CTB1_CERNC
ID CTB1_CERNC Reviewed; 2196 AA.
AC Q6DQW3;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Non-reducing polyketide synthase CTB1 {ECO:0000303|PubMed:12937958};
DE EC=2.3.1.- {ECO:0000269|PubMed:23108075};
DE AltName: Full=Cercosporin toxin biosynthesis cluster protein 1 {ECO:0000303|PubMed:12937958};
GN Name=CTB1 {ECO:0000303|PubMed:12937958};
OS Cercospora nicotianae (Barn spot disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=29003;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND
RP PATHWAY.
RX PubMed=15915645; DOI=10.1094/mpmi-18-0468;
RA Choquer M., Dekkers K.L., Chen H.Q., Cao L., Ueng P.P., Daub M.E.,
RA Chung K.R.;
RT "The CTB1 gene encoding a fungal polyketide synthase is required for
RT cercosporin biosynthesis and fungal virulence of Cercospora nicotianae.";
RL Mol. Plant Microbe Interact. 18:468-476(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1193-1416, FUNCTION, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 18366;
RX PubMed=12937958; DOI=10.1007/s00438-003-0902-7;
RA Chung K.R., Ehrenshaft M., Wetzel D.K., Daub M.E.;
RT "Cercosporin-deficient mutants by plasmid tagging in the asexual fungus
RT Cercospora nicotianae.";
RL Mol. Genet. Genomics 270:103-113(2003).
RN [3]
RP REVIEW ON CERCOSPORIN.
RX PubMed=11701851; DOI=10.1146/annurev.phyto.38.1.461;
RA Daub M.E., Ehrenshaft M.;
RT "The photoactivated cercospora toxin cercosporin: contributions to plant
RT disease and fundamental biology.";
RL Annu. Rev. Phytopathol. 38:461-490(2000).
RN [4]
RP FUNCTION.
RX PubMed=17074519; DOI=10.1016/j.fgb.2006.08.005;
RA Dekkers K.L., You B.J., Gowda V.S., Liao H.L., Lee M.H., Bau H.J.,
RA Ueng P.P., Chung K.R.;
RT "The Cercospora nicotianae gene encoding dual O-methyltransferase and FAD-
RT dependent monooxygenase domains mediates cercosporin toxin biosynthesis.";
RL Fungal Genet. Biol. 44:444-454(2007).
RN [5]
RP FUNCTION.
RX PubMed=17660442; DOI=10.1099/mic.0.2007/007294-0;
RA Chen H.Q., Lee M.H., Chung K.R.;
RT "Functional characterization of three genes encoding putative
RT oxidoreductases required for cercosporin toxin biosynthesis in the fungus
RT Cercospora nicotianae.";
RL Microbiology (Mosc.) 153:2781-2790(2007).
RN [6]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=17462021; DOI=10.1111/j.1365-2958.2007.05689.x;
RA Chen H., Lee M.H., Daub M.E., Chung K.R.;
RT "Molecular analysis of the cercosporin biosynthetic gene cluster in
RT Cercospora nicotianae.";
RL Mol. Microbiol. 64:755-770(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY.
RX PubMed=23108075; DOI=10.1039/c2cc36010a;
RA Newman A.G., Vagstad A.L., Belecki K., Scheerer J.R., Townsend C.A.;
RT "Analysis of the cercosporin polyketide synthase CTB1 reveals a new fungal
RT thioesterase function.";
RL Chem. Commun. (Camb.) 48:11772-11774(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=26938470; DOI=10.1021/jacs.6b00633;
RA Newman A.G., Townsend C.A.;
RT "Molecular characterization of the cercosporin biosynthetic pathway in the
RT fungal plant pathogen Cercospora nicotianae.";
RL J. Am. Chem. Soc. 138:4219-4228(2016).
RN [9]
RP FUNCTION.
RX PubMed=30809363; DOI=10.1039/c8sc02870b;
RA Hu J., Sarrami F., Li H., Zhang G., Stubbs K.A., Lacey E., Stewart S.G.,
RA Karton A., Piggott A.M., Chooi Y.H.;
RT "Heterologous biosynthesis of elsinochrome A sheds light on the formation
RT of the photosensitive perylenequinone system.";
RL Chem. Sci. 10:1457-1465(2019).
RN [10] {ECO:0007744|PDB:6FIJ, ECO:0007744|PDB:6FIK}
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 1-1293, DOMAIN, AND FUNCTION.
RX PubMed=29610486; DOI=10.1038/s41589-018-0026-3;
RA Herbst D.A., Huitt-Roehl C.R., Jakob R.P., Kravetz J.M., Storm P.A.,
RA Alley J.R., Townsend C.A., Maier T.;
RT "The structural organization of substrate loading in iterative polyketide
RT synthases.";
RL Nat. Chem. Biol. 14:474-479(2018).
CC -!- FUNCTION: Polyketide synthase; part of the gene cluster that mediates
CC the biosynthesis of cercosporin, a light-activated, non-host-selective
CC toxin (PubMed:12937958, PubMed:15915645, PubMed:26938470,
CC PubMed:29610486). The perylenequinone chromophore of cercosporin
CC absorbs light energy to attain an electronically-activated triplet
CC state and produces active oxygen species such as the hydroxyl radical,
CC superoxide, hydrogen peroxide or singlet oxygen upon reaction with
CC oxygen molecules (PubMed:11701851). These reactive oxygen species cause
CC damage to various cellular components including lipids, proteins and
CC nucleic acids (PubMed:11701851). The first step of cercosporin
CC biosynthesis is performed by the polyketide synthase CTB1 which
CC catalyzes the formation of nor-toralactone (PubMed:23108075,
CC PubMed:26938470, PubMed:29610486). The starter unit acyltransferase
CC (SAT) domain of CTB1 initiates polyketide extension by the selective
CC utilization of acetyl-CoA, which is elongated to the heptaketide in the
CC beta-ketoacyl synthase (KS) domain by successive condensations with six
CC malonyl units introduced by the malonyl acyltransferase (MAT) domain.
CC The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol
CC cyclizations and dehydrations to a trihydroxynaphthalene, which is
CC thought to be delivered to the thioesterase (TE) domain for product
CC release (PubMed:23108075, PubMed:29610486). The bifunctional enzyme
CC CTB3 then methylates nor-toralactone to toralactone before conducting
CC an unusual oxidative aromatic ring opening (PubMed:17074519,
CC PubMed:26938470). The O-methyltransferase CTB2 further methylates the
CC nascent OH-6 of the CBT3 product, blocking further oxidation at this
CC site before the reductase CTB6 reduces the 2-oxopropyl ketone at
CC position C7, giving naphthalene (PubMed:17660442, PubMed:26938470). The
CC FAD-dependent monooxygenase CTB5 in concert with the multicopper
CC oxidase CTB12 are responsible for homodimerization of naphthalene with
CC CTB7 installing the dioxepine moiety, finally producing cercosporin
CC (PubMed:17660442, PubMed:30809363, PubMed:26938470). The fasciclin
CC domain-containing protein CTB11 might act with CTB5 and CTB12 whereas
CC the roles of CTB9 and CTB10 have still to be elucidated (By
CC similarity). {ECO:0000250|UniProtKB:Q0UHZ9,
CC ECO:0000269|PubMed:12937958, ECO:0000269|PubMed:15915645,
CC ECO:0000269|PubMed:17074519, ECO:0000269|PubMed:17660442,
CC ECO:0000269|PubMed:23108075, ECO:0000269|PubMed:26938470,
CC ECO:0000269|PubMed:29610486, ECO:0000269|PubMed:30809363,
CC ECO:0000303|PubMed:11701851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + 2 H2O +
CC nor-toralactone; Xref=Rhea:RHEA:62892, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:146018;
CC Evidence={ECO:0000269|PubMed:23108075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62893;
CC Evidence={ECO:0000269|PubMed:23108075};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:Q9Y8A5};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:Q9Y8A5};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:12937958,
CC ECO:0000269|PubMed:15915645, ECO:0000269|PubMed:17462021,
CC ECO:0000269|PubMed:23108075, ECO:0000269|PubMed:26938470}.
CC -!- INDUCTION: Expression is positively regulated by the cercosporin
CC cluster-specific transcription factor CTB8 (PubMed:17462021).
CC Expression is also affected by nitrogen and carbon sources and pH, and
CC is also controlled by another transcription activator, CRG1, previously
CC shown to regulate cercosporin production and resistance
CC (PubMed:17462021). {ECO:0000269|PubMed:17462021}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; 2 acyl-carrier protein (ACP) domains that
CC serve as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm; and a C-terminal thioesterase (TE) domain that
CC facilitates the release of the final product from the enzyme.
CC {ECO:0000305|PubMed:15915645, ECO:0000305|PubMed:23108075,
CC ECO:0000305|PubMed:29610486}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of cercosporin
CC (PubMed:12937958, PubMed:15915645, PubMed:26938470). Does not display
CC any pigmentation (PubMed:26938470). Leads to fewer necrotic lesions on
CC inoculated tobacco leaves compared with the wild type
CC (PubMed:15915645). {ECO:0000269|PubMed:12937958,
CC ECO:0000269|PubMed:15915645, ECO:0000269|PubMed:26938470}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY649543; AAT69682.1; -; mRNA.
DR PDB; 6FIJ; X-ray; 2.77 A; A/B=1-1293.
DR PDB; 6FIK; EM; 7.10 A; A/B=1-1293, C=1775-1858.
DR PDBsum; 6FIJ; -.
DR PDBsum; 6FIK; -.
DR AlphaFoldDB; Q6DQW3; -.
DR SMR; Q6DQW3; -.
DR ESTHER; cernc-q6dqw3; Thioesterase.
DR PHI-base; PHI:433; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Repeat; Transferase; Virulence.
FT CHAIN 1..2196
FT /note="Non-reducing polyketide synthase CTB1"
FT /id="PRO_0000444965"
FT DOMAIN 1671..1748
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:15915645, ECO:0000305|PubMed:23108075,
FT ECO:0000305|PubMed:29610486"
FT DOMAIN 1775..1857
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:15915645, ECO:0000305|PubMed:23108075,
FT ECO:0000305|PubMed:29610486"
FT REGION 11..250
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15915645,
FT ECO:0000305|PubMed:23108075, ECO:0000305|PubMed:29610486"
FT REGION 384..817
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15915645,
FT ECO:0000305|PubMed:23108075, ECO:0000305|PubMed:29610486"
FT REGION 922..1223
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15915645,
FT ECO:0000305|PubMed:23108075, ECO:0000305|PubMed:29610486"
FT REGION 1298..1611
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15915645,
FT ECO:0000305|PubMed:23108075, ECO:0000305|PubMed:29610486"
FT REGION 1617..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..2187
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15915645,
FT ECO:0000305|PubMed:23108075, ECO:0000305|PubMed:29610486"
FT COMPBIAS 1856..1890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1708
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1816
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 134..162
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 384..393
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 446..449
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 453..457
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 468..483
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 523..527
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 531..540
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 555..569
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 573..581
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 586..594
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 619..627
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 628..633
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 639..649
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 654..658
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 661..675
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 682..686
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 693..707
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 728..731
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 738..752
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 762..765
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 773..775
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 795..801
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 805..813
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 830..838
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 839..855
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 863..873
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 879..888
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 889..904
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 919..923
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 926..928
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 931..934
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 935..940
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 942..957
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 964..968
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 971..973
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 978..998
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1003..1008
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1012..1019
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1025..1042
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1047..1053
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1057..1063
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1064..1066
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 1068..1070
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1073..1079
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1082..1088
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1089..1101
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1106..1108
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1118..1123
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1124..1132
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1143..1145
FT /evidence="ECO:0007829|PDB:6FIJ"
FT TURN 1146..1149
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1150..1152
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1155..1157
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1160..1168
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1173..1182
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1190..1200
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1201..1209
FT /evidence="ECO:0007829|PDB:6FIJ"
FT STRAND 1214..1218
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1225..1238
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1245..1250
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1253..1255
FT /evidence="ECO:0007829|PDB:6FIJ"
FT HELIX 1279..1282
FT /evidence="ECO:0007829|PDB:6FIJ"
SQ SEQUENCE 2196 AA; 236728 MW; B6F633E98FB4BE16 CRC64;
MEDGAQMRVV AFGDQTYDCS EAVSQLLRVR DDAIVVDFLE RAPAVLKAEL ARLSSEQQEE
TPRFATLAEL VPRYRAGTLN PAVSQALTCI AQLGLFIRQH SSGQEAYPTA HDSCITGVCT
GALTAVAVGS ASSVTALVPL ALHTVAVAVR LGARAWEIGS CLADARRGAN GRYASWTSAV
GGISPQDLQD RISAYTAEQA LASVSVPYLS AAVGPGQSSV SAAPVILDAF LSTLLRPLTT
TRLPITAPYH APHLFTAKDV QHVTDCLPPS EAWPTVRIPI ISFSRDEAVS RGASFPAAMS
EAVRDCLIRP IALDRMAVSI TNHARDLGKD SVLPSPIALS FSDKLGPQVN SHLPGAKAPT
PELTSKSIPS AIGAEQQPMA KSPIAILAAS GRFPQSSSMD QFWDVLINGV DTHELVPPTR
WNAATHVSED PKAKNVSGTG FGCWLHEAGE FDAAYFNMSP REAPQVDPAQ RLALLTATEA
LEQAGVVPNR TSSTQKNRVG VWYGATSNDW METNSAQNVD TYFIPGGNRA FIPGRVNYFH
KFSGPSYTID TACSSSLAAL HMACNALWRG EVDTAIVGGT NVLTNPDMTA GLDAGHFLSR
SGNCKTFDDE ADGYCRGEAV VTLILKRLPD AQADKDPIQA SILGIATNHS AEAASITRPH
AGAQQDLFQQ VLTETGLTAN DISVCEMHGT GTQAGDSGET TSVVETLAPL NRSGSAVRTT
PLYIGAVKSN VGHAESAAGV SSLAKILLML KHSKIPPHVG IKTKLNHRLP DLAARNTHIA
RSEVPWPRPK NGKRRVLLNN FSAAGGNTCL VLEDAPEPED SQEVDPREHH IVALSAKTPD
SMVNNLTNMI TWIDKHSGDS LATLPQLSYT TTARRVHHRH RAVATGTDLL QIRSSLQEQL
DRRVSGERSI PHPPNGPSFV LAFTGQGSAF AGMGVDLYKR FASFRSDIAR YDQICEGMSL
PSIKAMFEDE KVFSTASPTL QQLTHVCFQM ALYRLWKSLG VQAKAVVGHS LGEYAALYAA
GVLSQSDTLY LVGRRAQLME KHLSQGTHAM LAVRAKEEAI VAAIDGPPGE AYEFSCRNGE
QRNVLGGTVA QIQAAKAALE AKKIRCQYLD TPMAFHTGQV DPILPELLQV AAACSIQDPQ
IPVISPAYGK VIRSAKDFQP EYFTHHCRSS VNMVDALQSA VEEGLLDKNV IGLEIGPGPV
VTQFVKEAVG TTMQTFASIN KDKDTWQLMT QALAKFYLAG ASVEWSRYHE DFPGAQKVLE
LPAYGWALKN YWLQYVNDWS LRKGDPAVVV AASNLELSSS IHKVITNTIT ANSDGELVVD
ADLSREDLHP MVQGHQVYGV PLCTPSVYAD IALTLGEYIR QVIKPGEVAQ TSVEVAEMNI
QSALVANNTG RVQLLRTCAK FDPKAQVASC TFSSIVEQHA NCKIRFGSLE KEKTALKSAA
LAAQASMAAL KTQVGQDDNT YRFSKGMIYK MIGQLADFDE KYRGLCAITL DNDAMEASGK
VSFKGIPNEG KFHSSPAYLD ALSQLGGFVM NANEGVDLEK EVFVNHGWGS MRFFAALDPA
MTYYTHVKMT QGKDKLWTGD VLIFDDKQAL IGIVGGVALQ GVPKRLMHYI VTAANKKASG
PPTEKKTSSP PVEKKASAPV APTRPAIQRK NASIPPPATQ VTPQNKTIKT PSVSALIAPA
LEIVSEEIRM PIDELKDDID FTDAGLDSLL SLVISSRMRD QLGIEFESAQ FMEIGSIGGL
KEFLTRLSPP VAVAVATAVE IVKEEALTSL EELTDPSPNE IGTVWRDALK ILSEESGLTD
EELTDDTSFA DVGVDSLMSL VITSRLRDEL DIDFPDRALF EECQTIFDLR KRFSGSTESF
DSTTTKPSAG DATPPLTDSS ASSPPSSEFD GETPMTDLDE VFDSPPAQKR IPSPPKGRIP
PAWSMYLQGS QKRSKEILFL FPDGAGAATS YLSLPRLGED IGVVAFNSPF MKTPHKFADH
TLPDVIASYV EGIRGRQAQG PYHLGGWSAG GILAYAVAQE LIAAGEEVST LLLIDSPSPT
KGLDRLPTRF FDHCTNVGLF GTELSRGSGG PNKTPEWLMP HFRASIELLH GYHAPPMKLG
NKTKVMVIWA GECAFDGVRY AHIPPSAGDT DEDTEGMKFL TEKRKDFGAT EWASLFPGTD
VDARVVESEH HFSMMRDSGA QMLVEHMRDG LGIVSS
