ID GUX1_HYPJE Reviewed; 513 AA. AC P62694; P00725; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 08-NOV-2023, entry version 111. DE RecName: Full=Exoglucanase 1; DE EC=3.2.1.91 {ECO:0000269|Ref.4}; DE AltName: Full=1,4-beta-cellobiohydrolase; DE AltName: Full=Cellobiohydrolase 7A; DE Short=Cel7A; DE AltName: Full=Exocellobiohydrolase I; DE Short=CBHI; DE AltName: Full=Exoglucanase I; DE Flags: Precursor; GN Name=cbh1; OS Hypocrea jecorina (Trichoderma reesei). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma. OX NCBI_TaxID=51453; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=L27; RX DOI=10.1038/nbt1083-691; RA Shoemaker S., Schweickart V., Ladner M., Gelfand D., Kwok S., Myambo K., RA Innis M.; RT "Molecular cloning of exo-cellobiohydrolase I derived from Trichoderma RT reesei strain L27."; RL Biotechnology (N.Y.) 1:691-696(1983). RN [2] RP PROTEIN SEQUENCE. RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414; RA Faegerstam L.G.; RT "Cellulases from Trichoderma reesei QM 9414: enzymatic and structural RT properties."; RL Thesis (1981), University of Uppsala, Sweden. RN [3] RP PROTEIN SEQUENCE OF 18-37, AND PYROGLUTAMATE FORMATION AT GLN-18. RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414; RX DOI=10.1016/0014-5793(80)81006-4; RA Faegerstam L.G., Pettersson L.G.; RT "The 1,4-beta-glucan cellobiohydrolases of Trichoderma reesei QM 9414."; RL FEBS Lett. 119:97-100(1980). RN [4] RP PROTEIN SEQUENCE OF 18-48, PYROGLUTAMATE FORMATION AT GLN-18, FUNCTION, AND RP SUBCELLULAR LOCATION. RC STRAIN=L27; RX DOI=10.1038/nbt1083-687; RA Shoemaker S., Watt K., Tsitovsky G., Cox R.; RT "Characterization and properties of cellulases purified from Trichoderma RT reesei strain L27."; RL Biotechnology (N.Y.) 1:687-690(1983). RN [5] RP PROTEIN SEQUENCE OF 57-64; 285-289 AND 382-396, AND GLYCOSYLATION AT RP ASN-62; ASN-287; ASN-401; THR-461; THR-462; THR-463; THR-464; THR-469; RP THR-470; THR-471; SER-473; SER-474; THR-478 AND SER-480. RC STRAIN=ALKO2877; RX PubMed=9746354; DOI=10.1046/j.1432-1327.1998.2560119.x; RA Harrison M.J., Nouwens A.S., Jardine D.R., Zachara N.E., Gooley A.A., RA Nevalainen H., Packer N.H.; RT "Modified glycosylation of cellobiohydrolase I from a high cellulase- RT producing mutant strain of Trichoderma reesei."; RL Eur. J. Biochem. 256:119-127(1998). RN [6] RP PROTEIN SEQUENCE OF 141-151. RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414; RX DOI=10.1016/0014-5793(89)80136-X; RA Tomme P., Clayssens M.; RT "Identification of a functionally important carboxyl group in RT cellobiohydrolase I from Trichoderma reesei."; RL FEBS Lett. 243:239-243(1989). RN [7] RP STRUCTURE BY NMR OF 478-513, AND DISULFIDE BONDS. RX PubMed=2554967; DOI=10.1021/bi00444a016; RA Kraulis P.J., Clore G.M., Nilges M., Jones T.A., Pettersson G., Knowles J., RA Gronenborn A.M.; RT "Determination of the three-dimensional solution structure of the C- RT terminal domain of cellobiohydrolase I from Trichoderma reesei. A study RT using nuclear magnetic resonance and hybrid distance geometry-dynamical RT simulated annealing."; RL Biochemistry 28:7241-7257(1989). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 18-452, GLYCOSYLATION AT ASN-287, RP AND DISULFIDE BONDS. RX PubMed=8036495; DOI=10.1126/science.8036495; RA Divne C., Staahlberg J., Reinikainen T., Ruohonen L., Pettersson G., RA Knowles J.K.C., Teeri T.T., Jones T.A.; RT "The three-dimensional crystal structure of the catalytic core of RT cellobiohydrolase I from Trichoderma reesei."; RL Science 265:524-528(1994). RN [9] RP STRUCTURE BY NMR OF 478-513, AND DISULFIDE BONDS. RX PubMed=9041630; DOI=10.1002/pro.5560060204; RA Mattinen M.L., Kontteli M., Kerovuo J., Linder M., Annila A., Lindeberg G., RA Reinikainen T., Drakenberg T.; RT "Three-dimensional structures of three engineered cellulose-binding domains RT of cellobiohydrolase I from Trichoderma reesei."; RL Protein Sci. 6:294-303(1997). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-452, GLYCOSYLATION AT ASN-287 RP AND ASN-401, AND DISULFIDE BONDS. RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414; RX PubMed=9466911; DOI=10.1006/jmbi.1997.1437; RA Divne C., Staahlberg J., Teeri T.T., Jones T.A.; RT "High-resolution crystal structures reveal how a cellulose chain is bound RT in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei."; RL J. Mol. Biol. 275:309-325(1998). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 18-451, GLYCOSYLATION AT ASN-287 RP AND ASN-401, DISULFIDE BONDS, ACTIVE SITE, AND REACTION MECHANISM. RX PubMed=24341799; DOI=10.1021/ja410291u; RA Knott B.C., Haddad Momeni M., Crowley M.F., Mackenzie L.F., Gotz A.W., RA Sandgren M., Withers S.G., Stahlberg J., Beckham G.T.; RT "The mechanism of cellulose hydrolysis by a two-step, retaining RT cellobiohydrolase elucidated by structural and transition path sampling RT studies."; RL J. Am. Chem. Soc. 136:321-329(2014). RN [12] RP STRUCTURE BY NMR OF 478-513, GLYCOSYLATION AT THR-478; SER-480 AND SER-491, RP AND DISULFIDE BONDS. RX PubMed=26307003; DOI=10.1111/febs.13500; RA Happs R.M., Guan X., Resch M.G., Davis M.F., Beckham G.T., Tan Z., RA Crowley M.F.; RT "O-glycosylation effects on family 1 carbohydrate-binding module solution RT structures."; RL FEBS J. 282:4341-4356(2015). CC -!- FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of CC 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide CC cellobiose (Ref.4). The degradation of cellulose involves an interplay CC between different cellulolytic enzymes. Hydrolysis starts with CC endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in CC cellulose to reduce the polymerization degree of the substrate and CC create new chain ends for exocellobiohydrolases (CBHs). The CBHs CC release the disaccharide cellobiose from the non-reducing end of the CC cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the CC cellobiose and other short cello-oligosaccharides into glucose units CC (Probable). {ECO:0000269|Ref.4, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose CC and cellotetraose, releasing cellobiose from the non-reducing ends of CC the chains.; EC=3.2.1.91; Evidence={ECO:0000269|Ref.4}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.4}. CC -!- DOMAIN: The enzyme consists of two functional domains, a catalytic core CC joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, CC and proline-rich, highly glycosylated linker sequence. CC {ECO:0000305|PubMed:26307003, ECO:0000305|PubMed:9746354}. CC -!- PTM: N-glycosylated. The catalytic core domain comprises three N-linked CC glycans which each consist of a single N-acetylglucosamine residue. CC {ECO:0000269|PubMed:9746354}. CC -!- PTM: O-glycosylated. Within the linker domain, all 8 threonines are CC variably glycosylated with between at least one, and up to three, CC mannose residues per site. All serines in this domain are at least CC partially glycosylated with a single mannose residue (PubMed:9746354). CC O-glycosylation of the cellulase linker provides protection from CC proteolysis. Linker glycans also contribute to binding affinity of CC cellobiohydrolases to cellulose (Probable). CC {ECO:0000269|PubMed:9746354, ECO:0000305|PubMed:26307003}. CC -!- MISCELLANEOUS: T.reesei produces two different exocellobiohydrolases. CC They are unique in that they can hydrolyze crystalline cellulose in the CC absence of endoglucanases. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) 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 PIR; A00902; EUTQI. DR PDB; 1AZ6; NMR; -; A=478-513. DR PDB; 1AZH; NMR; -; A=478-513. DR PDB; 1AZJ; NMR; -; A=478-513. DR PDB; 1AZK; NMR; -; A=478-513. DR PDB; 1CBH; NMR; -; A=478-513. DR PDB; 1CEL; X-ray; 1.80 A; A/B=19-451. DR PDB; 1DY4; X-ray; 1.90 A; A=19-451. DR PDB; 1EGN; X-ray; 1.60 A; A=18-451. DR PDB; 1Q2B; X-ray; 1.60 A; A=18-451. DR PDB; 1Q2E; X-ray; 1.75 A; A/B=19-451. DR PDB; 2CBH; NMR; -; A=478-513. DR PDB; 2CEL; X-ray; 2.00 A; A/B=19-451. DR PDB; 2MWJ; NMR; -; A=478-513. DR PDB; 2MWK; NMR; -; A=478-513. DR PDB; 2V3I; X-ray; 1.05 A; A=19-451. DR PDB; 2V3R; X-ray; 1.60 A; A=19-451. DR PDB; 3CEL; X-ray; 2.00 A; A=19-451. DR PDB; 4C4C; X-ray; 1.45 A; A=19-451. DR PDB; 4C4D; X-ray; 1.32 A; A=19-451. DR PDB; 4CEL; X-ray; 2.20 A; A/B=19-451. DR PDB; 4D5I; X-ray; 1.42 A; A=19-451. DR PDB; 4D5J; X-ray; 1.50 A; A=19-451. DR PDB; 4D5O; X-ray; 1.52 A; A=19-451. DR PDB; 4D5P; X-ray; 1.89 A; A=19-451. DR PDB; 4D5Q; X-ray; 1.68 A; A=19-451. DR PDB; 4D5V; X-ray; 1.62 A; A=19-451. DR PDB; 4P1H; X-ray; 1.50 A; A=19-449. DR PDB; 4P1J; X-ray; 2.62 A; A=19-451. DR PDB; 4UWT; X-ray; 1.20 A; A=19-451. DR PDB; 4V0Z; X-ray; 1.70 A; A=19-451. DR PDB; 5CEL; X-ray; 1.90 A; A=19-451. DR PDB; 5OA5; X-ray; 2.10 A; A/B=18-451. DR PDB; 5X34; NMR; -; A=478-513. DR PDB; 5X35; NMR; -; A=478-513. DR PDB; 5X36; NMR; -; A=478-513. DR PDB; 5X37; NMR; -; A=478-513. DR PDB; 5X38; NMR; -; A=478-513. DR PDB; 5X39; NMR; -; A=478-513. DR PDB; 5X3C; NMR; -; A=478-513. DR PDB; 6CEL; X-ray; 1.70 A; A=19-451. DR PDB; 6GRN; X-ray; 1.79 A; A=18-451. DR PDB; 7CEL; X-ray; 1.90 A; A=19-451. DR PDB; 7NYT; X-ray; 1.09 A; A=18-451. DR PDB; 7OC8; X-ray; 1.60 A; A=18-451. DR PDB; 7YHF; NMR; -; A=478-513. DR PDB; 7YHG; NMR; -; A=478-513. DR PDB; 7YHH; NMR; -; A=478-513. DR PDB; 7YHI; NMR; -; A=478-513. DR PDBsum; 1AZ6; -. DR PDBsum; 1AZH; -. DR PDBsum; 1AZJ; -. DR PDBsum; 1AZK; -. DR PDBsum; 1CBH; -. DR PDBsum; 1CEL; -. DR PDBsum; 1DY4; -. DR PDBsum; 1EGN; -. DR PDBsum; 1Q2B; -. DR PDBsum; 1Q2E; -. DR PDBsum; 2CBH; -. DR PDBsum; 2CEL; -. DR PDBsum; 2MWJ; -. DR PDBsum; 2MWK; -. DR PDBsum; 2V3I; -. DR PDBsum; 2V3R; -. DR PDBsum; 3CEL; -. DR PDBsum; 4C4C; -. DR PDBsum; 4C4D; -. DR PDBsum; 4CEL; -. DR PDBsum; 4D5I; -. DR PDBsum; 4D5J; -. DR PDBsum; 4D5O; -. DR PDBsum; 4D5P; -. DR PDBsum; 4D5Q; -. DR PDBsum; 4D5V; -. DR PDBsum; 4P1H; -. DR PDBsum; 4P1J; -. DR PDBsum; 4UWT; -. DR PDBsum; 4V0Z; -. DR PDBsum; 5CEL; -. DR PDBsum; 5OA5; -. DR PDBsum; 5X34; -. DR PDBsum; 5X35; -. DR PDBsum; 5X36; -. DR PDBsum; 5X37; -. DR PDBsum; 5X38; -. DR PDBsum; 5X39; -. DR PDBsum; 5X3C; -. DR PDBsum; 6CEL; -. DR PDBsum; 6GRN; -. DR PDBsum; 7CEL; -. DR PDBsum; 7NYT; -. DR PDBsum; 7OC8; -. DR PDBsum; 7YHF; -. DR PDBsum; 7YHG; -. DR PDBsum; 7YHH; -. DR PDBsum; 7YHI; -. DR AlphaFoldDB; P62694; -. DR BMRB; P62694; -. DR SMR; P62694; -. DR CAZy; CBM1; Carbohydrate-Binding Module Family 1. DR CAZy; GH7; Glycoside Hydrolase Family 7. DR CLAE; CBH7A_TRIRE; -. DR GlyCosmos; P62694; 15 sites, No reported glycans. DR iPTMnet; P62694; -. DR BioCyc; MetaCyc:MONOMER-16499; -. DR BRENDA; 3.2.1.176; 6451. DR BRENDA; 3.2.1.4; 6451. DR BRENDA; 3.2.1.91; 6451. DR EvolutionaryTrace; P62694; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC. DR GO; GO:0030248; F:cellulose binding; IEA:InterPro. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR CDD; cd07999; GH7_CBH_EG; 1. DR Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1. DR InterPro; IPR035971; CBD_sf. DR InterPro; IPR000254; Cellulose-bd_dom_fun. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001722; Glyco_hydro_7. DR InterPro; IPR037019; Glyco_hydro_7_sf. DR PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1. DR PANTHER; PTHR33753:SF2; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1. DR Pfam; PF00734; CBM_1; 1. DR Pfam; PF00840; Glyco_hydro_7; 1. DR PRINTS; PR00734; GLHYDRLASE7. DR SMART; SM00236; fCBD; 1. DR SUPFAM; SSF57180; Cellulose-binding domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00562; CBM1_1; 1. DR PROSITE; PS51164; CBM1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid; KW Secreted; Signal. FT SIGNAL 1..17 FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4" FT CHAIN 18..513 FT /note="Exoglucanase 1" FT /id="PRO_0000007927" FT DOMAIN 477..513 FT /note="CBM1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597" FT REGION 18..453 FT /note="Catalytic" FT /evidence="ECO:0000305|PubMed:8036495" FT REGION 401..480 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 454..477 FT /note="Linker" FT /evidence="ECO:0000305" FT ACT_SITE 229 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000305|PubMed:8036495" FT ACT_SITE 234 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000305|PubMed:8036495" FT SITE 81 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:9746354" FT MOD_RES 18 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4, FT ECO:0007744|PDB:1EGN, ECO:0007744|PDB:1Q2B, FT ECO:0007744|PDB:1Q2E" FT CARBOHYD 62 FT /note="N-linked (GlcNAc) asparagine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 287 FT /note="N-linked (GlcNAc) asparagine" FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911, FT ECO:0000269|PubMed:9746354" FT CARBOHYD 401 FT /note="N-linked (GlcNAc) asparagine" FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:9466911, ECO:0000269|PubMed:9746354" FT CARBOHYD 461 FT /note="O-linked (Man) threonine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 462 FT /note="O-linked (Man...) threonine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 463 FT /note="O-linked (Man...) threonine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 464 FT /note="O-linked (Man...) threonine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 469 FT /note="O-linked (Man) threonine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 470 FT /note="O-linked (Man...) threonine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 471 FT /note="O-linked (Man...) threonine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 473 FT /note="O-linked (Man) serine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 474 FT /note="O-linked (Man) serine" FT /evidence="ECO:0000269|PubMed:9746354" FT CARBOHYD 478 FT /note="O-linked (Man) threonine" FT /evidence="ECO:0000269|PubMed:26307003, FT ECO:0000269|PubMed:9746354" FT CARBOHYD 480 FT /note="O-linked (Man) serine" FT /evidence="ECO:0000269|PubMed:26307003, FT ECO:0000269|PubMed:9746354" FT CARBOHYD 491 FT /note="O-linked (Man) serine" FT /evidence="ECO:0000269|PubMed:26307003" FT DISULFID 21..89 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 36..42 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 67..88 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 78..84 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 155..414 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 189..227 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 193..226 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 247..273 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 255..260 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 278..348 FT /evidence="ECO:0000269|PubMed:24341799, FT ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911" FT DISULFID 485..502 FT /evidence="ECO:0000269|PubMed:2554967, FT ECO:0000269|PubMed:26307003, ECO:0000269|PubMed:9041630" FT DISULFID 496..512 FT /evidence="ECO:0000269|PubMed:2554967, FT ECO:0000269|PubMed:26307003, ECO:0000269|PubMed:9041630" FT CONFLICT 459 FT /note="R -> PP (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:4P1J" FT STRAND 30..36 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 42..51 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:2V3I" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 81..87 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 95..99 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 107..121 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 123..130 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:7NYT" FT STRAND 142..149 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:2V3I" FT TURN 168..174 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:4P1J" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 229..235 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 257..260 FT /evidence="ECO:0007829|PDB:2V3I" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:1Q2B" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:7NYT" FT STRAND 268..273 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:5OA5" FT TURN 282..286 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 297..300 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 305..311 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 317..323 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 338..343 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 345..355 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 359..362 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 365..374 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 375..385 FT /evidence="ECO:0007829|PDB:2V3I" FT TURN 387..391 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 392..395 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 396..399 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:2V3I" FT HELIX 421..427 FT /evidence="ECO:0007829|PDB:2V3I" FT STRAND 432..442 FT /evidence="ECO:0007829|PDB:2V3I" FT TURN 479..482 FT /evidence="ECO:0007829|PDB:1AZH" FT STRAND 483..489 FT /evidence="ECO:0007829|PDB:1AZJ" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:1AZ6" FT STRAND 502..506 FT /evidence="ECO:0007829|PDB:1AZ6" FT STRAND 509..512 FT /evidence="ECO:0007829|PDB:1AZ6" SQ SEQUENCE 513 AA; 54073 MW; 9F5C0A8A854F2C12 CRC64; MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSGNSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT NETSSTPGAV RGSCSTSSGV PAQVESQSPN AKVTFSNIKF GPIGSTGNPS GGNPPGGNRG TTTTRRPATT TGSSPGPTQS HYGQCGGIGY SGPTVCASGT TCQVLNPYYS QCL //