POLG_JAEV1
ID POLG_JAEV1 Reviewed; 3432 AA.
AC P27395; Q82920; Q82921; Q82922; Q82923; Q82924; Q82925; Q82926; Q82927;
AC Q82928;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 171.
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 {ECO:0000269|PubMed:7897348};
DE EC=3.6.1.15 {ECO:0000269|PubMed:18201743};
DE EC=3.6.4.13 {ECO:0000269|PubMed:18201743};
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 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 Japanese encephalitis virus (strain SA-14) (JEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=11073;
OH NCBI_TaxID=8899; Ardeidae (herons).
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=308713; Culex gelidus.
OH NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2371768; DOI=10.1016/0042-6822(90)90519-w;
RA Nitayaphan S., Grant J.A., Chang G.J.J., Trent D.W.;
RT "Nucleotide sequence of the virulent SA-14 strain of Japanese encephalitis
RT virus and its attenuated vaccine derivative, SA-14-14-2.";
RL Virology 177:541-552(1990).
RN [2]
RP FUNCTION (SERINE PROTEASE NS3), CATALYTIC ACTIVITY (SERINE PROTEASE NS3),
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), FUNCTION (SERINE PROTEASE
RP SUBUNIT NS2B), INTERACTION WITH SERINE PROTEASE SUBUNIT NS2B (SERINE
RP PROTEASE NS3), AND INTERACTION WITH SERINE PROTEASE NS3 (SERINE PROTEASE
RP SUBUNIT NS2B).
RX PubMed=7897348; DOI=10.1099/0022-1317-76-3-573;
RA Jan L.R., Yang C.S., Trent D.W., Falgout B., Lai C.J.;
RT "Processing of Japanese encephalitis virus non-structural proteins: NS2B-
RT NS3 complex and heterologous proteases.";
RL J. Gen. Virol. 76:573-580(1995).
RN [3]
RP SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE NS5).
RC STRAIN=P20778;
RX PubMed=16699025; DOI=10.1128/jvi.01982-05;
RA Uchil P.D., Kumar A.V., Satchidanandam V.;
RT "Nuclear localization of flavivirus RNA synthesis in infected cells.";
RL J. Virol. 80:5451-5464(2006).
RN [4]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
RX PubMed=16731929; DOI=10.1128/jvi.02714-05;
RA Lin R.J., Chang B.L., Yu H.P., Liao C.L., Lin Y.L.;
RT "Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis
RT virus NS5 through a protein tyrosine phosphatase-mediated mechanism.";
RL J. Virol. 80:5908-5918(2006).
RN [5]
RP FUNCTION (ENVELOPE PROTEIN E), INTERACTION WITH HOST HSPA5 (ENVELOPE
RP PROTEIN E), AND SUBCELLULAR LOCATION (ENVELOPE PROTEIN E).
RX PubMed=28053106; DOI=10.1128/jvi.02274-16;
RA Nain M., Mukherjee S., Karmakar S.P., Paton A.W., Paton J.C., Abdin M.Z.,
RA Basu A., Kalia M., Vrati S.;
RT "GRP78 Is an Important Host Factor for Japanese Encephalitis Virus Entry
RT and Replication in Mammalian Cells.";
RL J. Virol. 91:0-0(2017).
RN [6]
RP INTERACTION WITH HUMAN SPCS1, AND MUTAGENESIS OF GLU-1379; GLY-1385;
RP PRO-1405; GLY-1410; GLY-1420; PRO-1485 AND ILE-1488.
RX PubMed=29593046; DOI=10.1128/jvi.00197-18;
RA Ma L., Li F., Zhang J.W., Li W., Zhao D.M., Wang H., Hua R.H., Bu Z.G.;
RT "Host Factor SPCS1 Regulates the Replication of Japanese Encephalitis Virus
RT through Interactions with Transmembrane Domains of NS2B.";
RL J. Virol. 92:0-0(2018).
RN [7]
RP INTERACTION WITH HUMAN PROTEIN ILF2 (SERINE PROTEASE NS3).
RX PubMed=31212927; DOI=10.3390/v11060559;
RA Cui X., Qian P., Rao T., Wei Y., Zhao F., Zhang H., Chen H., Li X.;
RT "Cellular Interleukin Enhancer-Binding Factor 2, ILF2, Inhibits Japanese
RT Encephalitis Virus Replication In Vitro.";
RL Viruses 11:0-0(2019).
RN [8] {ECO:0007744|PDB:2Z83}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1685-2123, MUTAGENESIS OF
RP GLY-1703; LYS-1704; THR-1705; GLN-1961; ARG-1962; ARG-1965 AND ARG-1968,
RP CATALYTIC ACTIVITY (SERINE PROTEASE NS3), AND FUNCTION (SERINE PROTEASE
RP NS3).
RX PubMed=18201743; DOI=10.1016/j.virol.2007.12.018;
RA Yamashita T., Unno H., Mori Y., Tani H., Moriishi K., Takamizawa A.,
RA Agoh M., Tsukihara T., Matsuura Y.;
RT "Crystal structure of the catalytic domain of Japanese encephalitis virus
RT NS3 helicase/nucleoside triphosphatase at a resolution of 1.8 A.";
RL Virology 373:426-436(2008).
RN [9] {ECO:0007744|PDB:3P54}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 295-700.
RX PubMed=22156523; DOI=10.1128/jvi.06072-11;
RA Luca V.C., AbiMansour J., Nelson C.A., Fremont D.H.;
RT "Crystal structure of the Japanese encephalitis virus envelope protein.";
RL J. Virol. 86:2337-2346(2012).
RN [10] {ECO:0007744|PDB:4K6M}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2528-3432 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND ZINC.
RX PubMed=23950717; DOI=10.1371/journal.ppat.1003549;
RA Lu G., Gong P.;
RT "Crystal Structure of the full-length Japanese encephalitis virus NS5
RT reveals a conserved methyltransferase-polymerase interface.";
RL PLoS Pathog. 9:E1003549-E1003549(2013).
RN [11] {ECO:0007744|PDB:4HDG, ECO:0007744|PDB:4HDH, ECO:0007744|PDB:4MTP}
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2799-3432 IN COMPLEX WITH ATP;
RP GTP AND ZINC, FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND COFACTOR
RP (RNA-DIRECTED RNA POLYMERASE NS5).
RX PubMed=24293643; DOI=10.1093/nar/gkt1106;
RA Surana P., Satchidanandam V., Nair D.T.;
RT "RNA-dependent RNA polymerase of Japanese encephalitis virus binds the
RT initiator nucleotide GTP to form a mechanistically important pre-initiation
RT state.";
RL Nucleic Acids Res. 42:2758-2773(2014).
CC -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC to the cell membrane and gathering the viral RNA into a nucleocapsid
CC that 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}.
CC -!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
CC with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC -!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
CC proteins in trans-Golgi by binding to envelope protein E at pH 6.0.
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 peptide. prM is the only viral peptide
CC matured by host furin in the trans-Golgi network probably to avoid
CC catastrophic activation of the viral fusion activity in acidic Golgi
CC compartment prior to virion release. prM-E cleavage is inefficient, and
CC many virions are only partially matured. These uncleaved prM would play
CC a 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]: Binds to host cell surface receptor and
CC mediates fusion between viral and cellular membranes. Efficient virus
CC attachment to cell is, at least in part, mediated by host HSPA5
CC (PubMed:28053106). 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 heterodimer between precursor prM
CC and envelope protein E. The virion is transported to the Golgi
CC apparatus where the low pH causes dissociation of PrM-E heterodimers
CC and formation of E homodimers. 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: [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).
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC replication complex that functions in virion assembly and antagonizes
CC the host alpha/beta interferon antiviral response.
CC {ECO:0000250|UniProtKB:P14335}.
CC -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC serine protease function of NS3 (PubMed:7897348). May have membrane-
CC destabilizing activity and form viroporins (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:7897348}.
CC -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC serine protease, NTPase and RNA helicase (PubMed:18201743,
CC PubMed:7897348). NS3 serine protease, in association with NS2B,
CC performs its autocleavage and cleaves the polyprotein at dibasic sites
CC in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and
CC NS4B-NS5 (Probable). NS3 RNA helicase binds RNA and unwinds dsRNA in
CC the 3' to 5' direction (By similarity). {ECO:0000255|PROSITE-
CC ProRule:PRU00860, ECO:0000269|PubMed:18201743,
CC ECO:0000269|PubMed:7897348, ECO:0000305|PubMed:7897348}.
CC -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to
CC conserve energy during unwinding (By similarity).
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
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 (By
CC similarity). Inhibits interferon (IFN)-induced host STAT1
CC phosphorylation and nuclear translocation, thereby preventing the
CC establishment of cellular antiviral state by blocking the IFN-
CC alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the
CC nucleus after IFN-alpha treatment (By similarity).
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC and (-) RNA genome (PubMed:24293643). Performs the capping of genomes
CC in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and
CC ribose 2'-O positions (By similarity). 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 (PubMed:16731929). Inhibits host TYK2 and STAT2
CC phosphorylation, thereby preventing activation of JAK-STAT signaling
CC pathway (PubMed:16731929). {ECO:0000250|UniProtKB:Q9Q6P4,
CC ECO:0000269|PubMed:16731929, ECO:0000269|PubMed:24293643}.
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; Evidence={ECO:0000269|PubMed:7897348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000269|PubMed:18201743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:18201743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-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 + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=For RNA-directed RNA polymerase NS5 activity; Mn(2+) is more
CC effective than Mg(2+). {ECO:0000269|PubMed:24293643};
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). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi (By similarity). Interacts with protein prM (By similarity).
CC Interacts with non-structural protein 1 (By similarity). Interacts with
CC host HSPA5 (PubMed:28053106). {ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:28053106}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted (By similarity). Interacts with envelope protein E (By
CC similarity). NS1 interacts with NS4B (By similarity). Interacts with
CC host complement protein CFH; this interaction leads to the degradation
CC of C3 (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC serine protease NS3. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC serine protease NS3 (PubMed:7897348). May form homooligomers (By
CC similarity). Interacts with human SPCS1 (PubMed:29593046).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:29593046,
CC ECO:0000269|PubMed:7897348}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B
CC (PubMed:7897348). Interacts with non-structural protein 2A (via N-
CC terminus) (By similarity). Interacts with NS4B (By similarity).
CC Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this
CC interaction stimulates RNA-directed RNA polymerase NS5
CC guanylyltransferase activity (By similarity). Interacts with host ILF2
CC (PubMed:31212927). {ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:7897348}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3 (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer. Interacts with
CC host STAT2; this interaction inhibits the phosphorylation of the
CC latter, and, when all viral proteins are present (polyprotein), targets
CC STAT2 for degradation. Interacts with serine protease NS3.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Genome polyprotein]: Host endoplasmic reticulum
CC membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
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:P06935}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:P06935}.
CC -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Host cell surface {ECO:0000269|PubMed:28053106}. Note=ER
CC membrane retention is mediated by the transmembrane domains.
CC {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC {ECO:0000250|UniProtKB:P17763}. 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:0000250|UniProtKB:P14335}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}.
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:0000250|UniProtKB:P14335}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
CC vesicles hosting the replication complex.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC vesicles hosting the replication complex.
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
CC endoplasmic reticulum membrane; Peripheral membrane protein;
CC Cytoplasmic side {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC {ECO:0000269|PubMed:16699025}. Note=Located in RE-associated vesicles
CC hosting the replication complex. NS5 protein is mainly localized in the
CC nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=P27395-1; Sequence=Displayed;
CC Name=Structural polyprotein;
CC IsoId=P0DOH7-1; Sequence=External;
CC -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC envelope protein E contain an endoplasmic reticulum retention signal.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins (PubMed:7897348). Cleavages in the lumen of endoplasmic
CC reticulum are performed by host signal peptidase, whereas cleavages in
CC the cytoplasmic side are performed by serine protease NS3. Signal
CC cleavage at the 2K-4B site requires a prior NS3 protease-mediated
CC cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:7897348}.
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: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
CC residues. This phosphorylation may trigger NS5 nuclear localization.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- MISCELLANEOUS: Strain SA-14 is classified as genotype III.
CC {ECO:0000305}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA46249.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M55506; AAA46248.1; -; Genomic_RNA.
DR EMBL; M55506; AAA46249.1; ALT_INIT; Genomic_RNA.
DR PIR; A35519; GNWVJS.
DR PDB; 2Z83; X-ray; 1.80 A; A=1685-2123.
DR PDB; 3P54; X-ray; 2.10 A; A=295-700.
DR PDB; 4HDG; X-ray; 2.38 A; A/B=2799-3432.
DR PDB; 4HDH; X-ray; 2.28 A; A/B=2799-3432.
DR PDB; 4K6M; X-ray; 2.60 A; A/B=2528-3432.
DR PDB; 4MTP; X-ray; 3.65 A; A/B/C/D=2799-3432.
DR PDB; 5MV1; X-ray; 2.25 A; A=295-700.
DR PDB; 5MV2; X-ray; 2.10 A; A=295-700.
DR PDB; 5O19; X-ray; 2.10 A; A=965-1146.
DR PDB; 5O36; X-ray; 2.60 A; A=965-1158.
DR PDB; 5OW2; X-ray; 1.98 A; A/B=1-105.
DR PDB; 5WSN; EM; 4.30 A; B/D/F=220-293.
DR PDB; 5YWO; EM; 4.70 A; B/D/F=220-293.
DR PDB; 5YWP; EM; 4.60 A; B/D/F=220-293.
DR PDBsum; 2Z83; -.
DR PDBsum; 3P54; -.
DR PDBsum; 4HDG; -.
DR PDBsum; 4HDH; -.
DR PDBsum; 4K6M; -.
DR PDBsum; 4MTP; -.
DR PDBsum; 5MV1; -.
DR PDBsum; 5MV2; -.
DR PDBsum; 5O19; -.
DR PDBsum; 5O36; -.
DR PDBsum; 5OW2; -.
DR PDBsum; 5WSN; -.
DR PDBsum; 5YWO; -.
DR PDBsum; 5YWP; -.
DR SMR; P27395; -.
DR MEROPS; S07.003; -.
DR PRIDE; P27395; -.
DR BRENDA; 3.4.21.91; 2787.
DR BRENDA; 3.6.4.12; 2787.
DR BRENDA; 3.6.4.13; 2787.
DR EvolutionaryTrace; P27395; -.
DR Proteomes; UP000008380; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO: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:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus 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; cd12149; Flavi_E_C; 1.
DR Gene3D; 1.10.10.930; -; 1.
DR Gene3D; 1.10.8.970; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.60.260.50; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.98.10; -; 1.
DR Gene3D; 3.30.387.10; -; 1.
DR Gene3D; 3.30.67.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
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; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR001850; Flavivirus_NS3_S7.
DR InterPro; IPR014412; Gen_Poly_FLV.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
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.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 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; 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; SSF101257; SSF101257; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Capsid protein; 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; Host nucleus;
KW 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 STAT1 by virus; Inhibition of host STAT2 by virus;
KW Inhibition of host TYK2 by virus; Membrane; Metal-binding;
KW Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Secreted; Serine protease;
KW Suppressor of RNA silencing; Transcription; Transcription regulation;
KW Transferase; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus endocytosis by host; Virus entry into host cell; Zinc.
FT CHAIN 1..3432
FT /note="Genome polyprotein"
FT /id="PRO_0000405188"
FT CHAIN 1..105
FT /note="Capsid protein C"
FT /id="PRO_0000037836"
FT PROPEP 106..127
FT /note="ER anchor for the capsid protein C, removed in
FT mature form by serine protease NS3"
FT /id="PRO_0000405189"
FT CHAIN 128..294
FT /note="Protein prM"
FT /id="PRO_0000405190"
FT CHAIN 128..219
FT /note="Peptide pr"
FT /id="PRO_0000037837"
FT CHAIN 220..294
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037838"
FT CHAIN 295..794
FT /note="Envelope protein E"
FT /id="PRO_0000037839"
FT CHAIN 795..1146
FT /note="Non-structural protein 1"
FT /id="PRO_0000037840"
FT CHAIN 1147..1373
FT /note="Non-structural protein 2A"
FT /id="PRO_0000037841"
FT CHAIN 1374..1504
FT /note="Serine protease subunit NS2B"
FT /id="PRO_0000037842"
FT CHAIN 1505..2123
FT /note="Serine protease NS3"
FT /id="PRO_0000037843"
FT CHAIN 2124..2249
FT /note="Non-structural protein 4A"
FT /id="PRO_0000037844"
FT PEPTIDE 2250..2272
FT /note="Peptide 2k"
FT /id="PRO_0000405191"
FT CHAIN 2273..2527
FT /note="Non-structural protein 4B"
FT /id="PRO_0000037845"
FT CHAIN 2528..3432
FT /note="RNA-directed RNA polymerase NS5"
FT /id="PRO_0000037846"
FT TOPO_DOM 2..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..294
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 295..746
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..1219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1241..1250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1251..1271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1272
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1273..1293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1294..1309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1310..1330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1331..1341
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1363..1374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1375..1395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1396..1398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1399..1419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1420..1476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1477..1497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1498..2173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2174..2194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2195..2199
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2200..2220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2221
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2222..2242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2243..2257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2258..2278
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2279..2311
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2312..2332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2333..2368
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2369..2389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2390..2444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2445..2465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2466..2469
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2470..2490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2491..3432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1505..1682
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1685..1841
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1852..2017
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2528..2793
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3057..3209
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2..15
FT /note="Interaction with host EXOC1"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT REGION 37..72
FT /note="Hydrophobic; homodimerization of capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT REGION 392..405
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1374..1423
FT /note="Interaction with human SPCS1"
FT /evidence="ECO:0000269|PubMed:29593046"
FT REGION 1427..1466
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT REGION 1458..1505
FT /note="Interaction with human SPCS1"
FT /evidence="ECO:0000269|PubMed:29593046"
FT REGION 1689..1692
FT /note="Important for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P14340"
FT REGION 1950..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2168..2172
FT /note="Regulates the ATPase activity of NS3 helicase"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT MOTIF 1789..1792
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT ACT_SITE 1555
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1579
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1639
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 2588
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2673
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2709
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2745
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT BINDING 1698..1705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2583
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2613
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2614
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2631
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2632
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2658
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2659
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2674
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2747
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2967
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24293643"
FT BINDING 2971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24293643"
FT BINDING 2976
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24293643"
FT BINDING 2979
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24293643"
FT BINDING 3244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24293643"
FT BINDING 3260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24293643"
FT BINDING 3379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24293643"
FT SITE 105..106
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 127..128
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 219..220
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 294..295
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 794..795
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1146..1147
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1373..1374
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1504..1505
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1962
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1965
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 2123..2124
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2249..2250
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2272..2273
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2527..2528
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2540
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2543
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2544
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2546
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2551
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2555
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2588
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2673
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2677
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2709
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2740
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2742
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2745
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 924
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 297..324
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 354..415
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 354..410
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 368..399
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 386..415
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 386..410
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 484..581
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 598..629
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 798..809
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 849..937
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 973..1017
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1074..1123
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1085..1106
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1107..1110
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT MUTAGEN 1379
FT /note="E->A: No effect on human SPCS1 binding."
FT /evidence="ECO:0000269|PubMed:29593046"
FT MUTAGEN 1385
FT /note="G->A: Reduces human SPCS1 binding."
FT /evidence="ECO:0000269|PubMed:29593046"
FT MUTAGEN 1405
FT /note="P->A: Slightly reduces human SPCS1 binding."
FT /evidence="ECO:0000269|PubMed:29593046"
FT MUTAGEN 1410
FT /note="G->A: Slightly reduces human SPCS1 binding."
FT /evidence="ECO:0000269|PubMed:29593046"
FT MUTAGEN 1420
FT /note="G->A: Slightly reduces human SPCS1 binding."
FT /evidence="ECO:0000269|PubMed:29593046"
FT MUTAGEN 1485
FT /note="P->A: Reduces SPCS1 human binding."
FT /evidence="ECO:0000269|PubMed:29593046"
FT MUTAGEN 1488
FT /note="I->A: Slightly reduces human SPCS1 binding."
FT /evidence="ECO:0000269|PubMed:29593046"
FT MUTAGEN 1703
FT /note="G->A: Complete loss of both the ATPase and helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:18201743"
FT MUTAGEN 1704
FT /note="K->D,E,H,N,Q,R: Complete loss of both the ATPase and
FT helicase activities."
FT /evidence="ECO:0000269|PubMed:18201743"
FT MUTAGEN 1705
FT /note="T->A: Complete loss of both the ATPase and helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:18201743"
FT MUTAGEN 1961
FT /note="Q->A: 80% loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:18201743"
FT MUTAGEN 1962
FT /note="R->A: 90% loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:18201743"
FT MUTAGEN 1965
FT /note="R->A: Complete loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:18201743"
FT MUTAGEN 1968
FT /note="R->A: Complete loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:18201743"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:5OW2"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:5OW2"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:5OW2"
FT HELIX 74..96
FT /evidence="ECO:0007829|PDB:5OW2"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 335..344
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 348..366
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 384..394
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 403..423
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 428..437
FT /evidence="ECO:0007829|PDB:3P54"
FT TURN 443..447
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:3P54"
FT TURN 509..514
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 553..559
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 561..575
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:3P54"
FT TURN 591..594
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 602..610
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 616..622
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 646..650
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 662..669
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 672..681
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 682..684
FT /evidence="ECO:0007829|PDB:3P54"
FT STRAND 686..692
FT /evidence="ECO:0007829|PDB:3P54"
FT HELIX 975..977
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 978..983
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 986..1013
FT /evidence="ECO:0007829|PDB:5O19"
FT HELIX 1021..1023
FT /evidence="ECO:0007829|PDB:5O19"
FT HELIX 1032..1034
FT /evidence="ECO:0007829|PDB:5O19"
FT HELIX 1039..1041
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 1064..1066
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 1068..1072
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 1078..1081
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 1092..1095
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 1104..1109
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 1115..1119
FT /evidence="ECO:0007829|PDB:5O19"
FT STRAND 1122..1125
FT /evidence="ECO:0007829|PDB:5O19"
FT HELIX 1686..1688
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1693..1696
FT /evidence="ECO:0007829|PDB:2Z83"
FT TURN 1704..1707
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1708..1718
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1723..1727
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1730..1739
FT /evidence="ECO:0007829|PDB:2Z83"
FT TURN 1740..1742
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1745..1747
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1761..1766
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1767..1775
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1784..1790
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1796..1810
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1815..1819
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1837..1841
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1854..1858
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1863..1866
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1870..1882
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1887..1891
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1894..1898
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1899..1901
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1902..1904
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1908..1914
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1925..1929
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1936..1939
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1941..1943
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1945..1948
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1956..1963
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 1975..1979
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 1991..2001
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2015..2020
FT /evidence="ECO:0007829|PDB:2Z83"
FT TURN 2025..2028
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2032..2043
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2049..2057
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2066..2068
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2073..2075
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 2085..2087
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 2093..2095
FT /evidence="ECO:0007829|PDB:2Z83"
FT STRAND 2099..2102
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2103..2106
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2109..2120
FT /evidence="ECO:0007829|PDB:2Z83"
FT HELIX 2535..2544
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2548..2554
FT /evidence="ECO:0007829|PDB:4K6M"
FT TURN 2555..2558
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2560..2562
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2565..2572
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2585..2593
FT /evidence="ECO:0007829|PDB:4K6M"
FT TURN 2594..2596
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2602..2607
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2613..2619
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2624..2630
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2648..2650
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2651..2654
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2659..2661
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2668..2672
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2681..2699
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2704..2711
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2716..2729
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2732..2734
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2746..2749
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2756..2770
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 2780..2782
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2802..2816
FT /evidence="ECO:0007829|PDB:4HDH"
FT TURN 2817..2820
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 2830..2839
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 2852..2856
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 2859..2863
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 2865..2868
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 2870..2872
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2877..2887
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 2897..2914
FT /evidence="ECO:0007829|PDB:4HDH"
FT TURN 2915..2917
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 2925..2932
FT /evidence="ECO:0007829|PDB:4HDH"
FT TURN 2933..2935
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 2943..2945
FT /evidence="ECO:0007829|PDB:4K6M"
FT TURN 2946..2948
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 2951..2956
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 2958..2972
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 2981..2987
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 2989..2991
FT /evidence="ECO:0007829|PDB:4K6M"
FT TURN 2994..2996
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3001..3005
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3008..3018
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3020..3023
FT /evidence="ECO:0007829|PDB:4HDH"
FT TURN 3024..3027
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3029..3032
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3033..3035
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3041..3053
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3054..3057
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3067..3069
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3073..3079
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3080..3085
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3088..3100
FT /evidence="ECO:0007829|PDB:4HDH"
FT TURN 3101..3103
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3104..3113
FT /evidence="ECO:0007829|PDB:4HDH"
FT TURN 3114..3116
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3117..3126
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3136..3155
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3161..3163
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3169..3187
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3190..3193
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3196..3199
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3204..3208
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3211..3215
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3220..3223
FT /evidence="ECO:0007829|PDB:4K6M"
FT STRAND 3232..3234
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 3235..3237
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3243..3249
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3255..3260
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3263..3270
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3272..3275
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 3280..3297
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3302..3314
FT /evidence="ECO:0007829|PDB:4HDH"
FT STRAND 3336..3339
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3341..3349
FT /evidence="ECO:0007829|PDB:4HDH"
FT TURN 3350..3352
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 3365..3367
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3373..3378
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3386..3406
FT /evidence="ECO:0007829|PDB:4HDH"
FT HELIX 3415..3417
FT /evidence="ECO:0007829|PDB:4K6M"
FT HELIX 3419..3421
FT /evidence="ECO:0007829|PDB:4K6M"
SQ SEQUENCE 3432 AA; 380211 MW; 11B9423735B1B5FE CRC64;
MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL ITFFKFTALA
PTKALLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR KQNKRGGNEG SIMWLASLAV
VIACAGAMKL SNFQGKLLMT INNTDIADVI VIPTSKGENR CWVRAIDVGY MCEDTITYEC
PKLTMGNDPE DVDCWCDNQE VYVQYGRCTR TRHSKRSRRS VSVQTHGESS LVNKKEAWLD
STKATRYLMK TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM
GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV RSYCYHASVT
DISTVARCPT TGEAHNEKRA DSSYVCKQGF TDRGWGNGCG LFGKGSIDTC AKFSCTSKAI
GRTIQPENIK YEVGIFVHGT TTSENHGNYS AQVGASQAAK FTVTPNAPSI TLKLGDYGEV
TLDCEPRSGL NTEAFYVMTV GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEGAH
ATKQSVVALG SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE
KFSFAKNPVD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT VNPFVATSSA
NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA FSTTLKGAQR LAALGDTAWD
FGSIGGVFNS IGRAVHQVFG GAFRTLFGGM SWITQGLMGA LLLWMGVNAR DRSIALAFLA
TGGVLVFLAT NVHADTGCAI DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV
HKAHKEGVCG VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM
TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE DFGFGITSTR
VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY NDTWKLERAV FGEVKSCTWP
ETHTLWGDDV EESELIIPHT IAGPKSKHNR REGYKTQNQG PWDENGIVLD FDYCPGTKVT
ITEDCSKRGP SVRTTTDSGK LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVMHDETTLV
RSQVDAFKGE MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGVLLVL MLGGITYTDL
ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN VILVLGAAFF
QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV LALLTPGMRA LYLDTYRIIL
LVIGICSLLH ERKKTMAKKK GAVLLGLALT STGWFSPTTI AAGLMVCNPN KKRGWPATEF
LSAVGLMFAI VGGLAELDIE SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA
ITGSSRRLDV KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK
TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF HTLWHTTRGA
AIMSGEGKLT PYWGSVREDR IAYGGPWRFD RKWNGTDDVQ VIVVEPGKAA VNIQTKPGVF
RTPFGEVGAV SLDYPRGTSG SPILDSNGDI IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP
EAYTPNMLRK RQMTVLDLHP GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL
RGLPVRYQTS AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA
ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS SGYEWITEYA
GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP KCKNGDWDFV ITTDISEMGA
NFGASRVIDC RKSVKPTILE EGEGRVILGN PSPITSASAA QRRGRVGRNP NQVGDEYHYG
GATSEDDSNL AHWTEAKIML DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE
LLRTADLPVW LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW
LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM YLVATAEKGG
KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI GKMGLGALVL TLATFFLWAA
EVPGTKIAGT LLIALLLMVV LIPEPEKQRS QTDNQLAVFL ICVLTVVGVV AANEYGMLEK
TKADLKSMFG GKTQASGLTG LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS
LASINSQAGS LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG
WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL IGVSVAAFLV
NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH VMRGSYLAGG SIAWTLIKNA
DKPSLKRGRP GGRTLGEQWK EKLNAMSREE FFKYRREAII EVDRTEARRA RRENNIVGGH
PVSRGSAKLR WLVEKGFVSP IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP
MLMQSYGWNL VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH
RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS GAAGNVVHAV
NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH SNQEKIKKRI QKLKEEFATT
WHKDPEHPYR TWTYHGSYEV KATGSASSLV NGVVELMSKP WDAIANVTTM AMTDTTPFGQ
QRVFKEKVDT KAPEPPAGAK EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA
VFAEQNQWST AREAVDDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS
RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD IAGKQGGKMY
ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL TYRHKVVKVM RPAAEGKTVM
DVISREDQRG SGQVVTYALN TFTNIAVQLV RLMEAEGVIG PQHLEQLPRK TKIAVRTWLF
ENGEERVTRM AISGDDCVVK PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF
CSNHFQEIVM KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH
RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLQVWNRVWI EENEWMMDKT
PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN QVRAVIGKEN YVDYMTSLRR
YEDVLIQEDR VI
