POLG_MVEV5
ID POLG_MVEV5 Reviewed; 3434 AA.
AC P05769; Q9Q9F7;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Peptide 2k;
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:0000269|PubMed:19793813};
DE EC=3.6.4.13 {ECO:0000269|PubMed:19793813};
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=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 Murray valley encephalitis virus (strain MVE-1-51) (MVEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus;
OC Murray Valley encephalitis virus.
OX NCBI_TaxID=301478;
OH NCBI_TaxID=162997; Culex annulirostris (Common banded mosquito).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10567642; DOI=10.1099/0022-1317-80-12-3115;
RA Hurrelbrink R.J., Nestorowicz A., McMinn P.C.;
RT "Characterization of infectious Murray Valley encephalitis virus derived
RT from a stably cloned genomic-length cDNA.";
RL J. Gen. Virol. 80:3115-3125(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1780.
RX PubMed=3009829; DOI=10.1016/0022-2836(86)90435-3;
RA Dalgarno L., Trent D.W., Strauss J.H., Rice C.M.;
RT "Partial nucleotide sequence of the Murray Valley encephalitis virus
RT genome. Comparison of the encoded polypeptides with yellow fever virus
RT structural and non-structural proteins.";
RL J. Mol. Biol. 187:309-323(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1773-3434, AND PROTEIN SEQUENCE OF 794-807;
RP 1504-1519 AND 2530-2537.
RX PubMed=1702914; DOI=10.1007/bf00265630;
RA Lee E., Fernon C., Simpson R., Weir R.C., Rice C.M., Dalgarno L.;
RT "Sequence of the 3' half of the Murray Valley encephalitis virus genome and
RT mapping of the nonstructural proteins NS1, NS3, and NS5.";
RL Virus Genes 4:197-213(1990).
RN [4]
RP GLYCOSYLATION (ENVELOPE PROTEIN E).
RX PubMed=2441520; DOI=10.1016/0042-6822(87)90460-0;
RA Winkler G., Heinz F.X., Kunz C.;
RT "Studies on the glycosylation of flavivirus E proteins and the role of
RT carbohydrate in antigenic structure.";
RL Virology 159:237-243(1987).
RN [5]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX PubMed=8392191; DOI=10.1073/pnas.90.13.6218;
RA Lobigs M.;
RT "Flavivirus premembrane protein cleavage and spike heterodimer secretion
RT require the function of the viral proteinase NS3.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6218-6222(1993).
RN [6]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), AND MUTAGENESIS OF
RP 121-GLY--ALA-124.
RX PubMed=9499070; DOI=10.1128/jvi.72.3.2141-2149.1998;
RA Stocks C.E., Lobigs M.;
RT "Signal peptidase cleavage at the flavivirus C-prM junction: dependence on
RT the viral NS2B-3 protease for efficient processing requires determinants in
RT C, the signal peptide, and prM.";
RL J. Virol. 72:2141-2149(1998).
RN [7]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX PubMed=7494334; DOI=10.1128/jvi.69.12.8123-8126.1995;
RA Stocks C.E., Lobigs M.;
RT "Posttranslational signal peptidase cleavage at the flavivirus C-prM
RT junction in vitro.";
RL J. Virol. 69:8123-8126(1995).
RN [8]
RP GLYCOSYLATION (NON-STRUCTURAL PROTEIN 1), AND DISULFIDE BONDS.
RX PubMed=11514736; DOI=10.1099/0022-1317-82-9-2251;
RA Blitvich B.J., Scanlon D., Shiell B.J., Mackenzie J.S., Pham K., Hall R.A.;
RT "Determination of the intramolecular disulfide bond arrangement and
RT biochemical identification of the glycosylation sites of the nonstructural
RT protein NS1 of Murray Valley encephalitis virus.";
RL J. Gen. Virol. 82:2251-2256(2001).
RN [9]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX PubMed=20207389; DOI=10.1016/j.virol.2010.02.008;
RA Lobigs M., Lee E., Ng M.L., Pavy M., Lobigs P.;
RT "A flavivirus signal peptide balances the catalytic activity of two
RT proteases and thereby facilitates virus morphogenesis.";
RL Virology 401:80-89(2010).
RN [10]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX PubMed=26377679; DOI=10.1186/s12985-015-0375-4;
RA Addis S.N., Lee E., Bettadapura J., Lobigs M.;
RT "Proteolytic cleavage analysis at the Murray Valley encephalitis virus NS1-
RT 2A junction.";
RL Virol. J. 12:144-144(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1681-2122.
RX PubMed=17893366; DOI=10.1110/ps.072843107;
RA Mancini E.J., Assenberg R., Verma A., Walter T.S., Tuma R., Grimes J.M.,
RA Owens R.J., Stuart D.I.;
RT "Structure of the Murray Valley encephalitis virus RNA helicase at 1.9
RT Angstrom resolution.";
RL Protein Sci. 16:2294-2300(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2530-2798.
RX PubMed=17622627; DOI=10.1099/vir.0.82757-0;
RA Assenberg R., Ren J., Verma A., Walter T.S., Alderton D., Hurrelbrink R.J.,
RA Fuller S.D., Bressanelli S., Owens R.J., Stuart D.I., Grimes J.M.;
RT "Crystal structure of the Murray Valley encephalitis virus NS5
RT methyltransferase domain in complex with cap analogues.";
RL J. Gen. Virol. 88:2228-2236(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1421-2122, CATALYTIC ACTIVITY
RP (SERINE PROTEASE NS3), AND FUNCTION (SERINE PROTEASE NS3).
RX PubMed=19793813; DOI=10.1128/jvi.00942-09;
RA Assenberg R., Mastrangelo E., Walter T.S., Verma A., Milani M., Owens R.J.,
RA Stuart D.I., Grimes J.M., Mancini E.J.;
RT "Crystal structure of a novel conformational state of the flavivirus NS3
RT protein: implications for polyprotein processing and viral replication.";
RL J. Virol. 83:12895-12906(2009).
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 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 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. Envelope protein
CC is synthesized in the endoplasmic reticulum in the form of heterodimer
CC with protein prM. They play a role in virion budding in the ER, and the
CC newly formed immature particle is covered with 60 spikes composed of
CC heterodimer between precursor prM and envelope protein E. The virion is
CC transported to the Golgi apparatus where the low pH causes dissociation
CC of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC inefficient, and many virions are only partially matured. These
CC uncleaved prM would play a role in immune evasion.
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).
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. 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, ECO:0000269|PubMed:19793813}.
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. {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.
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. Inhibits STAT2
CC translocation in the nucleus after IFN-alpha treatment.
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC and (-) RNA genome, and performs the capping of genomes in the
CC cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
CC positions. Besides its role in RNA genome replication, also prevents
CC the establishment of cellular antiviral state by blocking the
CC interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host
CC TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-
CC STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
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=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 -!- 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:19793813};
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 -!- 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).
CC {ECO:0000250|UniProtKB:P17763}.
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 (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 non-structural protein 2A (via N-terminus)
CC (By 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 (By similarity). {ECO:0000250|UniProtKB:P17763}.
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: [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}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {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. Host nucleus {ECO:0000250|UniProtKB:P06935}.
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. {ECO:0000250|UniProtKB:P17763}.
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. 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:0000269|PubMed:20207389,
CC ECO:0000269|PubMed:26377679, ECO:0000269|PubMed:7494334,
CC ECO:0000269|PubMed:8392191, ECO:0000269|PubMed:9499070}.
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:0000269|PubMed:2441520}.
CC -!- PTM: [Non-structural protein 1]: N-glycosylated (PubMed:11514736). The
CC excreted form is glycosylated and this is required for efficient
CC secretion of the protein from infected cells (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:11514736}.
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 -!- 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}.
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DR EMBL; AF161266; AAF05296.1; -; Genomic_RNA.
DR EMBL; X03467; CAA27184.1; -; Unassigned_RNA.
DR PIR; A24635; GNWVMV.
DR RefSeq; NP_051124.1; NC_000943.1.
DR PDB; 2PX2; X-ray; 2.00 A; A/B=2530-2798.
DR PDB; 2PX4; X-ray; 2.20 A; A=2530-2798.
DR PDB; 2PX5; X-ray; 2.30 A; A/B=2530-2798.
DR PDB; 2PX8; X-ray; 2.20 A; A/B=2530-2798.
DR PDB; 2PXA; X-ray; 2.30 A; A/B=2530-2798.
DR PDB; 2PXC; X-ray; 2.80 A; A=2530-2798.
DR PDB; 2V8O; X-ray; 1.90 A; A=1681-2122.
DR PDB; 2WV9; X-ray; 2.75 A; A=1421-1465, A=1504-2122.
DR PDBsum; 2PX2; -.
DR PDBsum; 2PX4; -.
DR PDBsum; 2PX5; -.
DR PDBsum; 2PX8; -.
DR PDBsum; 2PXA; -.
DR PDBsum; 2PXC; -.
DR PDBsum; 2V8O; -.
DR PDBsum; 2WV9; -.
DR BMRB; P05769; -.
DR SMR; P05769; -.
DR MEROPS; S07.003; -.
DR iPTMnet; P05769; -.
DR PRIDE; P05769; -.
DR GeneID; 1489715; -.
DR KEGG; vg:1489715; -.
DR BRENDA; 3.4.21.91; 14117.
DR BRENDA; 3.6.4.13; 14117.
DR EvolutionaryTrace; P05769; -.
DR Proteomes; UP000008863; 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: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: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 DisProt; DP02212; -.
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; Direct protein sequencing;
KW Disulfide bond; 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 Membrane; 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;
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..3434
FT /note="Genome polyprotein"
FT /id="PRO_0000405163"
FT CHAIN 1..105
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037782"
FT PROPEP 106..125
FT /note="ER anchor for the capsid protein C, removed in
FT mature form by serine protease NS3"
FT /id="PRO_0000405164"
FT CHAIN 126..292
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000405165"
FT CHAIN 126..217
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037783"
FT CHAIN 218..292
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037784"
FT CHAIN 293..793
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037785"
FT CHAIN 794..1145
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037786"
FT CHAIN 1146..1372
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037787"
FT CHAIN 1373..1503
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037788"
FT CHAIN 1504..2122
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037789"
FT CHAIN 2123..2248
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037790"
FT PEPTIDE 2249..2271
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000405166"
FT CHAIN 2272..2529
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037791"
FT CHAIN 2530..3434
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037792"
FT TOPO_DOM 2..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..292
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 293..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..1218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1219..1239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1240..1249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1250..1270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1271..1286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1287..1307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1309..1329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1330..1340
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1341..1361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1362..1373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1374..1394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1395..1397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1398..1418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1419..1475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1476..1496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1497..2172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2173..2193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2194..2197
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2198..2218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2219..2220
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2221..2241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2242..2256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2257..2271
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000305"
FT TOPO_DOM 2272..2309
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2310..2330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2331..2366
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2367..2394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2395..2446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2447..2467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2468..2498
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2499..2519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2520..3434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1504..1681
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1684..1840
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1851..2016
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2530..2795
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3059..3211
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 390..403
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1426..1465
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT REGION 1688..1691
FT /note="Important for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P14340"
FT REGION 1958..1979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2167..2171
FT /note="Regulates the ATPase activity of NS3 helicase"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT MOTIF 1788..1791
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT ACT_SITE 1554
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1578
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1638
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 2590
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2675
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2711
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2747
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT BINDING 1697..1704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2585
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2615
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2616
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2633
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2634
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2660
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2661
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2676
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2749
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2969
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 105..106
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 125..126
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000269|PubMed:20207389"
FT SITE 217..218
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT SITE 292..293
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 793..794
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 1145..1146
FT /note="Cleavage; by host"
FT /evidence="ECO:0000269|PubMed:26377679"
FT SITE 1372..1373
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 1503..1504
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 1961
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1964
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 2122..2123
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 2248..2249
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 2271..2272
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 2529..2530
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 2542
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2545
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2546
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2548
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2553
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2557
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2590
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2675
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2679
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2711
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2742
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2744
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2747
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:11514736"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:11514736"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) (high mannose) asparagine; by
FT host"
FT /evidence="ECO:0000269|PubMed:11514736"
FT DISULFID 295..322
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 352..413
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 352..408
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 366..397
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 384..413
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 384..408
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 482..580
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 597..628
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 797..808
FT /evidence="ECO:0000269|PubMed:11514736"
FT DISULFID 848..936
FT /evidence="ECO:0000269|PubMed:11514736"
FT DISULFID 972..1016
FT /evidence="ECO:0000269|PubMed:11514736"
FT DISULFID 1073..1122
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1084..1105
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1106..1109
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT MUTAGEN 121..124
FT /note="GFAA->PQAQ: Increased cleavage of prM."
FT /evidence="ECO:0000269|PubMed:9499070"
FT CONFLICT 115
FT /note="L -> V (in Ref. 2; CAA27184)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="P -> Q (in Ref. 2; CAA27184)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="G -> V (in Ref. 2; CAA27184)"
FT /evidence="ECO:0000305"
FT CONFLICT 1485
FT /note="R -> W (in Ref. 2; CAA27184)"
FT /evidence="ECO:0000305"
FT CONFLICT 1779
FT /note="V -> G (in Ref. 2; CAA27184)"
FT /evidence="ECO:0000305"
FT STRAND 1423..1430
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1436..1440
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1523..1531
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1536..1545
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1548..1551
FT /evidence="ECO:0007829|PDB:2WV9"
FT HELIX 1553..1556
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1564..1568
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1570..1574
FT /evidence="ECO:0007829|PDB:2WV9"
FT TURN 1575..1578
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1579..1585
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1598..1602
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1610..1614
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1617..1619
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1622..1624
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1626..1629
FT /evidence="ECO:0007829|PDB:2WV9"
FT HELIX 1635..1637
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1641..1643
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1649..1658
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1660..1662
FT /evidence="ECO:0007829|PDB:2WV9"
FT STRAND 1664..1669
FT /evidence="ECO:0007829|PDB:2WV9"
FT HELIX 1684..1687
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1692..1695
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1699..1701
FT /evidence="ECO:0007829|PDB:2V8O"
FT TURN 1703..1706
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1707..1717
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1722..1728
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1729..1738
FT /evidence="ECO:0007829|PDB:2V8O"
FT TURN 1739..1741
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1744..1746
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1761..1765
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1766..1773
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1775..1777
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1783..1789
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1795..1809
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1814..1818
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1836..1840
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1849..1851
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1853..1857
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1862..1865
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1869..1881
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1886..1889
FT /evidence="ECO:0007829|PDB:2V8O"
FT TURN 1891..1893
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1894..1901
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1907..1911
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1913..1916
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1924..1928
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1935..1938
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1944..1947
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1950..1952
FT /evidence="ECO:0007829|PDB:2WV9"
FT HELIX 1955..1962
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 1974..1978
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 1990..1999
FT /evidence="ECO:0007829|PDB:2V8O"
FT TURN 2005..2007
FT /evidence="ECO:0007829|PDB:2WV9"
FT HELIX 2014..2016
FT /evidence="ECO:0007829|PDB:2V8O"
FT TURN 2024..2027
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 2031..2042
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 2048..2055
FT /evidence="ECO:0007829|PDB:2V8O"
FT TURN 2056..2058
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 2064..2067
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 2072..2074
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 2078..2081
FT /evidence="ECO:0007829|PDB:2V8O"
FT STRAND 2098..2101
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 2102..2104
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 2108..2118
FT /evidence="ECO:0007829|PDB:2V8O"
FT HELIX 2537..2546
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2550..2557
FT /evidence="ECO:0007829|PDB:2PX2"
FT TURN 2558..2560
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2562..2564
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2566..2568
FT /evidence="ECO:0007829|PDB:2PX2"
FT TURN 2571..2576
FT /evidence="ECO:0007829|PDB:2PXA"
FT STRAND 2578..2580
FT /evidence="ECO:0007829|PDB:2PX5"
FT STRAND 2584..2586
FT /evidence="ECO:0007829|PDB:2PXA"
FT HELIX 2587..2596
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2604..2609
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2615..2620
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2626..2632
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2650..2652
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2653..2656
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2661..2663
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2670..2674
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2683..2701
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2706..2713
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2718..2731
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2734..2736
FT /evidence="ECO:0007829|PDB:2PX2"
FT STRAND 2748..2751
FT /evidence="ECO:0007829|PDB:2PX2"
FT HELIX 2758..2771
FT /evidence="ECO:0007829|PDB:2PX2"
FT TURN 2772..2774
FT /evidence="ECO:0007829|PDB:2PX4"
FT STRAND 2782..2784
FT /evidence="ECO:0007829|PDB:2PX2"
SQ SEQUENCE 3434 AA; 380577 MW; 20D7110791C567A9 CRC64;
MSKKPGGPGK PRVVNMLKRG IPRVFPLVGV KRVVMNLLDG RGPIRFVLAL LAFFRFTALA
PTKALMRRWK SVNKTTAMKH LTSFKKELGT LIDVVNKRGK KQKKRGGSET SVLMLIFMLI
GFAAALKLST FQGKIMMTVN ATDIADVIAI PTPKGPNQCW IRAIDIGFMC DDTITYECPK
LESGNDPEDI DCWCDKQAVY VNYGRCTRAR HSKRSRRSIT VQTHGESTLV NKKDAWLDST
KATRYLTKTE NWIIRNPGYA LVAVVLGWML GSNTGQKVIF TVLLLLVAPA YSFNCLGMSS
RDFIEGASGA TWVDLVLEGD SCITIMAADK PTLDIRMMNI EATNLALVRN YCYAATVSDV
STVSNCPTTG ESHNTKRADH NYLCKRGVTD RGWGNGCGLF GKGSIDTCAK FTCSNSAAGR
LILPEDIKYE VGVFVHGSTD STSHGNYSTQ IGANQAVRFT ISPNAPAITA KMGDYGEVTV
ECEPRSGLNT EAYYVMTIGT KHFLVHREWF NDLLLPWTSP ASTEWRNREI LVEFEEPHAT
KQSVVALGSQ EGALHQALAG AIPVEFSSST LKLTSGHLKC RVKMEKLKLK GTTYGMCTEK
FTFSKNPADT GHGTVVLELQ YTGSDGPCKI PISSVASLND MTPVGRMVTA NPYVASSTAN
AKVLVEIEPP FGDSYIVVGR GDKQINHHWH KEGSSIGKAF STTLKGAQRL AALGDTAWDF
GSVGGVFNSI GKAVHQVFGG AFRTLFGGMS WISPGLLGAL LLWMGVNARD KSIALAFLAT
GGVLLFLATN VHADTGCAID ITRRELKCGS GIFIHNDVEA WIDRYKYLPE TPKQLAKVVE
NAHKSGICGI RSVNRFEHQM WESVRDELNA LLKENAIDLS VVVEKQKGMY RAAPNRLRLT
VEELDIGWKA WGKSLLFAAE LANSTFVVDG PETAECPNSK RAWNSFEIED FGFGITSTRG
WLKLREENTS ECDSTIIGTA VKGNHAVHSD LSYWIESGLN GTWKLERAIF GEVKSCTWPE
THTLWGDAVE ETELIIPVTL AGPRSKHNRR EGYKVQVQGP WDEEDIKLDF DYCPGTTVTV
SEHCGKRGPS VRTTTDSGKL VTDWCCRSCT LPPLRFTTAS GCWYGMEIRP MKHDESTLVK
SRVQAFNGDM IDPFQLGLLV MFLATQEVLR KRWTARLTLP AAVGALLVLL LGGITYTDLV
RYLILVGSAF AESNNGGDVI HLALIAVFKV QPAFLVASLT RSRWTNQENL VLVLGAAFFQ
MAASDLELTI PGLLNSAATA WMVLRAMAFP STSAIAMPML AMLAPGMRML HLDTYRIVLL
LIGICSLLNE RRRSVEKKKG AVLIGLALTS TGYFSPTIMA AGLMICNPNK KRGWPATEVL
TAVGLMFAIV GGLAELDIDS MSVPFTIAGL MLVSYVISGK ATDMWLERAA DVSWEAGAAI
TGTSERLDVQ LDDDGDFHLL NDPGVPWKIW VLRMTCLSVA AITPRAILPS AFGYWLTLKY
TKRGGVFWDT PSPKVYPKGD TTPGVYRIMA RGILGRYQAG VGVMHEGVFH TLWHTTRGAA
IMSGEGRLTP YWGNVKEDRV TYGGPWKLDQ KWNGVDDVQM IVVEPGKPAI NVQTKPGIFK
TAHGEIGAVS LDYPIGTSGS PIVNSNGEII GLYGNGVILG NGAYVSAIVQ GERVEEPVPE
AYNPEMLKKR QLTVLDLHPG AGKTRRILPQ IIKDAIQKRL RTAVLAPTRV VAAEMAEALR
GLPVRYLTPA VQREHSGNEI VDVMCHATLT HRLMSPLRVP NYNLFVMDEA HFTDPASIAA
RGYIATRVEA GEAAAIFMTA TPPGTSDPFP DTNSPVHDVS SEIPDRAWSS GFEWITDYAG
KTVWFVASVK MSNEIAQCLQ RAGKRVIQLN RKSYDTEYPK CKNGDWDFVI TTDISEMGAN
FGASRVIDCR KSVKPTILDE GEGRVILSVP SAITSASAAQ RRGRVGRNPS QIGDEYHYGG
GTSEDDTMLA HWTEAKILLD NIHLPNGLVA QLYGPERDKT YTMDGEYRLR GEERKTFLEL
IKTADLPVWL AYKVASNGIQ YNDRKWCFDG PRSNIILEDN NEVEIITRIG ERKVLKPRWL
DARVYSDHQS LKWFKDFAAG KRSAIGFFEV LGRMPEHFAG KTREALDTMY LVATSEKGGK
AHRMALEELP DALETITLIA ALGVMTAGFF LLMMQRKGIG KLGLGALVLV VATFFLWMSD
VSGTKIAGVL LLALLMMVVL IPEPEKQRSQ TDNQLAVFLI CVLLVVGLVA ANEYGMLERT
KTDIRNLFGK SLIEENEVHI PPFDFFTLDL KPATAWALYG GSTVVLTPLI KHLVTSQYVT
TSLASINAQA GSLFTLPKGI PFTDFDLSVA LVFLGCWGQV TLTTLIMATI LVTLHYGYLL
PGWQAEALRA AQKRTAAGIM KNAVVDGIVA TDVPELERTT PQMQKRLGQI LLVLASVAAV
CVNPRITTIR EAGILCTAAA LTLWDNNASA AWNSTTATGL CHVMRGSWIA GASIAWTLIK
NAEKPAFKRG RAGGRTLGEQ WKEKLNAMGK EEFFSYRKEA ILEVDRTEAR RARREGNKVG
GHPVSRGTAK LRWLVERRFV QPIGKVVDLG CGRGGWSYYA ATMKNVQEVR GYTKGGPGHE
EPMLMQSYGW NIVTMKSGVD VFYKPSEISD TLLCDIGESS PSAEIEEQRT LRILEMVSDW
LSRGPKEFCI KILCPYMPKV IEKLESLQRR FGGGLVRVPL SRNSNHEMYW VSGASGNIVH
AVNMTSQVLI GRMDKKIWKG PKYEEDVNLG SGTRAVGKGV QHTDYKRIKS RIEKLKEEYA
ATWHTDDNHP YRTWTYHGSY EVKPSGSAST LVNGVVRLLS KPWDAITGVT TMAMTDTTPF
GQQRVFKEKV DTKAPEPPQG VKTVMDETTN WLWAYLARNK KARLCTREEF VKKVNSHAAL
GAMFEEQNQW KNAREAVEDP KFWEMVDEER ECHLRGECRT CIYNMMGKRE KKPGEFGKAK
GSRAIWFMWL GARFLEFEAL GFLNEDHWMS RENSGGGVEG AGIQKLGYIL RDVAQKPGGK
IYADDTAGWD TRITQADLEN EAKVLELMEG EQRTLARAII ELTYRHKVVK VMRPAAGGKT
VMDVISREDQ RGSGQVVTYA LNTFTNIAVQ LVRLMEAEAV IGPDDIESIE RKKKFAVRTW
LFENAEERVQ RMAVSGDDCV VKPLDDRFST ALHFLNAMSK VRKDIQEWKP SQGWYDWQQV
PFCSNHFQEV IMKDGRTLVV PCRGQDELIG RARISPGSGW NVRDTACLAK AYAQMWLVLY
FHRRDLRLMA NAICSSVPVD WVPTGRTTWS IHGKGEWMTT EDMLSVWNRV WILENEWMED
KTTVSDWTEV PYVGKREDIW CGSLIGTRTR ATWAENIYAA INQVRSVIGK EKYVDYVQSL
RRYEETHVSE DRVL
