ID   POLG_DEN2N              Reviewed;        3391 AA.
AC   P14340; Q66347; Q66348; Q66349; Q66350; Q66351; Q66352; Q66353; Q66354;
AC   Q66355; Q66356; Q89579;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 213.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM;
DE   Contains:
DE     RecName: Full=Peptide pr;
DE   Contains:
DE     RecName: Full=Small envelope protein M;
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A;
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9Q6P4};
DE              EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Peptide 2k;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase/Methyltransferase NS5;
DE              EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=Non-structural protein 5;
OS   Dengue virus type 2 (strain Thailand/NGS-C/1944) (DENV-2).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus denguei;
OC   Dengue virus.
OX   NCBI_TaxID=11065;
OH   NCBI_TaxID=53540; Aedimorphus.
OH   NCBI_TaxID=53539; Diceromyia.
OH   NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=53541; Stegomyia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2714651; DOI=10.1016/0378-1119(89)90266-7;
RA   Irie K., Mohan P.M., Sasaguri Y., Putnak R., Padmanabhan R.;
RT   "Sequence analysis of cloned dengue virus type 2 genome (New Guinea-C
RT   strain).";
RL   Gene 75:197-211(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 749-1225.
RX   PubMed=2964755; DOI=10.1016/0042-6822(88)90236-x;
RA   Putnak J.R., Charles P.C., Padmanabhan R., Irie K., Hoke C.H., Burke D.S.;
RT   "Functional and antigenic domains of the dengue-2 virus nonstructural
RT   glycoprotein NS-1.";
RL   Virology 163:93-103(1988).
RN   [3]
RP   PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
RX   PubMed=2952760; DOI=10.1099/0022-1317-68-5-1317;
RA   Biedrzycka A., Cauchi M.R., Bartholomeusz A., Gorman J.J., Wright P.J.;
RT   "Characterization of protease cleavage sites involved in the formation of
RT   the envelope glycoprotein and three non-structural proteins of dengue virus
RT   type 2, New Guinea C strain.";
RL   J. Gen. Virol. 68:1317-1326(1987).
RN   [4]
RP   PHOSPHORYLATION (RNA-DIRECTED RNA POLYMERASE/METHYLTRANSFERASE NS5).
RX   PubMed=7642575; DOI=10.1074/jbc.270.32.19100;
RA   Kapoor M., Zhang L., Ramachandra M., Kusukawa J., Ebner K.E.,
RA   Padmanabhan R.;
RT   "Association between NS3 and NS5 proteins of dengue virus type 2 in the
RT   putative RNA replicase is linked to differential phosphorylation of NS5.";
RL   J. Biol. Chem. 270:19100-19106(1995).
RN   [5]
RP   INTERACTION WITH SERINE PROTEASE NS3 (RNA-DIRECTED RNA
RP   POLYMERASE/METHYLTRANSFERASE NS5), INTERACTION WITH RNA-DIRECTED RNA
RP   POLYMERASE NS5 (SERINE PROTEASE NS3), BIOPHYSICOCHEMICAL PROPERTIES (SERINE
RP   PROTEASE NS3), CATALYTIC ACTIVITY (SERINE PROTEASE NS3), AND MUTAGENESIS OF
RP   1659-ARG--LYS-1662.
RX   PubMed=15917225; DOI=10.1074/jbc.m501393200;
RA   Yon C., Teramoto T., Mueller N., Phelan J., Ganesh V.K., Murthy K.H.,
RA   Padmanabhan R.;
RT   "Modulation of the nucleoside triphosphatase/RNA helicase and 5'-RNA
RT   triphosphatase activities of Dengue virus type 2 nonstructural protein 3
RT   (NS3) by interaction with NS5, the RNA-dependent RNA polymerase.";
RL   J. Biol. Chem. 280:27412-27419(2005).
RN   [6]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4B), AND MEMBRANE TOPOLOGY
RP   (NON-STRUCTURAL PROTEIN 4B).
RX   PubMed=16436383; DOI=10.1074/jbc.m512697200;
RA   Miller S., Sparacio S., Bartenschlager R.;
RT   "Subcellular localization and membrane topology of the Dengue virus type 2
RT   Non-structural protein 4B.";
RL   J. Biol. Chem. 281:8854-8863(2006).
RN   [7]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4A), SUBCELLULAR LOCATION (NON-STRUCTURAL
RP   PROTEIN 4A), AND MEMBRANE TOPOLOGY (NON-STRUCTURAL PROTEIN 4A).
RX   PubMed=17276984; DOI=10.1074/jbc.m609919200;
RA   Miller S., Kastner S., Krijnse-Locker J., Buhler S., Bartenschlager R.;
RT   "The non-structural protein 4A of dengue virus is an integral membrane
RT   protein inducing membrane alterations in a 2K-regulated manner.";
RL   J. Biol. Chem. 282:8873-8882(2007).
RN   [8]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 2A), AND TOPOLOGY
RP   (NON-STRUCTURAL PROTEIN 2A).
RX   PubMed=23408612; DOI=10.1128/jvi.02424-12;
RA   Xie X., Gayen S., Kang C., Yuan Z., Shi P.Y.;
RT   "Membrane topology and function of dengue virus NS2A protein.";
RL   J. Virol. 87:4609-4622(2013).
CC   -!- FUNCTION: [Capsid protein C]: Capsid protein C self-assembles to form
CC       an icosahedral capsid about 30 nm in diameter. The capsid encapsulates
CC       the genomic RNA (Probable). Plays a role in virus budding by binding to
CC       the cell membrane and gathering the viral RNA into a nucleocapsid that
CC       forms the core of a mature virus particle. During virus entry, may
CC       induce genome penetration into the host cytoplasm after hemifusion
CC       induced by the surface proteins. Can migrate to the cell nucleus where
CC       it modulates host functions. Overcomes the anti-viral effects of host
CC       EXOC1 by sequestering and degrading the latter through the proteasome
CC       degradation pathway. {ECO:0000250|UniProtKB:P17763, ECO:0000305}.
CC   -!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
CC       proteins in trans-Golgi by binding to envelope protein E at pH6.0.
CC       After virion release in extracellular space, gets dissociated from E
CC       dimers. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E
CC       during intracellular virion assembly by masking and inactivating
CC       envelope protein E fusion loop. prM is the only viral peptide matured
CC       by host furin in the trans-Golgi network probably to avoid catastrophic
CC       activation of the viral fusion activity in acidic Golgi compartment
CC       prior to virion release. prM-E cleavage is inefficient, and many
CC       virions are only partially matured. These uncleaved prM would play a
CC       role in immune evasion. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding.
CC       Exerts cytotoxic effects by activating a mitochondrial apoptotic
CC       pathway through M ectodomain. May display a viroporin activity.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Envelope protein E]: Type II fusion protein that binds to
CC       host cell surface receptor and mediates fusion between viral and
CC       cellular membranes (By similarity). The envelope protein E shifts from
CC       dimeric state to trimeric state to perform fusion with the host
CC       membrane (By similarity). The fusion loops of the three subunits come
CC       together to form a membrane-insertable tip containing aromatic residues
CC       (By similarity). Envelope protein is synthesized in the endoplasmic
CC       reticulum in the form of heterodimer with protein prM. They play a role
CC       in virion budding in the ER, and the newly formed immature particle is
CC       covered with 60 spikes composed of heterodimers of precursor prM and
CC       envelope protein E (By similarity). Envelope protein exposes a
CC       positively-charged pr-binding pocket at the E dimer interface, inducing
CC       (prM/E)2 dimer formation to generate smooth particles in the Golgi (By
CC       similarity). The virion is transported to the Golgi apparatus where the
CC       low pH causes dissociation of PrM-E heterodimers and formation of E
CC       homodimers (By similarity). prM-E cleavage is inefficient, and many
CC       virions are only partially matured. These uncleaved prM would play a
CC       role in immune evasion (By similarity). Pr is shed from the particle
CC       upon subsequent secretion into the extracellular environment, leaving
CC       an activated particle, prone to mediate acidic pH-triggered membrane
CC       fusion upon entry into a target cell (By similarity).
CC       {ECO:0000250|UniProtKB:P12823, ECO:0000250|UniProtKB:P14336,
CC       ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
CC       pathogenesis and viral replication. Once cleaved off the polyprotein,
CC       is targeted to three destinations: the viral replication cycle, the
CC       plasma membrane and the extracellular compartment. Essential for viral
CC       replication. Required for formation of the replication complex and
CC       recruitment of other non-structural proteins to the ER-derived membrane
CC       structures. Excreted as a hexameric lipoparticle that plays a role
CC       against host immune response. Antagonizing the complement function.
CC       Binds to the host macrophages and dendritic cells. Inhibits signal
CC       transduction originating from Toll-like receptor 3 (TLR3). Mediates
CC       complement activation, which may contribute to the pathogenesis of the
CC       vascular leakage that occurs in severe dengue disease. Activates
CC       autophagy through the AMPK/ERK/mTOR signaling pathway. Mechanistically,
CC       acts as the assembly platform for STK11-AMPK interactions and promotes
CC       STK11-AMPK interactions. In turn, promotes phosphorylation of the AMPK
CC       kinase structural domain and activates AMPK, thereby positively
CC       regulating the AMPK/ERK/mTOR signaling pathway and inducing autophagy.
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
CC   -!- FUNCTION: [Non-structural protein 1]: Disrupts the host endothelial
CC       glycocalyx layer of host pulmonary microvascular endothelial cells,
CC       inducing degradation of sialic acid and shedding of heparan sulfate
CC       proteoglycans. NS1 induces expression of sialidases, heparanase, and
CC       activates cathepsin L, which activates heparanase via enzymatic
CC       cleavage. These effects are probably linked to the endothelial
CC       hyperpermeability observed in severe dengue disease.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC       replication complex that functions in virion assembly and antagonizes
CC       the host immune response. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC       serine protease function of NS3. May have membrane-destabilizing
CC       activity and form viroporins (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
CC   -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC       serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS2B, performs its autocleavage and cleaves the
CC       polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC       NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC       unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC       the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC       during unwinding. Plays a role in the inhibition of the host innate
CC       immune response. Interacts with host MAVS and thereby prevents the
CC       interaction between RIGI and MAVS. In turn, IFN-beta production is
CC       impaired. Interacts with host AUP1 which mediates induction of
CC       lipophagy in host cells and facilitates production of virus progeny
CC       particles (By similarity). {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000250|UniProtKB:P29991, ECO:0000269|PubMed:17276984}.
CC   -!- FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is
CC       required for the interferon antagonism activity of the latter.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
CC       derived membrane vesicles where the viral replication takes place.
CC       Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
CC       nuclear translocation, thereby preventing the establishment of cellular
CC       antiviral state by blocking the IFN-alpha/beta pathway.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase/Methyltransferase NS5]:
CC       Replicates the viral (+) and (-) RNA genome, and performs the capping
CC       of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-
CC       7 and ribose 2'-O positions. Besides its role in RNA genome
CC       replication, also prevents the establishment of cellular antiviral
CC       state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling
CC       pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby
CC       preventing activation of JAK-STAT signaling pathway (By similarity).
CC       May reduce immune responses by preventing the recruitment of the host
CC       PAF1 complex to interferon-responsive genes (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC         the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC         EC=3.4.21.91;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + phosphate + H(+); 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:0000269|PubMed:15917225};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); 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:0000269|PubMed:15917225};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC         COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC         ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S-
CC         adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:67020, Rhea:RHEA-
CC         COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC         ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=29.3 uM for triphosphorylated RNA {ECO:0000269|PubMed:15917225};
CC         Note=Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with
CC         triphosphorylated RNA as substrate. {ECO:0000269|PubMed:15917225};
CC   -!- SUBUNIT: [Capsid protein C]: Homodimer (By similarity). Interacts (via
CC       N-terminus) with host EXOC1 (via C-terminus); this interaction results
CC       in EXOC1 degradation through the proteasome degradation pathway (By
CC       similarity). Interacts (via the NLS) with host KPNA2/Importin alpha-1;
CC       this interaction allows the nuclear import of the capsid protein (By
CC       similarity). {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000250|UniProtKB:Q01299}.
CC   -!- SUBUNIT: [Protein prM]: Heterodimer with envelope protein E; each spike
CC       of the immature virion in the ER/Golgi consists of three prM-E
CC       heterodimers. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Small envelope protein M]: Heterotetramer with envelope
CC       protein E, made up of two M-E dimers; in mature virion, prefusion
CC       state. {ECO:0000250|UniProtKB:Q01299}.
CC   -!- SUBUNIT: [Envelope protein E]: Homodimer; in mature virion, prefusion
CC       state (By similarity). Homotrimer; in mature virion, postfusion state
CC       (By similarity). Heterotetramer with the small membrane protein, made
CC       up of two M-E dimers; in mature virion, prefusion state (By
CC       similarity). Heterodimer with protein prM; each spike of the immature
CC       virion in the ER/Golgi consists of three prM-E heterodimers (By
CC       similarity). Interacts with the peptide pr; this interaction allows the
CC       stabilization of the E dimer at acidic pH (By similarity). Pr remains
CC       bound to the particle as long as the pH is acidic because of
CC       electrostatic complementarity, dissociation of pr occurs at neutral pH
CC       upon virus release from the infected cell (By similarity). Interacts
CC       with non-structural protein 1 (By similarity).
CC       {ECO:0000250|UniProtKB:P14336, ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC       secreted. Interacts with envelope protein E (By similarity). Interacts
CC       with host PRKAA1 (By similarity). {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000250|UniProtKB:P29990}.
CC   -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC       serine protease NS3 (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC       serine protease NS3 (By similarity). May form homooligomers (By
CC       similarity). {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By
CC       similarity). Interacts with NS4B (By similarity). Interacts with
CC       unphosphorylated RNA-directed RNA polymerase NS5; this interaction
CC       stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
CC       (PubMed:15917225). Interacts with host SHFL (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:15917225}.
CC   -!- SUBUNIT: [Non-structural protein 4A]: Interacts with host MAVS; this
CC       interaction inhibits the synthesis of IFN-beta (By similarity).
CC       Interacts with host MAVS; this interaction inhibits the synthesis of
CC       IFN-beta. Interacts with host SHFL (By similarity). Interacts with host
CC       AUP1; the interaction occurs in the presence of Dengue virus NS4B and
CC       induces lipophagy which facilitates production of virus progeny
CC       particles (By similarity). May interact with host SRPRA and SEC61G (By
CC       similarity). {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000250|UniProtKB:P29990, ECO:0000250|UniProtKB:P29991}.
CC   -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease NS
CC       (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase/Methyltransferase NS5]: Homodimer
CC       (By similarity). Interacts with host STAT2; this interaction inhibits
CC       the phosphorylation of the latter, and, when all viral proteins are
CC       present (polyprotein), targets STAT2 for degradation (By similarity).
CC       Interacts with serine protease NS3 (PubMed:15917225). Interacts (via C-
CC       terminus) with host SCRIB (via PDZ3); this interaction targets NS5 to
CC       the cell membrane periphery and nucleus, thereby allowing efficient
CC       host nuclear STAT1 inhibition (By similarity). Interacts with host PAF1
CC       complex; the interaction may prevent the recruitment of the PAF1
CC       complex to interferon-responsive genes, and thus reduces the immune
CC       response (By similarity). Interacts with host KPNA2/importin-alpha;
CC       this interaction allows the nuclear localization of NS5 (By
CC       similarity). {ECO:0000250|UniProtKB:P09866,
CC       ECO:0000250|UniProtKB:P12823, ECO:0000250|UniProtKB:P17763,
CC       ECO:0000250|UniProtKB:Q01299, ECO:0000269|PubMed:15917225}.
CC   -!- INTERACTION:
CC       P14340; P25963: NFKBIA; Xeno; NbExp=2; IntAct=EBI-465733, EBI-307386;
CC       P14340; Q15653: NFKBIB; Xeno; NbExp=2; IntAct=EBI-465733, EBI-352889;
CC       P14340; Q9UHY1: NRBP1; Xeno; NbExp=4; IntAct=EBI-465733, EBI-749731;
CC       PRO_0000037965; P55265: ADAR; Xeno; NbExp=2; IntAct=EBI-9825968, EBI-2462104;
CC       PRO_0000037965; P25963: NFKBIA; Xeno; NbExp=2; IntAct=EBI-9825968, EBI-307386;
CC       PRO_0000037965; Q15653: NFKBIB; Xeno; NbExp=2; IntAct=EBI-9825968, EBI-352889;
CC       PRO_0000037966; P08670: VIM; Xeno; NbExp=10; IntAct=EBI-9844509, EBI-353844;
CC   -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus, host nucleolus
CC       {ECO:0000250|UniProtKB:Q01299}.
CC   -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Note=Pr remains bound to the immature
CC       particle as long as the pH is acidic because of electrostatic
CC       complementarity, dissociation of pr occurs at neutral pH upon virus
CC       release from the infected cell. {ECO:0000250|UniProtKB:P14336}.
CC   -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P29990}. Host endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles
CC       hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:23408612}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:23408612}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
CC       membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
CC       associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:17276984}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:17276984}. Host mitochondrion
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles
CC       hosting the replication complex. Interacts with host MAVS in the
CC       mitochondrion-associated endoplasmic reticulum membranes.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:16436383}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:16436383}. Note=Located in RE-derived
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase/Methyltransferase
CC       NS5]: Host endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}.
CC       Note=Located in RE-associated vesicles hosting the replication complex.
CC       NS5 protein is mainly localized in the nucleus rather than in ER
CC       vesicles, especially in the DENV 2, 3, 4 serotypes.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: [Small envelope protein M]: The transmembrane domains contain
CC       an endoplasmic reticulum retention signal.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: [Envelope protein E]: The transmembrane domains contain an
CC       endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: [Protein prM]: The pr domain has a critical role in holding the
CC       spikes made of three prM-E heterodimers in a metastable conformation.
CC       {ECO:0000250|UniProtKB:P14336}.
CC   -!- DOMAIN: [RNA-directed RNA polymerase/Methyltransferase NS5]: The C-
CC       terminal 18 amino acids are important for the subcellular location of
CC       NS5. {ECO:0000250|UniProtKB:P12823}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC       performed by host signal peptidase, whereas cleavages in the
CC       cytoplasmic side are performed by serine protease NS3. Signal cleavage
CC       at the 2K-4B site requires a prior NS3 protease-mediated cleavage at
CC       the 4A-2K site. {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000269|PubMed:2952760}.
CC   -!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr. This
CC       cleavage is incomplete as up to 30% of viral particles still carry
CC       uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Envelope protein E]: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC       glycosylated and this is required for efficient secretion of the
CC       protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation
CC       modulates NS3 RNA-binding and unwinding activities and plays an
CC       important positive role for viral replication.
CC       {ECO:0000250|UniProtKB:Q32ZE1}.
CC   -!- PTM: [RNA-directed RNA polymerase/Methyltransferase NS5]: Sumoylation
CC       of RNA-directed RNA polymerase NS5 increases NS5 protein stability
CC       allowing proper viral RNA replication. {ECO:0000250|UniProtKB:P29990}.
CC   -!- PTM: [RNA-directed RNA polymerase/Methyltransferase NS5]:
CC       Phosphorylated on serines residues (PubMed:7642575). This
CC       phosphorylation may trigger NS5 nuclear localization.
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:7642575}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC       binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M29095; AAA42941.1; -; Genomic_RNA.
DR   PDB; 3IYA; EM; 22.00 A; A/B/C=281-326, D/E/F=115-168.
DR   PDB; 3J27; EM; 3.60 A; A/C/E=281-775, B/D/F=206-280.
DR   PDB; 3J2P; EM; 3.60 A; A/C=281-775, B/D=206-280.
DR   PDB; 4CBF; EM; 4.10 A; A/C/E=281-775.
DR   PDB; 4UIH; EM; 20.00 A; A/B/C=281-775.
DR   PDB; 6FLA; X-ray; 2.90 A; G=577-674.
DR   PDB; 6FLB; X-ray; 2.20 A; G=578-677.
DR   PDB; 6FLC; X-ray; 2.00 A; G/I=577-674.
DR   PDB; 6IZX; X-ray; 2.43 A; A=2735-3387.
DR   PDB; 6IZY; X-ray; 2.11 A; A=2735-3387.
DR   PDB; 7CTH; EM; 3.50 A; A/B/C=281-775, D/E/F=206-280.
DR   PDB; 7V3F; EM; 3.10 A; A/B/C=281-775, D/E/F=206-277.
DR   PDB; 7V3G; EM; 3.30 A; A/B/C=281-775, D/E/F=206-277.
DR   PDB; 7V3H; EM; 3.60 A; A/B/C=281-775, D/E/F=206-277.
DR   PDB; 7V3I; EM; 4.40 A; A/B/C=281-775, D/E/F=206-277.
DR   PDB; 7V3J; EM; 4.90 A; A/B/C/O/P/Q=281-775, D/E/F/R/S/T=206-277.
DR   PDB; 9DOF; EM; 4.24 A; D/E/F=115-280.
DR   PDB; 9DOG; EM; 6.50 A; D000/D001/D002/D003/D004/D005/D006/D007/D008/D009/D010/D011/D012/D013/D014/D015/D016/D017/D018/D019/D020/D021/D022/D023/E000/E001/E002/E003/E004/E005=115-280.
DR   PDB; 9DTT; EM; 3.60 A; A=2492-3391.
DR   BMRB; P14340; -.
DR   EMDB; EMD-31677; -.
DR   EMDB; EMD-31678; -.
DR   EMDB; EMD-31679; -.
DR   EMDB; EMD-31680; -.
DR   EMDB; EMD-31681; -.
DR   EMDB; EMD-47082; -.
DR   EMDB; EMD-47083; -.
DR   EMDB; EMD-47165; -.
DR   MDposit; P14340; -.
DR   SASBDB; P14340; -.
DR   SMR; P14340; -.
DR   IntAct; P14340; 13.
DR   BindingDB; P14340; -.
DR   MEROPS; S07.001; -.
DR   TCDB; 1.G.3.1.2; the viral pore-forming membrane fusion protein-3 (vmfp3) family.
DR   iPTMnet; P14340; -.
DR   ABCD; P14340; 9 sequenced antibodies.
DR   EvolutionaryTrace; P14340; -.
DR   PRO; PR:P14340; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; EXP:UniProtKB.
DR   GO; GO:0033650; C:host cell mitochondrion; ISS:UniProtKB.
DR   GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; EXP:UniProtKB.
DR   GO; GO:0015267; F:channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004483; F:methyltransferase cap1 activity; IEA:UniProtKB-EC.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; EXP:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:symbiont-mediated activation of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039545; P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039574; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:symbiont-mediated suppression of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR   CDD; cd17931; DEXHc_viral_Ns3; 1.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   CDD; cd17038; Flavi_M; 1.
DR   CDD; cd23204; Flavivirus_RdRp; 1.
DR   CDD; cd18806; SF2_C_viral; 1.
DR   DisProt; DP00876; -.
DR   FunFam; 1.20.1280.260:FF:000001; Envelope glycoprotein; 1.
DR   FunFam; 2.60.40.350:FF:000001; Envelope glycoprotein; 1.
DR   FunFam; 1.10.10.930:FF:000001; Genome polyprotein; 1.
DR   FunFam; 1.10.260.90:FF:000001; Genome polyprotein; 1.
DR   FunFam; 2.60.260.50:FF:000001; Genome polyprotein; 1.
DR   FunFam; 3.30.70.2840:FF:000001; Genome polyprotein; 1.
DR   FunFam; 3.30.70.2840:FF:000002; Genome polyprotein; 1.
DR   FunFam; 3.40.50.150:FF:000105; Genome polyprotein; 1.
DR   FunFam; 3.40.50.300:FF:000763; Genome polyprotein; 1.
DR   Gene3D; 1.10.10.930; -; 1.
DR   Gene3D; 1.10.260.90; -; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.40.10.120; -; 2.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 1.10.8.970; Flavivirus envelope glycoprotein M-like; 1.
DR   Gene3D; 2.60.260.50; Flavivirus polyprotein propeptide domain; 1.
DR   Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 3.30.67.10; Viral Envelope Glycoprotein, domain 2; 1.
DR   Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR037172; Flavi_capsidC_sf.
DR   InterPro; IPR011492; Flavi_DEAD.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR011998; Flavi_Glycoprot_E_cen/dimer.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR001850; Flavi_NS3_S7.
DR   InterPro; IPR000404; Flavi_NS4A.
DR   InterPro; IPR001528; Flavi_NS4B.
DR   InterPro; IPR046811; Flavi_NS5_thumb.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR047530; Flavi_RdRp.
DR   InterPro; IPR000208; Flavi_RdRp_fingers/palm.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR   InterPro; IPR049486; NS3-hel_C_flaviviridae.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR04240; flavi_E_stem; 1.
DR   Pfam; PF20907; Flav_NS3-hel_C; 1.
DR   Pfam; PF01003; Flavi_capsid; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF21659; Flavi_E_stem; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF01004; Flavi_M; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01002; Flavi_NS2B; 1.
DR   Pfam; PF01350; Flavi_NS4A; 1.
DR   Pfam; PF01349; Flavi_NS4B; 1.
DR   Pfam; PF00972; Flavi_NS5; 1.
DR   Pfam; PF20483; Flavi_NS5_thumb; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF00949; Peptidase_S7; 1.
DR   PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF101257; Flavivirus capsid protein C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
DR   PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR   PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
DR   PDBsum; 3IYA; -.
DR   PDBsum; 3J27; -.
DR   PDBsum; 3J2P; -.
DR   PDBsum; 4CBF; -.
DR   PDBsum; 4UIH; -.
DR   PDBsum; 6FLA; -.
DR   PDBsum; 6FLB; -.
DR   PDBsum; 6FLC; -.
DR   PDBsum; 6IZX; -.
DR   PDBsum; 6IZY; -.
DR   PDBsum; 7CTH; -.
DR   PDBsum; 7V3F; -.
DR   PDBsum; 7V3G; -.
DR   PDBsum; 7V3H; -.
DR   PDBsum; 7V3I; -.
DR   PDBsum; 7V3J; -.
DR   PDBsum; 9DOF; -.
DR   PDBsum; 9DOG; -.
DR   PDBsum; 9DTT; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activation of host autophagy by virus;
KW   ATP-binding; Capsid protein;
KW   Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW   Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW   Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
KW   Interferon antiviral system evasion; Ion channel; Ion transport; Membrane;
KW   Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Secreted; Serine protease; Transcription;
KW   Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion; Viral ion channel;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN           1..3391
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000405216"
FT   CHAIN           1..100
FT                   /note="Capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037958"
FT   PROPEP          101..114
FT                   /note="ER anchor for the capsid protein C, removed in
FT                   mature form by serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000261388"
FT   CHAIN           115..280
FT                   /note="Protein prM"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000261389"
FT   CHAIN           115..205
FT                   /note="Peptide pr"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037959"
FT   CHAIN           206..280
FT                   /note="Small envelope protein M"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037960"
FT   CHAIN           281..775
FT                   /note="Envelope protein E"
FT                   /evidence="ECO:0000269|PubMed:2952760"
FT                   /id="PRO_0000037961"
FT   CHAIN           776..1127
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037962"
FT   CHAIN           1128..1345
FT                   /note="Non-structural protein 2A"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037963"
FT   CHAIN           1346..1475
FT                   /note="Serine protease subunit NS2B"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037964"
FT   CHAIN           1476..2093
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037965"
FT   CHAIN           2094..2220
FT                   /note="Non-structural protein 4A"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037966"
FT   PEPTIDE         2221..2243
FT                   /note="Peptide 2k"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000261391"
FT   CHAIN           2244..2491
FT                   /note="Non-structural protein 4B"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037967"
FT   CHAIN           2492..3391
FT                   /note="RNA-directed RNA polymerase/Methyltransferase NS5"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037968"
FT   TOPO_DOM        1..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..725
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        726..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        747..752
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        753..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        774..1195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1196..1220
FT                   /note="Helical"
FT                   /evidence="ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1221..1226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1227..1245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1246..1269
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1270..1290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1292..1310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1311..1317
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1318..1338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1339..1346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1347..1367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1368..1370
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1371..1391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1392..1447
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1448..1468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1469..2147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2148..2168
FT                   /note="Helical"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2169..2170
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   INTRAMEM        2171..2191
FT                   /note="Helical"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2192
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   TRANSMEM        2193..2213
FT                   /note="Helical"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2214..2228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2229..2249
FT                   /note="Helical; Note=Signal for NS4B"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2250..2274
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2275..2295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2296..2316
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2317..2337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2338..2347
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2348..2368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2369..2413
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2414..2434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2435..2459
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2460..2480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2481..3391
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1476..1653
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   DOMAIN          1655..1811
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1821..1988
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2493..2755
FT                   /note="mRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   DOMAIN          3019..3168
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          1..15
FT                   /note="Interaction with host EXOC1"
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   REGION          37..72
FT                   /note="Hydrophobic; homodimerization of capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   REGION          378..391
FT                   /note="Fusion peptide loop"
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   REGION          1398..1437
FT                   /note="Interacts with and activates NS3 protease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT   REGION          1659..1662
FT                   /note="Important for RNA-binding"
FT                   /evidence="ECO:0000269|PubMed:15917225"
FT   REGION          2708..2712
FT                   /note="Interaction with host SCRIB"
FT                   /evidence="ECO:0000250|UniProtKB:Q01299"
FT   REGION          3375..3377
FT                   /note="Interaction with host KPNA2"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   MOTIF           83..101
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   MOTIF           1759..1762
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           2568..2571
FT                   /note="SUMO-interacting motif"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   MOTIF           2812..2859
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   MOTIF           3375..3382
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   ACT_SITE        1526
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1550
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1610
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        2552
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2637
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2672
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2708
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         1668..1675
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         2547
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2577
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2578
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2595
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2596
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2622
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2623
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2638
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2710
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2929
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         2933
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         2938
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         2941
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         3203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         3219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         3338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   SITE            78
FT                   /note="Homodimerization of capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   SITE            81
FT                   /note="Homodimerization of capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   SITE            88
FT                   /note="Homodimerization of capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   SITE            92
FT                   /note="Homodimerization of capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   SITE            95
FT                   /note="Homodimerization of capsid protein"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   SITE            100..101
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            114..115
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            205..206
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250|UniProtKB:P29990, ECO:0000255"
FT   SITE            280..281
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000269|PubMed:2952760"
FT   SITE            775..776
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000269|PubMed:2952760"
FT   SITE            1127..1128
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1345..1346
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1475..1476
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:2952760"
FT   SITE            1932
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            1935
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            2093..2094
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2220..2221
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2243..2244
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2491..2492
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000269|PubMed:2952760"
FT   SITE            2505
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2508
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2509
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2511
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2516
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2520
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2552
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2637
FT                   /note="Essential for 2'-O-methyltransferase and N-7
FT                   methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2641
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2672
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2703
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2705
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2708
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            3375
FT                   /note="Important for NS5 nuclear subcellular location"
FT                   /evidence="ECO:0000250|UniProtKB:P12823"
FT   MOD_RES         1863
FT                   /note="N6-acetyllysine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q32ZE1"
FT   MOD_RES         2547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        905
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        982
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT   CARBOHYD        2301
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2305
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2457
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        148..182
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        159..194
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        167..180
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        283..310
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        340..401
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        354..385
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        372..396
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        465..565
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        582..613
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        779..790
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        830..918
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        954..998
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1055..1104
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1066..1087
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1088..1091
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   MUTAGEN         1659..1662
FT                   /note="RKRK->QNGN: Complete loss of RNA-stimulated NTPase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15917225"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:7CTH"
FT   STRAND          214..216
FT                   /evidence="ECO:0007829|PDB:7V3G"
FT   STRAND          224..231
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           232..243
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           246..257
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           262..274
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          291..293
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   TURN            297..299
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          300..308
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          321..330
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          334..353
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           363..366
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          367..380
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   TURN            381..384
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          389..401
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          404..409
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          412..426
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          434..436
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          438..440
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          452..454
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          456..458
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          460..466
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   TURN            467..469
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          474..480
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          485..489
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           490..494
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          500..502
FT                   /evidence="ECO:0007829|PDB:7CTH"
FT   HELIX           514..516
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          518..521
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          524..526
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          529..532
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           537..540
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   TURN            541..546
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          548..558
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          562..571
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          586..588
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   TURN            596..598
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          600..606
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          608..610
FT                   /evidence="ECO:0007829|PDB:7CTH"
FT   STRAND          611..614
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          617..620
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          622..625
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          627..631
FT                   /evidence="ECO:0007829|PDB:6FLB"
FT   STRAND          633..635
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          637..639
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          640..643
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          645..650
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          653..661
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          663..665
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   STRAND          667..673
FT                   /evidence="ECO:0007829|PDB:6FLC"
FT   HELIX           679..694
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          695..697
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           698..700
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          702..704
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   TURN            708..710
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           711..724
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   TURN            725..727
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   STRAND          728..730
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           733..748
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           755..759
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   TURN            760..762
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           763..772
FT                   /evidence="ECO:0007829|PDB:7V3F"
FT   HELIX           2765..2778
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   TURN            2779..2782
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          2792..2801
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2814..2819
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2821..2825
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2827..2831
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2839..2845
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2846..2850
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2854..2858
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2859..2876
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2884..2886
FT                   /evidence="ECO:0007829|PDB:6IZX"
FT   HELIX           2887..2894
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          2895..2897
FT                   /evidence="ECO:0007829|PDB:6IZX"
FT   HELIX           2913..2918
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2920..2934
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          2943..2945
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          2966..2968
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2970..2980
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2982..2985
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   TURN            2986..2989
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           2991..2994
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          2995..2997
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3003..3014
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3016..3019
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3029..3032
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3035..3042
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3043..3047
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3050..3058
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3059..3064
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3065..3075
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3078..3088
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3097..3116
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3128..3146
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3149..3152
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3155..3158
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3163..3167
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3170..3174
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3187..3189
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3191..3193
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3194..3196
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3202..3208
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3214..3219
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3222..3229
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   STRAND          3233..3236
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3239..3256
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3261..3273
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3279..3281
FT                   /evidence="ECO:0007829|PDB:6IZX"
FT   STRAND          3295..3298
FT                   /evidence="ECO:0007829|PDB:6IZX"
FT   HELIX           3300..3305
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3306..3310
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3319..3321
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3324..3326
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3328..3331
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3332..3335
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   TURN            3336..3339
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3345..3352
FT                   /evidence="ECO:0007829|PDB:6IZY"
FT   HELIX           3354..3365
FT                   /evidence="ECO:0007829|PDB:6IZY"
SQ   SEQUENCE   3391 AA;  379501 MW;  FFF98B4FF5B4BC57 CRC64;
     MNNQRKKARN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP
     PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR TAGMIIMLIP TVMAFHLTTR
     NGEPHMIVSR QEKGKSLLFK TEDGVNMCTL MAMDLGELCE DTITYKCPFL KQNEPEDIDC
     WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW
     ILRHPGFTIM AAILAYTIGT THFQRALIFI LLTAVAPSMT MRCIGISNRD FVEGVSGGSW
     VDIVLEHGSC VTTMAKNKPT LDFELIETEA KQPATLRKYC IEAKLTNTTT DSRCPTQGEP
     SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMKGKVV QPENLEYTIV
     ITPHSGEEHA VGNDTGKHGK EIKITPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ
     MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM
     HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
     VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII
     GVEPGQLKLN WFKKGSSIGQ MIETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF
     GAIYGAAFSG VSWIMKILIG VIITWIGMNS RSTSLSVSLV LVGVVTLYLG VMVQADSGCV
     VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN
     LMWKQITPEL NHILSENEVK LTIMTGDIKG IMQAGKRSLQ PQPTELKYSW KTWGKAKMLS
     TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLREKQ DVFCDSKLMS
     AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW PKSHTLWSNG VLESEMIIPK
     NFAGPVSQHN YRPGYHTQTA GPWHLGKLEM DFDFCEGTTV VVTEDCGNRG PSLRTTTASG
     KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QIDNFSLGVL
     GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT
     YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ STIPETILEL TDALALGMMV
     LKMVRKMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKADWIP
     LALTIKGLNP TAIFLTTLSR TNKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG
     GLLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL
     TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVGK AELEDGAYRI
     KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL
     EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNAGTIGA VSLDFSPGTS GSPIIDKKGK
     VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RKLTIMDLHP GAGKTKRYLP
     AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF
     TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
     PQSNAPIMDE EREIPERSWS SGHEWVTDFK GKTVWFVPSI KAGNDIAACL RKNGKKVIQL
     SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG
     PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII
     PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD
     GIKNNQILEE NVEVEIWTKE GERKKLKPRW LDAKIYSDPL ALKEFKEFAA GRKSLTLNLI
     TEMGRLPTFM TQKARDALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG
     IFLFLMSGRG IGKMTLGMCC IITASILLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR
     TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS ITTQQPESNI LDIDLRPASA
     WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG
     CYSQVNPITL TAALFLLVAH YAIIGPGLQA KATREAQKRA AAGIMKNPTV DGITVIDLDP
     IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPISTLWEG NPGRFWNTTI
     AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RGTGNIGETL GEKWKSRLNA LGKSEFQIYK
     KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY
     YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFTPPEK CDTLLCDIGE
     SSPNPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP
     LSRNSTHEMY WLSNASGNIV SSVNMISRML INRFTMRHKK ATYEPDVDLG SGTRNIGIES
     EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MGNGVVRLLT
     KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK
     TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET
     CVYNMMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
     EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG EHKKLAEAIF
     KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF
     KSIQHLTVTE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRFASALT ALNDMGKVRK
     DIQQWEPSRG WNDWTQVPFC SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR
     ETACLGKSYA QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
     LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW AKNIQTAINQ
     VRSLIGNEEY TDYMPSMKRF RKEEEEAGVL W
//