GUX1_HYPJE
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 03-AUG-2022, entry version 105.
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}.
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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 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 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 iPTMnet; P62694; -.
DR BioCyc; MetaCyc:MON-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; -; 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; PTHR33753; 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; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 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:4UWT"
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:4C4D"
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
