METK1_ARATH
ID METK1_ARATH Reviewed; 393 AA.
AC P23686; Q941A8; Q9FEE0;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=S-adenosylmethionine synthase 1;
DE Short=AdoMet synthase 1;
DE EC=2.5.1.6 {ECO:0000269|PubMed:16365035};
DE AltName: Full=Methionine adenosyltransferase 1;
DE Short=MAT 1;
GN Name=SAM1; OrderedLocusNames=At1g02500; ORFNames=T14P4.17, T14P4_22;
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].
RX PubMed=2535470; DOI=10.2307/3869064;
RA Peleman J., Boerjan W., Engler G., Seurinck J., Botterman J., Alliotte T.,
RA van Montagu M., Inze D.;
RT "Strong cellular preference in the expression of a housekeeping gene of
RT Arabidopsis thaliana encoding S-adenosylmethionine synthetase.";
RL Plant Cell 1:81-93(1989).
RN [2]
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 [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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116 AND 363-393.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
RP 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, S-NITROSYLATION AT CYS-114,
RP MUTAGENESIS OF CYS-114, 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 [9]
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: Reversibly inhibited by NO. Inhibited by 5,5'-
CC dithiobis-2-nitrobenzoic acid (DTNB) and N-ethylmaleimide (NEM) (in
CC vitro). {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 {ECO:0000269|PubMed:2482229}.
CC -!- PTM: S-nitrosylated in the presence of NO. The inhibition of SAM1
CC activity by S-nitrosylation could contribute to the cross-talk between
CC ethylene and NO signaling. {ECO:0000269|PubMed:16365035}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96504.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL31222.1; Type=Frameshift; Evidence={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; M55077; AAA32868.1; -; Genomic_DNA.
DR EMBL; AC022521; AAG10639.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27437.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27438.1; -; Genomic_DNA.
DR EMBL; AF325061; AAG40413.1; -; mRNA.
DR EMBL; AY092955; AAM12954.1; -; mRNA.
DR EMBL; AF428440; AAL16209.1; -; mRNA.
DR EMBL; AY052311; AAK96504.1; ALT_FRAME; mRNA.
DR EMBL; AY061895; AAL31222.1; ALT_FRAME; mRNA.
DR EMBL; AY087703; AAM65240.1; -; mRNA.
DR EMBL; Z17672; CAA79031.1; -; mRNA.
DR EMBL; Z17762; CAA79057.1; -; mRNA.
DR PIR; C86155; C86155.
DR PIR; JN0131; JN0131.
DR RefSeq; NP_171751.1; NM_100131.3.
DR RefSeq; NP_849577.1; NM_179246.1.
DR PDB; 6VCX; X-ray; 1.10 A; A=1-393.
DR PDB; 6VCY; X-ray; 1.82 A; A=1-393.
DR PDBsum; 6VCX; -.
DR PDBsum; 6VCY; -.
DR AlphaFoldDB; P23686; -.
DR SMR; P23686; -.
DR BioGRID; 24736; 6.
DR STRING; 3702.AT1G02500.1; -.
DR iPTMnet; P23686; -.
DR SWISS-2DPAGE; P99056; -.
DR PaxDb; P23686; -.
DR PRIDE; P23686; -.
DR ProteomicsDB; 250846; -.
DR EnsemblPlants; AT1G02500.1; AT1G02500.1; AT1G02500.
DR EnsemblPlants; AT1G02500.2; AT1G02500.2; AT1G02500.
DR GeneID; 839501; -.
DR Gramene; AT1G02500.1; AT1G02500.1; AT1G02500.
DR Gramene; AT1G02500.2; AT1G02500.2; AT1G02500.
DR KEGG; ath:AT1G02500; -.
DR Araport; AT1G02500; -.
DR TAIR; locus:2196160; AT1G02500.
DR eggNOG; KOG1506; Eukaryota.
DR HOGENOM; CLU_041802_0_1_1; -.
DR InParanoid; P23686; -.
DR OMA; HFTKCPE; -.
DR OrthoDB; 685006at2759; -.
DR PhylomeDB; P23686; -.
DR BioCyc; ARA:AT1G02500-MON; -.
DR BioCyc; MetaCyc:AT1G02500-MON; -.
DR UniPathway; UPA00315; UER00080.
DR PRO; PR:P23686; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P23686; baseline and differential.
DR Genevisible; P23686; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IDA:TAIR.
DR GO; GO:0009693; P:ethylene biosynthetic process; TAS:TAIR.
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 S-nitrosylation; Transferase.
FT CHAIN 1..393
FT /note="S-adenosylmethionine synthase 1"
FT /id="PRO_0000174456"
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 MOD_RES 114
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:16365035"
FT MUTAGEN 114
FT /note="C->R: Loss of the NO-mediated inhibition by S-
FT nitrosylation."
FT /evidence="ECO:0000269|PubMed:16365035"
FT CONFLICT 117
FT /note="E -> D (in Ref. 1; AAA32868)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 16..34
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6VCX"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:6VCX"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:6VCX"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 164..179
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 182..197
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6VCX"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:6VCX"
FT TURN 254..261
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 278..295
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:6VCX"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:6VCX"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6VCX"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6VCX"
SQ SEQUENCE 393 AA; 43158 MW; 27B0AF8AF55D2FF3 CRC64;
METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPDSKV ACETCTKTNM VMVFGEITTK
ATVDYEKIVR DTCRAIGFVS DDVGLDADKC KVLVNIEQQS PDIAQGVHGH FTKCPEEIGA
GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGT CAWLRPDGKT QVTVEYYNDK
GAMVPIRVHT VLISTQHDET VTNDEIARDL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVANGMAR
RALVQVSYAI GVPEPLSVFV DTYETGLIPD KEILKIVKES FDFRPGMMTI NLDLKRGGNG
RFLKTAAYGH FGRDDPDFTW EVVKPLKWDK PQA
