ID N6MT1_HUMAN Reviewed; 214 AA. AC Q9Y5N5; B2RA97; Q96F73; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2017, sequence version 4. DT 26-FEB-2020, entry version 158. DE RecName: Full=Methyltransferase N6AMT1 {ECO:0000305}; DE AltName: Full=HemK methyltransferase family member 2 {ECO:0000303|PubMed:18539146}; DE Short=M.HsaHemK2P; DE AltName: Full=Methylarsonite methyltransferase N6AMT1; DE EC=2.1.1.- {ECO:0000269|PubMed:21193388, ECO:0000269|PubMed:25997655}; DE AltName: Full=N(6)-adenine-specific DNA methyltransferase 1 {ECO:0000303|PubMed:30017583}; DE EC=2.1.1.72 {ECO:0000269|PubMed:30017583}; DE AltName: Full=Protein N(5)-glutamine methyltransferase {ECO:0000305}; DE EC=2.1.1.- {ECO:0000269|PubMed:18539146}; GN Name=N6AMT1 {ECO:0000303|PubMed:30017583, ECO:0000312|HGNC:HGNC:16021}; GN Synonyms=C21orf127 {ECO:0000312|HGNC:HGNC:16021}, GN HEMK2 {ECO:0000303|PubMed:18539146}, PRED28 {ECO:0000250|UniProtKB:Q6SKR2}; 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] (ISOFORM 1). RA Reboul J., Misseri Y., Bonnerot C., Mogensen E., Lutfalla G.; RT "Identification of a novel putative eukaryotic DNA-methyltransferase."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-146 AND RP LYS-166. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skin; 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 [6] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TRMT112. RX PubMed=18539146; DOI=10.1016/j.febslet.2008.05.045; RA Figaro S., Scrima N., Buckingham R.H., Heurgue-Hamard V.; RT "HemK2 protein, encoded on human chromosome 21, methylates translation RT termination factor eRF1."; RL FEBS Lett. 582:2352-2356(2008). RN [7] RP FUNCTION. RX PubMed=20606008; DOI=10.1128/mcb.00218-10; RA Liu P., Nie S., Li B., Yang Z.Q., Xu Z.M., Fei J., Lin C., Zeng R., RA Xu G.L.; RT "Deficiency in a glutamine-specific methyltransferase for release factor RT causes mouse embryonic lethality."; RL Mol. Cell. Biol. 30:4245-4253(2010). RN [8] 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 [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=21193388; DOI=10.1289/ehp.1002733; RA Ren X., Aleshin M., Jo W.J., Dills R., Kalman D.A., Vulpe C.D., Smith M.T., RA Zhang L.; RT "Involvement of N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) in RT arsenic biomethylation and its role in arsenic-induced toxicity."; RL Environ. Health Perspect. 119:771-777(2011). RN [10] RP SUBUNIT. RX PubMed=25851604; DOI=10.1091/mbc.e15-02-0073; RA Zorbas C., Nicolas E., Wacheul L., Huvelle E., Heurgue-Hamard V., RA Lafontaine D.L.; RT "The human 18S rRNA base methyltransferases DIMT1L and WBSCR22-TRMT112 but RT not rRNA modification are required for ribosome biogenesis."; RL Mol. Biol. Cell 26:2080-2095(2015). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25997655; DOI=10.1093/toxsci/kfv101; RA Zhang H., Ge Y., He P., Chen X., Carina A., Qiu Y., Aga D.S., Ren X.; RT "Interactive effects of N6AMT1 and As3MT in arsenic biomethylation."; RL Toxicol. Sci. 146:354-362(2015). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 122-ASN--TYR-125. RX PubMed=30017583; DOI=10.1016/j.molcel.2018.06.015; RA Xiao C.L., Zhu S., He M., Chen D., Zhang Q., Chen Y., Yu G., Liu J., RA Xie S.Q., Luo F., Liang Z., Wang D.P., Bo X.C., Gu X.F., Wang K., Yan G.R.; RT "N6-methyladenine DNA modification in the human genome."; RL Mol. Cell 71:306-318(2018). CC -!- FUNCTION: Methyltransferase that can methylate both proteins and DNA, CC and to a lower extent, arsenic (PubMed:18539146, PubMed:21193388, CC PubMed:30017583). Catalytic subunit of a heterodimer with TRMT112, CC which catalyzes N5-methylation of Glu residue of proteins with a Gly- CC Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:18539146) (By similarity). Methylates CC ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound CC form to be efficiently methylated (PubMed:18539146, PubMed:20606008). CC Also acts as a N(6)-adenine-specific DNA methyltransferase by mediating CC methylation of DNA on the 6th position of adenine (N(6)- CC methyladenosine) (PubMed:30017583). N(6)-methyladenosine (m6A) DNA is CC significantly enriched in exonic regions and is associated with gene CC transcriptional activation (PubMed:30017583). May also play a role in CC the modulation of arsenic-induced toxicity by mediating the conversion CC of monomethylarsonous acid (3+) into the less toxic dimethylarsonic CC acid (PubMed:21193388, PubMed:25997655). It however only plays a CC limited role in arsenic metabolism compared with AS3MT CC (PubMed:25997655). {ECO:0000250|UniProtKB:Q6SKR2, CC ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:20606008, CC ECO:0000269|PubMed:21193388, ECO:0000269|PubMed:25997655, CC ECO:0000269|PubMed:30017583}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + S-adenosyl-L-methionine = H(+) + CC N(5)-methyl-L-glutaminyl-[protein] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:57452, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14895, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; CC Evidence={ECO:0000269|PubMed:18539146}; CC -!- CATALYTIC ACTIVITY: CC Reaction=methylarsonous acid + S-adenosyl-L-methionine = CC dimethylarsinate + 2 H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:11684, ChEBI:CHEBI:15378, ChEBI:CHEBI:16223, CC ChEBI:CHEBI:17826, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; CC Evidence={ECO:0000269|PubMed:21193388, ECO:0000269|PubMed:25997655}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA- CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72; CC Evidence={ECO:0000269|PubMed:30017583}; CC -!- SUBUNIT: Heterodimer; heterodimerizes with TRMT112. CC {ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:25851604}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6SKR2}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Alpha {ECO:0000303|PubMed:18539146}; CC IsoId=Q9Y5N5-1; Sequence=Displayed; CC Name=2; Synonyms=Beta {ECO:0000303|PubMed:18539146}; CC IsoId=Q9Y5N5-2; Sequence=VSP_040294; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in CC parathyroid and pituitary glands, followed by adrenal gland and kidney, CC and lowest expression in leukocytes and mammary gland. CC {ECO:0000269|PubMed:21193388}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related family. CC {ECO:0000305}. CC -!- CAUTION: Although predicted to act as a DNA methyltransferase, DNA CC methyltransferase activity has been elusive for many years due to CC inability to detect N(6)-methyladenosine (m6A) in vertebrate cells. The CC development of deep sequencing allowed identification of m6A in mammal CC cells and identification of N6AMT1 as a N(6)-adenine-specific DNA CC methyltransferase (PubMed:30017583). {ECO:0000250|UniProtKB:Q6SKR2, CC ECO:0000269|PubMed:30017583}. 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; AF139682; AAD38520.1; -; mRNA. DR EMBL; AK314100; BAG36794.1; -; mRNA. DR EMBL; AF227510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL163248; CAB90428.1; -; Genomic_DNA. DR EMBL; AMYH02037685; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF570251; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF457188; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09939.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09940.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09941.1; -; Genomic_DNA. DR EMBL; BC011554; AAH11554.1; -; mRNA. DR CCDS; CCDS33525.1; -. [Q9Y5N5-2] DR CCDS; CCDS33526.1; -. [Q9Y5N5-1] DR RefSeq; NP_037372.4; NM_013240.5. [Q9Y5N5-1] DR RefSeq; NP_877426.4; NM_182749.4. [Q9Y5N5-2] DR PDB; 6H1D; X-ray; 1.94 A; A=8-214. DR PDB; 6H1E; X-ray; 1.90 A; A=8-214. DR PDB; 6K0X; X-ray; 2.20 A; A=2-214. DR PDB; 6KMR; X-ray; 2.00 A; B=1-214. DR PDB; 6KMS; X-ray; 3.20 A; C/D=1-214. DR PDB; 6PED; X-ray; 2.30 A; A=1-214. DR PDBsum; 6H1D; -. DR PDBsum; 6H1E; -. DR PDBsum; 6K0X; -. DR PDBsum; 6KMR; -. DR PDBsum; 6KMS; -. DR PDBsum; 6PED; -. DR SMR; Q9Y5N5; -. DR BioGrid; 118872; 7. DR IntAct; Q9Y5N5; 5. DR MINT; Q9Y5N5; -. DR STRING; 9606.ENSP00000303584; -. DR BioMuta; N6AMT1; -. DR DMDM; 313104228; -. DR EPD; Q9Y5N5; -. DR jPOST; Q9Y5N5; -. DR MassIVE; Q9Y5N5; -. DR PaxDb; Q9Y5N5; -. DR PeptideAtlas; Q9Y5N5; -. DR PRIDE; Q9Y5N5; -. DR ProteomicsDB; 86454; -. [Q9Y5N5-1] DR ProteomicsDB; 86455; -. [Q9Y5N5-2] DR DNASU; 29104; -. DR Ensembl; ENST00000303775; ENSP00000303584; ENSG00000156239. [Q9Y5N5-1] DR Ensembl; ENST00000351429; ENSP00000286764; ENSG00000156239. [Q9Y5N5-2] DR Ensembl; ENST00000460212; ENSP00000436490; ENSG00000156239. [Q9Y5N5-1] DR GeneID; 29104; -. DR KEGG; hsa:29104; -. DR UCSC; uc002ymo.3; human. DR UCSC; uc002ymp.3; human. [Q9Y5N5-1] DR CTD; 29104; -. DR DisGeNET; 29104; -. DR GeneCards; N6AMT1; -. DR HGNC; HGNC:16021; N6AMT1. DR HPA; CAB034133; -. DR HPA; CAB034135; -. DR HPA; HPA059242; -. DR MIM; 614553; gene. DR neXtProt; NX_Q9Y5N5; -. DR OpenTargets; ENSG00000156239; -. DR PharmGKB; PA162396656; -. DR eggNOG; KOG3191; Eukaryota. DR eggNOG; COG2890; LUCA. DR GeneTree; ENSGT00390000013073; -. DR InParanoid; Q9Y5N5; -. DR KO; K19589; -. DR OMA; EWDDWME; -. DR OrthoDB; 1450330at2759; -. DR PhylomeDB; Q9Y5N5; -. DR TreeFam; TF314919; -. DR BRENDA; 2.1.1.72; 2681. DR Reactome; R-HSA-156581; Methylation. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR ChiTaRS; N6AMT1; human. DR GenomeRNAi; 29104; -. DR Pharos; Q9Y5N5; Tbio. DR PRO; PR:Q9Y5N5; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; Q9Y5N5; protein. DR Bgee; ENSG00000156239; Expressed in corpus callosum and 160 other tissues. DR Genevisible; Q9Y5N5; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0035657; C:eRF1 methyltransferase complex; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0030792; F:methylarsonite methyltransferase activity; IDA:UniProtKB. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0008276; F:protein methyltransferase activity; IDA:MGI. DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IDA:UniProtKB. DR GO; GO:0018872; P:arsonoacetate metabolic process; IDA:UniProtKB. DR GO; GO:0032775; P:DNA methylation on adenine; IDA:UniProtKB. DR GO; GO:0032259; P:methylation; IDA:UniProtKB. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IDA:UniProtKB. DR GO; GO:0030307; P:positive regulation of cell growth; IDA:MGI. DR GO; GO:0009404; P:toxin metabolic process; IDA:UniProtKB. DR GO; GO:0006415; P:translational termination; TAS:Reactome. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004557; PrmC-related. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00537; hemK_rel_arch; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Methyltransferase; Nucleus; KW Polymorphism; Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..214 FT /note="Methyltransferase N6AMT1" FT /id="PRO_0000088049" FT REGION 53..57 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000250|UniProtKB:P0ACC1, ECO:0000255|HAMAP- FT Rule:MF_02126" FT REGION 122..125 FT /note="Substrate binding" FT /evidence="ECO:0000250|UniProtKB:P0ACC1" FT BINDING 77 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000250|UniProtKB:P0ACC1" FT BINDING 122 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000305|PubMed:30017583" FT VAR_SEQ 105..132 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040294" FT VARIANT 34 FT /note="D -> N (in dbSNP:rs1997607)" FT /id="VAR_060445" FT VARIANT 146 FT /note="R -> K (in dbSNP:rs2205447)" FT /evidence="ECO:0000269|PubMed:10830953" FT /id="VAR_060446" FT VARIANT 166 FT /note="R -> K (in dbSNP:rs2205446)" FT /evidence="ECO:0000269|PubMed:10830953" FT /id="VAR_060447" FT MUTAGEN 122..125 FT /note="NPPY->AAAA: Abolished DNA methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:30017583" FT TURN 12..15 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 17..19 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 27..38 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 39..43 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 47..53 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 58..67 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 71..79 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 80..92 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 98..103 FT /evidence="ECO:0000244|PDB:6H1E" FT TURN 104..115 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 116..121 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 130..132 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 138..141 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 146..148 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 150..155 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 156..158 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 159..162 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 163..174 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 175..177 FT /evidence="ECO:0000244|PDB:6H1E" FT HELIX 179..188 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 192..201 FT /evidence="ECO:0000244|PDB:6H1E" FT STRAND 204..212 FT /evidence="ECO:0000244|PDB:6H1E" SQ SEQUENCE 214 AA; 22957 MW; 65512C91DC85ADDB CRC64; MAGENFATPF HGHVGRGAFS DVYEPAEDTF LLLDALEAAA AELAGVEICL EVGSGSGVVS AFLASMIGPQ ALYMCTDINP EAAACTLETA RCNKVHIQPV ITDLVKGLLP RLTEKVDLLV FNPPYVVTPP QEVGSHGIEA AWAGGRNGRE VMDRFFPLVP DLLSPRGLFY LVTIKENNPE EILKIMKTKG LQGTTALSRQ AGQETLSVLK FTKS //