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 16-OCT-2019, entry version 155. 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, GN ECO:0000312|HGNC:HGNC:16021}; GN Synonyms=C21orf127 {ECO:0000312|HGNC:HGNC:16021}, GN HEMK2 {ECO:0000303|PubMed:18539146}, GN PRED28 {ECO:0000250|UniProtKB:Q6SKR2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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- RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 RP AND LYS-166. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT factor 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., RA Buerckstuemmer T., 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., RA Smith M.T., Zhang L.; RT "Involvement of N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) RT in 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 RT but 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., RA 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 CC DNA, and to a lower extent, arsenic (PubMed:18539146, CC PubMed:21193388, PubMed:30017583). Catalytic subunit of a CC heterodimer with TRMT112, which catalyzes N5-methylation of Glu CC residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif CC (PubMed:18539146) (By similarity). Methylates ETF1 on 'Gln-185'; CC ETF1 needs to be complexed to ERF3 in its GTP-bound form to be CC efficiently methylated (PubMed:18539146, PubMed:20606008). Also CC 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 CC is significantly enriched in exonic regions and is associated with CC gene transcriptional activation (PubMed:30017583). May also play a CC role in the modulation of arsenic-induced toxicity by mediating CC the conversion of monomethylarsonous acid (3+) into the less toxic CC dimethylarsonic acid (PubMed:21193388, PubMed:25997655). It CC however only plays a limited role in arsenic metabolism compared CC with AS3MT (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- CC COMP:14895, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, CC ChEBI:CHEBI:57856, 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, CC 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, CC Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; CC EC=2.1.1.72; 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 CC kidney, and lowest expression in leukocytes and mammary gland. CC {ECO:0000269|PubMed:21193388}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related CC family. {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 CC cells. The development of deep sequencing allowed identification CC of m6A in mammal cells and identification of N6AMT1 as a N(6)- CC adenine-specific DNA methyltransferase (PubMed:30017583). CC {ECO:0000250|UniProtKB:Q6SKR2, 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; 6PED; X-ray; 2.30 A; A=1-214. DR PDBsum; 6H1D; -. DR PDBsum; 6H1E; -. DR PDBsum; 6K0X; -. 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 HOGENOM; HOG000219949; -. 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; -. DR PRO; PR:Q9Y5N5; -. DR Proteomes; UP000005640; Chromosome 21. DR Bgee; ENSG00000156239; Expressed in 161 organ(s), highest expression level in corpus callosum. 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; Complete proteome; KW Methyltransferase; Nucleus; Polymorphism; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 214 Methyltransferase N6AMT1. FT /FTId=PRO_0000088049. FT REGION 53 57 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0ACC1, FT ECO:0000255|HAMAP-Rule:MF_02126}. FT REGION 122 125 Substrate binding. FT {ECO:0000250|UniProtKB:P0ACC1}. FT BINDING 77 77 S-adenosyl-L-methionine. FT {ECO:0000250|UniProtKB:P0ACC1}. FT BINDING 122 122 S-adenosyl-L-methionine. FT {ECO:0000305|PubMed:30017583}. FT VAR_SEQ 105 132 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_040294. FT VARIANT 34 34 D -> N (in dbSNP:rs1997607). FT /FTId=VAR_060445. FT VARIANT 146 146 R -> K (in dbSNP:rs2205447). FT {ECO:0000269|PubMed:10830953}. FT /FTId=VAR_060446. FT VARIANT 166 166 R -> K (in dbSNP:rs2205446). FT {ECO:0000269|PubMed:10830953}. FT /FTId=VAR_060447. FT MUTAGEN 122 125 NPPY->AAAA: Abolished DNA FT methyltransferase activity. FT {ECO:0000269|PubMed:30017583}. FT TURN 12 15 {ECO:0000244|PDB:6H1E}. FT HELIX 17 19 {ECO:0000244|PDB:6H1E}. FT HELIX 27 38 {ECO:0000244|PDB:6H1E}. FT HELIX 39 43 {ECO:0000244|PDB:6H1E}. FT STRAND 47 53 {ECO:0000244|PDB:6H1E}. FT HELIX 58 67 {ECO:0000244|PDB:6H1E}. FT STRAND 71 79 {ECO:0000244|PDB:6H1E}. FT HELIX 80 92 {ECO:0000244|PDB:6H1E}. FT STRAND 98 103 {ECO:0000244|PDB:6H1E}. FT TURN 104 115 {ECO:0000244|PDB:6H1E}. FT STRAND 116 121 {ECO:0000244|PDB:6H1E}. FT HELIX 130 132 {ECO:0000244|PDB:6H1E}. FT HELIX 138 141 {ECO:0000244|PDB:6H1E}. FT HELIX 146 148 {ECO:0000244|PDB:6H1E}. FT HELIX 150 155 {ECO:0000244|PDB:6H1E}. FT HELIX 156 158 {ECO:0000244|PDB:6H1E}. FT HELIX 159 162 {ECO:0000244|PDB:6H1E}. FT STRAND 163 174 {ECO:0000244|PDB:6H1E}. FT HELIX 175 177 {ECO:0000244|PDB:6H1E}. FT HELIX 179 188 {ECO:0000244|PDB:6H1E}. FT STRAND 192 201 {ECO:0000244|PDB:6H1E}. FT STRAND 204 212 {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 //