAVLNSEK LACIHPLAEQ VLVMTHKGRA GRYKVEPYHG
     RVVVPSGTAI PIPDFQALSE SATIVYNERE FVNRYLHHIA INGGAINTDE EYYKVLRSSE
     ADSEYVFDID ARKCVKKADA GPMCLVGELV DPPFHEFAYE SLKTRPAAPH KVPTIGVYGV
     PGSGKSGIIK SAVTKRDLVV SAKKENCTEI IKDVKRMRGM DIAARTVDSV LLNGVKHPVD
     TLYIDEAFAC HAGTLLALIA IVKPKKVVLC GDPKQCGFFN MMCLKVHFNH EICTEVYHKS
     ISRRCTKTVT AIVSTLFYDK RMRTVNPCSD KIIIDTTSTT KPQRDDIILT CFRGWVKQLQ
     IDYKNHEIMT AAASQGLTRK GVYAVRYKVN ENPLYAQTSE HVNVLLTRTE KRIVWKTLAG
     DPWIKTLTAH YPGEFSATLE EWQAEHDAIM ERILETPASS DVYQNKVHVC WAKALEPVLA
     TANITLTRSQ WETIPAFKDD KAFSPEMALN FLCTRFFGVD IDSGLFSAPT VPLTYTNEHW
     DNSPGPNRYG LCMRTAKELA RRYPCILKAV DTGRLADVRT NTIKDYSPLI NVVPLNRRLP
     HSLVVSHRYT GDGNYSQLLS KLIGKTVLVI GTPISVPGKR VETLGPGPQC TYKADLDLGI
     PSTIGKYDII FVNVRTPYKH HHYQQCEDHA IHHSMLTRKA VDHLNKGGTC VALGYGTADR
     ATENIISAVA RSFRFSRVCQ PKCAWENTEV AFVFFGKDNG NHLRDQDQLS IVLNNIYQGS
     TQYEAGRAPA YRVIRGDISK STDEAIVNAA NNKGQPGAGV CGALYKKWPG AFDKVPIATG
     TAHLVKHTPN IIHAVGPNFS RVSEVEGNQK LSEVYMDIAK IINRERYNKV SIPLLSTGIY
     AGGKDRVMQS LNHLFTAMDT TDADVTIYCL DKQWEARIKD AIARKESVEE LVEDDKPVDI
     ELVRVHPLSS LVGRPGYSTD EGKVHSYLEG TRFHQTAKDI AEIYAMWPNK QEANEQICLY
     VLGESMTSIR SKCPVEDSEA SSPPHTIPCL CNYAMTAERV YRLRMAKNEQ FAVCSSFQLP
     KYRITGVQKI QCNKPVIFSG VVPPAIHPRK FSAIEETVPV TIERLVPRRP APPVPVPARI
     PSPRCSPAVS MQSLGGSSTS DVVISEAEVH DSDSDCSIPP MPFVVEAEVH ASQGSHWSIP
     SASGFEIREL PEDRSISGSP TRTSVISDHS VNLITFDSVT DIFENFKQAP FQFLSEIRPI
     PAPRRRVGGF ETDTKRYDKT EEKPIPKPRT RTTKYKQPPG VARSISEAEL DEFIRRHSNX
     RYEAGAYIFS SETGQGHLQQ KSTRQCKLQN PILERSVHEK FYAPRLDLER EKLLQKKLQL
     CASEGNRSRY QSRKVENMKA ITAERLLQGI GAYLSAESQP VECYKVNYPV PIYSTTRSNR
     FSSADVAVRV CNLVLQENFP TVASYTITDE YDAYLDMVDG ASCCLDTATF CPAKLRSFPK
     KHSYLRPEIR SAVPSPIQNT LQNVLAAATK RNCNVTQMRE LPVLDSAAFN VECFKKYACN
     DEYWDTFKNN PIRLTTENVT QYVTKLKGPK AAALFAKTHN LQPLHEIPMD RFVMDLKRDV
     KVTPGTKHTE ERPKVQVIQA AEPLATAYLC GIHRELVRRL NAVLLPNIHT LFDMSAEDFD
     AIIAEHFQFG DAVLETDIAS FDKSEDDAIA MSALMILEDL GVDQALLDLI EAAFGNITSV
     HLPTGTRFKF GAMMKSGMFL TLFINTVVNI MIASRVLRER LTNSPCAAFI GDDNIVKGVK
     SDALMAERCA TWLNMEVKII DATVGVKAPY FCGGFIVVDQ VTGTACRVAD PLKRLFKLGK
     PLPLDDDQDG DRRRALYDEA LRWNRIGITD ELIKAVESRY EVFYISLVIT ALTTLAATVS
     NFKYIRGNPI TLYG
 
 
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