HEN1_ARATH
ID HEN1_ARATH Reviewed; 942 AA.
AC Q9C5Q8; O65309; Q945R3; Q9SUC2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Small RNA 2'-O-methyltransferase;
DE EC=2.1.1.n8;
DE AltName: Full=Protein CORYMBOSA 2;
DE AltName: Full=Protein HUA ENHANCER 1;
DE AltName: Full=S-adenosylmethionine-dependent RNA methyltransferase HEN1;
GN Name=HEN1; Synonyms=CRM2; OrderedLocusNames=At4g20910; ORFNames=T13K14.70;
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 [GENOMIC DNA].
RC STRAIN=cv. Wassilewskija;
RX AGRICOLA=IND21977244;
RA Sanders P.M., Bui A.Q., Weterings K., McIntire K.N., Hsu Y.C., Lee P.Y.,
RA Truong M.T., Beals T.B., Goldberg R.B.;
RT "Anther development defects in Arabidopsis thaliana male-sterile mutants.";
RL Sex. Plant Reprod. 11:297-322(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-719.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11874905; DOI=10.1242/dev.129.5.1085;
RA Chen X., Liu J., Cheng Y., Jia D.;
RT "HEN1 functions pleiotropically in Arabidopsis development and acts in C
RT function in the flower.";
RL Development 129:1085-1094(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-68.
RX PubMed=11917084; DOI=10.1093/pcp/pcf036;
RA Suzuki M., Takahashi T., Komeda Y.;
RT "Formation of corymb-like inflorescences due to delay in bolting and flower
RT development in the corymbosa2 mutant of Arabidopsis.";
RL Plant Cell Physiol. 43:298-306(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15024409; DOI=10.1371/journal.pbio.0020104;
RA Xie Z., Johansen L.K., Gustafson A.M., Kasschau K.D., Lellis A.D.,
RA Zilberman D., Jacobsen S.E., Carrington J.C.;
RT "Genetic and functional diversification of small RNA pathways in plants.";
RL PLoS Biol. 2:E104-E104(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16111943; DOI=10.1016/j.cub.2005.07.029;
RA Li J., Yang Z., Yu B., Liu J., Chen X.;
RT "Methylation protects miRNAs and siRNAs from a 3'-end uridylation activity
RT in Arabidopsis.";
RL Curr. Biol. 15:1501-1507(2005).
RN [8]
RP FUNCTION.
RX PubMed=15705854; DOI=10.1126/science.1107130;
RA Yu B., Yang Z., Li J., Minakhina S., Yang M., Padgett R.W., Steward R.,
RA Chen X.;
RT "Methylation as a crucial step in plant microRNA biogenesis.";
RL Science 307:932-935(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE;
RP S-ADENOSYL L-HOMOCYSTEINE AND MAGNESIUM ION, COFACTOR, SUBUNIT, AND
RP MUTAGENESIS OF TYR-109; TRP-333; LEU-604; ARG-701; GLU-796; GLU-799;
RP HIS-800; ARG-856 AND HIS-860.
RX PubMed=19812675; DOI=10.1038/nature08433;
RA Huang Y., Ji L., Huang Q., Vassylyev D.G., Chen X., Ma J.B.;
RT "Structural insights into mechanisms of the small RNA methyltransferase
RT HEN1.";
RL Nature 461:823-827(2009).
CC -!- FUNCTION: Methyltransferase that adds a methyl group to the ribose of
CC the last nucleotide of small RNAs (sRNAs). This protects the 3'-end of
CC sRNAs from uridylation activity and subsequent degradation. Can
CC methylate 3'-end of microRNAs (miRNAs), small interfering RNAs (siRNas)
CC and trans-acting small interfering RNAs (ta-siRNAs). Involved in plant
CC development through its role in small RNAs processing. Required for the
CC specification of reproductive organ identities and the probable
CC repression of A class genes. May control floral determinacy possibly by
CC regulating the expression of the C class floral homeotic gene AGAMOUS
CC (AG). {ECO:0000269|PubMed:11874905, ECO:0000269|PubMed:11917084,
CC ECO:0000269|PubMed:15705854, ECO:0000269|PubMed:16111943}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) +
CC S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide;
CC Xref=Rhea:RHEA:37887, Rhea:RHEA-COMP:10415, Rhea:RHEA-COMP:10416,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:74898; EC=2.1.1.n8;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19812675};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:19812675};
CC -!- SUBUNIT: Binds small RNA duplexes as monomer.
CC {ECO:0000269|PubMed:19812675}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15024409}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves and inflorescences.
CC {ECO:0000269|PubMed:11874905, ECO:0000269|PubMed:11917084}.
CC -!- DISRUPTION PHENOTYPE: Reduced organ size, altered rosette leaf shape
CC and increased number of coflorescences. Urydilation of miRNA 3'-ends.
CC {ECO:0000269|PubMed:11874905, ECO:0000269|PubMed:11917084,
CC ECO:0000269|PubMed:16111943}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45886.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79091.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF060248; AAC97105.1; -; Genomic_DNA.
DR EMBL; AF411383; AAL05056.1; -; mRNA.
DR EMBL; AF327068; AAK16435.1; -; mRNA.
DR EMBL; AL080282; CAB45886.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161553; CAB79091.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84374.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84375.1; -; Genomic_DNA.
DR PIR; T10633; T10633.
DR RefSeq; NP_001190782.1; NM_001203853.2.
DR RefSeq; NP_567616.1; NM_118209.3.
DR PDB; 3HTX; X-ray; 3.10 A; A/D=1-942.
DR PDBsum; 3HTX; -.
DR AlphaFoldDB; Q9C5Q8; -.
DR SMR; Q9C5Q8; -.
DR BioGRID; 13130; 3.
DR STRING; 3702.AT4G20910.2; -.
DR iPTMnet; Q9C5Q8; -.
DR PaxDb; Q9C5Q8; -.
DR PRIDE; Q9C5Q8; -.
DR ProteomicsDB; 230384; -.
DR EnsemblPlants; AT4G20910.1; AT4G20910.1; AT4G20910.
DR EnsemblPlants; AT4G20910.2; AT4G20910.2; AT4G20910.
DR GeneID; 827839; -.
DR Gramene; AT4G20910.1; AT4G20910.1; AT4G20910.
DR Gramene; AT4G20910.2; AT4G20910.2; AT4G20910.
DR KEGG; ath:AT4G20910; -.
DR Araport; AT4G20910; -.
DR TAIR; locus:2133114; AT4G20910.
DR eggNOG; KOG1045; Eukaryota.
DR HOGENOM; CLU_001342_0_0_1; -.
DR OMA; ACYSVEE; -.
DR OrthoDB; 189384at2759; -.
DR PhylomeDB; Q9C5Q8; -.
DR EvolutionaryTrace; Q9C5Q8; -.
DR PRO; PR:Q9C5Q8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9C5Q8; baseline and differential.
DR Genevisible; Q9C5Q8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IDA:TAIR.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0010589; P:leaf proximal/distal pattern formation; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; IMP:TAIR.
DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IMP:TAIR.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR GO; GO:0010093; P:specification of floral organ identity; IMP:TAIR.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR040870; HEN1_dsRBD2.
DR InterPro; IPR040813; Hen1_Lam_C.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF17842; dsRBD2; 1.
DR Pfam; PF18441; Hen1_Lam_C; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..942
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000404658"
FT DOMAIN 19..87
FT /note="DRBM"
FT DOMAIN 93..204
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 505..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 726
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT BINDING 745
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT BINDING 778..779
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT BINDING 795
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT BINDING 796
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT BINDING 799
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT BINDING 800
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT BINDING 860
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19812675,
FT ECO:0007744|PDB:3HTX"
FT MUTAGEN 68
FT /note="Missing: In crm2-1; compact inflorescence with
FT several flower buds at the tip."
FT /evidence="ECO:0000269|PubMed:11917084"
FT MUTAGEN 109
FT /note="Y->A: No effect on RNA binding and transferase
FT activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 333
FT /note="W->A: Loss of RNA binding and transferase activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 604
FT /note="L->P: No effect on transferase activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 701
FT /note="R->A: Reduces transferase activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 719
FT /note="D->N: In hen1-2; alters organ development and floral
FT determinacy."
FT /evidence="ECO:0000269|PubMed:11874905"
FT MUTAGEN 796
FT /note="E->A: Loss of transferase activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 799
FT /note="E->A: Loss of transferase activity; when associated
FT with A-800."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 800
FT /note="H->A: Loss of transferase activity; when associated
FT with A-799."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 800
FT /note="H->Q: Strongly decreases transferase activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 856
FT /note="R->A: Reduces transferase activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT MUTAGEN 860
FT /note="H->A,Q: Loss of transferase activity."
FT /evidence="ECO:0000269|PubMed:19812675"
FT CONFLICT 39
FT /note="L -> P (in Ref. 1; AAC97105 and 2; AAL05056)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="S -> Y (in Ref. 1; AAC97105)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="R -> K (in Ref. 1; AAC97105)"
FT /evidence="ECO:0000305"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 357..365
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 478..494
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 548..551
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 557..569
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 603..615
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 622..628
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 636..643
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 648..654
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 658..664
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 669..681
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 697..711
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 715..720
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 726..731
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 740..746
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 748..761
FT /evidence="ECO:0007829|PDB:3HTX"
FT TURN 762..765
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 770..777
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 791..796
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 798..800
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 803..815
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 820..826
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:3HTX"
FT HELIX 866..879
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 882..891
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 900..909
FT /evidence="ECO:0007829|PDB:3HTX"
FT STRAND 926..931
FT /evidence="ECO:0007829|PDB:3HTX"
SQ SEQUENCE 942 AA; 104454 MW; 7D8B5222C0D28779 CRC64;
MAGGGKHTPT PKAIIHQKFG AKASYTVEEV HDSSQSGCLG LAIPQKGPCL YRCHLQLPEF
SVVSNVFKKK KDSEQSAAEL ALDKLGIRPQ NDDLTVDEAR DEIVGRIKYI FSDEFLSAEH
PLGAHLRAAL RRDGERCGSV PVSVIATVDA KINSRCKIIN PSVESDPFLA ISYVMKAAAK
LADYIVASPH GLRRKNAYPS EIVEALATHV SDSLHSREVA AVYIPCIDEE VVELDTLYIS
SNRHYLDSIA ERLGLKDGNQ VMISRMFGKA SCGSECRLYS EIPKKYLDNS SDASGTSNED
SSHIVKSRNA RASYICGQDI HGDAILASVG YRWKSDDLDY DDVTVNSFYR ICCGMSPNGI
YKISRQAVIA AQLPFAFTTK SNWRGPLPRE ILGLFCHQHR LAEPILSSST APVKSLSDIF
RSHKKLKVSG VDDANENLSR QKEDTPGLGH GFRCEVKIFT KSQDLVLECS PRKFYEKEND
AIQNASLKAL LWFSKFFADL DVDGEQSCDT DDDQDTKSSS PNVFAAPPIL QKEHSSESKN
TNVLSAEKRV QSITNGSVVS ICYSLSLAVD PEYSSDGESP REDNESNEEM ESEYSANCES
SVELIESNEE IEFEVGTGSM NPHIESEVTQ MTVGEYASFR MTPPDAAEAL ILAVGSDTVR
IRSLLSERPC LNYNILLLGV KGPSEERMEA AFFKPPLSKQ RVEYALKHIR ESSASTLVDF
GCGSGSLLDS LLDYPTSLQT IIGVDISPKG LARAAKMLHV KLNKEACNVK SATLYDGSIL
EFDSRLHDVD IGTCLEVIEH MEEDQACEFG EKVLSLFHPK LLIVSTPNYE FNTILQRSTP
ETQEENNSEP QLPKFRNHDH KFEWTREQFN QWASKLGKRH NYSVEFSGVG GSGEVEPGFA
SQIAIFRREA SSVENVAESS MQPYKVIWEW KKEDVEKKKT DL
