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POLN_EEVVM
ID   POLN_EEVVM              Reviewed;        2499 AA.
AC   Q9WJC7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 3.
DT   03-AUG-2022, entry version 131.
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   Venezuelan equine encephalitis virus (strain Mena II) (VEEV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=36384;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9268; Didelphis marsupialis (Southern opossum).
OH   NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=53535; Melanoconion.
OH   NCBI_TaxID=9272; Philander opossum (Gray four-eyed opossum).
OH   NCBI_TaxID=10162; Proechimys.
OH   NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9886206; DOI=10.4269/ajtmh.1998.59.952;
RA   Kinney R.M., Pfeffer M., Tsuchiya K.R., Chang G.J., Roehrig J.T.;
RT   "Nucleotide sequences of the 26S mRNAs of the viruses defining the
RT   Venezuelan equine encephalitis antigenic complex.";
RL   Am. J. Trop. Med. Hyg. 59:952-964(1998).
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       family and sequesters them into the viral RNA replication complexes
CC       thereby inhibiting the formation of host stress granules on viral mRNAs
CC       (By similarity). The nsp3-FXR complexes bind viral RNAs and probably
CC       orchestrate the assembly of viral replication complexes, thanks to the
CC       ability of FXR family members to self-assemble and bind DNA (By
CC       similarity). {ECO:0000250|UniProtKB:P03317,
CC       ECO:0000250|UniProtKB:P27282}.
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 family
CC       and sequesters them into the viral RNA replication complexes thereby
CC       inhibiting the formation of host stress granules on viral mRNAs
CC       (Probable). The nsp3'-FXR complexes bind viral RNAs and probably
CC       orchestrate the assembly of viral replication complexes, thanks to the
CC       ability of FXR family members to self-assemble and bind DNA (Probable).
CC       {ECO:0000250|UniProtKB:P03317, 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: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). {ECO:0000250|UniProtKB:P27282,
CC       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: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: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 a region necessary and sufficient for formation of
CC       the nsP3/FXR complex (By similarity). {ECO:0000250|UniProtKB:P03317,
CC       ECO:0000250|UniProtKB:P27282}.
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 a region necessary and sufficient for formation of
CC       the nsP3'/FXR complex (By similarity). {ECO:0000250|UniProtKB:P03317,
CC       ECO:0000250|UniProtKB:P27282}.
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 Gln-1885 and Arg-
CC       1887 giving rise to P1234. P1234 is cleaved quickly by nsP2 into P123'
CC       and nsP4 (By similarity). Further processing of p123' gives nsP1, nsP2
CC       and nsP3' which is 6 amino acids longer than nsP3 since the cleavage
CC       site is after the readthrough (By similarity). This unusual molecular
CC       mechanism ensures that few nsP4 are produced compared to other non-
CC       structural proteins (By similarity). Mutant viruses with no alternative
CC       termination site grow significantly slower than wild-type virus (By
CC       similarity). The opal termination codon is frequently mutated to a
CC       sense codon on passage in cell culture (By similarity). The presence of
CC       the opal codon may be a requirement for viral maintenance in both
CC       vertebrate and invertebrate hosts and a selective advantage may be
CC       conferred in cell culture for the sense codon (By similarity).
CC       {ECO:0000250|UniProtKB:O90368, ECO:0000250|UniProtKB:P03317}.
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DR   EMBL; AF075252; AAD14552.1; -; Genomic_RNA.
DR   MEROPS; C09.002; -.
DR   PRIDE; Q9WJC7; -.
DR   BRENDA; 3.4.22.B79; 9640.
DR   Proteomes; UP000008300; 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; Protease; Repeat; RNA suppression of termination; RNA-binding;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Thiol protease;
KW   Transferase; Ubl conjugation; Viral RNA replication; Zinc.
FT   CHAIN           1..2498
FT                   /note="Polyprotein P1234"
FT                   /id="PRO_0000308389"
FT   CHAIN           1..1892
FT                   /note="Polyprotein P123'"
FT                   /id="PRO_0000232110"
FT   CHAIN           1..1885
FT                   /note="Polyprotein P123"
FT                   /id="PRO_0000232109"
FT   CHAIN           1..535
FT                   /note="mRNA-capping enzyme nsP1"
FT                   /id="PRO_0000232111"
FT   CHAIN           536..1329
FT                   /note="Protease nsP2"
FT                   /id="PRO_0000232112"
FT   CHAIN           1330..1892
FT                   /note="Non-structural protein 3'"
FT                   /id="PRO_0000232114"
FT   CHAIN           1330..1885
FT                   /note="Non-structural protein 3"
FT                   /id="PRO_0000232113"
FT   CHAIN           1893..2499
FT                   /note="RNA-directed RNA polymerase nsP4"
FT                   /id="PRO_0000232115"
FT   DOMAIN          28..259
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          690..841
FT                   /note="(+)RNA virus helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          842..990
FT                   /note="(+)RNA virus helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   DOMAIN          1003..1322
FT                   /note="Peptidase C9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00853"
FT   DOMAIN          1328..1489
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          2256..2371
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          244..263
FT                   /note="NsP1 membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P08411"
FT   REGION          1004..1023
FT                   /note="Nucleolus localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P08411"
FT   REGION          1831..1867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1858..1879
FT                   /note="Binding to host FXR family members"
FT                   /evidence="ECO:0000250|UniProtKB:P27282"
FT   MOTIF           1056..1065
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P27282"
FT   MOTIF           1179..1183
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P27282"
FT   COMPBIAS        1831..1845
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1850..1867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1012
FT                   /note="For cysteine protease nsP2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00853"
FT   ACT_SITE        1081
FT                   /note="For cysteine protease nsP2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00853"
FT   BINDING         721..728
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT   BINDING         1339
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:P36328"
FT   BINDING         1353
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
FT   BINDING         1361
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
FT   BINDING         1441
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:P36328"
FT   BINDING         1442
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:P36328"
FT   BINDING         1443
FT                   /ligand="ADP-D-ribose"
FT                   /ligand_id="ChEBI:CHEBI:57967"
FT                   /evidence="ECO:0000250|UniProtKB:P36328"
FT   BINDING         1596
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   BINDING         1598
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   BINDING         1621
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   BINDING         1639
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            535..536
FT                   /note="Cleavage; by protease nsP2"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   SITE            1329..1330
FT                   /note="Cleavage; by protease nsP2"
FT                   /evidence="ECO:0000250|UniProtKB:P03317"
FT   SITE            1892..1893
FT                   /note="Cleavage; by protease nsP2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
FT   LIPID           419
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JUX6"
SQ   SEQUENCE   2499 AA;  278684 MW;  33B1AD4E16745DE0 CRC64;
     MEKVHVDIEE DSPFLRALQR SFPQFEVEAK QVTDNDHANA RAFSHLASKL IETEVEPSDT
     ILDIGSAPAR RMYSKHKYHC ICPMKCAEDP DRLFKYAAKL KKNCKEITDK ELDKKMKELA
     EVMNDPDLET ETICLHDDET CRFEGQVAVY QDVYAVDGPT SLYHQANKGV RVAYWIGFDT
     TPFMFKNLAG AYPSYSTNWA DETVLTARNI GLCSSDVMER SRRGMSILRK KFLKPSNNVL
     FSVGSTIYHE KRDLLRSWHL PSVFHLRGKQ NYTCRCETIV SCDGYVVKRI AISPGLYGKP
     SGYAATMHRE GFLCCKVTDT LNGERVSFPV CTYVPATLCD QMTGILATDV SADDAQKLLV
     GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FARWAKEYKE DQEDERPLGL RDRQLVMGCC
     WAFRKHKITS VYKRPDTQTI IKVNSDFHSF VLPRIGSSTL EIGLRTRIKK LLEEPVDRPP
     LITADDIQEA KNAADEAKEV KEAEELRAAL PPLSADVEEP ALEADVDLML QEAGAGSVET
     PRGLIKVTSY GGEDKIGSYA VLSPQAVLRS EKLTCIHPLA EQVIVITHSG RKGRYAVEPY
     HGKVVVPEGQ AIPVQDFQAL SESATIVYNE REFVNRYLHH IATHGGALNT DEEYYRVVKP
     SEHEGEYLYD IDKKQCVKKE LVSGLGLTGE LVDPPFHEFA YESLRTRPAA PYQVPTIGVY
     GVPGSGKSGI IKSAVTKKDL VVSAKKENCA EIIRDVKKMK GLDVNARTVD SVLLNGCKHP
     VETLYIDEAF ACHAGTLRAL IAIIRPKKAV LCGDPKQCGF FNMMCLKVHF NHEICTQVFH
     KSISRRCTKS VTSVVSTLFY DKRMRTTNPR DSKIEIDTTG STKSKKEDLI LTCFRGWVKQ
     LQIDYKGNEI MTAAASQGLT RKSVYAVRYK VNENPLYAPT SEHVNVLLTR TEDKIVWKTL
     AGDPWIKTLT AKYPGDFTAT MEEWQAEHDA IMRHILEKPD PTDVFQNKAN VCWAKALVPV
     LKTAGIDLTT EQWNTVDYFK EDKAHSAEIV LNQLCVRYFG LDLDSGLFSA PTVPLSIRNN
     HWDNSPSPNM YGLNHEVVRQ LSRRYPQLPR AVTTGRVYDM NTGTLRNYDP RINLVPVNRR
     LPHALVTQHA DHPPSDFSAF VSKLKGRTVL VVGEKMNISG KAVDWLSETP DATFRARLDL
     GIPTELPKYD IVFVNVRTQY RYHHYQQCED HAIKLSMLTK KACLHLNPGG TCVSIGYGYA
     DRASESIIGA VARQFKFSRV CKPKVSKEET EVLFVFIGFD RKTRTHNPYK LSSTLTNIYT
     GSGLHEAGCA PSYHVVRGDI ATATEGVIVN AANSKGQPGS GVCGALYRKY PESFDLQPIE
     VGKARLVKGS SKHIIHAVGP NFSKVSEVEG DKQLAEAYES IAKIINDNNY RSVAIPLLST
     GIFAGNKDRL MQSLNHLLTA LDTTDADVAI YCRDKKWEVT LKEVVARREA VEEICISEDS
     SVAEPDAELV RVHPKSSLAG RKGYSTSDGK TFSYLEGTKF HQAAKDMAEI NAMWPTATEA
     NEQVCLYILG ESMSSIRSKC PVEESEASTP PSTLPCLCIH AMTPERVQRL KASRPEQITV
     CSSFPLPKYR ITGVQKIQCS HPILFSPKVP EYIHPRKYLA DATPADNEAA EPTMECVQPL
     QEERPANTEQ PVEEDDSISV LSEDAPHQVH QVEAEVHRSL CASAQSSSWS IPRASDFESL
     SVLDSLGAND TISMGSSSNE TALALRTIFR TPPIPKPRVR STSTDVDSIS VLESLGSTSD
     VRSIGSSSDE TDVSVFDKGL EFMARPVPAP RTIFRTPPVP KPRARRPLHP LSSRSSSRSS
     LVSNPPGVNR VITREEFEAF VAQQQXRFDA GAYIFSSDTG QGHLQQKSVR QTVLSEVVLE
     RTELEISYAP RLDLNKEEIL RKKLQLNPTQ ANRSRYQSRR VENMKAITTK RILQGLGHYL
     KSEGKVECYR TLHPVPLYSA SVNRAFSSPK VAVEACNVVL KENFPTVASY CIIPEYDAYL
     DMVDGASCCL DTASFCPAKL RSFPKKHAYL EPTIRSAVPS AIQNTLQNVL AAATKRNCNV
     TQMRELPVLD SAAFNVECFK KYACNNEYWE TYKKNPIRLT EENVVNYITK LKGPKAAALY
     AKTHNLDMLQ DIPMDRFIMD LKRDVKVTPG TKHTEERPKV QVIQAADPLA TAYLCGIHRE
     LVRRLNAVLL PNIHTLFDMS AEDFDAIIAE HFQPGDWVLE TDIASFDKSE DDAMALTALM
     ILEDLGVDPE LLTLIEAAFG EISSIHLPTK TKFRFGAMMK SGMFLTLFVN TVINMVIASR
     VLRERLTNSP CAAFIGDDNI VKGVKSDKLM ADRCATWLNM EVKIIDAVVG EKAPYFCGGF
     ILCDSVTGTA CRVADPLKRL FKLGKPLAVD DEHDDDRRRA LQEESARWNR VGIFSELCKA
     VESRYETVGT AVIIMAMTTL ASSVGSFGYL RGAPISLYG
 
 
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