NNMT_HUMAN
ID NNMT_HUMAN Reviewed; 264 AA.
AC P40261;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Nicotinamide N-methyltransferase {ECO:0000303|PubMed:21823666};
DE EC=2.1.1.1 {ECO:0000269|PubMed:21823666, ECO:0000269|PubMed:23455543};
GN Name=NNMT {ECO:0000303|PubMed:23455543};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-16 AND 151-184, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8182091; DOI=10.1016/s0021-9258(17)36700-5;
RA Aksoy S., Szumlanski C.L., Weinshilboum R.M.;
RT "Human liver nicotinamide N-methyltransferase. cDNA cloning, expression,
RT and biochemical characterization.";
RL J. Biol. Chem. 269:14835-14840(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8575745; DOI=10.1006/geno.1995.9966;
RA Aksoy S., Brandriff B.F., Ward A., Little P.F., Weinshilboum R.M.;
RT "Human nicotinamide N-methyltransferase gene: molecular cloning, structural
RT characterization and chromosomal localization.";
RL Genomics 29:555-561(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=11271497;
RX DOI=10.1002/1522-2683(200011)21:17<3785::aid-elps3785>3.0.co;2-2;
RA Hubbard M.J., McHugh N.J.;
RT "Human ERp29: isolation, primary structural characterisation and two-
RT dimensional gel mapping.";
RL Electrophoresis 21:3785-3796(2000).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF TYR-20.
RX PubMed=23455543; DOI=10.1038/nchembio.1204;
RA Ulanovskaya O.A., Zuhl A.M., Cravatt B.F.;
RT "NNMT promotes epigenetic remodeling in cancer by creating a metabolic
RT methylation sink.";
RL Nat. Chem. Biol. 9:300-306(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP FUNCTION.
RX PubMed=26571212; DOI=10.1038/ncb3264;
RA Sperber H., Mathieu J., Wang Y., Ferreccio A., Hesson J., Xu Z.,
RA Fischer K.A., Devi A., Detraux D., Gu H., Battle S.L., Showalter M.,
RA Valensisi C., Bielas J.H., Ericson N.G., Margaretha L., Robitaille A.M.,
RA Margineantu D., Fiehn O., Hockenbery D., Blau C.A., Raftery D.,
RA Margolin A.A., Hawkins R.D., Moon R.T., Ware C.B., Ruohola-Baker H.;
RT "The metabolome regulates the epigenetic landscape during naive-to-primed
RT human embryonic stem cell transition.";
RL Nat. Cell Biol. 17:1523-1535(2015).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, CITRULLINATION AT ARG-18; ARG-132 AND
RP ARG-181, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF ARG-18;
RP ARG-132 AND ARG-181.
RX PubMed=30044909; DOI=10.1021/acschembio.8b00578;
RA Nemmara V.V., Tilvawala R., Salinger A.J., Miller L., Nguyen S.H.,
RA Weerapana E., Thompson P.R.;
RT "Citrullination Inactivates Nicotinamide- N-methyltransferase.";
RL ACS Chem. Biol. 13:2663-2672(2018).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31043742; DOI=10.1038/s41586-019-1173-8;
RA Eckert M.A., Coscia F., Chryplewicz A., Chang J.W., Hernandez K.M., Pan S.,
RA Tienda S.M., Nahotko D.A., Li G., Blazenovic I., Lastra R.R., Curtis M.,
RA Yamada S.D., Perets R., McGregor S.M., Andrade J., Fiehn O.,
RA Moellering R.E., Mann M., Lengyel E.;
RT "Proteomics reveals NNMT as a master metabolic regulator of cancer-
RT associated fibroblasts.";
RL Nature 569:723-728(2019).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human nicotinamide N-methyltransferase in complex
RT with SAH.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND NICOTINAMIDE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND MUTAGENESIS OF TYR-20; ASP-197;
RP SER-201 AND SER-213.
RX PubMed=21823666; DOI=10.1021/bi2007614;
RA Peng Y., Sartini D., Pozzi V., Wilk D., Emanuelli M., Yee V.C.;
RT "Structural basis of substrate recognition in human nicotinamide N-
RT methyltransferase.";
RL Biochemistry 50:7800-7808(2011).
CC -!- FUNCTION: Catalyzes the N-methylation of nicotinamide using the
CC universal methyl donor S-adenosyl-L-methionine to form N1-
CC methylnicotinamide and S-adenosyl-L-homocysteine, a predominant
CC nicotinamide/vitamin B3 clearance pathway (PubMed:8182091.
CC PubMed:21823666, PubMed:23455543). Plays a central role in regulating
CC cellular methylation potential, by consuming S-adenosyl-L-methionine
CC and limiting its availability for other methyltransferases. Actively
CC mediates genome-wide epigenetic and transcriptional changes through
CC hypomethylation of repressive chromatin marks, such as H3K27me3
CC (PubMed:26571212, PubMed:23455543, PubMed:31043742). In a developmental
CC context, contributes to low levels of the repressive histone marks that
CC characterize pluripotent embryonic stem cell pre-implantation state
CC (PubMed:26571212). Acts as a metabolic regulator primarily on white
CC adipose tissue energy expenditure as well as hepatic gluconeogenesis
CC and cholesterol biosynthesis. In white adipocytes, regulates polyamine
CC flux by consuming S-adenosyl-L-methionine which provides for
CC propylamine group in polyamine biosynthesis, whereas by consuming
CC nicotinamide controls NAD(+) levels through the salvage pathway (By
CC similarity). Via its product N1-methylnicotinamide regulates protein
CC acetylation in hepatocytes, by repressing the ubiquitination and
CC increasing the stability of SIRT1 deacetylase (By similarity). Can also
CC N-methylate other pyridines structurally related to nicotinamide and
CC play a role in xenobiotic detoxification (PubMed:30044909).
CC {ECO:0000250|UniProtKB:O55239, ECO:0000269|PubMed:21823666,
CC ECO:0000269|PubMed:23455543, ECO:0000269|PubMed:26571212,
CC ECO:0000269|PubMed:30044909, ECO:0000269|PubMed:31043742,
CC ECO:0000269|PubMed:8182091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nicotinamide + S-adenosyl-L-methionine = 1-methylnicotinamide
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23884, ChEBI:CHEBI:16797,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.1;
CC Evidence={ECO:0000269|PubMed:21823666, ECO:0000269|PubMed:23455543,
CC ECO:0000269|PubMed:8182091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23885;
CC Evidence={ECO:0000269|PubMed:21823666, ECO:0000269|PubMed:23455543,
CC ECO:0000269|PubMed:31043742};
CC -!- ACTIVITY REGULATION: Inactivated by deimination on Arg-132.
CC {ECO:0000269|PubMed:30044909}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.43 mM for nicotinamide (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21823666};
CC KM=0.105 mM for nicotinamide (at pH 8.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21823666};
CC KM=1.8 uM for S-adenosyl-L-methionine (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21823666};
CC KM=5 uM for S-adenosyl-L-methionine (at pH 8.6 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21823666};
CC -!- PATHWAY: Cofactor metabolism. {ECO:0000305|PubMed:21823666,
CC ECO:0000305|PubMed:23455543}.
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:21823666,
CC ECO:0000305|PubMed:23455543}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.12}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the liver. A lower
CC expression is seen in the kidney, lung, skeletal muscle, placenta and
CC heart. Not detected in the brain or pancreas.
CC {ECO:0000269|PubMed:8182091}.
CC -!- PTM: Deiminated by PADI1 and PADI2. {ECO:0000269|PubMed:30044909}.
CC -!- MISCELLANEOUS: Prominently expressed in the stroma of high-grade serous
CC carcinomas (PubMed:31043742). In tumorigenesis, regulates the
CC epigenetic reprograming of cancer cells associated with increased cell
CC migration and metastasis (PubMed:23455543, PubMed:31043742).
CC {ECO:0000269|PubMed:23455543, ECO:0000269|PubMed:31043742}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. NNMT/PNMT/TEMT family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NNMTID44506ch11q23.html";
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DR EMBL; U08021; AAA19904.1; -; mRNA.
DR EMBL; U20971; AAA93158.1; -; Genomic_DNA.
DR EMBL; U20970; AAA93158.1; JOINED; Genomic_DNA.
DR EMBL; BC000234; AAH00234.1; -; mRNA.
DR CCDS; CCDS8368.1; -.
DR PIR; A54060; A54060.
DR RefSeq; NP_006160.1; NM_006169.2.
DR PDB; 2IIP; X-ray; 2.05 A; A/B/C/D=1-264.
DR PDB; 3ROD; X-ray; 2.72 A; A/B/C/D=1-264.
DR PDB; 5YJF; X-ray; 2.49 A; A/B/C/D=1-264.
DR PDB; 6CHH; X-ray; 2.30 A; A/B/C/D=1-264.
DR PDB; 6ORR; X-ray; 2.25 A; A/B/C/D=1-264.
DR PDB; 6PVE; X-ray; 2.30 A; A/B/C/D=1-264.
DR PDB; 6PVS; X-ray; 2.58 A; A/B/C/D=1-264.
DR PDB; 7BKG; X-ray; 2.33 A; A/B/C/D=1-264.
DR PDB; 7BLE; X-ray; 2.81 A; A/B/C/D=1-264.
DR PDB; 7EGU; X-ray; 1.90 A; A=3-260.
DR PDB; 7EHZ; X-ray; 2.50 A; A=3-260.
DR PDB; 7EI2; X-ray; 2.08 A; A=3-260.
DR PDB; 7NBJ; X-ray; 2.27 A; A/B/C/D=1-264.
DR PDB; 7NBM; X-ray; 2.69 A; A/B/C/D=1-264.
DR PDB; 7NBQ; X-ray; 2.48 A; A/B/C/D=1-264.
DR PDBsum; 2IIP; -.
DR PDBsum; 3ROD; -.
DR PDBsum; 5YJF; -.
DR PDBsum; 6CHH; -.
DR PDBsum; 6ORR; -.
DR PDBsum; 6PVE; -.
DR PDBsum; 6PVS; -.
DR PDBsum; 7BKG; -.
DR PDBsum; 7BLE; -.
DR PDBsum; 7EGU; -.
DR PDBsum; 7EHZ; -.
DR PDBsum; 7EI2; -.
DR PDBsum; 7NBJ; -.
DR PDBsum; 7NBM; -.
DR PDBsum; 7NBQ; -.
DR AlphaFoldDB; P40261; -.
DR SMR; P40261; -.
DR BioGRID; 110900; 8.
DR IntAct; P40261; 3.
DR MINT; P40261; -.
DR STRING; 9606.ENSP00000441434; -.
DR BindingDB; P40261; -.
DR ChEMBL; CHEMBL2346486; -.
DR DrugBank; DB00627; Niacin.
DR DrugCentral; P40261; -.
DR GlyGen; P40261; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40261; -.
DR MetOSite; P40261; -.
DR PhosphoSitePlus; P40261; -.
DR BioMuta; NNMT; -.
DR DMDM; 730163; -.
DR EPD; P40261; -.
DR jPOST; P40261; -.
DR MassIVE; P40261; -.
DR PaxDb; P40261; -.
DR PeptideAtlas; P40261; -.
DR PRIDE; P40261; -.
DR ProteomicsDB; 55358; -.
DR TopDownProteomics; P40261; -.
DR Antibodypedia; 18379; 499 antibodies from 34 providers.
DR DNASU; 4837; -.
DR Ensembl; ENST00000299964.4; ENSP00000299964.3; ENSG00000166741.8.
DR Ensembl; ENST00000535401.5; ENSP00000441434.1; ENSG00000166741.8.
DR GeneID; 4837; -.
DR KEGG; hsa:4837; -.
DR MANE-Select; ENST00000299964.4; ENSP00000299964.3; NM_006169.3; NP_006160.1.
DR CTD; 4837; -.
DR DisGeNET; 4837; -.
DR GeneCards; NNMT; -.
DR HGNC; HGNC:7861; NNMT.
DR HPA; ENSG00000166741; Tissue enhanced (liver).
DR MIM; 600008; gene.
DR neXtProt; NX_P40261; -.
DR OpenTargets; ENSG00000166741; -.
DR PharmGKB; PA251; -.
DR VEuPathDB; HostDB:ENSG00000166741; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00390000011708; -.
DR HOGENOM; CLU_082526_1_1_1; -.
DR InParanoid; P40261; -.
DR OMA; YNFGSRH; -.
DR OrthoDB; 1054662at2759; -.
DR PhylomeDB; P40261; -.
DR TreeFam; TF313114; -.
DR BRENDA; 2.1.1.1; 2681.
DR PathwayCommons; P40261; -.
DR Reactome; R-HSA-156581; Methylation.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR SignaLink; P40261; -.
DR BioGRID-ORCS; 4837; 6 hits in 1075 CRISPR screens.
DR ChiTaRS; NNMT; human.
DR EvolutionaryTrace; P40261; -.
DR GeneWiki; NNMT; -.
DR GenomeRNAi; 4837; -.
DR Pharos; P40261; Tchem.
DR PRO; PR:P40261; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P40261; protein.
DR Bgee; ENSG00000166741; Expressed in tendon of biceps brachii and 196 other tissues.
DR ExpressionAtlas; P40261; baseline and differential.
DR Genevisible; P40261; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008170; F:N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008112; F:nicotinamide N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030760; F:pyridine N-methyltransferase activity; TAS:Reactome.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; TAS:Reactome.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
DR GO; GO:0006769; P:nicotinamide metabolic process; IDA:UniProtKB.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0090312; P:positive regulation of protein deacetylation; ISS:UniProtKB.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:0031060; P:regulation of histone methylation; IMP:UniProtKB.
DR GO; GO:0010967; P:regulation of polyamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
DR InterPro; IPR000940; NNMT_TEMT_trans.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10867; PTHR10867; 1.
DR Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR PIRSF; PIRSF000384; PNMTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
DR PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Cytoplasm;
KW Direct protein sequencing; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..264
FT /note="Nicotinamide N-methyltransferase"
FT /id="PRO_0000159706"
FT BINDING 20
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 142..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21823666, ECO:0000269|Ref.12"
FT BINDING 197
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000269|PubMed:21823666"
FT BINDING 213
FT /ligand="nicotinamide"
FT /ligand_id="ChEBI:CHEBI:17154"
FT /evidence="ECO:0000269|PubMed:21823666"
FT MOD_RES 18
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:30044909"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 132
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:30044909"
FT MOD_RES 181
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:30044909"
FT MUTAGEN 18
FT /note="R->K: Has no effect on N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30044909"
FT MUTAGEN 20
FT /note="Y->A: Loss of N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:21823666,
FT ECO:0000269|PubMed:23455543"
FT MUTAGEN 20
FT /note="Y->F: Decreases N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:21823666"
FT MUTAGEN 132
FT /note="R->K: Loss of N-methyltransferase activity like its
FT citrullinated counterpart."
FT /evidence="ECO:0000269|PubMed:30044909"
FT MUTAGEN 181
FT /note="R->K: Has no effect on N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:30044909"
FT MUTAGEN 197
FT /note="D->A: Loss of N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:21823666"
FT MUTAGEN 201
FT /note="S->A: Has no effect on N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:21823666"
FT MUTAGEN 213
FT /note="S->A: Has no effect on N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:21823666"
FT TURN 1..3
FT /evidence="ECO:0007829|PDB:2IIP"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:7NBJ"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:7EGU"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:7EGU"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:7EGU"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:7EGU"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:7EGU"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:7EGU"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:7EGU"
SQ SEQUENCE 264 AA; 29574 MW; 280B12748F4488AC CRC64;
MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI
DIGSGPTIYQ LLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN
RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL
RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ
SYSSTMANNE GLFSLVARKL SRPL
