POLG_DEN2T
ID POLG_DEN2T Reviewed; 1683 AA.
AC P27914;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Envelope protein E;
DE Contains:
DE RecName: Full=Non-structural protein 1;
DE Short=NS1;
DE Contains:
DE RecName: Full=Non-structural protein 2A;
DE Short=NS2A;
DE Contains:
DE RecName: Full=Serine protease NS3;
DE EC=3.4.21.91;
DE EC=3.6.1.15;
DE EC=3.6.4.13;
DE AltName: Full=Non-structural protein 3;
DE Flags: Fragments;
OS Dengue virus type 2 (strain Tonga/EKB194/1974) (DENV-2).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=11067;
OH NCBI_TaxID=53540; Aedimorphus.
OH NCBI_TaxID=53539; Diceromyia.
OH NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=53541; Stegomyia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-495.
RX PubMed=2216784; DOI=10.1093/nar/18.19.5889;
RA Chen W., Maguire T.;
RT "Nucleotide sequence of the envelope glycoprotein gene of a dengue-2 virus
RT isolated during an epidemic of benign dengue fever in Tonga in 1974.";
RL Nucleic Acids Res. 18:5889-5889(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 496-1683.
RA Qu X., Chen W., Maguire T.;
RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.5 ANGSTROMS) OF 1-395, AND X-RAY
RP CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-395.
RX PubMed=15341726; DOI=10.1016/j.str.2004.06.019;
RA Zhang Y., Zhang W., Ogata S., Clements D., Strauss J.H., Baker T.S.,
RA Kuhn R.J., Rossmann M.G.;
RT "Conformational changes of the flavivirus E glycoprotein.";
RL Structure 12:1607-1618(2004).
CC -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC mediates fusion between viral and cellular membranes. Envelope protein
CC is synthesized in the endoplasmic reticulum in the form of heterodimer
CC with protein prM. They play a role in virion budding in the ER, and the
CC newly formed immature particle is covered with 60 spikes composed of
CC heterodimer between precursor prM and envelope protein E. The virion is
CC transported to the Golgi apparatus where the low pH causes dissociation
CC of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC inefficient, and many virions are only partially matured. These
CC uncleaved prM would play a role in immune evasion.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
CC pathogenesis and viral replication. Once cleaved off the polyprotein,
CC is targeted to three destinations: the viral replication cycle, the
CC plasma membrane and the extracellular compartment. Essential for viral
CC replication. Required for formation of the replication complex and
CC recruitment of other non-structural proteins to the ER-derived membrane
CC structures. Excreted as a hexameric lipoparticle that plays a role
CC against host immune response. Antagonizing the complement function.
CC Binds to the host macrophages and dendritic cells. Inhibits signal
CC transduction originating from Toll-like receptor 3 (TLR3).
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [Non-structural protein 1]: Disrupts the host endothelial
CC glycocalyx layer of host pulmonary microvascular endothelial cells,
CC inducing degradation of sialic acid and shedding of heparan sulfate
CC proteoglycans. NS1 induces expression of sialidases, heparanase, and
CC activates cathepsin L, which activates heparanase via enzymatic
CC cleavage. These effects are probably linked to the endothelial
CC hyperpermeability observed in severe dengue disease.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC replication complex that functions in virion assembly and antagonizes
CC the host immune response. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
CC serine protease function of NS3. May have membrane-destabilizing
CC activity and form viroporins (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
CC -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC association with NS2B, performs its autocleavage and cleaves the
CC polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
CC ProRule:PRU00860}.
CC -!- 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 + 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 -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus) with
CC host EXOC1 (via C-terminus); this interaction results in EXOC1
CC degradation through the proteasome degradation pathway. Protein prM:
CC Forms heterodimers with envelope protein E in the endoplasmic reticulum
CC and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi. Interacts with protein prM. Interacts with non-structural
CC protein 1. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted. Interacts with envelope protein E.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC serine protease NS3. Non-structural protein 2B: Forms a heterodimer
CC with serine protease NS3. May form homooligomers.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B.
CC Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA
CC polymerase NS5; this interaction stimulates RNA-directed RNA polymerase
CC NS5 guanylyltransferase activity. Interacts with host SHFL.
CC {ECO:0000250|UniProtKB:P17763}.
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 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 -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC envelope protein E contain an endoplasmic reticulum retention signal.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC performed by host signal peptidase, wereas cleavages in the cytoplasmic
CC side are performed by the Serine protease NS3. Signal cleavage at the
CC 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K
CC site. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC glycosylated and this is required for efficient secretion of the
CC protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Envelope protein E]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC performed by host signal peptidase, wereas cleavages in the cytoplasmic
CC side are performed by serine protease NS3. Signal cleavage at the 2K-4B
CC site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- WEB RESOURCE: Name=Virus Pathogen Resource;
CC URL="https://www.viprbrc.org/brc/home.spg?decorator=flavi_dengue";
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DR EMBL; X54319; CAA38217.1; -; Genomic_RNA.
DR EMBL; X57469; CAA40705.1; -; Genomic_RNA.
DR EMBL; X57468; CAA40704.1; -; Genomic_RNA.
DR PIR; PQ0507; PQ0507.
DR PIR; S11482; S11482.
DR PDB; 1TG8; X-ray; 2.61 A; A=1-395.
DR PDB; 1TGE; EM; 12.50 A; A/B/C=1-395.
DR PDBsum; 1TG8; -.
DR PDBsum; 1TGE; -.
DR BMRB; P27914; -.
DR SMR; P27914; -.
DR DrugBank; DB04473; alpha-L-fucose.
DR MEROPS; S07.001; -.
DR EvolutionaryTrace; P27914; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd12149; Flavi_E_C; 1.
DR Gene3D; 1.20.1280.260; -; 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; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
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; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR001850; Flavivirus_NS3_S7.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR Pfam; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW Hydrolase; Membrane; Nucleotide-binding; Protease; Secreted;
KW Serine protease; Suppressor of RNA silencing; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral nucleoprotein; Viral penetration into host cytoplasm; Virion;
KW Virus endocytosis by host; Virus entry into host cell; Zinc.
FT CHAIN <1..>1683
FT /note="Genome polyprotein"
FT /id="PRO_0000405219"
FT CHAIN 1..495
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000037980"
FT CHAIN 496..847
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000037981"
FT CHAIN 848..1065
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000308290"
FT CHAIN 1066..1683
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT /id="PRO_0000037983"
FT TOPO_DOM <1..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..915
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 916..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 947..965
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 966..989
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 990..1010
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1011
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1031..1037
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1059..>1683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1066..1243
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1245..1401
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1411..1582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 98..111
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1249..1252
FT /note="Important for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P14340"
FT MOTIF 1349..1352
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT ACT_SITE 1116
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1140
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1200
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT BINDING 1258..1265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 495..496
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 847..848
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 1065..1066
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT SITE 1522
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1525
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 3..30
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 60..121
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 74..105
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 92..116
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 185..285
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 302..333
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 499..510
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 550..638
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 674..718
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 775..824
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 786..808
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 807..811
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT NON_CONS 1065..1066
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 1683
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 55..72
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1TG8"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:1TG8"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 109..128
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:1TG8"
FT TURN 148..152
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1TG8"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:1TG8"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1TG8"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1TG8"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1TG8"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:1TG8"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:1TG8"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:1TG8"
SQ SEQUENCE 1683 AA; 187440 MW; 3B0438D96196BFC8 CRC64;
MRCIGISNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC
IEAKLTNTTT DSRCPTQGEP TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT
CKKNMEGKIV QPENLEYTVV ITPHSGEEHA VGNDTGKHGK EVKITPQSSI TEAELTGYGT
VTMECSPRTG LDFNEMVLLQ MEDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF
KNPHAKKQDV VVLGSQEGAM HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS
MCTGKFKIVK EIAETQHGTI VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE
KDSPVNIEAE PPFGDSYIII GVEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV
LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFVTDNV HTWTEQYKFQ PESPSKLASA
IQKAHEEGIC GIRSVTRLEN LMWKQITSEL NHILSENEVK LTIMTGDIKG IMQVGKRSLR
PQPTELRYSW KTWGKAKMLS TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT
NIWLRLREKQ DVFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW
PKSHTLWSNG VLESEMVIPK NFAGPVSQHN NRPGYYTQTA GPWHLGKLEM DFDFCEGTTV
VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL
VSSLVTAGHG QIDNFSLGIL GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL
GRVMVMVGAT MTDDIGMGVT YLALLAAFRV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ
SSIPETILEL TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA
VVSVSPLLLT SSQQKADWIP LALTIKGLNP TAIFLTTLSR TSKKRAGVLW DVPSPPPVGK
AELEDGAYRI KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD
LISYGGGWKL EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FRTNTGTIGA VSLDFSPGTS
GSPIVDKKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP
GAGKTKRYLP AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE
IVDLMCHATF TMRLLSPIRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT
ATPPGSRDPF PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL
RKNGKRVIQL SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT
DGEERVILAG PMPVTHSSAA QRRGRIGRNP RNENDQYIYM GEPLENDEDC AHWKEAKMLL
DNINTPEGII PSIFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI
NYADRRWCFD GTRNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA
GRK
