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Database: UniProt
Entry: POLG_ZIKV
LinkDB: POLG_ZIKV
Original site: POLG_ZIKV 
ID   POLG_ZIKV               Reviewed;        3419 AA.
AC   Q32ZE1;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   11-DEC-2019, entry version 130.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein C {ECO:0000250|UniProtKB:P17763};
DE     AltName: Full=Capsid protein;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM {ECO:0000250|UniProtKB:P17763};
DE     AltName: Full=Precursor membrane protein;
DE   Contains:
DE     RecName: Full=Peptide pr {ECO:0000250|UniProtKB:P17763};
DE     AltName: Full=Peptide precursor;
DE   Contains:
DE     RecName: Full=Small envelope protein M {ECO:0000250|UniProtKB:P17763};
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E {ECO:0000250|UniProtKB:P17763};
DE   Contains:
DE     RecName: Full=Non-structural protein 1 {ECO:0000250|UniProtKB:P17763};
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A {ECO:0000250|UniProtKB:P17763};
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B {ECO:0000250|UniProtKB:P17763};
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3 {ECO:0000250|UniProtKB:P17763};
DE              EC=3.4.21.91;
DE              EC=3.6.1.15;
DE              EC=3.6.4.13;
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A {ECO:0000250|UniProtKB:P17763};
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Peptide 2k {ECO:0000250|UniProtKB:P17763};
DE   Contains:
DE     RecName: Full=Non-structural protein 4B {ECO:0000250|UniProtKB:P17763};
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase NS5 {ECO:0000250|UniProtKB:P17763};
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:PRU00924};
DE     AltName: Full=NS5;
OS   Zika virus (ZIKV).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=64320;
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Uganda/MR 766;
RX   PubMed=16223950; DOI=10.1128/cmr.18.4.608-637.2005;
RA   Kuno G., Chang G.J.;
RT   "Biological transmission of arboviruses: reexamination of and new insights
RT   into components, mechanisms, and unique traits as well as their
RT   evolutionary trends.";
RL   Clin. Microbiol. Rev. 18:608-637(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Uganda/MR 766;
RX   PubMed=17195954; DOI=10.1007/s00705-006-0903-z;
RA   Kuno G., Chang G.J.;
RT   "Full-length sequencing and genomic characterization of Bagaza, Kedougou,
RT   and Zika viruses.";
RL   Arch. Virol. 152:687-696(2007).
RN   [3]
RP   REVIEW (NON-STRUCTURAL PROTEIN 1).
RC   STRAIN=Uganda/MR 766;
RX   PubMed=27473856; DOI=10.1186/s12985-016-0590-7;
RA   Rastogi M., Sharma N., Singh S.K.;
RT   "Flavivirus NS1: a multifaceted enigmatic viral protein.";
RL   Virol. J. 13:131-131(2016).
RN   [4]
RP   DOMAIN (CAPSID PROTEIN C).
RC   STRAIN=Uganda/MR 766;
RX   PubMed=27867910; DOI=10.3389/fcimb.2016.00144;
RA   Giri R., Kumar D., Sharma N., Uversky V.N.;
RT   "Intrinsically disordered side of the zika virus proteome.";
RL   Front. Cell. Infect. Microbiol. 6:144-144(2016).
RN   [5]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4A), AND FUNCTION (NON-STRUCTURAL PROTEIN
RP   4B).
RC   STRAIN=Uganda/MR 766;
RX   PubMed=27524440; DOI=10.1016/j.stem.2016.07.019;
RA   Liang Q., Luo Z., Zeng J., Chen W., Foo S.S., Lee S.A., Ge J., Wang S.,
RA   Goldman S.A., Zlokovic B.V., Zhao Z., Jung J.U.;
RT   "Zika virus NS4A and NS4B proteins deregulate Akt-mTOR signaling in human
RT   fetal neural stem cells to inhibit neurogenesis and induce autophagy.";
RL   Cell Stem Cell 19:663-671(2016).
RN   [6]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 2A).
RC   STRAIN=Uganda/MR 766;
RX   PubMed=28826723; DOI=10.1016/j.stem.2017.07.014;
RA   Yoon K.J., Song G., Qian X., Pan J., Xu D., Rho H.S., Kim N.S., Habela C.,
RA   Zheng L., Jacob F., Zhang F., Lee E.M., Huang W.K., Ringeling F.R.,
RA   Vissers C., Li C., Yuan L., Kang K., Kim S., Yeo J., Cheng Y., Liu S.,
RA   Wen Z., Qin C.F., Wu Q., Christian K.M., Tang H., Jin P., Xu Z., Qian J.,
RA   Zhu H., Song H., Ming G.L.;
RT   "Zika-Virus-encoded NS2A disrupts mammalian cortical neurogenesis by
RT   degrading adherens junction proteins.";
RL   Cell Stem Cell 21:349-358(2017).
RN   [7]
RP   CAUTION (ENVELOPE PROTEIN E).
RX   PubMed=28880955; DOI=10.1371/journal.ppat.1006528;
RA   Theys K., Libin P., Dallmeier K., Pineda-Pena A.C., Vandamme A.M.,
RA   Cuypers L., Abecasis A.B.;
RT   "Zika genomics urgently need standardized and curated reference
RT   sequences.";
RL   PLoS Pathog. 13:E1006528-E1006528(2017).
RN   [8]
RP   DOMAIN (SERINE PROTEASE SUBUNIT NS2B).
RC   STRAIN=Uganda/MR 766;
RX   PubMed=29080786; DOI=10.1016/j.jmb.2017.10.018;
RA   Mishra P.M., Uversky V.N., Giri R.;
RT   "Molecular recognition features in zika virus proteome.";
RL   J. Mol. Biol. 430:2372-2388(2018).
RN   [9]
RP   INTERACTION WITH HUMAN SPCS1.
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 790-1142, GLYCOSYLATION AT
RP   ASN-920 AND ASN-997, AND SUBUNIT (NON-STRUCTURAL PROTEIN 1).
RC   STRAIN=Uganda/MR 766;
RX   PubMed=27455458; DOI=10.1038/nsmb.3268;
RA   Brown W.C., Akey D.L., Konwerski J.R., Tarrasch J.T., Skiniotis G.,
RA   Kuhn R.J., Smith J.L.;
RT   "Extended surface for membrane association in Zika virus NS1 structure.";
RL   Nat. Struct. Mol. Biol. 23:865-867(2016).
RN   [11] {ECO:0000244|PDB:5GPI}
RP   X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1412-1464 AND 1499-1675.
RX   PubMed=27940580; DOI=10.1126/science.aai9309;
RA   Zhang Z., Li Y., Loh Y.R., Phoo W.W., Hung A.W., Kang C., Luo D.;
RT   "Crystal structure of unlinked NS2B-NS3 protease from Zika virus.";
RL   Science 354:1597-1600(2016).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) (SERINE PROTEASE SUBUNIT NS2B AND
RP   SERINE PROTEASE NS3).
RC   STRAIN=Isolate BeH823339;
RX   PubMed=27386922; DOI=10.1126/science.aag2419;
RA   Lei J., Hansen G., Nitsche C., Klein C.D., Zhang L., Hilgenfeld R.;
RT   "Crystal structure of Zika virus NS2B-NS3 protease in complex with a
RT   boronate inhibitor.";
RL   Science 353:503-505(2016).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 1669-2115.
RX   PubMed=27399257; DOI=10.1038/nsmb.3258;
RA   Jain R., Coloma J., Garcia-Sastre A., Aggarwal A.K.;
RT   "Structure of the NS3 helicase from Zika virus.";
RL   Nat. Struct. Mol. Biol. 23:752-754(2016).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2822-3419 IN COMPLEX WITH ZINC.
RC   STRAIN=Uganda/MR 766;
RX   PubMed=28345596; DOI=10.1038/ncomms14764;
RA   Godoy A.S., Lima G.M., Oliveira K.I., Torres N.U., Maluf F.V., Guido R.V.,
RA   Oliva G.;
RT   "Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase.";
RL   Nat. Commun. 8:14764-14764(2017).
RN   [15] {ECO:0000244|PDB:5VI7, ECO:0000244|PDB:5VIM}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1677-2115 AND 2521-2781, AND
RP   SUBUNIT (RNA-DIRECTED RNA POLYMERASE NS5).
RC   STRAIN=Uganda/MR 766;
RX   PubMed=28876240; DOI=10.1107/s2059798317010737;
RA   Bukrejewska M., Derewenda U., Radwanska M., Engel D.A., Derewenda Z.S.;
RT   "Crystal structures of the methyltransferase and helicase from the ZIKA
RT   1947 MR766 Uganda strain.";
RL   Acta Crystallogr. D 73:767-774(2017).
RN   [16] {ECO:0000244|PDB:5TFR}
RP   X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 2517-3419 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE AND ZINC.
RX   PubMed=28291746; DOI=10.1107/s2053230x17001601;
RA   Upadhyay A.K., Cyr M., Longenecker K., Tripathi R., Sun C., Kempf D.J.;
RT   "Crystal structure of full-length Zika virus NS5 protein reveals a
RT   conformation similar to Japanese encephalitis virus NS5.";
RL   Acta Crystallogr. F 73:116-122(2017).
RN   [17] {ECO:0000244|PDB:5U0B, ECO:0000244|PDB:5U0C}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2517-3419 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE AND ZINC.
RX   PubMed=28345656; DOI=10.1038/ncomms14762;
RA   Zhao B., Yi G., Du F., Chuang Y.C., Vaughan R.C., Sankaran B., Kao C.C.,
RA   Li P.;
RT   "Structure and function of the Zika virus full-length NS5 protein.";
RL   Nat. Commun. 8:14762-14762(2017).
RN   [18] {ECO:0000244|PDB:5Y4Z}
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 1676-2115.
RX   PubMed=29633968; DOI=10.1107/s2053230x18003813;
RA   Li L., Wang J., Jia Z., Shaw N.;
RT   "Structural view of the helicase reveals that Zika virus uses a conserved
RT   mechanism for unwinding RNA.";
RL   Acta Crystallogr. F 74:205-213(2018).
RN   [19] {ECO:0000244|PDB:5YOD, ECO:0000244|PDB:5YOF}
RP   X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 1412-1464 AND 1499-1675, AND
RP   ACTIVE SITE.
RC   STRAIN=Isolate Nigeria/IbH_30656/1968;
RX   PubMed=29526431; DOI=10.1016/j.str.2018.02.005;
RA   Li Y., Zhang Z., Phoo W.W., Loh Y.R., Li R., Yang H.Y., Jansson A.E.,
RA   Hill J., Keller T.H., Nacro K., Luo D., Kang C.;
RT   "Structural Insights into the Inhibition of Zika Virus NS2B-NS3 Protease by
RT   a Small-Molecule Inhibitor.";
RL   Structure 26:555-564(2018).
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 the mature virus particle. During virus entry,
CC       may 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. {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]: Plays a role in host immune defense modulation
CC       and protection of envelope protein E during virion synthesis. PrM-E
CC       cleavage is inefficient, many virions are only partially matured and
CC       immature prM-E proteins could play a role in immune evasion.
CC       Contributes to fetal microcephaly in humans. Acts as a chaperone for
CC       envelope protein E during intracellular virion assembly by masking and
CC       inactivating envelope protein E fusion peptide. prM is the only viral
CC       peptide matured by host furin in the trans-Golgi network probably to
CC       avoid catastrophic activation of the viral fusion activity in acidic
CC       Golgi compartment prior to virion release.
CC       {ECO:0000250|UniProtKB:A0A024B7W1, 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 and forms a heterodimer
CC       with protein prM. The heterodimer plays a role in virion budding in the
CC       ER, and the newly formed immature particle is covered with 60 spikes
CC       composed of heterodimers between precursor prM and envelope protein E.
CC       The virion is transported to the Golgi apparatus where the low pH
CC       causes the dissociation of PrM-E heterodimers and formation of E
CC       homodimers. PrM-E cleavage is inefficient, many virions are only
CC       partially matured and immature prM-E proteins could play a role in
CC       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. Required for
CC       formation of the replication complex and recruitment of other non-
CC       structural proteins to the ER-derived membrane structures. Excreted as
CC       a hexameric lipoparticle that plays a role against host immune
CC       response. Antagonizes the complement function. Binds to the host
CC       macrophages and dendritic cells. Inhibits the signal transduction
CC       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 (By similarity). May
CC       disrupt adherens junction formation and thereby impair proliferation of
CC       radial cells in the host cortex (PubMed:28826723).
CC       {ECO:0000250|UniProtKB:P14335, ECO:0000269|PubMed:28826723}.
CC   -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC       serine protease function of NS3. {ECO:0000255|PROSITE-
CC       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. Leads to translation arrest
CC       when expressed ex vivo (By similarity).
CC       {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC       the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC       during unwinding. Cooperatively with NS4B suppresses the Akt-mTOR
CC       pathway and leads to cellular dysregulation (PubMed:27524440). Leads to
CC       translation arrest when expressed ex vivo (By similarity).
CC       {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:Q9Q6P4,
CC       ECO:0000269|PubMed:27524440}.
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. Cooperatively
CC       with NS4A suppresses the Akt-mTOR pathway and leads to cellular
CC       dysregulation. {ECO:0000250|UniProtKB:Q9Q6P4,
CC       ECO:0000269|PubMed:27524440}.
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 a 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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
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:0000250|UniProtKB:Q9Q6P4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681, Rhea:RHEA-COMP:15683,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143971,
CC         ChEBI:CHEBI:143975; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680, Rhea:RHEA-COMP:15682,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143973,
CC         ChEBI:CHEBI:143974; 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)-guanosine in
CC         mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-guanosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60864, Rhea:RHEA-COMP:15683,
CC         Rhea:RHEA-COMP:15685, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:143975, ChEBI:CHEBI:143977;
CC         EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine in
CC         mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-adenosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60860, Rhea:RHEA-COMP:15682,
CC         Rhea:RHEA-COMP:15684, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:143974, ChEBI:CHEBI:143976;
CC         EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- SUBUNIT: Capsid protein C: Homodimer. Protein prM: Forms heterodimers
CC       with envelope protein E in the endoplasmic reticulum and Golgi (By
CC       similarity). Envelope protein E: Homodimer; in the endoplasmic
CC       reticulum and Golgi (By similarity). Interacts with host Tyro3, AXL and
CC       DC-SIGN proteins (By similarity). Non-structural protein 1: Homodimer;
CC       Homohexamer when secreted (PubMed:27455458). Interacts with envelope
CC       protein E (By similarity). Non-structural protein 2B: Forms a
CC       heterodimer with serine protease NS3. May form homooligomers (By
CC       similarity). Non-structural protein 2B: Forms a heterodimer with serine
CC       protease NS3. May form homooligomers (By similarity). Interacts with
CC       human SPCS1 (PubMed:29593046). Serine protease NS3: Forms a heterodimer
CC       with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-
CC       directed RNA polymerase NS5; this interaction stimulates RNA-directed
CC       RNA polymerase NS5 guanylyltransferase activity (By similarity). Non-
CC       structural protein 4B: Interacts with serine protease NS3. Interacts
CC       with NS1 (By similarity). RNA-directed RNA polymerase NS5: Homodimer
CC       (PubMed:28876240). Interacts with host STAT2; this interaction inhibits
CC       the phosphorylation of the latter, and, when all viral proteins are
CC       present (polyprotein), targets STAT2 for degradation (By similarity).
CC       {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:P17763,
CC       ECO:0000269|PubMed:27455458, ECO:0000269|PubMed:28876240,
CC       ECO:0000269|PubMed:29593046}.
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:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host 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:P17763}; 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:P17763}; 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:P17763}.
CC       Note=Located in RE-associated vesicles hosting the replication complex.
CC       NS5 protein is mainly localized in the nucleus rather than in ER
CC       vesicles. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: [Small envelope protein M]: The transmembrane domain contains
CC       an endoplasmic reticulum retention signal.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: [Envelope protein E]: The transmembrane domain contains an
CC       endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: [Capsid protein C]: The disordered region at the N-terminus may
CC       be involved in lipid-droplet binding. {ECO:0000250|UniProtKB:P12823,
CC       ECO:0000269|PubMed:27867910}.
CC   -!- DOMAIN: [Serine protease subunit NS2B]: The central disordered region
CC       transitions to ordered by binding to NS3.
CC       {ECO:0000269|PubMed:29080786}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC       performed by host signal peptidase, whereas cleavages in the
CC       cytoplasmic side are performed by serine protease NS3. Signal cleavage
CC       at the 2K-4B site requires a prior NS3 protease-mediated cleavage at
CC       the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.
CC   -!- 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-glycosylation plays a role in virulence in
CC       mammalian and mosquito hosts, but may have no effect on neurovirulence.
CC       {ECO:0000250|UniProtKB:A0A024B7W1}.
CC   -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC       glycosylated, which is required for efficient secretion of the protein
CC       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   -!- 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   -!- CAUTION: [Envelope protein E]: The strain Mr 766 lacks four amino-acids
CC       compared to circulating strains, removing the glycosylation site. This
CC       may be due to many cell culture passages since its isolation.
CC       {ECO:0000305|PubMed:28880955}.
DR   EMBL; AY632535; AAV34151.1; -; Genomic_RNA.
DR   RefSeq; YP_002790881.1; NC_012532.1.
DR   PDB; 5GJ4; X-ray; 1.84 A; A/C/E/G=1414-1464, B/D/F/H=1499-1675.
DR   PDB; 5GPI; X-ray; 1.58 A; A/C/E/G=1414-1464, B/D/F/H=1499-1675.
DR   PDB; 5GXJ; X-ray; 2.60 A; A/B=1416-1668.
DR   PDB; 5JPS; X-ray; 1.78 A; A=1674-2115.
DR   PDB; 5JRZ; X-ray; 1.62 A; A=1669-2115.
DR   PDB; 5K6K; X-ray; 1.89 A; A/B=790-1142.
DR   PDB; 5T1V; X-ray; 3.10 A; A/B=1414-1467, A/B=1499-1685.
DR   PDB; 5TFN; X-ray; 3.00 A; A/B=1416-1456, A/B=1499-1553.
DR   PDB; 5TFO; X-ray; 2.51 A; A/B=1416-1443, A/B=1455-1462, A/B=1499-1680.
DR   PDB; 5TFR; X-ray; 3.05 A; A/B=2517-3419.
DR   PDB; 5TMH; X-ray; 3.28 A; A/B=2517-3418.
DR   PDB; 5U04; X-ray; 1.90 A; A=2822-3419.
DR   PDB; 5U0B; X-ray; 3.00 A; A/B=2517-3419.
DR   PDB; 5U0C; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2781-3419.
DR   PDB; 5VI7; X-ray; 2.00 A; A=1677-2115.
DR   PDB; 5VIM; X-ray; 2.10 A; A/B=2521-2781.
DR   PDB; 5W41; X-ray; 2.20 A; B=2887-2923.
DR   PDB; 5Y4Z; X-ray; 1.30 A; A=1676-2115.
DR   PDB; 5YOD; X-ray; 1.90 A; A/C/E/G=1412-1464, B/D/F/H=1499-1675.
DR   PDB; 5YOF; X-ray; 1.51 A; A=1412-1464, B=1499-1675.
DR   PDB; 5Z0R; X-ray; 2.05 A; A/B=24-98.
DR   PDB; 5Z0V; X-ray; 2.91 A; A/B/C/D=24-98.
DR   PDB; 5ZMQ; X-ray; 1.99 A; A/C/E/G=1414-1464.
DR   PDB; 5ZMS; X-ray; 1.80 A; A/D/G/J=1414-1464.
DR   PDB; 5ZOB; X-ray; 2.00 A; A/C/E/G=1414-1464.
DR   PDB; 6ADW; X-ray; 2.20 A; A=1679-2115.
DR   PDB; 6ADX; X-ray; 1.75 A; A=1679-2115.
DR   PDB; 6ADY; X-ray; 1.90 A; A=1679-2115.
DR   PDB; 6JPW; X-ray; 1.95 A; A/C/E/G=1414-1464.
DR   PDB; 6MH3; X-ray; 1.92 A; A=1681-2115.
DR   PDBsum; 5GJ4; -.
DR   PDBsum; 5GPI; -.
DR   PDBsum; 5GXJ; -.
DR   PDBsum; 5JPS; -.
DR   PDBsum; 5JRZ; -.
DR   PDBsum; 5K6K; -.
DR   PDBsum; 5T1V; -.
DR   PDBsum; 5TFN; -.
DR   PDBsum; 5TFO; -.
DR   PDBsum; 5TFR; -.
DR   PDBsum; 5TMH; -.
DR   PDBsum; 5U04; -.
DR   PDBsum; 5U0B; -.
DR   PDBsum; 5U0C; -.
DR   PDBsum; 5VI7; -.
DR   PDBsum; 5VIM; -.
DR   PDBsum; 5W41; -.
DR   PDBsum; 5Y4Z; -.
DR   PDBsum; 5YOD; -.
DR   PDBsum; 5YOF; -.
DR   PDBsum; 5Z0R; -.
DR   PDBsum; 5Z0V; -.
DR   PDBsum; 5ZMQ; -.
DR   PDBsum; 5ZMS; -.
DR   PDBsum; 5ZOB; -.
DR   PDBsum; 6ADW; -.
DR   PDBsum; 6ADX; -.
DR   PDBsum; 6ADY; -.
DR   PDBsum; 6JPW; -.
DR   PDBsum; 6MH3; -.
DR   SMR; Q32ZE1; -.
DR   MEROPS; S07.003; -.
DR   iPTMnet; Q32ZE1; -.
DR   ABCD; Q32ZE1; -.
DR   GeneID; 7751225; -.
DR   KEGG; vg:7751225; -.
DR   Proteomes; UP000054557; 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:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039574; P:suppression by virus of host TYK2 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; cd12149; Flavi_E_C; 1.
DR   DisProt; DP01256; -.
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   InterPro; IPR011492; DEAD_Flavivir.
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; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
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; 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; GTP-binding;
KW   Helicase; Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW   Host nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host 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; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW   RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
KW   Secreted; Serine protease; Suppressor of RNA silencing; Transcription;
KW   Transcription regulation; 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..3419
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000435828"
FT   CHAIN           1..104
FT                   /note="Capsid protein C"
FT                   /id="PRO_0000435829"
FT   PROPEP          105..122
FT                   /note="ER anchor for capsid protein C, removed in mature
FT                   form by serine protease NS3"
FT                   /id="PRO_0000435830"
FT   CHAIN           123..290
FT                   /note="Protein prM"
FT                   /id="PRO_0000435831"
FT   CHAIN           123..215
FT                   /note="Peptide pr"
FT                   /id="PRO_0000435832"
FT   CHAIN           216..290
FT                   /note="Small envelope protein M"
FT                   /id="PRO_0000435833"
FT   CHAIN           291..790
FT                   /note="Envelope protein E"
FT                   /id="PRO_0000435834"
FT   CHAIN           791..1142
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000435835"
FT   CHAIN           1143..1368
FT                   /note="Non-structural protein 2A"
FT                   /id="PRO_0000435836"
FT   CHAIN           1369..1498
FT                   /note="Serine protease subunit NS2B"
FT                   /id="PRO_0000435837"
FT   CHAIN           1499..2115
FT                   /note="Serine protease NS3"
FT                   /id="PRO_0000435838"
FT   CHAIN           2116..2242
FT                   /note="Non-structural protein 4A"
FT                   /id="PRO_0000435839"
FT   PEPTIDE         2243..2265
FT                   /note="Peptide 2k"
FT                   /id="PRO_0000435840"
FT   CHAIN           2266..2516
FT                   /note="Non-structural protein 4B"
FT                   /id="PRO_0000435841"
FT   CHAIN           2517..3419
FT                   /note="RNA-directed RNA polymerase NS5"
FT                   /id="PRO_0000435842"
FT   TOPO_DOM        1..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..249
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        250..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        275..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        291..741
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        742..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        764..769
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        770..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        791..1173
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1174..1194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1195..1216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1217..1237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1238..1266
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1267..1287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1288..1291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1292..1312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1313..1341
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1342..1362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1363..1369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1370..1390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1391..1393
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1394..1414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1415..1468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1469..1489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1490..2166
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2167..2187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2188..2191
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        2192..2212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2213..2214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2215..2235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2236..2250
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        2251..2265
FT                   /note="Helical; Note=Signal for NS4B"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        2266..2303
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        2304..2324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2325..2340
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2341..2361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2362..2371
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2372..2392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2393..2437
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2438..2458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2459..3419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1499..1676
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   DOMAIN          1679..1835
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1830..2009
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2517..2781
FT                   /note="mRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   DOMAIN          3045..3195
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1692..1699
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   NP_BIND         2529..2535
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT   NP_BIND         2665..2671
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT   NP_BIND         2729..2731
FT                   /note="GTP"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000269|PubMed:27867910"
FT   REGION          37..72
FT                   /note="Hydrophobic; homodimerization of capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   REGION          388..401
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   REGION          1421..1460
FT                   /note="Interacts with and activates NS3 protease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT   REGION          1425..1447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000269|PubMed:29080786"
FT   REGION          1683..1686
FT                   /note="Important for RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14340"
FT   MOTIF           1783..1786
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   ACT_SITE        1549
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1573
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1633
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860,
FT                   ECO:0000269|PubMed:29526431"
FT   ACT_SITE        2577
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2662
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2698
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2734
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2955
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT   METAL           2959
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT   METAL           2964
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT   METAL           2967
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT   METAL           3230
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT   METAL           3246
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT   METAL           3365
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT   BINDING         2544
FT                   /note="mRNA cap"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2572
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:28291746, ECO:0000269|PubMed:28345656"
FT   BINDING         2602
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:28291746"
FT   BINDING         2603
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:28291746"
FT   BINDING         2620
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2621
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000269|PubMed:27386922,
FT                   ECO:0000269|PubMed:27399257, ECO:0000269|PubMed:29080786"
FT   BINDING         2621
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2626
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000269|PubMed:28345656"
FT   BINDING         2627
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT   BINDING         2647
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:28291746, ECO:0000269|PubMed:28345656"
FT   BINDING         2648
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:28291746, ECO:0000269|PubMed:28345656"
FT   BINDING         2662
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000269|PubMed:28291746,
FT                   ECO:0000269|PubMed:28345656"
FT   BINDING         2663
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2736
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            104..105
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000303|PubMed:17195954"
FT   SITE            122..123
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000303|PubMed:17195954"
FT   SITE            215..216
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000303|PubMed:17195954"
FT   SITE            290..291
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            790..791
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            1142..1143
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            1368..1369
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            1498..1499
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            1954
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            1957
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            2115..2116
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            2242..2243
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            2265..2266
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            2516..2517
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P09732"
FT   SITE            2529
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2532
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2533
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2535
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2540
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2544
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2577
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2662
FT                   /note="Essential for 2'-O-methyltransferase and N-7
FT                   methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2666
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2698
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2729
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2731
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2734
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   MOD_RES         2572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        920
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:27455458"
FT   CARBOHYD        997
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:27455458"
FT   DISULFID        293..320
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        350..411
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        350..406
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        364..395
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        382..411
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        382..406
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        476..577
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        594..625
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        794..805
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        845..933
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        969..1013
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        1070..1119
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        1081..1102
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   DISULFID        1103..1106
FT                   /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT   HELIX           25..27
FT                   /evidence="ECO:0000244|PDB:5Z0V"
FT   TURN            35..40
FT                   /evidence="ECO:0000244|PDB:5Z0R"
FT   HELIX           44..56
FT                   /evidence="ECO:0000244|PDB:5Z0R"
FT   HELIX           63..71
FT                   /evidence="ECO:0000244|PDB:5Z0R"
FT   HELIX           74..96
FT                   /evidence="ECO:0000244|PDB:5Z0R"
FT   STRAND          791..797
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   TURN            798..801
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          802..812
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          815..819
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          822..827
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           829..841
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           852..871
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          877..880
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          885..887
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          922..928
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   TURN            930..932
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           935..937
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          943..949
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          952..961
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           971..973
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          975..979
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          982..986
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          988..1008
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           1017..1019
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           1028..1030
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           1035..1037
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           1043..1045
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1060..1068
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1074..1077
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1088..1091
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1100..1105
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1111..1115
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1118..1121
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1126..1130
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   HELIX           1132..1134
FT                   /evidence="ECO:0000244|PDB:5K6K"
FT   STRAND          1419..1425
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1434..1436
FT                   /evidence="ECO:0000244|PDB:5ZOB"
FT   STRAND          1441..1446
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1452..1454
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1518..1530
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1532..1540
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1543..1546
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   HELIX           1548..1551
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1556..1558
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1561..1563
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1565..1569
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   TURN            1570..1573
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1574..1580
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1589..1591
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1593..1597
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1605..1609
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1612..1616
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1619..1624
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   HELIX           1630..1632
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1636..1638
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1640..1642
FT                   /evidence="ECO:0000244|PDB:5GXJ"
FT   STRAND          1644..1648
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1651..1653
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   STRAND          1655..1657
FT                   /evidence="ECO:0000244|PDB:6JPW"
FT   STRAND          1659..1662
FT                   /evidence="ECO:0000244|PDB:5YOF"
FT   HELIX           1679..1682
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1687..1690
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   TURN            1698..1701
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1702..1712
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1717..1723
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1724..1733
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   TURN            1734..1736
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1739..1741
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1756..1760
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1761..1769
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1770..1772
FT                   /evidence="ECO:0000244|PDB:5JRZ"
FT   STRAND          1778..1784
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1790..1804
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1809..1813
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1831..1835
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1844..1846
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1848..1851
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1857..1860
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1864..1876
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1881..1884
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   TURN            1886..1888
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1889..1898
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1902..1906
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1908..1911
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1919..1923
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1926..1933
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   TURN            1934..1936
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1937..1945
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1948..1955
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          1967..1971
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   TURN            1978..1981
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           1983..1992
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2007..2012
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   TURN            2017..2020
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2024..2035
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2041..2049
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2058..2060
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2065..2067
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          2070..2075
FT                   /evidence="ECO:0000244|PDB:6MH3"
FT   STRAND          2077..2079
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          2085..2087
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          2091..2094
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2095..2097
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   STRAND          2098..2100
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2101..2111
FT                   /evidence="ECO:0000244|PDB:5Y4Z"
FT   HELIX           2524..2534
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   HELIX           2537..2543
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   TURN            2544..2547
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2549..2552
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   HELIX           2554..2561
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   HELIX           2574..2583
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2591..2596
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   TURN            2599..2601
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2602..2607
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2613..2619
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2623..2626
FT                   /evidence="ECO:0000244|PDB:5TFR"
FT   HELIX           2637..2639
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2640..2643
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   HELIX           2648..2650
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2657..2661
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   HELIX           2670..2688
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2693..2700
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   HELIX           2705..2718
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2721..2723
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2726..2728
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   STRAND          2735..2738
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   HELIX           2745..2760
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   STRAND          2761..2763
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   STRAND          2768..2771
FT                   /evidence="ECO:0000244|PDB:5VIM"
FT   TURN            2791..2793
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2795..2804
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   TURN            2805..2808
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   STRAND          2818..2827
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2840..2844
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           2847..2851
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   TURN            2853..2855
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          2858..2860
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2865..2875
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2885..2902
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   TURN            2903..2905
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2913..2920
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   TURN            2921..2923
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           2931..2933
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2935..2944
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           2946..2959
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   TURN            2960..2962
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          2969..2973
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   STRAND          2977..2979
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           2989..3006
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3008..3011
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   TURN            3012..3015
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3017..3020
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3021..3023
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3029..3041
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3042..3045
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3055..3057
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           3061..3067
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3068..3073
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3076..3091
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3102..3104
FT                   /evidence="ECO:0000244|PDB:5U0C"
FT   STRAND          3106..3116
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           3123..3143
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3149..3152
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3159..3173
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3176..3179
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3182..3185
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3190..3194
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3197..3201
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3206..3209
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   STRAND          3218..3220
FT                   /evidence="ECO:0000244|PDB:5TMH"
FT   HELIX           3221..3223
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3229..3235
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3237..3239
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   STRAND          3241..3246
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3249..3256
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3258..3261
FT                   /evidence="ECO:0000244|PDB:5U0C"
FT   HELIX           3266..3283
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3288..3300
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3322..3325
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3327..3335
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   TURN            3336..3338
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3351..3353
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3359..3364
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3369..3371
FT                   /evidence="ECO:0000244|PDB:5U0B"
FT   HELIX           3372..3379
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   HELIX           3381..3392
FT                   /evidence="ECO:0000244|PDB:5U04"
FT   STRAND          3394..3396
FT                   /evidence="ECO:0000244|PDB:5TMH"
SQ   SEQUENCE   3419 AA;  378736 MW;  B20F0526BB24B098 CRC64;
     MKNPKEEIRR IRIVNMLKRG VARVNPLGGL KRLPAGLLLG HGPIRMVLAI LAFLRFTAIK
     PSLGLINRWG SVGKKEAMEI IKKFKKDLAA MLRIINARKE RKRRGADTSI GIIGLLLTTA
     MAAEITRRGS AYYMYLDRSD AGKAISFATT LGVNKCHVQI MDLGHMCDAT MSYECPMLDE
     GVEPDDVDCW CNTTSTWVVY GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY
     TKHLIKVENW IFRNPGFALV AVAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD
     FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS
     DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK GSLVTCAKFT CSKKMTGKSI
     QPENLEYRIM LSVHGSQHSG MIGYETDEDR AKVEVTPNSP RAEATLGGFG SLGLDCEPRT
     GLDFSDLYYL TMNNKHWLVH KEWFHDIPLP WHAGADTGTP HWNNKEALVE FKDAHAKRQT
     VVVLGSQEGA VHTALAGALE AEMDGAKGRL FSGHLKCRLK MDKLRLKGVS YSLCTAAFTF
     TKVPAETLHG TVTVEVQYAG TDGPCKIPVQ MAVDMQTLTP VGRLITANPV ITESTENSKM
     MLELDPPFGD SYIVIGVGDK KITHHWHRSG STIGKAFEAT VRGAKRMAVL GDTAWDFGSV
     GGVFNSLGKG IHQIFGAAFK SLFGGMSWFS QILIGTLLVW LGLNTKNGSI SLTCLALGGV
     MIFLSTAVSA DVGCSVDFSK KETRCGTGVF IYNDVEAWRD RYKYHPDSPR RLAAAVKQAW
     EEGICGISSV SRMENIMWKS VEGELNAILE ENGVQLTVVV GSVKNPMWRG PQRLPVPVNE
     LPHGWKAWGK SYFVRAAKTN NSFVVDGDTL KECPLEHRAW NSFLVEDHGF GVFHTSVWLK
     VREDYSLECD PAVIGTAVKG REAAHSDLGY WIESEKNDTW RLKRAHLIEM KTCEWPKSHT
     LWTDGVEESD LIIPKSLAGP LSHHNTREGY RTQVKGPWHS EELEIRFEEC PGTKVYVEET
     CGTRGPSLRS TTASGRVIEE WCCRECTMPP LSFRAKDGCW YGMEIRPRKE PESNLVRSMV
     TAGSTDHMDH FSLGVLVILL MVQEGLKKRM TTKIIMSTSM AVLVVMILGG FSMSDLAKLV
     ILMGATFAEM NTGGDVAHLA LVAAFKVRPA LLVSFIFRAN WTPRESMLLA LASCLLQTAI
     SALEGDLMVL INGFALAWLA IRAMAVPRTD NIALPILAAL TPLARGTLLV AWRAGLATCG
     GIMLLSLKGK GSVKKNLPFV MALGLTAVRV VDPINVVGLL LLTRSGKRSW PPSEVLTAVG
     LICALAGGFA KADIEMAGPM AAVGLLIVSY VVSGKSVDMY IERAGDITWE KDAEVTGNSP
     RLDVALDESG DFSLVEEDGP PMREIILKVV LMAICGMNPI AIPFAAGAWY VYVKTGKRSG
     ALWDVPAPKE VKKGETTDGV YRVMTRRLLG STQVGVGVMQ EGVFHTMWHV TKGAALRSGE
     GRLDPYWGDV KQDLVSYCGP WKLDAAWDGL SEVQLLAVPP GERARNIQTL PGIFKTKDGD
     IGAVALDYPA GTSGSPILDK CGRVIGLYGN GVVIKNGSYV SAITQGKREE ETPVECFEPS
     MLKKKQLTVL DLHPGAGKTR RVLPEIVREA IKKRLRTVIL APTRVVAAEM EEALRGLPVR
     YMTTAVNVTH SGTEIVDLMC HATFTSRLLQ PIRVPNYNLN IMDEAHFTDP SSIAARGYIS
     TRVEMGEAAA IFMTATPPGT RDAFPDSNSP IMDTEVEVPE RAWSSGFDWV TDHSGKTVWF
     VPSVRNGNEI AACLTKAGKR VIQLSRKTFE TEFQKTKNQE WDFVITTDIS EMGANFKADR
     VIDSRRCLKP VILDGERVIL AGPMPVTHAS AAQRRGRIGR NPNKPGDEYM YGGGCAETDE
     GHAHWLEARM LLDNIYLQDG LIASLYRPEA DKVAAIEGEF KLRTEQRKTF VELMKRGDLP
     VWLAYQVASA GITYTDRRWC FDGTTNNTIM EDSVPAEVWT KYGEKRVLKP RWMDARVCSD
     HAALKSFKEF AAGKRGAALG VMEALGTLPG HMTERFQEAI DNLAVLMRAE TGSRPYKAAA
     AQLPETLETI MLLGLLGTVS LGIFFVLMRN KGIGKMGFGM VTLGASAWLM WLSEIEPARI
     ACVLIVVFLL LVVLIPEPEK QRSPQDNQMA IIIMVAVGLL GLITANELGW LERTKNDIAH
     LMGRREEGAT MGFSMDIDLR PASAWAIYAA LTTLITPAVQ HAVTTSYNNY SLMAMATQAG
     VLFGMGKGMP FMHGDLGVPL LMMGCYSQLT PLTLIVAIIL LVAHYMYLIP GLQAAAARAA
     QKRTAAGIMK NPVVDGIVVT DIDTMTIDPQ VEKKMGQVLL IAVAISSAVL LRTAWGWGEA
     GALITAATST LWEGSPNKYW NSSTATSLCN IFRGSYLAGA SLIYTVTRNA GLVKRRGGGT
     GETLGEKWKA RLNQMSALEF YSYKKSGITE VCREEARRAL KDGVATGGHA VSRGSAKIRW
     LEERGYLQPY GKVVDLGCGR GGWSYYAATI RKVQEVRGYT KGGPGHEEPM LVQSYGWNIV
     RLKSGVDVFH MAAEPCDTLL CDIGESSSSP EVEETRTLRV LSMVGDWLEK RPGAFCIKVL
     CPYTSTMMET MERLQRRHGG GLVRVPLCRN STHEMYWVSG AKSNIIKSVS TTSQLLLGRM
     DGPRRPVKYE EDVNLGSGTR AVASCAEAPN MKIIGRRIER IRNEHAETWF LDENHPYRTW
     AYHGSYEAPT QGSASSLVNG VVRLLSKPWD VVTGVTGIAM TDTTPYGQQR VFKEKVDTRV
     PDPQEGTRQV MNIVSSWLWK ELGKRKRPRV CTKEEFINKV RSNAALGAIF EEEKEWKTAV
     EAVNDPRFWA LVDREREHHL RGECHSCVYN MMGKREKKQG EFGKAKGSRA IWYMWLGARF
     LEFEALGFLN EDHWMGRENS GGGVEGLGLQ RLGYILEEMN RAPGGKMYAD DTAGWDTRIS
     KFDLENEALI TNQMEEGHRT LALAVIKYTY QNKVVKVLRP AEGGKTVMDI ISRQDQRGSG
     QVVTYALNTF TNLVVQLIRN MEAEEVLEMQ DLWLLRKPEK VTRWLQSNGW DRLKRMAVSG
     DDCVVKPIDD RFAHALRFLN DMGKVRKDTQ EWKPSTGWSN WEEVPFCSHH FNKLYLKDGR
     SIVVPCRHQD ELIGRARVSP GAGWSIRETA CLAKSYAQMW QLLYFHRRDL RLMANAICSA
     VPVDWVPTGR TTWSIHGKGE WMTTEDMLMV WNRVWIEEND HMEDKTPVTK WTDIPYLGKR
     EDLWCGSLIG HRPRTTWAEN IKDTVNMVRR IIGDEEKYMD YLSTQVRYLG EEGSTPGVL
//
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