SOT18_ARATH
ID SOT18_ARATH Reviewed; 350 AA.
AC Q9C9C9; Q8LA18;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytosolic sulfotransferase 18;
DE Short=AtSOT18;
DE EC=2.8.2.38 {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
DE AltName: Full=Desulfo-glucosinolate sulfotransferase B;
DE AltName: Full=Sulfotransferase 5B;
DE Short=AtST5b;
GN Name=SOT18; Synonyms=ST5B; OrderedLocusNames=At1g74090; ORFNames=F2P9.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=15358770; DOI=10.1074/jbc.m407681200;
RA Piotrowski M., Schemenewitz A., Lopukhina A., Mueller A., Janowitz T.,
RA Weiler E.W., Oecking C.;
RT "Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze
RT the final step in the biosynthesis of the glucosinolate core structure.";
RL J. Biol. Chem. 279:50717-50725(2004).
RN [7]
RP GENE FAMILY, SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX PubMed=15234990; DOI=10.1093/jxb/erh183;
RA Klein M., Papenbrock J.;
RT "The multi-protein family of Arabidopsis sulphotransferases and their
RT relatives in other plant species.";
RL J. Exp. Bot. 55:1809-1820(2004).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=15866872; DOI=10.1074/jbc.m502332200;
RA Hirai M.Y., Klein M., Fujikawa Y., Yano M., Goodenowe D.B., Yamazaki Y.,
RA Kanaya S., Nakamura Y., Kitayama M., Suzuki H., Sakurai N., Shibata D.,
RA Tokuhisa J., Reichelt M., Gershenzon J., Papenbrock J., Saito K.;
RT "Elucidation of gene-to-gene and metabolite-to-gene networks in Arabidopsis
RT by integration of metabolomics and transcriptomics.";
RL J. Biol. Chem. 280:25590-25595(2005).
RN [9]
RP MUTAGENESIS OF ASP-301, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND VARIANTS GLY-301 AND ASN-339.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=16367753; DOI=10.1111/j.1742-4658.2005.05048.x;
RA Klein M., Reichelt M., Gershenzon J., Papenbrock J.;
RT "The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis
RT have different substrate specificities and are differentially expressed.";
RL FEBS J. 273:122-136(2006).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=19077143; DOI=10.1111/j.1399-3054.2008.01182.x;
RA Klein M., Papenbrock J.;
RT "Kinetics and substrate specificities of desulfo-glucosinolate
RT sulfotransferases in Arabidopsis thaliana.";
RL Physiol. Plantarum 135:140-149(2009).
RN [11]
RP FUNCTION.
RX PubMed=21281472; DOI=10.1186/1472-6750-11-12;
RA Moeldrup M.E., Geu-Flores F., Olsen C.E., Halkier B.A.;
RT "Modulation of sulfur metabolism enables efficient glucosinolate
RT engineering.";
RL BMC Biotechnol. 11:12-12(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of
CC the glucosinolate core structure. Preferred substrate are the long-
CC chain desulfo-glucosinolates, 7-methylthioheptyl and 8-methylthiooctyl,
CC derived from methionine. Substrate preference is desulfo-benzyl
CC glucosinolate > desulfo-4-methylthiobutyl glucosinolate > desulfo-6-
CC methylthiohexyl glucosinolate > desulfo-3-methylthiopropyl
CC glucosinolate > desulfo-indol-3-yl methyl glucosinolate > desulfo-
CC singrin > desulfo-3-butenyl glucosinolate.
CC {ECO:0000269|PubMed:15358770, ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143,
CC ECO:0000269|PubMed:21281472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + an aliphatic (Z)-desulfo-
CC glucosinolate = a (Z)-omega-(methylsulfanyl)-N-sulfo-alkylhydroximate
CC S-glucoside + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52724, Rhea:RHEA-COMP:13191, Rhea:RHEA-COMP:13194,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:136425, ChEBI:CHEBI:136434; EC=2.8.2.38;
CC Evidence={ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC -!- ACTIVITY REGULATION: Inhibited by phosphoadenosine 5'-phosphate (PAP).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for desulfobenzyl glucosinolate (in cv. Columbia)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC KM=35 uM for 3'-phospho-5'-adenylyl sulfate (in cv. C24)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC KM=60 uM for 3'-phospho-5'-adenylyl sulfate (in cv. Columbia)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC KM=100 uM for desulfo-3-methylthiopropyl glucosinolate (in cv. C24)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC KM=55 uM for desulfo-3-methylthiopropyl glucosinolate (in cv.
CC Columbia) {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC KM=130 uM for desulfo-4-methylthiobutyl glucosinolate (in cv. C24)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC KM=43 uM for desulfo-4-methylthiobutyl glucosinolate (in cv.
CC Columbia) {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC Vmax=171 pmol/sec/mg enzyme with desulfo-benzyl glucosinolate as
CC substrate (in cv. C24) {ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=851 pmol/sec/mg enzyme with desulfo-benzyl glucosinolate as
CC substrate (in cv. Columbia) {ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=467 pmol/sec/mg enzyme with desulfo-allyl glucosinolate as
CC substrate (in cv. Columbia) {ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=27 pmol/sec/mg enzyme with 3'-phosphoadenosine 5'-phosphosulfate
CC as substrate (in cv. C24) {ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=860 pmol/sec/mg enzyme with 3'-phosphoadenosine 5'-
CC phosphosulfate as substrate (in cv. Columbia)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC Vmax=99 pmol/sec/mg enzyme with desulfo-3-methylthiopropyl
CC glucosinolate as substrate (in cv. C24) {ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC Vmax=2763 pmol/sec/mg enzyme with desulfo-3-methylthiopropyl
CC glucosinolate as substrate (in cv. Columbia)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC Vmax=131 pmol/sec/mg enzyme with desulfo-4-
CC methylthiobutylglucosinolate as substrate (in cv. C24)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC Vmax=1883 pmol/sec/mg enzyme with desulfo-4-methylthiobutyl
CC glucosinolate as substrate (in cv. Columbia)
CC {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
CC ECO:0000269|PubMed:19077143};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:15866872,
CC ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15234990,
CC ECO:0000269|PubMed:16367753}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems. Barely
CC detected in siliques and flowers. {ECO:0000269|PubMed:16367753}.
CC -!- DEVELOPMENTAL STAGE: Low expression in young plants (up to 4 weeks),
CC then slight increase in older plants. {ECO:0000269|PubMed:16367753}.
CC -!- INDUCTION: Not induced by coronatine, methyl jasmonate or high sulfate
CC concentration. {ECO:0000269|PubMed:15358770,
CC ECO:0000269|PubMed:16367753}.
CC -!- POLYMORPHISM: In cv. C24, the substrate preference is restricted to a
CC small number of desulfo-gulcosinolates: desulfo-6-methylthiohexyl
CC glucosinolate > desulfo-benzyl glucosinolate > desulfo-2-phenylethyl
CC glucosinolate (PubMed:16367753). {ECO:0000269|PubMed:16367753}.
CC -!- MISCELLANEOUS: Strong differences in the kinetic behavior between the
CC same protein from different cultivars.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AC016662; AAG52515.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35549.1; -; Genomic_DNA.
DR EMBL; BT004984; AAO50517.1; -; mRNA.
DR EMBL; AK117463; BAC42128.1; -; mRNA.
DR EMBL; AY088081; AAM65627.1; -; mRNA.
DR PIR; H96768; H96768.
DR RefSeq; NP_177549.1; NM_106069.3.
DR PDB; 5MEK; X-ray; 1.74 A; A=26-347.
DR PDB; 5MEX; X-ray; 1.92 A; A=26-347.
DR PDBsum; 5MEK; -.
DR PDBsum; 5MEX; -.
DR AlphaFoldDB; Q9C9C9; -.
DR SMR; Q9C9C9; -.
DR STRING; 3702.AT1G74090.1; -.
DR iPTMnet; Q9C9C9; -.
DR MetOSite; Q9C9C9; -.
DR PaxDb; Q9C9C9; -.
DR PRIDE; Q9C9C9; -.
DR ProteomicsDB; 245327; -.
DR EnsemblPlants; AT1G74090.1; AT1G74090.1; AT1G74090.
DR GeneID; 843749; -.
DR Gramene; AT1G74090.1; AT1G74090.1; AT1G74090.
DR KEGG; ath:AT1G74090; -.
DR Araport; AT1G74090; -.
DR TAIR; locus:2031516; AT1G74090.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_0_3_1; -.
DR InParanoid; Q9C9C9; -.
DR OMA; VMTITYE; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q9C9C9; -.
DR BioCyc; MetaCyc:AT1G74090-MON; -.
DR BRENDA; 2.8.2.38; 399.
DR PRO; PR:Q9C9C9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9C9; baseline and differential.
DR Genevisible; Q9C9C9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0080066; F:3-methylthiopropyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0080067; F:4-methylthiobutyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0080068; F:5-methylthiopentyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0080069; F:7-methylthioheptyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0080070; F:8-methylthiooctyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0047364; F:desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0080071; F:indol-3-yl-methyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:TAIR.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..350
FT /note="Cytosolic sulfotransferase 18"
FT /id="PRO_0000315847"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 93..98
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 313..315
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VARIANT 301
FT /note="D -> G (in strain: cv. C24)"
FT /evidence="ECO:0000269|PubMed:16367753"
FT VARIANT 339
FT /note="K -> N (in strain: cv. C24)"
FT /evidence="ECO:0000269|PubMed:16367753"
FT MUTAGEN 301
FT /note="D->G: 25 time reduction of activity with desulfo-
FT benzyl glucosinolate as substrate."
FT /evidence="ECO:0000269|PubMed:16367753"
FT CONFLICT 31
FT /note="E -> K (in Ref. 5; AAM65627)"
FT /evidence="ECO:0000305"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:5MEK"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5MEK"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:5MEK"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5MEK"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:5MEK"
FT HELIX 326..340
FT /evidence="ECO:0007829|PDB:5MEK"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:5MEK"
SQ SEQUENCE 350 AA; 40465 MW; AB68B7477262EB57 CRC64;
MESETLTAKA TITTTTLPSH DETKTESTEF EKNQKRYQDL ISTFPHEKGW RPKEPLIEYG
GYWWLPSLLE GCIHAQEFFQ ARPSDFLVCS YPKTGTTWLK ALTFAIANRS RFDDSSNPLL
KRNPHEFVPY IEIDFPFFPE VDVLKDKGNT LFSTHIPYEL LPDSVVKSGC KMVYIWREPK
DTFISMWTFL HKERTELGPV SNLEESFDMF CRGLSGYGPY LNHILAYWKA YQENPDRILF
LKYETMRADP LPYVKSLAEF MGHGFTAEEE EKGVVEKVVN LCSFETLKNL EANKGEKDRE
DRPGVYANSA YFRKGKVGDW SNYLTPEMAA RIDGLMEEKF KGTGLLEHGK
