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 03-AUG-2022, entry version 143.
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, ECO:0000269|PubMed:31090058};
DE AltName: Full=NS5;
OS Zika virus (ZIKV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; 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 (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH HOST STAT2
RP (RNA-DIRECTED RNA POLYMERASE NS5).
RX PubMed=27797853; DOI=10.15252/embr.201642627;
RA Kumar A., Hou S., Airo A.M., Limonta D., Mancinelli V., Branton W.,
RA Power C., Hobman T.C.;
RT "Zika virus inhibits type-I interferon production and downstream
RT signaling.";
RL EMBO Rep. 17:1766-1775(2016).
RN [7]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), INTERACTION WITH HOST STAT2
RP (RNA-DIRECTED RNA POLYMERASE NS5), AND SUBCELLULAR LOCATION (RNA-DIRECTED
RP RNA POLYMERASE NS5).
RX PubMed=27212660; DOI=10.1016/j.chom.2016.05.009;
RA Grant A., Ponia S.S., Tripathi S., Balasubramaniam V., Miorin L.,
RA Sourisseau M., Schwarz M.C., Sanchez-Seco M.P., Evans M.J., Best S.M.,
RA Garcia-Sastre A.;
RT "Zika Virus Targets Human STAT2 to Inhibit Type I Interferon Signaling.";
RL Cell Host Microbe 19:882-890(2016).
RN [8]
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 [9]
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 [10]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1), FUNCTION (NON-STRUCTURAL PROTEIN 4B),
RP INTERACTION WITH HOST TBK1 (NON-STRUCTURAL PROTEIN 1), AND INTERACTION WITH
RP HOST TBK1 (NON-STRUCTURAL PROTEIN 4B).
RX PubMed=28373913; DOI=10.1038/celldisc.2017.6;
RA Wu Y., Liu Q., Zhou J., Xie W., Chen C., Wang Z., Yang H., Cui J.;
RT "Zika virus evades interferon-mediated antiviral response through the co-
RT operation of multiple nonstructural proteins in vitro.";
RL Cell Discov. 3:17006-17006(2017).
RN [11]
RP FUNCTION (NON-STRUCTURAL PROTEIN 4A), INTERACTION WITH HUMAN SRPRA
RP (NON-STRUCTURAL PROTEIN 4A), INTERACTION WITH HUMAN SEC61G (NON-STRUCTURAL
RP PROTEIN 4A), AND INTERACTION WITH HUMAN ANKLE2 (NON-STRUCTURAL PROTEIN 4A).
RX PubMed=30550790; DOI=10.1016/j.cell.2018.11.028;
RA Shah P.S., Link N., Jang G.M., Sharp P.P., Zhu T., Swaney D.L.,
RA Johnson J.R., Von Dollen J., Ramage H.R., Satkamp L., Newton B.,
RA Huettenhain R., Petit M.J., Baum T., Everitt A., Laufman O., Tassetto M.,
RA Shales M., Stevenson E., Iglesias G.N., Shokat L., Tripathi S.,
RA Balasubramaniam V., Webb L.G., Aguirre S., Willsey A.J., Garcia-Sastre A.,
RA Pollard K.S., Cherry S., Gamarnik A.V., Marazzi I., Taunton J.,
RA Fernandez-Sesma A., Bellen H.J., Andino R., Krogan N.J.;
RT "Comparative Flavivirus-Host Protein Interaction Mapping Reveals Mechanisms
RT of Dengue and Zika Virus Pathogenesis.";
RL Cell 175:1931-1945(2018).
RN [12]
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 [13]
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 [14]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1), AND INTERACTION WITH HOST USP8
RP (NON-STRUCTURAL PROTEIN 1).
RC STRAIN=GZ01;
RX PubMed=30065070; DOI=10.15252/embj.201899347;
RA Zheng Y., Liu Q., Wu Y., Ma L., Zhang Z., Liu T., Jin S., She Y., Li Y.P.,
RA Cui J.;
RT "Zika virus elicits inflammation to evade antiviral response by cleaving
RT cGAS via NS1-caspase-1 axis.";
RL EMBO J. 37:0-0(2018).
RN [15]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), SUBCELLULAR LOCATION
RP (RNA-DIRECTED RNA POLYMERASE NS5), MUTAGENESIS OF ARG-3099, DOMAIN
RP (RNA-DIRECTED RNA POLYMERASE NS5), AND CATALYTIC ACTIVITY (RNA-DIRECTED RNA
RP POLYMERASE NS5).
RX PubMed=31090058; DOI=10.1002/1873-3468.13437;
RA Saw W.G., Chan K.W., Vasudevan S.G., Grueber G.;
RT "Zika virus nonstructural protein 5 residue R681 is critical for dimer
RT formation and enzymatic activity.";
RL FEBS Lett. 593:1272-1291(2019).
RN [16]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), SUBCELLULAR LOCATION
RP (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH HOST IKBKE
RP (RNA-DIRECTED RNA POLYMERASE NS5).
RX PubMed=31690057; DOI=10.3390/v11111024;
RA Lundberg R., Melen K., Westenius V., Jiang M., Oesterlund P., Khan H.,
RA Vapalahti O., Julkunen I., Kakkola L.;
RT "Zika Virus Non-Structural Protein NS5 Inhibits the RIG-I Pathway and
RT Interferon Lambda 1 Promoter Activation by Targeting IKK Epsilon.";
RL Viruses 11:0-0(2019).
RN [17]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH HOST TBK1
RP (RNA-DIRECTED RNA POLYMERASE NS5).
RX PubMed=30530224; DOI=10.1016/j.virol.2018.11.009;
RA Lin S., Yang S., He J., Guest J.D., Ma Z., Yang L., Pierce B.G., Tang Q.,
RA Zhang Y.J.;
RT "Zika virus NS5 protein antagonizes type I interferon production via
RT blocking TBK1 activation.";
RL Virology 527:180-187(2019).
RN [18]
RP FUNCTION (NON-STRUCTURAL PROTEIN 2A), AND MUTAGENESIS OF ALA-1259.
RC STRAIN=Paraiba;
RX PubMed=31882898; DOI=10.1038/s41598-019-56291-4;
RA Avila-Perez G., Nogales A., Park J.G., Marquez-Jurado S., Iborra F.J.,
RA Almazan F., Martinez-Sobrido L.;
RT "A natural polymorphism in Zika virus NS2A protein responsible of virulence
RT in mice.";
RL Sci. Rep. 9:19968-19968(2019).
RN [19]
RP FUNCTION (NON-STRUCTURAL PROTEIN 2A), AND FUNCTION (NON-STRUCTURAL PROTEIN
RP 4A).
RX PubMed=31581385; DOI=10.4014/jmb.1909.09017;
RA Ngueyen T.T.N., Kim S.J., Lee J.Y., Myoung J.;
RT "Zika Virus Proteins NS2A and NS4A Are Major Antagonists that Reduce IFN-
RT beta Promoter Activity Induced by the MDA5/RIG-I Signaling Pathway.";
RL J. Microbiol. Biotechnol. 29:1665-1674(2019).
RN [20]
RP INTERACTION WITH HOST PROTEIN SHFL (SERINE PROTEASE NS3), AND SUBCELLULAR
RP LOCATION (SERINE PROTEASE NS3).
RX PubMed=32150556; DOI=10.1371/journal.pntd.0008083;
RA Wu Y., Yang X., Yao Z., Dong X., Zhang D., Hu Y., Zhang S., Lin J.,
RA Chen J., An S., Ye H., Zhang S., Qiu Z., He Z., Huang M., Wei G., Zhu X.;
RT "C19orf66 interrupts Zika virus replication by inducing lysosomal
RT degradation of viral NS3.";
RL PLoS Negl. Trop. Dis. 14:e0008083-e0008083(2020).
RN [21]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
RC STRAIN=Isolate BeH819015;
RX PubMed=32313955; DOI=10.1093/nar/gkaa242;
RA Fajardo T., Sanford T.J., Mears H.V., Jasper A., Storrie S., Mansur D.S.,
RA Sweeney T.R.;
RT "The flavivirus polymerase NS5 regulates translation of viral genomic
RT RNA.";
RL Nucleic Acids Res. 48:5081-5093(2020).
RN [22]
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 [23] {ECO:0007744|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 [24]
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 [25]
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 [26]
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 [27] {ECO:0007744|PDB:5VI7, ECO:0007744|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 [28] {ECO:0007744|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 [29] {ECO:0007744|PDB:5U0B, ECO:0007744|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 [30] {ECO:0007744|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 [31] {ECO:0007744|PDB:5YOD, ECO:0007744|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).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2887-2923, SUBCELLULAR LOCATION
RP (RNA-DIRECTED RNA POLYMERASE NS5), MUTAGENESIS OF LYS-2906 AND ARG-2909,
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), NUCLEAR LOCALIZATION SIGNAL
RP (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH HOST KPNA2
RP (RNA-DIRECTED RNA POLYMERASE NS5).
RX PubMed=30848123; DOI=10.1021/acsinfecdis.8b00373;
RA Ng I.H.W., Chan K.W., Tan M.J.A., Gwee C.P., Smith K.M., Jeffress S.J.,
RA Saw W.G., Swarbrick C.M.D., Watanabe S., Jans D.A., Grueber G.,
RA Forwood J.K., Vasudevan S.G.;
RT "Zika Virus NS5 Forms Supramolecular Nuclear Bodies That Sequester
RT Importin-alpha and Modulate the Host Immune and Pro-Inflammatory Response
RT in Neuronal Cells.";
RL ACS Infect. Dis. 5:932-948(2019).
CC -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC to the host cell membrane and packages the viral RNA into a
CC nucleocapsid that forms the core of the mature virus particle. During
CC virus entry, may induce genome penetration into the host cytoplasm
CC after hemifusion induced by the surface proteins. Can migrate to the
CC cell nucleus where it modulates host functions.
CC {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 receptors
CC and mediates fusion between viral and cellular membranes. Efficient
CC virus attachment to cell is, at least in part, mediated by host HAVCR1
CC in a cell-type specific manner (By similarity). In addition, host NCAM1
CC can also be used as entry receptor (By similarity). Interaction with
CC host HSPA5 plays an important role in the early stages of infection as
CC well (By similarity). Envelope protein is synthesized in the
CC endoplasmic reticulum and forms a heterodimer with protein prM. The
CC heterodimer plays a role in virion budding in the ER, and the newly
CC formed immature particle is covered with 60 spikes composed of
CC heterodimers between precursor prM and envelope protein E. The virion
CC is transported to the Golgi apparatus where the low pH causes the
CC dissociation of PrM-E heterodimers and formation of E homodimers. 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 (By
CC similarity). {ECO:0000250|UniProtKB:A0A142I5B9,
CC ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 1]: Plays a role in the inhibition of
CC host RLR-induced interferon-beta activation by targeting TANK-binding
CC kinase 1/TBK1 (PubMed:28373913). In addition, recruits the host
CC deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from
CC caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn,
CC stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability
CC to recognize mitochondrial DNA release and initiate type I interferon
CC signaling (PubMed:28373913). {ECO:0000269|PubMed:28373913}.
CC -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC replication complex that recruits genomic RNA, the structural protein
CC prM/E complex, and the NS2B/NS3 protease complex to the virion assembly
CC site and orchestrates virus morphogenesis (By similarity). Antagonizes
CC also the host MDA5-mediated induction of alpha/beta interferon
CC antiviral response (PubMed:31882898, PubMed:31581385). May disrupt
CC adherens junction formation and thereby impair proliferation of radial
CC cells in the host cortex (PubMed:28826723).
CC {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000269|PubMed:28826723,
CC ECO:0000269|PubMed:31581385, ECO:0000269|PubMed:31882898}.
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 (By similarity). NS4A allows NS3 helicase to
CC conserve energy during unwinding (By similarity). Cooperatively with
CC NS4B suppresses the Akt-mTOR pathway and leads to cellular
CC dysregulation (PubMed:27524440). By inhibiting host ANKLE2 functions,
CC may cause defects in brain development, such as microcephaly
CC (PubMed:30550790). Antagonizes also the host MDA5-mediated induction of
CC alpha/beta interferon antiviral response (PubMed:31581385). 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, ECO:0000269|PubMed:30550790,
CC ECO:0000269|PubMed:31581385}.
CC -!- FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is
CC required for the interferon antagonism activity of the latter.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
CC derived membrane vesicles where the viral replication takes place (By
CC similarity). Also plays a role in the inhibition of host RLR-induced
CC interferon-beta production at TANK-binding kinase 1/TBK1 level
CC (PubMed:28373913). Cooperatively with NS4A suppresses the Akt-mTOR
CC pathway and leads to cellular dysregulation (PubMed:27524440).
CC {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440,
CC ECO:0000269|PubMed:28373913}.
CC -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC and (-) RNA genome, and performs the capping of genomes in the
CC cytoplasm (PubMed:31090058). Methylates viral RNA cap at guanine N-7
CC and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to
CC the cap-proximal structure and inhibits further translation of the
CC viral genome (PubMed:32313955). Besides its role in RNA genome
CC replication, also prevents the establishment of a cellular antiviral
CC state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling
CC pathway. Mechanistically, interferes with host kinases TBK1 and IKKE
CC upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I
CC pathway (PubMed:31690057, PubMed:30530224). Antagonizes also type I
CC interferon signaling by targeting STAT2 for degradation by the
CC proteasome thereby preventing activation of JAK-STAT signaling pathway
CC (PubMed:27212660, PubMed:27797853). Within the host nucleus, disrupts
CC host SUMO1 and STAT2 co-localization with PML, resulting in PML
CC degradation (By similarity). May also reduce immune responses by
CC preventing the recruitment of the host PAF1 complex to interferon-
CC responsive genes (By similarity). {ECO:0000250|UniProtKB:A0A024B7W1,
CC ECO:0000269|PubMed:27212660, ECO:0000269|PubMed:27797853,
CC ECO:0000269|PubMed:30530224, ECO:0000269|PubMed:31690057,
CC ECO:0000269|PubMed:32313955}.
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 ECO:0000269|PubMed:31090058};
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)-(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. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi (By similarity). Interacts with
CC non-structural protein 2A (By similarity).
CC {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi (By similarity). Interacts with host TYRO3, AXL and DC-SIGN
CC proteins (By similarity). Interacts with non-structural protein 2A (By
CC similarity). Interacts with host HAVCR1; this interaction likely
CC mediates virus attachment to host cell (By similarity). Interacts with
CC host NCAM1 (By similarity). Interacts with host HSPA5 (By similarity).
CC {ECO:0000250|UniProtKB:A0A024B7W1, ECO:0000250|UniProtKB:A0A142I5B9,
CC ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted (PubMed:27455458). Interacts with host TBK1 (PubMed:28373913).
CC Interacts with host USP8 (PubMed:30065070). Interacts with envelope
CC protein E (By similarity). {ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:27455458, ECO:0000269|PubMed:28373913,
CC ECO:0000269|PubMed:30065070}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts with the structural
CC protein prM/E complex, and the NS2B/NS3 protease complex.
CC {ECO:0000250|UniProtKB:A0A142I5B9}.
CC -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC serine protease NS3 (By similarity). May form homooligomers (By
CC similarity). Interacts with human SPCS1 (PubMed:29593046). Interacts
CC with non-structural protein 2A (By similarity).
CC {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:29593046}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By
CC similarity). Interacts with NS4B (By similarity). Interacts with
CC unphosphorylated RNA-directed RNA polymerase NS5; this interaction
CC stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
CC (By similarity). Interacts with non-structural protein 2A (By
CC similarity). Interacts with host SHFL; this interaction promotes NS3
CC degradation via a lysosome-dependent pathway (PubMed:32150556).
CC {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:32150556}.
CC -!- SUBUNIT: [Non-structural protein 4A]: May interact with host ANKLE2;
CC the interaction may cause defects in brain development, such as
CC microcephaly (PubMed:30550790). May interact with host SRPRA and SEC61G
CC (PubMed:30550790). {ECO:0000269|PubMed:30550790}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3. Interacts with NS1 (By similarity). Interacts with host TBK1.
CC {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:28373913}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer (PubMed:28876240,
CC PubMed:31090058). 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 (PubMed:27212660,
CC PubMed:27797853). Interacts with host TBK1 and IKBKE; these
CC interactions lead to the inhibition of the host RIG-I signaling pathway
CC (PubMed:30530224, PubMed:31690057). Interacts with host KPNA2
CC (PubMed:30848123). Interacts with host PAF1 complex; the interaction
CC may prevent the recruitment of the host PAF1 complex to interferon-
CC responsive genes, and thus reduces the immune response (By similarity).
CC Interacts with serine protease NS3 (By similarity). Interacts with host
CC KPNA2 (PubMed:30848123). {ECO:0000250|UniProtKB:A0A024B7W1,
CC ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:27212660,
CC ECO:0000269|PubMed:27797853, ECO:0000269|PubMed:28876240,
CC ECO:0000269|PubMed:30530224, ECO:0000269|PubMed:30848123,
CC ECO:0000269|PubMed:31090058, ECO:0000269|PubMed:31690057}.
CC -!- INTERACTION:
CC PRO_0000435835; PRO_0000435835 [Q32ZE1]; NbExp=2; IntAct=EBI-20717588, EBI-20717588;
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 cytoplasm
CC {ECO:0000269|PubMed:32150556}. Host endoplasmic reticulum membrane
CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein
CC {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:0000269|PubMed:27212660,
CC ECO:0000269|PubMed:30848123, ECO:0000269|PubMed:31090058,
CC ECO:0000269|PubMed:31690057}. Note=Located in RE-associated vesicles
CC hosting the replication complex. NS5 protein is mainly localized in the
CC nucleus rather than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
CC -!- 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 -!- DOMAIN: [RNA-directed RNA polymerase NS5]: Comprises a
CC methyltransferase (MTase) in the N-terminal region and an RNA-dependent
CC RNA polymerase in the C-terminal region. {ECO:0000269|PubMed:31090058}.
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: [Envelope protein E]: Ubiquitination by host TRIM7 promotes virus
CC attachment and fusion of the virus and the host endosome membrane.
CC {ECO:0000250|UniProtKB:A0A142I5B9}.
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 -!- PTM: [RNA-directed RNA polymerase NS5]: Sumoylated, required for
CC regulating IFN induced interferon stimulated genes/ISGs.
CC {ECO:0000250|UniProtKB:A0A024B7W1}.
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}.
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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; 5RHG; X-ray; 1.41 A; A=1681-2115.
DR PDB; 5RHH; X-ray; 1.59 A; A=1681-2115.
DR PDB; 5RHI; X-ray; 1.45 A; A=1681-2115.
DR PDB; 5RHJ; X-ray; 1.50 A; A=1681-2115.
DR PDB; 5RHK; X-ray; 1.52 A; A=1681-2115.
DR PDB; 5RHL; X-ray; 1.43 A; A=1681-2115.
DR PDB; 5RHM; X-ray; 1.68 A; A=1681-2115.
DR PDB; 5RHO; X-ray; 1.49 A; A=1681-2115.
DR PDB; 5RHP; X-ray; 1.61 A; A=1681-2115.
DR PDB; 5RHQ; X-ray; 1.49 A; A=1681-2115.
DR PDB; 5RHR; X-ray; 1.46 A; A=1681-2115.
DR PDB; 5RHS; X-ray; 1.53 A; A=1681-2115.
DR PDB; 5RHT; X-ray; 1.63 A; A=1681-2115.
DR PDB; 5RHU; X-ray; 1.61 A; A=1681-2115.
DR PDB; 5RHV; X-ray; 1.71 A; A=1681-2115.
DR PDB; 5RHW; X-ray; 1.62 A; A=1681-2115.
DR PDB; 5RHX; X-ray; 1.73 A; A=1681-2115.
DR PDB; 5RHY; X-ray; 1.36 A; A=1681-2115.
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; 6KK2; X-ray; 2.02 A; A=1414-1464.
DR PDB; 6KK3; X-ray; 2.05 A; A=1418-1455.
DR PDB; 6KK4; X-ray; 1.74 A; A=1414-1464.
DR PDB; 6KK5; X-ray; 2.03 A; A=1414-1464.
DR PDB; 6KK6; X-ray; 1.74 A; A=1414-1464.
DR PDB; 6KPQ; X-ray; 2.62 A; A=1414-1464.
DR PDB; 6L50; X-ray; 1.95 A; A/C/E/G=1414-1464.
DR PDB; 6MH3; X-ray; 1.92 A; A=1681-2115.
DR PDB; 6UX2; X-ray; 3.01 A; B=2789-3419.
DR PDB; 6WCZ; EM; 4.00 A; B=2517-3419.
DR PDB; 6Y3B; X-ray; 1.59 A; A=1412-1464, B=1499-1675.
DR PDB; 7O55; X-ray; 1.95 A; A=1414-1464, B=1499-1675.
DR PDB; 7OBV; X-ray; 1.30 A; A=1414-1464, B=1499-1675.
DR PDB; 7OC2; X-ray; 1.50 A; A=1414-1464, B=1499-1675.
DR PDBsum; 5GJ4; -.
DR PDBsum; 5GPI; -.
DR PDBsum; 5GXJ; -.
DR PDBsum; 5JPS; -.
DR PDBsum; 5JRZ; -.
DR PDBsum; 5K6K; -.
DR PDBsum; 5RHG; -.
DR PDBsum; 5RHH; -.
DR PDBsum; 5RHI; -.
DR PDBsum; 5RHJ; -.
DR PDBsum; 5RHK; -.
DR PDBsum; 5RHL; -.
DR PDBsum; 5RHM; -.
DR PDBsum; 5RHO; -.
DR PDBsum; 5RHP; -.
DR PDBsum; 5RHQ; -.
DR PDBsum; 5RHR; -.
DR PDBsum; 5RHS; -.
DR PDBsum; 5RHT; -.
DR PDBsum; 5RHU; -.
DR PDBsum; 5RHV; -.
DR PDBsum; 5RHW; -.
DR PDBsum; 5RHX; -.
DR PDBsum; 5RHY; -.
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; 6KK2; -.
DR PDBsum; 6KK3; -.
DR PDBsum; 6KK4; -.
DR PDBsum; 6KK5; -.
DR PDBsum; 6KK6; -.
DR PDBsum; 6KPQ; -.
DR PDBsum; 6L50; -.
DR PDBsum; 6MH3; -.
DR PDBsum; 6UX2; -.
DR PDBsum; 6WCZ; -.
DR PDBsum; 6Y3B; -.
DR PDBsum; 7O55; -.
DR PDBsum; 7OBV; -.
DR PDBsum; 7OC2; -.
DR SMR; Q32ZE1; -.
DR IntAct; Q32ZE1; 1.
DR BindingDB; Q32ZE1; -.
DR ChEMBL; CHEMBL4523307; -.
DR MEROPS; S07.003; -.
DR iPTMnet; Q32ZE1; -.
DR PRIDE; Q32ZE1; -.
DR ABCD; Q32ZE1; 41 sequenced antibodies.
DR GeneID; 7751225; -.
DR KEGG; vg:7751225; -.
DR BRENDA; 2.7.7.48; 9645.
DR BRENDA; 3.4.21.91; 9645.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; 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:0039723; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity; 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; 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 Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR InterPro; IPR001122; Flavi_capsidC.
DR InterPro; IPR037172; Flavi_capsidC_sf.
DR InterPro; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR001850; Flavivirus_NS3_S7.
DR InterPro; IPR014412; Gen_Poly_FLV.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR Pfam; PF01004; Flavi_M; 1.
DR Pfam; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 1.
DR Pfam; PF01002; Flavi_NS2B; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF01570; Flavi_propep; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF101257; SSF101257; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; 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 TBK1 by virus; Inhibition of host TLR pathway by virus;
KW Inhibition of host TYK2 by virus; Isopeptide bond; 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 Ubl conjugation; Viral attachment to host cell; Viral envelope protein;
KW Viral immunoevasion; Viral penetration into host cytoplasm;
KW Viral RNA replication; Virion; Virus endocytosis by host;
KW 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 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 REGION 2593..2596
FT /note="SUMO-interacting motif (SIM)"
FT /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT MOTIF 1783..1786
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 2904..2910
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000269|PubMed:30848123"
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 BINDING 1692..1699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2529..2535
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT BINDING 2529
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2532
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2533
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2535
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2540
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2544
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2572
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT ECO:0000269|PubMed:28291746, ECO:0000269|PubMed:28345656"
FT BINDING 2602
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT ECO:0000269|PubMed:28291746"
FT BINDING 2603
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT ECO:0000269|PubMed:28291746"
FT BINDING 2620
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2621
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2621
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27386922,
FT ECO:0000269|PubMed:27399257, ECO:0000269|PubMed:29080786"
FT BINDING 2626
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:28345656"
FT BINDING 2627
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT BINDING 2647
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT ECO:0000269|PubMed:28291746, ECO:0000269|PubMed:28345656"
FT BINDING 2648
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT ECO:0000269|PubMed:28291746, ECO:0000269|PubMed:28345656"
FT BINDING 2662
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345656"
FT BINDING 2663
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2665..2671
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT BINDING 2666
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2729..2731
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:A0A024B7W1"
FT BINDING 2729
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2731
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2736
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2955
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT BINDING 2959
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT BINDING 2964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT BINDING 2967
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT BINDING 3230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT BINDING 3246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
FT BINDING 3365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28291746,
FT ECO:0000269|PubMed:28345596, ECO:0000269|PubMed:28345656"
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:P06935"
FT SITE 790..791
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1142..1143
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1368..1369
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1498..1499
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
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:P06935"
FT SITE 2242..2243
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2265..2266
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2516..2517
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
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 2698
FT /note="Essential for 2'-O-methyltransferase activity"
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 CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:A0A142I5B9"
FT CROSSLNK 567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:A0A142I5B9"
FT MUTAGEN 1259
FT /note="A->V: Strong reduction of host innate immune
FT responses and viral-induced apoptosis."
FT /evidence="ECO:0000269|PubMed:31882898"
FT MUTAGEN 2906
FT /note="K->A: Complete loss of nuclear localization; when
FT associated with A-2909."
FT /evidence="ECO:0000269|PubMed:30848123"
FT MUTAGEN 2909
FT /note="R->A: Complete loss of nuclear localization; when
FT associated with A-2906."
FT /evidence="ECO:0000269|PubMed:30848123"
FT MUTAGEN 3099
FT /note="R->A: Disrupts dimer formation, subcellular
FT localization as well as enzymatic activity."
FT /evidence="ECO:0000269|PubMed:31090058"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:5Z0V"
FT TURN 35..40
FT /evidence="ECO:0007829|PDB:5Z0R"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:5Z0R"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:5Z0R"
FT HELIX 74..96
FT /evidence="ECO:0007829|PDB:5Z0R"
FT STRAND 791..797
FT /evidence="ECO:0007829|PDB:5K6K"
FT TURN 798..801
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 802..812
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 815..819
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 822..827
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 829..841
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 852..871
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 877..880
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 885..887
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 922..928
FT /evidence="ECO:0007829|PDB:5K6K"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 935..937
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 943..949
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 952..961
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 971..973
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 975..979
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 982..986
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 988..1008
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 1017..1019
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 1028..1030
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 1035..1037
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 1043..1045
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1060..1068
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1074..1077
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1088..1091
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1100..1105
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1111..1115
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1118..1121
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1126..1130
FT /evidence="ECO:0007829|PDB:5K6K"
FT HELIX 1132..1134
FT /evidence="ECO:0007829|PDB:5K6K"
FT STRAND 1419..1425
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1434..1436
FT /evidence="ECO:0007829|PDB:5ZOB"
FT STRAND 1441..1446
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1452..1454
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1518..1530
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1532..1540
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1543..1546
FT /evidence="ECO:0007829|PDB:5YOF"
FT HELIX 1548..1551
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1556..1558
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1561..1563
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1565..1569
FT /evidence="ECO:0007829|PDB:5YOF"
FT TURN 1570..1573
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1574..1580
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1589..1591
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1593..1597
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1605..1609
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1612..1616
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1619..1624
FT /evidence="ECO:0007829|PDB:5YOF"
FT HELIX 1630..1632
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1636..1638
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1640..1642
FT /evidence="ECO:0007829|PDB:5GXJ"
FT STRAND 1644..1648
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1651..1653
FT /evidence="ECO:0007829|PDB:5YOF"
FT STRAND 1655..1657
FT /evidence="ECO:0007829|PDB:6JPW"
FT STRAND 1659..1662
FT /evidence="ECO:0007829|PDB:5YOF"
FT HELIX 1679..1682
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1687..1690
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT TURN 1698..1701
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1702..1712
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1717..1723
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1724..1733
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT TURN 1734..1736
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1739..1741
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1756..1760
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1761..1769
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1770..1772
FT /evidence="ECO:0007829|PDB:5JRZ"
FT STRAND 1778..1784
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1790..1804
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1809..1813
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1831..1835
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1844..1846
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1848..1851
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1857..1860
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1864..1876
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1881..1884
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT TURN 1886..1888
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1889..1898
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1902..1906
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1908..1911
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1919..1923
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1926..1933
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT TURN 1934..1936
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1937..1945
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1948..1955
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 1967..1971
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT TURN 1978..1981
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 1983..1992
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2007..2012
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT TURN 2017..2020
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2024..2035
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2041..2049
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2058..2060
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2065..2067
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 2070..2075
FT /evidence="ECO:0007829|PDB:6MH3"
FT STRAND 2077..2079
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 2085..2087
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 2091..2094
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2095..2097
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT STRAND 2098..2100
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2101..2111
FT /evidence="ECO:0007829|PDB:5Y4Z"
FT HELIX 2524..2534
FT /evidence="ECO:0007829|PDB:5VIM"
FT HELIX 2537..2543
FT /evidence="ECO:0007829|PDB:5VIM"
FT TURN 2544..2547
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2549..2552
FT /evidence="ECO:0007829|PDB:5VIM"
FT HELIX 2554..2561
FT /evidence="ECO:0007829|PDB:5VIM"
FT HELIX 2574..2583
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2591..2596
FT /evidence="ECO:0007829|PDB:5VIM"
FT TURN 2599..2601
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2602..2607
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2613..2619
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2623..2626
FT /evidence="ECO:0007829|PDB:5TFR"
FT HELIX 2637..2639
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2640..2643
FT /evidence="ECO:0007829|PDB:5VIM"
FT HELIX 2648..2650
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2657..2661
FT /evidence="ECO:0007829|PDB:5VIM"
FT HELIX 2670..2688
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2693..2700
FT /evidence="ECO:0007829|PDB:5VIM"
FT HELIX 2705..2718
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2721..2723
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2726..2728
FT /evidence="ECO:0007829|PDB:5U0B"
FT STRAND 2735..2738
FT /evidence="ECO:0007829|PDB:5VIM"
FT HELIX 2745..2760
FT /evidence="ECO:0007829|PDB:5VIM"
FT STRAND 2761..2763
FT /evidence="ECO:0007829|PDB:5U0B"
FT STRAND 2768..2771
FT /evidence="ECO:0007829|PDB:5VIM"
FT TURN 2791..2793
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2795..2804
FT /evidence="ECO:0007829|PDB:5U0B"
FT TURN 2805..2808
FT /evidence="ECO:0007829|PDB:5U0B"
FT STRAND 2818..2827
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2840..2844
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 2847..2851
FT /evidence="ECO:0007829|PDB:5U04"
FT TURN 2853..2855
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 2858..2860
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2865..2875
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2885..2902
FT /evidence="ECO:0007829|PDB:5U04"
FT TURN 2903..2905
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2913..2920
FT /evidence="ECO:0007829|PDB:5U04"
FT TURN 2921..2923
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 2931..2933
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2935..2944
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 2946..2959
FT /evidence="ECO:0007829|PDB:5U04"
FT TURN 2960..2962
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 2969..2973
FT /evidence="ECO:0007829|PDB:5U0B"
FT STRAND 2977..2979
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 2989..3006
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3008..3011
FT /evidence="ECO:0007829|PDB:5U04"
FT TURN 3012..3015
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3017..3020
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3021..3023
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3029..3041
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3042..3045
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3055..3057
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 3061..3067
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3068..3073
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3076..3091
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3102..3104
FT /evidence="ECO:0007829|PDB:5U0C"
FT STRAND 3106..3116
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 3123..3143
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3149..3152
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3159..3173
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3176..3179
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3182..3185
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3190..3194
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3197..3201
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3206..3209
FT /evidence="ECO:0007829|PDB:5U0B"
FT STRAND 3218..3220
FT /evidence="ECO:0007829|PDB:6UX2"
FT HELIX 3221..3223
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3229..3235
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3237..3239
FT /evidence="ECO:0007829|PDB:5U0B"
FT STRAND 3241..3246
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3249..3256
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3258..3261
FT /evidence="ECO:0007829|PDB:5U0C"
FT HELIX 3266..3283
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3288..3300
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3322..3325
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3327..3335
FT /evidence="ECO:0007829|PDB:5U04"
FT TURN 3336..3338
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3351..3353
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3359..3364
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3369..3371
FT /evidence="ECO:0007829|PDB:5U0B"
FT HELIX 3372..3379
FT /evidence="ECO:0007829|PDB:5U04"
FT HELIX 3381..3392
FT /evidence="ECO:0007829|PDB:5U04"
FT STRAND 3394..3396
FT /evidence="ECO:0007829|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
