SBT3_SOLLC
ID SBT3_SOLLC Reviewed; 761 AA.
AC O82777;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Subtilisin-like protease SBT3 {ECO:0000303|PubMed:27259555};
DE EC=3.4.21.- {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19407393, ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27259555, ECO:0000269|PubMed:27451395};
DE AltName: Full=LeSBT3 {ECO:0000303|PubMed:10350089};
DE AltName: Full=SlSBT3 {ECO:0000303|PubMed:19332543};
DE AltName: Full=Subtilase 3 {ECO:0000303|PubMed:19332543, ECO:0000303|PubMed:19805099, ECO:0000303|PubMed:27451395};
DE Flags: Precursor;
GN Name=sbt3 {ECO:0000312|EMBL:CAA07001.1};
GN OrderedLocusNames=Solyc01g087850 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|EMBL:CAA07001.1};
RN [1] {ECO:0000312|EMBL:CAA06997.1, ECO:0000312|EMBL:CAA07001.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=VFW8 {ECO:0000303|PubMed:10350089};
RC TISSUE=Leaf {ECO:0000303|PubMed:10350089};
RX PubMed=10350089; DOI=10.1023/a:1006193414434;
RA Meichtry J., Amrhein N., Schaller A.;
RT "Characterization of the subtilase gene family in tomato (Lycopersicon
RT esculentum Mill.).";
RL Plant Mol. Biol. 39:749-760(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP PROTEIN SEQUENCE OF 113-141; 142-165; 168-183; 184-193; 194-210; 211-242;
RP 248-365; 370-377; 419-487; 492-499; 553-604; 676-696; 697-701; 711-732;
RP 733-749 AND 750-761, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, REGION, GLYCOSYLATION AT
RP ASN-177; ASN-203; ASN-376; ASN-697 AND ASN-745, AND MUTAGENESIS OF
RP 363-PRO--VAL-456 AND SER-538.
RX PubMed=19332543; DOI=10.1074/jbc.m900370200;
RA Cedzich A., Huttenlocher F., Kuhn B.M., Pfannstiel J., Gabler L.,
RA Stintzi A., Schaller A.;
RT "The protease-associated domain and C-terminal extension are required for
RT zymogen processing, sorting within the secretory pathway, and activity of
RT tomato subtilase 3 (SlSBT3).";
RL J. Biol. Chem. 284:14068-14078(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND CRYSTALLIZATION.
RX PubMed=19407393; DOI=10.1107/s1744309109013979;
RA Rose R., Huttenlocher F., Cedzich A., Kaiser M., Schaller A., Ottmann C.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of a plant subtilase.";
RL Acta Crystallogr. F 65:522-525(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, CIRCULAR DICHROISM ANALYSIS, SUBCELLULAR LOCATION, DOMAIN, PTM,
RP SITE, AND MUTAGENESIS OF 23-GLN--HIS-112 AND 57-SER--LYS-70.
RX PubMed=27451395; DOI=10.1074/jbc.m116.744151;
RA Meyer M., Leptihn S., Welz M., Schaller A.;
RT "Functional Characterization of Propeptides in Plant Subtilases as
RT Intramolecular Chaperones and Inhibitors of the Mature Protease.";
RL J. Biol. Chem. 291:19449-19461(2016).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27259555; DOI=10.1093/jxb/erw220;
RA Meyer M., Huttenlocher F., Cedzich A., Procopio S., Stroeder J.,
RA Pau-Roblot C., Lequart-Pillon M., Pelloux J., Stintzi A., Schaller A.;
RT "The subtilisin-like protease SBT3 contributes to insect resistance in
RT tomato.";
RL J. Exp. Bot. 67:4325-4338(2016).
RN [7] {ECO:0007744|PDB:3I6S, ECO:0007744|PDB:3I74}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 113-761 AND IN COMPLEX WITH
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN,
RP BIOTECHNOLOGY, ACTIVE SITE, GLYCOSYLATION AT ASN-177; ASN-203 AND ASN-376,
RP DISULFIDE BONDS, AND MUTAGENESIS OF ARG-365; PHE-367 AND ARG-418.
RX PubMed=19805099; DOI=10.1073/pnas.0907587106;
RA Ottmann C., Rose R., Huttenlocher F., Cedzich A., Hauske P., Kaiser M.,
RA Huber R., Schaller A.;
RT "Structural basis for Ca2+-independence and activation by homodimerization
RT of tomato subtilase 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17223-17228(2009).
CC -!- FUNCTION: Serine protease (PubMed:19332543, PubMed:19407393,
CC PubMed:19805099, PubMed:27451395, PubMed:27259555). Has preference for
CC Gln in the P1 position and Lys in the P2 position of oligopeptide
CC substrates. Active also with His in the P1 position (PubMed:19332543).
CC Involved in resistance against insects partly by regulating expression
CC of systemic wound response genes and possibly by its post-ingestive
CC activity in the insect gut. Apart from the role in defense, may be
CC involved in regulation of pectin methylesterases (PMEs) activity and
CC pectin methylesterification of the cell wall (PubMed:27259555).
CC {ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19407393,
CC ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27259555,
CC ECO:0000269|PubMed:27451395}.
CC -!- ACTIVITY REGULATION: Inhibited by 1 mM 4-(2-aminoethyl)-benzenesulfonyl
CC fluoride (AEBSF), a general inhibitor of serine proteinases, but not by
CC the more selective serine protease inhibitors N-alpha-tosyl-L-lysinyl-
CC chloromethylketone (TLCK), N-tosyl-L-phenylalaninyl-chloromethylketone
CC (TPCK), leupeptin, aprotinin or benzamidine (PubMed:19332543). Its
CC proteolytic activity is autoinhibited by the non-covalent binding of
CC the propeptide to the catalytic domain (PubMed:27451395). No effect on
CC activity by the addition of CaCl(2) or calcium chelators
CC (PubMed:19805099). {ECO:0000269|PubMed:19332543,
CC ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32.8 uM for aminobenzoyl-SKRDPPKMQTDLY(NO2) derived from the plant
CC peptide hormone systemin (at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:19332543};
CC Vmax=0.151 nmol/min/mg enzyme with aminobenzoyl-SKRDPPKMQTDLY(NO2)
CC derived from the plant peptide hormone systemin as substrate (at pH
CC 8.0 and 25 degrees Celsius) {ECO:0000269|PubMed:19332543};
CC pH dependence:
CC Optimum pH is 7.5-8.0. 60% of the activity is retained at pH 11.0
CC (PubMed:19332543). No autolysis at pH 4.0-9.0 in the presence of 5 mM
CC EDTA or 5 mM CaCl(2) (PubMed:19805099). {ECO:0000269|PubMed:19332543,
CC ECO:0000269|PubMed:19805099};
CC Temperature dependence:
CC Thermostable (PubMed:19332543, PubMed:27451395, PubMed:19805099).
CC Activity is unaffected by heating to 60 degrees Celsius and only
CC partially reduced after incubation at 70 degrees Celsius
CC (PubMed:19332543). {ECO:0000269|PubMed:19332543,
CC ECO:0000269|PubMed:19805099, ECO:0000269|PubMed:27451395};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19805099}.
CC -!- INTERACTION:
CC O82777; O82777: sbt3; NbExp=3; IntAct=EBI-15805051, EBI-15805051;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19332543,
CC ECO:0000269|PubMed:19407393, ECO:0000269|PubMed:19805099,
CC ECO:0000269|PubMed:27451395}. Note=Autocatalytic cleavage is required
CC for the secretion of the mature protein. {ECO:0000269|PubMed:19332543}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, cotyledons and leaves with
CC the highest expression in roots. {ECO:0000269|PubMed:10350089}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early seedling development in the
CC micropylar endosperm as well as in the developing root. Also expressed
CC in the mature root system, particularly at the junction between primary
CC and lateral roots. Expressed in the shoot vasculature in both external
CC and internal phloem including sieve elements and companion cells, and
CC also in the vascular (xylem and phloem) parenchyma in 3-week old
CC plants. {ECO:0000269|PubMed:27259555}.
CC -!- INDUCTION: Expressed in response to mechanical wounding and insect
CC herbivory in leaves. Not expressed in uninjured leaves.
CC {ECO:0000269|PubMed:27259555}.
CC -!- DOMAIN: The mature polypeptide has three domains: The catalytic domain,
CC an interposed protease-associated (PA) domain required for
CC homodimerization and a C-terminal seven-stranded jelly-roll fibronectin
CC (Fn) III-like domain. {ECO:0000305|PubMed:19805099}.
CC -!- DOMAIN: The propeptide is required as an intramolecular chaperone for
CC zymogen maturation and secretion. {ECO:0000305|PubMed:27451395}.
CC -!- PTM: Propeptide is internally cleaved at Asn-38 and Asp-52 in a pH-
CC dependent manner leading to the dissociation of the propeptide from the
CC catalytic domain and resulting in the release of the active subtilase.
CC Cleavage occurs at pH 5.7 and to a stronger extent at pH 5.2.
CC {ECO:0000269|PubMed:27451395}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in partial loss
CC of resistance against M.sexta larvae, impaired systemic induction of
CC late wound response genes and in reduced levels of cell wall
CC homogalacturonan (HG) and pectin methylesterification (DM).
CC {ECO:0000269|PubMed:27259555}.
CC -!- BIOTECHNOLOGY: Has the potential to be used as an additive in laundry
CC and dishwashing detergents, because it is a calcium-free thermostable
CC subtilase alternative. {ECO:0000305|PubMed:19805099}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AJ006376; CAA06997.1; -; mRNA.
DR EMBL; AJ006380; CAA07001.1; -; Genomic_DNA.
DR PIR; T07169; T07169.
DR RefSeq; NP_001234774.1; NM_001247845.1.
DR PDB; 3I6S; X-ray; 2.50 A; A/B=113-761.
DR PDB; 3I74; X-ray; 2.60 A; A/B=113-761.
DR PDBsum; 3I6S; -.
DR PDBsum; 3I74; -.
DR AlphaFoldDB; O82777; -.
DR SMR; O82777; -.
DR DIP; DIP-48980N; -.
DR STRING; 4081.Solyc01g087850.2.1; -.
DR MEROPS; S08.151; -.
DR iPTMnet; O82777; -.
DR PaxDb; O82777; -.
DR PRIDE; O82777; -.
DR EnsemblPlants; Solyc01g087850.2.1; Solyc01g087850.2.1.1; Solyc01g087850.2.
DR GeneID; 543726; -.
DR Gramene; Solyc01g087850.2.1; Solyc01g087850.2.1.1; Solyc01g087850.2.
DR KEGG; sly:543726; -.
DR eggNOG; ENOG502QT5U; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; O82777; -.
DR OMA; QLSTDYI; -.
DR OrthoDB; 337164at2759; -.
DR PhylomeDB; O82777; -.
DR SABIO-RK; O82777; -.
DR EvolutionaryTrace; O82777; -.
DR Proteomes; UP000004994; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR GO; GO:0009827; P:plant-type cell wall modification; IMP:UniProtKB.
DR GO; GO:1900367; P:positive regulation of defense response to insect; IEP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:1902066; P:regulation of cell wall pectin metabolic process; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; IMP:UniProtKB.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PTHR10795; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Plant defense; Protease; Reference proteome; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..112
FT /evidence="ECO:0000255, ECO:0000305|PubMed:19332543"
FT /id="PRO_0000446634"
FT CHAIN 113..761
FT /note="Subtilisin-like protease SBT3"
FT /evidence="ECO:0000305|PubMed:19332543"
FT /id="PRO_5015096818"
FT DOMAIN 26..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 116..606
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 574..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..761
FT /note="Necessary for prodomain cleavage and secretion"
FT /evidence="ECO:0000269|PubMed:19332543"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:19805099"
FT ACT_SITE 538
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099"
FT SITE 38..39
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:27451395"
FT SITE 52..53
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:27451395"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT partial"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:19332543"
FT DISULFID 170..181
FT /evidence="ECO:0000269|PubMed:19805099,
FT ECO:0007744|PDB:3I6S, ECO:0007744|PDB:3I74"
FT DISULFID 382..401
FT /evidence="ECO:0000269|PubMed:19805099,
FT ECO:0007744|PDB:3I6S, ECO:0007744|PDB:3I74"
FT DISULFID 624..645
FT /evidence="ECO:0000269|PubMed:19805099,
FT ECO:0007744|PDB:3I6S, ECO:0007744|PDB:3I74"
FT MUTAGEN 23..112
FT /note="Missing: Not secreted."
FT /evidence="ECO:0000269|PubMed:27451395"
FT MUTAGEN 57..70
FT /note="Missing: Weakly decreased autoinhibition. Loss of
FT ability to act as a chaperone."
FT /evidence="ECO:0000269|PubMed:27451395"
FT MUTAGEN 363..456
FT /note="Missing: Accumulates intracellularly as an
FT unprocessed zymogen."
FT /evidence="ECO:0000269|PubMed:19332543"
FT MUTAGEN 365
FT /note="R->A: Decreased catalytic activity and dimerization
FT ability; when associated with A-418."
FT /evidence="ECO:0000269|PubMed:19805099"
FT MUTAGEN 367
FT /note="F->A: Decreased catalytic activity and dimerization
FT ability; when associated with A-418."
FT /evidence="ECO:0000269|PubMed:19805099"
FT MUTAGEN 418
FT /note="R->A: Decreased catalytic activity and dimerization
FT ability; when associated with A-367 or A-365."
FT /evidence="ECO:0000269|PubMed:19805099"
FT MUTAGEN 538
FT /note="S->A: Loss of catalytic activity. Accumulates
FT intracellularly as an unprocessed zymogen. No cleavage of
FT the prodomain by the wild-type SBT3 indicating that the
FT zymogen maturation is an intramolecular autocatalytic
FT process. Sensitive to endoglycosidases Endo H and PNGase F
FT in contrast to the wild-type which is resistant to both."
FT /evidence="ECO:0000269|PubMed:19332543"
FT MUTAGEN 538
FT /note="S->C: Loss of catalytic activity. Accumulates
FT intracellularly as an unprocessed zymogen. Sensitive to
FT endoglycosidases Endo H and PNGase F in contrast to the
FT wild-type which is resistant to both."
FT /evidence="ECO:0000269|PubMed:19332543"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:3I6S"
FT TURN 377..381
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 463..472
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3I6S"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 537..554
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 560..569
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:3I6S"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 616..624
FT /evidence="ECO:0007829|PDB:3I6S"
FT HELIX 630..637
FT /evidence="ECO:0007829|PDB:3I6S"
FT TURN 638..640
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 670..680
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 686..693
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 698..709
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 715..724
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:3I6S"
FT STRAND 747..756
FT /evidence="ECO:0007829|PDB:3I6S"
SQ SEQUENCE 761 AA; 82226 MW; 642A3378A2914683 CRC64;
MELLHLLLFS WALSAHLFLA LAQRSTYIVH LDKSLMPNVF TDHHHWHSST IDSIKASVPS
SVDRFHSAPK LVYSYDNVLH GFSAVLSKDE LAALKKLPGF ISAYKDRTVE PHTTHTSDFL
KLNPSSGLWP ASGLGQDVIV AVLDSGIWPE SASFQDDGMP EIPKRWKGIC KPGTQFNASM
CNRKLIGANY FNKGILANDP TVNITMNSAR DTDGHGTHCA SITAGNFAKG VSHFGYAPGT
ARGVAPRARL AVYKFSFNEG TFTSDLIAAM DQAVADGVDM ISISYGYRFI PLYEDAISIA
SFGAMMKGVL VSASAGNRGP GIGSLNNGSP WILCVASGHT DRTFAGTLTL GNGLKIRGWS
LFPARAFVRD SPVIYNKTLS DCSSEELLSQ VENPENTIVI CDDNGDFSDQ MRIITRARLK
AAIFISEDPG VFRSATFPNP GVVVNKKEGK QVINYVKNSV TPTATITFQE TYLDTKPAPV
VAASSARGPS RSYLGISKPD ILAPGVLILA AYPPNVFATS IGTNILLSTD YILESGTSMA
APHAAGIAAM LKAAHPEWSP SAIRSAMMTT ADPLDNTRKP IKDSDNNKAA TPLDMGAGHV
DPNRALDPGL VYDATPQDYV NLLCSLNFTE EQFKTIARSS ASHNCSNPSA DLNYPSFIAL
YSIEGNFTLL EQKFKRTVTN VGKGAATYKA KLKAPKNSTI SVSPQILVFK NKNEKQSYTL
TIRYIGDEGQ SRNVGSITWV EQNGNHSVRS PIVTSPIIEV W
