ID EXG1_CANAL Reviewed; 438 AA. AC P29717; A0A1D8PCW5; Q5AI63; Q5AIZ3; Q9URL8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 5. DT 27-MAR-2024, entry version 162. DE RecName: Full=Glucan 1,3-beta-glucosidase; DE EC=2.4.1.- {ECO:0000269|PubMed:10469155}; DE EC=3.2.1.58 {ECO:0000269|PubMed:10469155, ECO:0000269|PubMed:20875088, ECO:0000269|PubMed:21713010}; DE AltName: Full=Exo-1,3-beta-glucanase {ECO:0000303|PubMed:8436950}; DE Flags: Precursor; GN Name=XOG1; Synonyms=EXG, EXG1, XOG; GN OrderedLocusNames=CAALFM_C102990CA; GN ORFNames=Ca49C10.05, CaO19.10507, CaO19.2990; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 39-73. RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061; RX PubMed=8436950; DOI=10.1099/00221287-139-2-325; RA Chambers R.S., Broughton M.J., Cannon R.D., Carne A., Emerson G.W., RA Sullivan P.A.; RT "An exo-beta-(1,3)-glucanase of Candida albicans: purification of the RT enzyme and molecular cloning of the gene."; RL J. Gen. Microbiol. 139:325-334(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE CAO19.10507). RC STRAIN=1161; RA Taylor K., Harris D., Barrell B.G., Rajandream M.A.; RT "Candida albicans strain 1161 genome pilot sequencing project."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [4] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). RN [6] RP PROTEIN SEQUENCE OF 39-73, SUBCELLULAR LOCATION, AND SUBUNIT. RC STRAIN=3153A; RX PubMed=1789004; DOI=10.1002/yea.320070808; RA Luna-Arias J.P., Analuz E., Ridruejo J.C., Olivero I., Larriba G.; RT "The major exoglucanase from Candida albicans: a non-glycosylated secretory RT monomer related to its counterpart from Saccharomyces cerevisiae."; RL Yeast 7:833-841(1991). RN [7] RP ACTIVE SITE GLU-330. RX PubMed=9013549; DOI=10.1074/jbc.272.6.3161; RA MacKenzie L.F., Brooke G.S., Cutfield J.F., Sullivan P.A., Withers S.G.; RT "Identification of Glu-330 as the catalytic nucleophile of Candida albicans RT exo-beta-(1,3)-glucanase."; RL J. Biol. Chem. 272:3161-3167(1997). RN [8] RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10469155; DOI=10.1046/j.1432-1327.1999.00581.x; RA Stubbs H.J., Brasch D.J., Emerson G.W., Sullivan P.A.; RT "Hydrolase and transferase activities of the beta-1,3-exoglucanase of RT Candida albicans."; RL Eur. J. Biochem. 263:889-895(1999). RN [9] RP INDUCTION. RX PubMed=14731272; DOI=10.1111/j.1365-2958.2003.03879.x; RA Lee C.M., Nantel A., Jiang L., Whiteway M., Shen S.H.; RT "The serine/threonine protein phosphatase SIT4 modulates yeast-to-hypha RT morphogenesis and virulence in Candida albicans."; RL Mol. Microbiol. 51:691-709(2004). RN [10] RP INDUCTION. RX PubMed=17030998; DOI=10.1128/ec.00186-06; RA Brown V., Sexton J.A., Johnston M.; RT "A glucose sensor in Candida albicans."; RL Eukaryot. Cell 5:1726-1737(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=19555771; DOI=10.1016/j.fgb.2009.06.005; RA Maddi A., Bowman S.M., Free S.J.; RT "Trifluoromethanesulfonic acid-based proteomic analysis of cell wall and RT secreted proteins of the ascomycetous fungi Neurospora crassa and Candida RT albicans."; RL Fungal Genet. Biol. 46:768-781(2009). RN [12] RP INDUCTION. RX PubMed=20402792; DOI=10.1111/j.1567-1364.2010.00626.x; RA Li X., Du W., Zhao J., Zhang L., Zhu Z., Jiang L.; RT "The MAP kinase-activated protein kinase Rck2p regulates cellular responses RT to cell wall stresses, filamentation and virulence in the human fungal RT pathogen Candida albicans."; RL FEMS Yeast Res. 10:441-451(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=20167299; DOI=10.1016/j.jprot.2010.02.008; RA Hernaez M.L., Ximenez-Embun P., Martinez-Gomariz M., RA Gutierrez-Blazquez M.D., Nombela C., Gil C.; RT "Identification of Candida albicans exposed surface proteins in vivo by a RT rapid proteomic approach."; RL J. Proteomics 73:1404-1409(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION. RX PubMed=20392151; DOI=10.3109/13693780903405782; RA Kelly J., Kavanagh K.; RT "Proteomic analysis of proteins released from growth-arrested Candida RT albicans following exposure to caspofungin."; RL Med. Mycol. 48:598-605(2010). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=20641015; DOI=10.1002/yea.1775; RA Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.; RT "Mass spectrometric analysis of the secretome of Candida albicans."; RL Yeast 27:661-672(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=21622905; DOI=10.1128/ec.05011-11; RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G., RA de Koning L.J., Klis F.M.; RT "Effects of fluconazole on the secretome, the wall proteome, and wall RT integrity of the clinical fungus Candida albicans."; RL Eukaryot. Cell 10:1071-1081(2011). RN [17] RP INTERACTION WITH ANTIMICROBIAL PEPTIDE LL-37, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, AND FUNCTION. RX PubMed=21713010; DOI=10.1371/journal.pone.0021394; RA Tsai P.W., Yang C.Y., Chang H.T., Lan C.Y.; RT "Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in RT Candida albicans adhesion by the human antimicrobial peptide LL-37."; RL PLoS ONE 6:E21394-E21394(2011). RN [18] RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION. RX PubMed=22876186; DOI=10.1371/journal.ppat.1002848; RA Taff H.T., Nett J.E., Zarnowski R., Ross K.M., Sanchez H., Cain M.T., RA Hamaker J., Mitchell A.P., Andes D.R.; RT "A Candida biofilm-induced pathway for matrix glucan delivery: implications RT for drug resistance."; RL PLoS Pathog. 8:E1002848-E1002848(2012). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=23243062; DOI=10.1128/ec.00278-12; RA Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G., RA Brul S., de Koning L.J., Klis F.M.; RT "Surface stress induces a conserved cell wall stress response in the RT pathogenic fungus Candida albicans."; RL Eukaryot. Cell 12:254-264(2013). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=23136884; DOI=10.1111/mmi.12087; RA Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D., RA Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.; RT "A family of secreted pathogenesis-related proteins in Candida albicans."; RL Mol. Microbiol. 87:132-151(2013). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 45-438, DISULFIDE BOND, AND RP SUBSTRATE-BINDING. RX PubMed=10610795; DOI=10.1006/jmbi.1999.3287; RA Cutfield S.M., Davies G.J., Murshudov G., Anderson B.F., Moody P.C., RA Sullivan P.A., Cutfield J.F.; RT "The structure of the exo-beta-(1,3)-glucanase from Candida albicans in RT native and bound forms: relationship between a pocket and groove in family RT 5 glycosyl hydrolases."; RL J. Mol. Biol. 294:771-783(1999). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 39-438 IN COMPLEX WITH SUBSTRATE, RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-182; PHE-267; PHE-296 AND RP GLU-330. RX PubMed=20875088; DOI=10.1111/j.1742-4658.2010.07869.x; RA Patrick W.M., Nakatani Y., Cutfield S.M., Sharpe M.L., Ramsay R.J., RA Cutfield J.F.; RT "Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and RT the role of the Phe-Phe 'clamp' at the active site entrance."; RL FEBS J. 277:4549-4561(2010). CC -!- FUNCTION: Major glucan 1,3-beta-glucosidase required for cell wall CC integrity. Beta-glucanases participate in the metabolism of beta- CC glucan, the main structural component of the cell wall. Can also CC function biosynthetically as a transglycosylase. Functions to deliver CC glucan from the cell to the extracellular matrix. Does not appear to CC impact cell wall glucan content of biofilm cells, nor is it necessary CC for filamentation or biofilm formation. Involved in cell-substrate and CC cell-cell adhesion. Adhesion to host-cell surfaces is the first CC critical step during mucosal infection. XOG1 is target of human CC antimicrobial peptide LL-37 for inhibition of cell adhesion. CC {ECO:0000269|PubMed:21713010, ECO:0000269|PubMed:22876186}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Successive hydrolysis of beta-D-glucose units from the non- CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; CC EC=3.2.1.58; Evidence={ECO:0000269|PubMed:10469155, CC ECO:0000269|PubMed:20875088, ECO:0000269|PubMed:21713010}; CC -!- ACTIVITY REGULATION: Binding of human antimicrobial peptide LL-37 CC decreases the catalytic activity, which leads to the decrease of cell CC adhesion. {ECO:0000269|PubMed:21713010}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=23 mM for laminaribiose {ECO:0000269|PubMed:10469155}; CC KM=12.7 mM for laminaritriose {ECO:0000269|PubMed:10469155}; CC KM=5 mM for laminaritetraose {ECO:0000269|PubMed:10469155}; CC KM=2.6 mM for laminaripentaose {ECO:0000269|PubMed:10469155}; CC KM=2.7 mM for laminarihexaose {ECO:0000269|PubMed:10469155}; CC KM=2.4 mM for laminariheptaose {ECO:0000269|PubMed:10469155}; CC KM=3.9 mM for laminarin {ECO:0000269|PubMed:10469155}; CC KM=17.9 mM for pustulan {ECO:0000269|PubMed:10469155}; CC KM=260 mM for gentiobiose {ECO:0000269|PubMed:10469155}; CC KM=120 mM for gentiotriose {ECO:0000269|PubMed:10469155}; CC KM=70 mM for cellobiose {ECO:0000269|PubMed:10469155}; CC KM=9.4 mM for cellotetraose {ECO:0000269|PubMed:10469155}; CC KM=12 mM for cellohexaose {ECO:0000269|PubMed:10469155}; CC KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG) CC {ECO:0000269|PubMed:10469155}; CC -!- SUBUNIT: Monomer. Interacts with the human antimicrobial peptide LL-37. CC {ECO:0000269|PubMed:1789004, ECO:0000269|PubMed:20875088, CC ECO:0000269|PubMed:21713010}. CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:1789004, CC ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:20167299, CC ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:21622905, CC ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}. Note=Is non- CC covalently attached to the cell wall. CC -!- INDUCTION: Expression is maximal during the early rapid growth phase CC and increases during biofilm growth. Induced by caspofungin. CC Transcripts is also regulated by RCK2, SIT4, and HTG4. CC {ECO:0000269|PubMed:14731272, ECO:0000269|PubMed:17030998, CC ECO:0000269|PubMed:20392151, ECO:0000269|PubMed:20402792, CC ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:22876186}. CC -!- DISRUPTION PHENOTYPE: Leads to enhanced susceptibility to the commonly CC used antifungal, fluconazole, during biofilm growth only. CC {ECO:0000269|PubMed:22876186}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family. CC {ECO:0000305}. 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; X56556; CAA39908.1; -; Genomic_DNA. DR EMBL; AL033497; CAA21969.1; -; Genomic_DNA. DR EMBL; CP017623; AOW25980.1; -; Genomic_DNA. DR PIR; A47702; A47702. DR PIR; T52149; T52149. DR RefSeq; XP_721488.2; XM_716395.2. DR PDB; 1CZ1; X-ray; 1.85 A; A=45-438. DR PDB; 1EQC; X-ray; 1.85 A; A=45-438. DR PDB; 1EQP; X-ray; 1.90 A; A=45-438. DR PDB; 2PB1; X-ray; 1.90 A; A=39-438. DR PDB; 2PBO; X-ray; 1.85 A; A=39-438. DR PDB; 2PC8; X-ray; 1.80 A; A=39-438. DR PDB; 2PF0; X-ray; 1.90 A; A=39-438. DR PDB; 3N9K; X-ray; 1.70 A; A=40-438. DR PDB; 3O6A; X-ray; 2.00 A; A=40-438. DR PDB; 4M80; X-ray; 1.86 A; A=40-438. DR PDB; 4M81; X-ray; 1.86 A; A=40-438. DR PDB; 4M82; X-ray; 1.59 A; A=40-438. DR PDBsum; 1CZ1; -. DR PDBsum; 1EQC; -. DR PDBsum; 1EQP; -. DR PDBsum; 2PB1; -. DR PDBsum; 2PBO; -. DR PDBsum; 2PC8; -. DR PDBsum; 2PF0; -. DR PDBsum; 3N9K; -. DR PDBsum; 3O6A; -. DR PDBsum; 4M80; -. DR PDBsum; 4M81; -. DR PDBsum; 4M82; -. DR AlphaFoldDB; P29717; -. DR SMR; P29717; -. DR BioGRID; 1219931; 3. DR STRING; 237561.P29717; -. DR DrugBank; DB01816; Castanospermine. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR CLAE; EXG5A_CANAL; -. DR EnsemblFungi; C1_02990C_A-T; C1_02990C_A-T-p1; C1_02990C_A. DR GeneID; 3636837; -. DR KEGG; cal:CAALFM_C102990CA; -. DR CGD; CAL0000190583; XOG1. DR VEuPathDB; FungiDB:C1_02990C_A; -. DR eggNOG; ENOG502QPYU; Eukaryota. DR HOGENOM; CLU_004624_0_1_1; -. DR InParanoid; P29717; -. DR OMA; MDYHEYQ; -. DR OrthoDB; 1431012at2759; -. DR BRENDA; 3.2.1.58; 1096. DR SABIO-RK; P29717; -. DR EvolutionaryTrace; P29717; -. DR PHI-base; PHI:10734; -. DR PRO; PR:P29717; -. DR Proteomes; UP000000559; Chromosome 1. DR GO; GO:0009986; C:cell surface; IDA:CGD. DR GO; GO:0005576; C:extracellular region; IDA:CGD. DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD. DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:CGD. DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:CGD. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0031589; P:cell-substrate adhesion; IDA:CGD. DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. DR GO; GO:0044042; P:glucan metabolic process; IMP:CGD. DR GO; GO:0044407; P:single-species biofilm formation in or on host organism; IMP:CGD. DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1. DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cell wall; Cell wall biogenesis/degradation; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted; KW Signal; Transferase; Virulence; Zymogen. FT SIGNAL 1..21 FT /note="Or 25" FT /evidence="ECO:0000255" FT PROPEP 22..38 FT /evidence="ECO:0000269|PubMed:1789004, FT ECO:0000269|PubMed:8436950" FT /id="PRO_0000007878" FT CHAIN 39..438 FT /note="Glucan 1,3-beta-glucosidase" FT /id="PRO_0000007879" FT ACT_SITE 230 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O85465" FT ACT_SITE 330 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:9013549" FT BINDING 65 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20875088" FT BINDING 67 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20875088" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20875088" FT BINDING 293 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20875088" FT BINDING 300 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20875088" FT DISULFID 313..435 FT /evidence="ECO:0000269|PubMed:10610795" FT DISULFID 338..364 FT /evidence="ECO:0000269|PubMed:10610795" FT MUTAGEN 182 FT /note="F->A: Decreases catalytic activity. Impairs FT catalytic activity; when associated with Ala-296." FT /evidence="ECO:0000269|PubMed:20875088" FT MUTAGEN 267 FT /note="F->A: Decreases catalytic activity. Impairs FT catalytic activity; when associated with Ala-296 or FT Ser-330." FT /evidence="ECO:0000269|PubMed:20875088" FT MUTAGEN 296 FT /note="F->A: Impairs catalytic activity; when associated FT with Ala-182." FT /evidence="ECO:0000269|PubMed:20875088" FT MUTAGEN 296 FT /note="F->W,I: Decreases catalytic activity." FT /evidence="ECO:0000269|PubMed:20875088" FT MUTAGEN 330 FT /note="E->Q: Impairs catalytic activity." FT /evidence="ECO:0000269|PubMed:20875088" FT MUTAGEN 330 FT /note="E->S: Impairs catalytic activity; when associated FT with Ala-267." FT /evidence="ECO:0000269|PubMed:20875088" FT CONFLICT 102 FT /note="S -> L (in Ref. 2; CAA21969)" FT /evidence="ECO:0000305" FT CONFLICT 193 FT /note="F -> S (in Ref. 2; CAA21969)" FT /evidence="ECO:0000305" FT TURN 48..50 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:4M82" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 89..112 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 115..123 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 150..163 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 167..174 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 198..213 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:4M82" FT TURN 219..221 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 238..254 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:4M82" FT TURN 270..275 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 285..292 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 298..301 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 305..321 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 323..331 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:4M82" FT TURN 340..343 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 365..367 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 375..393 FT /evidence="ECO:0007829|PDB:4M82" FT TURN 394..396 FT /evidence="ECO:0007829|PDB:4M82" FT STRAND 397..401 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 409..411 FT /evidence="ECO:0007829|PDB:4M82" FT HELIX 413..418 FT /evidence="ECO:0007829|PDB:4M82" SQ SEQUENCE 438 AA; 50056 MW; 6FEAEA80C1B0121C CRC64; MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN NVIRGVNLGG WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA ASRILQKHWS TWITEQDFKQ ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ VQYLEKALGW ARKNNIRVWI DLHGAPGSQN GFDNSGLRDS YNFQNGDNTQ VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK LKQFFLDGYN SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR YEGAYDNAPY IGSCQPMLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF WSWKTENAPE WSFQTLTYNG LFPQPVTDRQ FPNQCGFH //