ID   TFB1M_HUMAN             Reviewed;         346 AA.
AC   Q8WVM0; Q05DR0; Q9Y384;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Dimethyladenosine transferase 1, mitochondrial;
DE            EC=2.1.1.-;
DE   AltName: Full=Mitochondrial 12S rRNA dimethylase 1;
DE   AltName: Full=Mitochondrial transcription factor B1;
DE            Short=h-mtTFB;
DE            Short=h-mtTFB1;
DE            Short=hTFB1M;
DE            Short=mtTFB1;
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1;
DE   Flags: Precursor;
GN   Name=TFB1M; ORFNames=CGI-75;
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 [LARGE SCALE MRNA].
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Lung;
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   FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND SAM-BINDING.
RX   PubMed=11809803; DOI=10.1128/mcb.22.4.1116-1125.2002;
RA   McCulloch V., Seidel-Rogol B.L., Shadel G.S.;
RT   "A human mitochondrial transcription factor is related to RNA adenine
RT   methyltransferases and binds S-adenosylmethionine.";
RL   Mol. Cell. Biol. 22:1116-1125(2002).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH POLRMT.
RX   PubMed=12068295; DOI=10.1038/ng909;
RA   Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G.,
RA   Gustafsson C.M.;
RT   "Mitochondrial transcription factors B1 and B2 activate transcription of
RT   human mtDNA.";
RL   Nat. Genet. 31:289-294(2002).
RN   [6]
RP   FUNCTION, INTERACTION WITH TFAM, AND MUTAGENESIS OF GLY-65; ASN-141 AND
RP   LYS-220.
RX   PubMed=12897151; DOI=10.1128/mcb.23.16.5816-5824.2003;
RA   McCulloch V., Shadel G.S.;
RT   "Human mitochondrial transcription factor B1 interacts with the C-terminal
RT   activation region of h-mtTFA and stimulates transcription independently of
RT   its RNA methyltransferase activity.";
RL   Mol. Cell. Biol. 23:5816-5824(2003).
RN   [7]
RP   ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-65 AND LYS-220.
RX   PubMed=12496758; DOI=10.1038/ng1064;
RA   Seidel-Rogol B.L., McCulloch V., Shadel G.S.;
RT   "Human mitochondrial transcription factor B1 methylates ribosomal RNA at a
RT   conserved stem-loop.";
RL   Nat. Genet. 33:23-24(2003).
RN   [8]
RP   POSSIBLE INVOLVEMENT IN AMINOGLYCOSIDE-INDUCED DEAFNESS.
RX   PubMed=15110318; DOI=10.1016/j.ymgme.2004.01.020;
RA   Bykhovskaya Y., Mengesha E., Wang D., Yang H., Estivill X., Shohat M.,
RA   Fischel-Ghodsian N.;
RT   "Human mitochondrial transcription factor B1 as a modifier gene for hearing
RT   loss associated with the mitochondrial A1555G mutation.";
RL   Mol. Genet. Metab. 82:27-32(2004).
RN   [9]
RP   INDUCTION.
RX   PubMed=15684387; DOI=10.1128/mcb.25.4.1354-1366.2005;
RA   Gleyzer N., Vercauteren K., Scarpulla R.C.;
RT   "Control of mitochondrial transcription specificity factors (TFB1M and
RT   TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family
RT   coactivators.";
RL   Mol. Cell. Biol. 25:1354-1366(2005).
RN   [10]
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   VARIANTS PRO-120; ALA-211 AND GLN-256.
RX   PubMed=19096125; DOI=10.1155/2008/575323;
RA   Alonso-Montes C., Castro M.G., Reguero J.R., Perrot A., Ozcelik C.,
RA   Geier C., Posch M.G., Moris C., Alvarez V., Ruiz-Ortega M., Coto E.;
RT   "Mitochondrial transcription factors TFA, TFB1 and TFB2: a search for DNA
RT   variants/haplotypes and the risk of cardiac hypertrophy.";
RL   Dis. Markers 25:131-139(2008).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which
CC       specifically dimethylates mitochondrial 12S rRNA at the conserved stem
CC       loop. Also required for basal transcription of mitochondrial DNA,
CC       probably via its interaction with POLRMT and TFAM. Stimulates
CC       transcription independently of the methyltransferase activity.
CC       {ECO:0000269|PubMed:11809803, ECO:0000269|PubMed:12068295,
CC       ECO:0000269|PubMed:12897151}.
CC   -!- SUBUNIT: Interacts with mitochondrial RNA polymerase POLRMT. Interacts
CC       with TFAM. {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151}.
CC   -!- INTERACTION:
CC       Q8WVM0; Q00059: TFAM; NbExp=2; IntAct=EBI-2615570, EBI-1049924;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11809803}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:12068295}.
CC   -!- INDUCTION: By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and
CC       PGC-1 coactivators. {ECO:0000269|PubMed:15684387}.
CC   -!- DISEASE: Note=Variations in TFB1M may influence the clinical expression
CC       of aminoglycoside-induced deafness caused by the A1555G mutation in the
CC       mitochondrial 12S rRNA.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05183.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF151833; AAD34070.1; -; mRNA.
DR   EMBL; AL139101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005183; AAH05183.1; ALT_SEQ; mRNA.
DR   EMBL; BC017788; AAH17788.1; -; mRNA.
DR   CCDS; CCDS5248.1; -.
DR   RefSeq; NP_057104.2; NM_016020.3.
DR   PDB; 6AAX; X-ray; 2.99 A; A/C=28-346.
DR   PDB; 6AJK; X-ray; 3.00 A; A=27-346.
DR   PDB; 8CSP; EM; 2.66 A; 5=1-346.
DR   PDB; 8CSQ; EM; 2.54 A; 5=1-346.
DR   PDB; 8CSR; EM; 2.54 A; 5=1-346.
DR   PDB; 8CSU; EM; 3.03 A; 5=1-346.
DR   PDBsum; 6AAX; -.
DR   PDBsum; 6AJK; -.
DR   PDBsum; 8CSP; -.
DR   PDBsum; 8CSQ; -.
DR   PDBsum; 8CSR; -.
DR   PDBsum; 8CSU; -.
DR   AlphaFoldDB; Q8WVM0; -.
DR   EMDB; EMD-26966; -.
DR   EMDB; EMD-26967; -.
DR   EMDB; EMD-26968; -.
DR   EMDB; EMD-26971; -.
DR   SMR; Q8WVM0; -.
DR   BioGRID; 119295; 116.
DR   IntAct; Q8WVM0; 24.
DR   MINT; Q8WVM0; -.
DR   STRING; 9606.ENSP00000356134; -.
DR   GlyGen; Q8WVM0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8WVM0; -.
DR   PhosphoSitePlus; Q8WVM0; -.
DR   SwissPalm; Q8WVM0; -.
DR   BioMuta; TFB1M; -.
DR   DMDM; 74751555; -.
DR   EPD; Q8WVM0; -.
DR   jPOST; Q8WVM0; -.
DR   MassIVE; Q8WVM0; -.
DR   MaxQB; Q8WVM0; -.
DR   PaxDb; 9606-ENSP00000356134; -.
DR   PeptideAtlas; Q8WVM0; -.
DR   ProteomicsDB; 74803; -.
DR   Pumba; Q8WVM0; -.
DR   Antibodypedia; 33417; 231 antibodies from 28 providers.
DR   DNASU; 51106; -.
DR   Ensembl; ENST00000367166.5; ENSP00000356134.4; ENSG00000029639.11.
DR   GeneID; 51106; -.
DR   KEGG; hsa:51106; -.
DR   MANE-Select; ENST00000367166.5; ENSP00000356134.4; NM_016020.4; NP_057104.2.
DR   UCSC; uc003qqj.5; human.
DR   AGR; HGNC:17037; -.
DR   CTD; 51106; -.
DR   DisGeNET; 51106; -.
DR   GeneCards; TFB1M; -.
DR   HGNC; HGNC:17037; TFB1M.
DR   HPA; ENSG00000029639; Low tissue specificity.
DR   MalaCards; TFB1M; -.
DR   MIM; 607033; gene.
DR   neXtProt; NX_Q8WVM0; -.
DR   OpenTargets; ENSG00000029639; -.
DR   Orphanet; 90641; Rare mitochondrial non-syndromic sensorineural deafness.
DR   PharmGKB; PA38198; -.
DR   VEuPathDB; HostDB:ENSG00000029639; -.
DR   eggNOG; KOG0821; Eukaryota.
DR   GeneTree; ENSGT00950000183142; -.
DR   HOGENOM; CLU_041220_7_0_1; -.
DR   InParanoid; Q8WVM0; -.
DR   OMA; RIEQPFK; -.
DR   OrthoDB; 25601at2759; -.
DR   PhylomeDB; Q8WVM0; -.
DR   TreeFam; TF300798; -.
DR   PathwayCommons; Q8WVM0; -.
DR   Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; R-HSA-6793080; rRNA modification in the mitochondrion.
DR   SignaLink; Q8WVM0; -.
DR   BioGRID-ORCS; 51106; 182 hits in 1159 CRISPR screens.
DR   ChiTaRS; TFB1M; human.
DR   GeneWiki; TFB1M; -.
DR   GenomeRNAi; 51106; -.
DR   Pharos; Q8WVM0; Tbio.
DR   PRO; PR:Q8WVM0; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8WVM0; Protein.
DR   Bgee; ENSG00000029639; Expressed in right adrenal gland and 182 other cell types or tissues.
DR   ExpressionAtlas; Q8WVM0; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034246; F:mitochondrial transcription factor activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; EXP:Reactome.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR   GO; GO:0000154; P:rRNA modification; TAS:Reactome.
DR   GO; GO:0006391; P:transcription initiation at mitochondrial promoter; IBA:GO_Central.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00755; ksgA; 1.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF17; DIMETHYLADENOSINE TRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
DR   Genevisible; Q8WVM0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Methyltransferase; Mitochondrion;
KW   Reference proteome; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..346
FT                   /note="Dimethyladenosine transferase 1, mitochondrial"
FT                   /id="PRO_0000273171"
FT   BINDING         35..38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   VARIANT         120
FT                   /note="A -> P (in dbSNP:rs144355958)"
FT                   /evidence="ECO:0000269|PubMed:19096125"
FT                   /id="VAR_071246"
FT   VARIANT         211
FT                   /note="T -> A (in dbSNP:rs769497533)"
FT                   /evidence="ECO:0000269|PubMed:19096125"
FT                   /id="VAR_071247"
FT   VARIANT         256
FT                   /note="R -> Q (in dbSNP:rs73579353)"
FT                   /evidence="ECO:0000269|PubMed:19096125"
FT                   /id="VAR_071248"
FT   MUTAGEN         65
FT                   /note="G->A: Abolishes methyltransferase activity,
FT                   DNA-binding and SAM-binding. Does not abolish transcription
FT                   activator function."
FT                   /evidence="ECO:0000269|PubMed:12496758,
FT                   ECO:0000269|PubMed:12897151"
FT   MUTAGEN         141
FT                   /note="N->A: Does not affect SAM-binding, DNA-binding nor
FT                   transcription activator function."
FT                   /evidence="ECO:0000269|PubMed:12897151"
FT   MUTAGEN         220
FT                   /note="K->A: Abolishes methyltransferase activity. Does not
FT                   affect SAM-binding, DNA-binding nor transcription activator
FT                   function."
FT                   /evidence="ECO:0000269|PubMed:12496758,
FT                   ECO:0000269|PubMed:12897151"
FT   CONFLICT        31..32
FT                   /note="KQ -> NE (in Ref. 1; AAD34070)"
FT                   /evidence="ECO:0000305"
FT   HELIX           18..24
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           68..75
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          79..86
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           91..100
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:8CSP"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:8CSR"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           144..160
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          171..177
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           178..184
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:6AJK"
FT   HELIX           195..201
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          204..212
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   STRAND          225..232
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           242..253
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           260..264
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:8CSP"
FT   HELIX           273..284
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           292..294
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           297..312
FT                   /evidence="ECO:0007829|PDB:8CSQ"
FT   HELIX           315..319
FT                   /evidence="ECO:0007829|PDB:8CSP"
FT   HELIX           322..327
FT                   /evidence="ECO:0007829|PDB:8CSQ"
SQ   SEQUENCE   346 AA;  39543 MW;  4C34F4FD72B01286 CRC64;
     MAASGKLSTC RLPPLPTIRE IIKLLRLQAA KQLSQNFLLD LRLTDKIVRK AGNLTNAYVY
     EVGPGPGGIT RSILNADVAE LLVVEKDTRF IPGLQMLSDA APGKLRIVHG DVLTFKVEKA
     FSESLKRPWE DDPPNVHIIG NLPFSVSTPL IIKWLENISC RDGPFVYGRT QMTLTFQKEV
     AERLAANTGS KQRSRLSVMA QYLCNVRHIF TIPGQAFVPK PEVDVGVVHF TPLIQPKIEQ
     PFKLVEKVVQ NVFQFRRKYC HRGLRMLFPE AQRLESTGRL LELADIDPTL RPRQLSISHF
     KSLCDVYRKM CDEDPQLFAY NFREELKRRK SKNEEKEEDD AENYRL
//