METK2_ARATH
ID METK2_ARATH Reviewed; 393 AA.
AC P17562; Q42263;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=S-adenosylmethionine synthase 2;
DE Short=AdoMet synthase 2;
DE EC=2.5.1.6 {ECO:0000269|PubMed:16365035};
DE AltName: Full=Methionine adenosyltransferase 2;
DE Short=MAT 2;
GN Name=SAM2; OrderedLocusNames=At4g01850; ORFNames=T7B11.11;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=2482229; DOI=10.1016/0378-1119(89)90510-6;
RA Peleman J., Saito K., Cottyn B., Engler G., Seurinck J., van Montagu M.,
RA Inze D.;
RT "Structure and expression analyses of the S-adenosylmethionine synthetase
RT gene family in Arabidopsis thaliana.";
RL Gene 84:359-369(1989).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-248 AND 322-393.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [6]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15276459; DOI=10.1016/j.phytochem.2004.03.026;
RA Wienkoop S., Zoeller D., Ebert B., Simon-Rosin U., Fisahn J., Glinski M.,
RA Weckwerth W.;
RT "Cell-specific protein profiling in Arabidopsis thaliana trichomes:
RT identification of trichome-located proteins involved in sulfur metabolism
RT and detoxification.";
RL Phytochemistry 65:1641-1649(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=16365035; DOI=10.1074/jbc.m511635200;
RA Lindermayr C., Saalbach G., Bahnweg G., Durner J.;
RT "Differential inhibition of Arabidopsis methionine adenosyltransferases by
RT protein S-nitrosylation.";
RL J. Biol. Chem. 281:4285-4291(2006).
RN [8]
RP INTERACTION WITH GRF3.
RX PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025;
RA Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.;
RT "14-3-3 proteins fine-tune plant nutrient metabolism.";
RL FEBS Lett. 585:143-147(2011).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. The reaction comprises two steps that are both
CC catalyzed by the same enzyme: formation of S-adenosylmethionine
CC (AdoMet) and triphosphate, and subsequent hydrolysis of the
CC triphosphate. {ECO:0000269|PubMed:16365035}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-
CC adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6;
CC Evidence={ECO:0000269|PubMed:16365035};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:16365035};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Note=Binds 2 divalent ions per subunit. The metal ions interact
CC primarily with the substrate (By similarity). Can utilize magnesium,
CC manganese or cobalt (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P13444, ECO:0000250|UniProtKB:Q96551};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000305|PubMed:16365035};
CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC primarily with the substrate (By similarity).
CC {ECO:0000250|UniProtKB:P13444};
CC -!- ACTIVITY REGULATION: Inhibited by 5,5'-dithiobis-2-nitrobenzoic acid
CC (DTNB) and N-ethylmaleimide (NEM) (in vitro).
CC {ECO:0000269|PubMed:16365035}.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000269|PubMed:16365035}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with GRF3.
CC {ECO:0000250|UniProtKB:Q00266, ECO:0000269|PubMed:21094157}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9LUT2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stems and roots
CC (PubMed:2482229). Detected in trichomes (at the protein level)
CC (PubMed:15276459). {ECO:0000269|PubMed:15276459,
CC ECO:0000269|PubMed:2482229}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {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 EMBL; M33217; AAA32869.1; -; Genomic_DNA.
DR EMBL; AC007138; AAD22647.1; -; Genomic_DNA.
DR EMBL; AL161493; CAB80678.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82084.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82085.1; -; Genomic_DNA.
DR EMBL; AY072327; AAL61934.1; -; mRNA.
DR EMBL; AY094454; AAM19825.1; -; mRNA.
DR EMBL; BT000575; AAN18144.1; -; mRNA.
DR EMBL; Z33778; CAA83930.1; -; mRNA.
DR EMBL; Z29136; CAA82393.1; -; mRNA.
DR PIR; JQ0410; JQ0410.
DR RefSeq; NP_001078345.1; NM_001084876.1.
DR RefSeq; NP_192094.1; NM_116415.4.
DR PDB; 6VCZ; X-ray; 1.52 A; A/B=1-392.
DR PDB; 6VD0; X-ray; 2.00 A; A/B/C/D=1-392.
DR PDB; 6VD1; X-ray; 1.32 A; A/B=1-392.
DR PDB; 6VD2; X-ray; 1.97 A; A/B=1-392.
DR PDBsum; 6VCZ; -.
DR PDBsum; 6VD0; -.
DR PDBsum; 6VD1; -.
DR PDBsum; 6VD2; -.
DR AlphaFoldDB; P17562; -.
DR SMR; P17562; -.
DR BioGRID; 12284; 7.
DR STRING; 3702.AT4G01850.1; -.
DR iPTMnet; P17562; -.
DR PaxDb; P17562; -.
DR PRIDE; P17562; -.
DR ProteomicsDB; 250626; -.
DR EnsemblPlants; AT4G01850.1; AT4G01850.1; AT4G01850.
DR EnsemblPlants; AT4G01850.2; AT4G01850.2; AT4G01850.
DR GeneID; 826987; -.
DR Gramene; AT4G01850.1; AT4G01850.1; AT4G01850.
DR Gramene; AT4G01850.2; AT4G01850.2; AT4G01850.
DR KEGG; ath:AT4G01850; -.
DR Araport; AT4G01850; -.
DR TAIR; locus:2141385; AT4G01850.
DR eggNOG; KOG1506; Eukaryota.
DR HOGENOM; CLU_041802_0_1_1; -.
DR InParanoid; P17562; -.
DR OMA; YDDNGAM; -.
DR OrthoDB; 685006at2759; -.
DR PhylomeDB; P17562; -.
DR BioCyc; ARA:AT4G01850-MON; -.
DR UniPathway; UPA00315; UER00080.
DR PRO; PR:P17562; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P17562; baseline and differential.
DR Genevisible; P17562; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0070062; C:extracellular exosome; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_00086; S_AdoMet_synth1; 1.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cobalt; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..393
FT /note="S-adenosylmethionine synthase 2"
FT /id="PRO_0000174457"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 43
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 56
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 99
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 167..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 235..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 246
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 252..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 277
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 16..34
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6VD1"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:6VD1"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:6VD1"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6VCZ"
FT STRAND 164..179
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 182..197
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:6VD1"
FT TURN 214..218
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6VCZ"
FT TURN 254..261
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 278..295
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:6VD1"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:6VD1"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:6VD1"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6VD1"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6VD1"
SQ SEQUENCE 393 AA; 43255 MW; CE008EA565FD1FBC CRC64;
METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPDSKV ACETCTKTNM VMVFGEITTK
ATIDYEKIVR DTCRSIGFIS DDVGLDADKC KVLVNIEQQS PDIAQGVHGH FTKRPEDIGA
GDQGHMFGYA TDETPELMPL SHVLATKIGA RLTEVRKNGT CRWLRPDGKT QVTVEYYNDN
GAMVPVRVHT VLISTQHDET VTNDEIARDL KEHVIKPIIP EKYLDDKTIF HLNPSGRFVI
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVANGMAR
RALVQVSYAI GVPEPLSVFV DTYGTGLIPD KEILKIVKET FDFRPGMMTI NLDLKRGGNG
RFQKTAAYGH FGRDDPDFTW EVVKPLKWDK PQA
