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Genome polyprotein [Cleaved into: Protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

 POLG_DEN1B              Reviewed;        3392 AA.
P27909; P29983; Q8B648;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
23-MAY-2018, entry version 138.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Non-structural protein 2A-alpha;
Short=NS2A-alpha;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Peptide 2k;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56;
EC=2.1.1.57;
EC=2.7.7.48;
AltName: Full=Non-structural protein 5;
Dengue virus type 1 (strain Brazil/97-11/1997) (DENV-1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=408685;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 232-786.
STRAIN=Isolate Caribbean/924-1;
PubMed=2738579; DOI=10.1099/0022-1317-70-7-1701;
Chu M.C., O'Rourke E.J., Trent D.W.;
"Genetic relatedness among structural protein genes of dengue 1 virus
strains.";
J. Gen. Virol. 70:1701-1712(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 281-778.
STRAIN=Isolate Thailand/TH-Sman/1958;
PubMed=1339466; DOI=10.1099/0022-1317-73-1-207;
Shiu S.Y.W., Jiang W.R., Porterfield J.S., Gould E.A.;
"Envelope protein sequences of dengue virus isolates TH-36 and TH-
Sman, and identification of a type-specific genetic marker for dengue
and tick-borne flaviviruses.";
J. Gen. Virol. 73:207-212(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=12457974; DOI=10.1016/S0168-1702(02)00180-6;
Duarte dos Santos C.N., Rocha C.F.S., Cordeiro M., Fragoso S.P.,
Rey F., Deubel V., Despres P.;
"Genome analysis of dengue type-1 virus isolated between 1990 and 2001
in Brazil reveals a remarkable conservation of the structural proteins
but amino acid differences in the non-structural proteins.";
Virus Res. 90:197-205(2002).
-!- FUNCTION: Protein C: Plays a role in virus budding by binding to
membrane and gathering the viral RNA into a nucleocapsid that
forms the core of a mature virus particle. During virus entry, may
induce genome penetration in host cytoplasm after hemifusion
induced by surface proteins. Can migrate tot cell nucleus where it
modulates host functions. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network. Presumably to
avoid catastrophic activation of the viral fusion activity in
acidic GolGi compartment prior to virion release. prM-E cleavage
is ineficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M extodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
ineficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. May play a role in viral genome replication. Assist
membrane bending and envelopment of genomic RNA at the endoplasmic
reticulum. Excreted as a hexameric lipoparticle that plays a role
against host immune responce. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 2B: Required cofactor for the
serine protease function of NS3 (By similarity). May have
membrane-destabilizing activity and form viroporins (By
similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
{ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. Plays a role in the inhibition of the
host innate immune response. Interacts with host MAVS and thereby
prevents the interaction between DDX58 and MAVS. In turn, IFN-beta
production is impaired. {ECO:0000250|UniProtKB:P17763,
ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 4B: Inhibits interferon (IFN)-
induced host STAT1 phosphorylation and nuclear translocation,
thereby preventing the establishment of cellular antiviral state
by blocking the IFN-alpha/beta pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) genome, and performs the capping of genomes in the
cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
2'-O positions. Besides its role in RNA genome replication, also
prevents the establishment of cellular antiviral state by blocking
the interferon-alpha/beta (IFN-alpha/beta) signaling pathway.
Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
activation of JAK-STAT signaling pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway.
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
the endoplasmic reticulum and Golgi. Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1:
Homodimer; Homohexamer when secreted. Interacts with envelope
protein E. Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3. Non-structural protein 2B: Forms a
heterodimer with serine protease NS3. May form homooligomers.
Serine protease NS3: Forms a heterodimer with NS2B. Interacts with
NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase
NS5; this interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity. Non-structural protein 4A: Interacts
with host MAVS; this interaction inhibits the synthesis of IFN-
beta. Non-structural protein 4B: Interacts with serine protease
NS3. RNA-directed RNA polymerase NS5: Homodimer. Interacts with
host STAT2; this interaction inhibits the phosphorylation of the
latter, and, when all viral proteins are present (polyprotein),
targets STAT2 for degradation. Interacts with serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral
membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal
side {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Peripheral membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
Peripheral membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
ProRule:PRU00860}. Note=Remains non-covalently associated to NS3
protease. {ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Host
mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-
associated vesicles hosting the replication complex. Interacts
with host MAVS in the mitochondrion-associated endoplasmic
reticulum membranes. {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Peripheral membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
{ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: Transmembrane domains of the small envelope protein M and
envelope protein E contains an endoplasmic reticulum retention
signals. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, wereas cleavages
in the cytoplasmic side are performed by the Serine protease NS3.
Signal cleavage at the 2K-4B site requires a prior NS3 protease-
mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 2A-alpha: A C-terminally truncated
form of non-structural protein 2A, results from partial cleavage
by NS3. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
This cleavage is incomplete as up to 30% of viral particles still
carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: The excreted form is glycosylated
and this is required for efficient secretion of the protein from
infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
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EMBL; D00504; BAA00396.1; -; Genomic_RNA.
EMBL; D10513; BAA01388.1; -; Genomic_RNA.
EMBL; AF311956; AAN60368.1; -; Genomic_RNA.
PIR; JQ1405; JQ1405.
PDB; 3UZQ; X-ray; 1.60 A; B=578-680.
PDBsum; 3UZQ; -.
ProteinModelPortal; P27909; -.
SMR; P27909; -.
ELM; P27909; -.
PRIDE; P27909; -.
OrthoDB; VOG0900007N; -.
PRO; PR:P27909; -.
Proteomes; UP000007764; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
CDD; cd00079; HELICc; 1.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host endoplasmic reticulum; Host membrane; Host mitochondrion;
Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
Ion channel; Ion transport; Membrane; Metal-binding;
Methyltransferase; mRNA capping; mRNA processing;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
S-adenosyl-L-methionine; Secreted; Serine protease; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Transport; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 3392 Genome polyprotein.
/FTId=PRO_0000405203.
CHAIN 1 100 Protein C.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264634.
PROPEP 101 114 ER anchor for the protein C, removed in
mature form by serine protease NS3.
/FTId=PRO_0000264635.
CHAIN 115 280 Protein prM.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264636.
CHAIN 115 205 Peptide pr.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264637.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264638.
CHAIN 281 775 Envelope protein E.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264639.
CHAIN 776 1127 Non-structural protein 1.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264640.
CHAIN 1128 1345 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264641.
CHAIN 1128 1315 Non-structural protein 2A-alpha.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264642.
CHAIN 1346 1475 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264643.
CHAIN 1476 2094 Serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264644.
CHAIN 2095 2221 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264645.
PEPTIDE 2222 2244 Peptide 2k.
/FTId=PRO_0000264646.
CHAIN 2245 2493 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264647.
CHAIN 2494 3392 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000264648.
TOPO_DOM 1 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 119 Helical. {ECO:0000255}.
TOPO_DOM 120 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 260 Helical. {ECO:0000255}.
TOPO_DOM 261 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 280 Helical. {ECO:0000255}.
TOPO_DOM 281 725 Extracellular. {ECO:0000255}.
INTRAMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 752 Extracellular. {ECO:0000255}.
INTRAMEM 753 775 Helical. {ECO:0000255}.
TOPO_DOM 776 1125 Extracellular. {ECO:0000255}.
TRANSMEM 1126 1146 Helical. {ECO:0000255}.
TOPO_DOM 1147 1157 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1158 1178 Helical. {ECO:0000255}.
TOPO_DOM 1179 1199 Lumenal. {ECO:0000255}.
TRANSMEM 1200 1220 Helical. {ECO:0000255}.
TOPO_DOM 1221 1289 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1290 1310 Helical. {ECO:0000255}.
TOPO_DOM 1311 1315 Lumenal. {ECO:0000255}.
TRANSMEM 1316 1336 Helical. {ECO:0000255}.
TOPO_DOM 1337 1346 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1347 1367 Helical. {ECO:0000255}.
TOPO_DOM 1368 1370 Lumenal. {ECO:0000255}.
TRANSMEM 1371 1391 Helical. {ECO:0000255}.
TOPO_DOM 1392 1447 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1448 1468 Helical. {ECO:0000255}.
TOPO_DOM 1469 2148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2149 2169 Helical. {ECO:0000255}.
TOPO_DOM 2170 2171 Lumenal. {ECO:0000255}.
INTRAMEM 2172 2192 Helical. {ECO:0000255}.
TOPO_DOM 2193 2193 Lumenal. {ECO:0000255}.
TRANSMEM 2194 2214 Helical. {ECO:0000255}.
TOPO_DOM 2215 2229 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2230 2250 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2251 2276 Lumenal. {ECO:0000255}.
INTRAMEM 2277 2297 Helical. {ECO:0000255}.
TOPO_DOM 2298 2349 Lumenal. {ECO:0000255}.
TRANSMEM 2350 2370 Helical. {ECO:0000255}.
TOPO_DOM 2371 2415 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2416 2436 Helical. {ECO:0000255}.
TOPO_DOM 2437 2461 Lumenal. {ECO:0000255}.
TRANSMEM 2462 2482 Helical. {ECO:0000255}.
TOPO_DOM 2483 3392 Cytoplasmic. {ECO:0000255}.
DOMAIN 1476 1653 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1656 1812 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1822 1989 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2495 2756 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3021 3170 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1669 1676 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 33 74 Hydrophobic; homodimerization of capsid
protein C. {ECO:0000250}.
REGION 1398 1437 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
MOTIF 1760 1763 DEAH box.
ACT_SITE 1526 1526 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1550 1550 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1610 1610 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
BINDING 2507 2507 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2510 2510 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2511 2511 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2513 2513 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2522 2522 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2549 2549 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2579 2579 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2580 2580 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2597 2597 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2598 2598 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2624 2624 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2625 2625 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2643 2643 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2704 2704 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2706 2706 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2711 2711 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 100 101 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 205 206 Cleavage; by host furin. {ECO:0000255}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 775 776 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 1127 1128 Cleavage; by host. {ECO:0000255}.
SITE 1345 1346 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 1475 1476 Cleavage; by autolysis. {ECO:0000255}.
SITE 2094 2095 Cleavage; by autolysis. {ECO:0000255}.
SITE 2221 2222 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2244 2245 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 2493 2494 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2518 2518 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2554 2554 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2639 2639 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2640 2640 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2673 2673 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2709 2709 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 905 905 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 982 982 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1190 1190 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2303 2303 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2307 2307 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2459 2459 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 283 310 {ECO:0000250|UniProtKB:P17763}.
DISULFID 340 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 354 385 {ECO:0000250|UniProtKB:P17763}.
DISULFID 372 396 {ECO:0000250|UniProtKB:P17763}.
DISULFID 465 565 {ECO:0000250|UniProtKB:P17763}.
DISULFID 582 613 {ECO:0000250|UniProtKB:P17763}.
DISULFID 779 790 {ECO:0000250|UniProtKB:P17763}.
DISULFID 830 918 {ECO:0000250|UniProtKB:P17763}.
DISULFID 954 998 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1055 1104 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1066 1088 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1087 1091 {ECO:0000250|UniProtKB:P17763}.
VARIANT 394 394 L -> I (in strain: Isolate Thailand/TH-
Sman/1958).
VARIANT 402 402 V -> A (in strain: Isolate Thailand/TH-
Sman/1958).
VARIANT 441 441 I -> T (in strain: Isolate Thailand/TH-
Sman/1958).
VARIANT 475 476 EM -> RV (in strain: Isolate 924-1).
VARIANT 483 483 E -> K (in strain: Isolate 924-1).
VARIANT 531 531 V -> A (in strain: Isolate 924-1 and
Isolate Thailand/TH-Sman/1958).
VARIANT 577 577 T -> M (in strain: Isolate 924-1 and
Isolate Thailand/TH-Sman/1958).
VARIANT 619 619 T -> S (in strain: Isolate 924-1).
VARIANT 649 649 T -> E (in strain: Isolate 924-1 and
Isolate Thailand/TH-Sman/1958).
VARIANT 677 677 S -> I (in strain: Isolate Thailand/TH-
Sman/1958n).
VARIANT 712 712 V -> M (in strain: Isolate Thailand/TH-
Sman/1958).
VARIANT 716 716 V -> I (in strain: Isolate 924-1).
VARIANT 719 719 V -> I (in strain: Isolate 924-1).
VARIANT 752 752 S -> N (in strain: Isolate Thailand/TH-
Sman/1958).
VARIANT 758 758 T -> M (in strain: Isolate Thailand/TH-
Sman/1958).
STRAND 586 590 {ECO:0000244|PDB:3UZQ}.
STRAND 600 606 {ECO:0000244|PDB:3UZQ}.
STRAND 612 614 {ECO:0000244|PDB:3UZQ}.
STRAND 617 621 {ECO:0000244|PDB:3UZQ}.
STRAND 633 635 {ECO:0000244|PDB:3UZQ}.
STRAND 637 639 {ECO:0000244|PDB:3UZQ}.
STRAND 645 649 {ECO:0000244|PDB:3UZQ}.
STRAND 653 663 {ECO:0000244|PDB:3UZQ}.
STRAND 666 673 {ECO:0000244|PDB:3UZQ}.
SEQUENCE 3392 AA; 378905 MW; BBD894175578E164 CRC64;
MNNQRKKTGR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP
PTAGILARWS SFKKNGAIKV LRGFKKEISS MLNIMNRRKR SVTMLLMLLP TALAFHLTTR
GGEPHMIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC
WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW
ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
VDVVLEHGSC VTTMAKNKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK CVTKLEGKIV QYENLKYSVI
VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT
MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGTSYV MCTGSFKLEK EVAETQHGTV
LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR LITANPIVTD KEKPVNIETE PPFGESYIVV
GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQVF
GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV
INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGRAWEEGVC GIRSATRLEN
IMWKQISNEL NHILLENDIK FTVVVGNANG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
ADIQNTTFII DGPDTPECPD EQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQMCDHRLMS
AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK
MYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGSRG PSLRTTTVTG
KIIHEWCCRS CTLPPLRFRG EDGCWYGMEI RPVKEKEENL VRSMVSAGSG EVDSFSLGIL
CVSIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMVGAN ASDKMGMGTT
YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL GDGLAMGIMM
LKLLTEFQPH QLWTTLLSLT FIKTTLSLDY AWKTTAMVLS IVSLFPLCLS TTSQKTTWLP
VLLGSFGCKP LTMFLITENE IWGRKSWPLN EGIMAIGIVS ILLSSLLKND VPLAGPLIAG
GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGTSHNIL VEVQDDGTMK IKDEERDDTL
TILLKATLLA VSGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI
LQRGLLGRSQ VGVGVFQDGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRF
QGSWNTGEEV QVIAVEPGKN PKNVQTTPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK
IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFK KRNLTIMDLH PGSGKTRRYL
PAIVREAIKR KLRTLILAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGR EIVDLMCHAT
FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA
FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ
LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA
GPMPVTVASA AQRRGRIGRN QNKEGDQYVY MGQPLNNDED HAHWTEAKML LDNINTPEGI
IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF
DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL
ILEIGKLPQH LTLRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG
GVTLFFLSGK GLGKTSIGLL CVTASSALLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ
RTPQDNQLAY VVIGLLFMIL TVAANEMGLL ETTKKDLGIG HVAAENHQHA TILDVDLHPA
SAWTLYAVAT TVITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDLGVPLLA
LGCYSQVNPL TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL
DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT
TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT
YKRSGIMEVD RSEAKEGLKR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW
SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLH SGKDVFFMPP EKCDTLLCDI
GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE
PEVANLDIIG QRIENIKNEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL
TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPRAKR GTAQIMEVTA KWLWGFLSRN
KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA
TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI
FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEVQ LIRQMESEGI
FFPSELESPN LAERVLDWLE KHGAERLKRM AISGDDCVVK PIDDRFATAL IALNDMGKVR
KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL
RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED
MLSVWNRVWI EENPWMEDKT HVSSWEEVPY LGKREDQWCG SLIGLTARAT WATNIQVAIN
QVRRLIGNEN YLDYMTSMKR FKNESDPEGA LW


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29-223 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg
29-217 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg
29-218 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.1 mg
29-219 Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structural 0.05 mg


 

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