ID TFB2M_HUMAN Reviewed; 396 AA. AC Q9H5Q4; Q9H626; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 189. DE RecName: Full=Dimethyladenosine transferase 2, mitochondrial {ECO:0000305}; DE EC=2.1.1.- {ECO:0000305|PubMed:17031457}; DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 5; DE Short=HCV NS5A-transactivated protein 5; DE AltName: Full=Mitochondrial 12S rRNA dimethylase 2; DE AltName: Full=Mitochondrial transcription factor B2; DE Short=h-mtTFB; DE Short=h-mtTFB2; DE Short=hTFB2M; DE Short=mtTFB2; DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2; DE Flags: Precursor; GN Name=TFB2M {ECO:0000312|HGNC:HGNC:18559}; Synonyms=NS5ATP5; 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]. RA Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.; RT "Cloning and identification of human gene 5 transactivated by hepatitis C RT virus NS5A protein."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Small intestine; 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]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [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 SAM-BINDING. 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 FUNCTION. RX PubMed=15526033; DOI=10.1038/sj.emboj.7600465; RA Gaspari M., Falkenberg M., Larsson N.-G., Gustafsson C.M.; RT "The mitochondrial RNA polymerase contributes critically to promoter RT specificity in mammalian cells."; RL EMBO J. 23:4606-4614(2004). RN [8] 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 [9] RP ENZYME ACTIVITY, MUTAGENESIS OF GLY-105, AND FUNCTION. RX PubMed=17031457; DOI=10.1007/s00239-006-0075-1; RA Cotney J., Shadel G.S.; RT "Evidence for an early gene duplication event in the evolution of the RT mitochondrial transcription factor B family and maintenance of rRNA RT methyltransferase activity in human mtTFB1 and mtTFB2."; RL J. Mol. Evol. 63:707-717(2006). RN [10] RP FUNCTION. RX PubMed=20410300; DOI=10.1074/jbc.c110.128918; RA Litonin D., Sologub M., Shi Y., Savkina M., Anikin M., Falkenberg M., RA Gustafsson C.M., Temiakov D.; RT "Human mitochondrial transcription revisited: only TFAM and TFB2M are RT required for transcription of the mitochondrial genes in vitro."; RL J. Biol. Chem. 285:18129-18133(2010). RN [11] 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 [12] {ECO:0007744|PDB:6ERO, ECO:0007744|PDB:6ERP, ECO:0007744|PDB:6ERQ} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 63-267 AND 295-396 IN COMPLEX RP WITH POLRMT; TFAM AND DNA, SUBUNIT, MUTAGENESIS OF ARG-330 AND ARG-331, RP REGION, AND FUNCTION. RX PubMed=29149603; DOI=10.1016/j.cell.2017.10.036; RA Hillen H.S., Morozov Y.I., Sarfallah A., Temiakov D., Cramer P.; RT "Structural Basis of Mitochondrial Transcription Initiation."; RL Cell 171:1072-1081.e10(2017). RN [13] RP VARIANTS THR-64 AND TYR-264. 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). RN [14] RP VARIANTS PHE-48 AND THR-64. RX PubMed=18980857; DOI=10.1016/j.parkreldis.2008.09.004; RA Sanchez-Ferrero E., Coto E., Blazquez M., Ribacoba R., Guisasola L.M., RA Salvador C., Alvarez V.; RT "Mutational screening of the mitochondrial transcription factors B1 and B2 RT (TFB1M and TFB2M) in Parkinson's disease."; RL Parkinsonism Relat. Disord. 15:468-470(2009). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent rRNA methyltransferase CC which may methylate two specific adjacent adenosines in the loop of a CC conserved hairpin near the 3'-end of 12S mitochondrial rRNA (Probable). CC Component of the mitochondrial transcription initiation complex, CC composed at least of TFB2M, TFAM and POLRMT that is required for basal CC transcription of mitochondrial DNA (PubMed:29149603, PubMed:12068295, CC PubMed:20410300, PubMed:15526033). In this complex, TFAM recruits CC POLRMT to a specific promoter whereas TFB2M induces structural changes CC in POLRMT to enable promoter opening and trapping of the DNA non- CC template strand (PubMed:29149603, PubMed:15526033). Stimulates CC transcription independently of the methyltransferase activity CC (PubMed:12897151). {ECO:0000269|PubMed:12068295, CC ECO:0000269|PubMed:12897151, ECO:0000269|PubMed:15526033, CC ECO:0000269|PubMed:20410300, ECO:0000269|PubMed:29149603, CC ECO:0000305|PubMed:12897151, ECO:0000305|PubMed:17031457}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine in rRNA + S-adenosyl-L-methionine = H(+) + N(6)- CC methyladenosine in rRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:58728, Rhea:RHEA-COMP:15198, Rhea:RHEA-COMP:15199, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; CC Evidence={ECO:0000305|PubMed:17031457}; CC -!- SUBUNIT: Homodimer (PubMed:29149603). Component of the mitochondrial CC transcription initiation complex, composed at least of TFB2M, TFAM and CC POLRMT (PubMed:29149603). In this complex TFAM recruits POLRMT to the CC promoter whereas TFB2M induces structural changes in POLRMT to enable CC promoter opening and trapping of the DNA non-template strand CC (PubMed:29149603). Interacts with mitochondrial RNA polymerase POLRMT CC (PubMed:12068295). Interacts with TFAM (PubMed:12897151). CC {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151, CC ECO:0000269|PubMed:29149603}. CC -!- SUBCELLULAR LOCATION: Mitochondrion. 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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. rRNA adenine N(6)-methyltransferase family. KsgA CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01026}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15441.1; Type=Erroneous initiation; 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; AF529366; AAQ09600.1; -; mRNA. DR EMBL; AK026314; BAB15441.1; ALT_INIT; mRNA. DR EMBL; AK026835; BAB15566.1; -; mRNA. DR EMBL; AL356583; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003383; AAH03383.1; -; mRNA. DR CCDS; CCDS1627.1; -. DR RefSeq; NP_071761.1; NM_022366.2. DR PDB; 6ERO; X-ray; 1.75 A; A/B=63-267, A/B=295-396. DR PDB; 6ERP; X-ray; 4.50 A; F/J=21-396. DR PDB; 6ERQ; X-ray; 4.50 A; F/J=22-396. DR PDBsum; 6ERO; -. DR PDBsum; 6ERP; -. DR PDBsum; 6ERQ; -. DR AlphaFoldDB; Q9H5Q4; -. DR EMDB; EMD-2529; -. DR SMR; Q9H5Q4; -. DR BioGRID; 122106; 113. DR ComplexPortal; CPX-7241; Mitochondrial transcription initiation complex. DR DIP; DIP-50540N; -. DR IntAct; Q9H5Q4; 25. DR MINT; Q9H5Q4; -. DR STRING; 9606.ENSP00000355471; -. DR GlyGen; Q9H5Q4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H5Q4; -. DR MetOSite; Q9H5Q4; -. DR PhosphoSitePlus; Q9H5Q4; -. DR SwissPalm; Q9H5Q4; -. DR BioMuta; TFB2M; -. DR DMDM; 74752681; -. DR EPD; Q9H5Q4; -. DR jPOST; Q9H5Q4; -. DR MassIVE; Q9H5Q4; -. DR MaxQB; Q9H5Q4; -. DR PaxDb; 9606-ENSP00000355471; -. DR PeptideAtlas; Q9H5Q4; -. DR ProteomicsDB; 80926; -. DR Pumba; Q9H5Q4; -. DR Antibodypedia; 34721; 276 antibodies from 29 providers. DR DNASU; 64216; -. DR Ensembl; ENST00000366514.5; ENSP00000355471.4; ENSG00000162851.8. DR GeneID; 64216; -. DR KEGG; hsa:64216; -. DR MANE-Select; ENST00000366514.5; ENSP00000355471.4; NM_022366.3; NP_071761.1. DR UCSC; uc001ibn.4; human. DR AGR; HGNC:18559; -. DR CTD; 64216; -. DR DisGeNET; 64216; -. DR GeneCards; TFB2M; -. DR HGNC; HGNC:18559; TFB2M. DR HPA; ENSG00000162851; Low tissue specificity. DR MIM; 607055; gene. DR neXtProt; NX_Q9H5Q4; -. DR OpenTargets; ENSG00000162851; -. DR PharmGKB; PA38348; -. DR VEuPathDB; HostDB:ENSG00000162851; -. DR eggNOG; KOG0820; Eukaryota. DR GeneTree; ENSGT00950000183142; -. DR HOGENOM; CLU_051778_1_0_1; -. DR InParanoid; Q9H5Q4; -. DR OMA; GRCEMIL; -. DR OrthoDB; 5320952at2759; -. DR PhylomeDB; Q9H5Q4; -. DR TreeFam; TF325100; -. DR PathwayCommons; Q9H5Q4; -. DR Reactome; R-HSA-163282; Mitochondrial transcription initiation. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR SignaLink; Q9H5Q4; -. DR SIGNOR; Q9H5Q4; -. DR BioGRID-ORCS; 64216; 417 hits in 1148 CRISPR screens. DR ChiTaRS; TFB2M; human. DR GeneWiki; TFB2M; -. DR GenomeRNAi; 64216; -. DR Pharos; Q9H5Q4; Tbio. DR PRO; PR:Q9H5Q4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9H5Q4; Protein. DR Bgee; ENSG00000162851; Expressed in secondary oocyte and 192 other cell types or tissues. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0034246; F:mitochondrial transcription factor activity; IDA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central. DR GO; GO:0006390; P:mitochondrial transcription; IDA:GO_Central. DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central. DR GO; GO:0006391; P:transcription initiation at mitochondrial promoter; IDA:UniProtKB. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1. DR PANTHER; PTHR11727:SF13; DIMETHYLADENOSINE TRANSFERASE 2, MITOCHONDRIAL; 1. DR Pfam; PF00398; RrnaAD; 1. DR PIRSF; PIRSF027833; MtTFB2; 1. DR SMART; SM00650; rADc; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1. DR Genevisible; Q9H5Q4; HS. PE 1: Evidence at protein level; KW 3D-structure; Methyltransferase; Mitochondrion; Reference proteome; KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transcription; KW Transcription regulation; Transferase; Transit peptide. FT TRANSIT 1..19 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 20..396 FT /note="Dimethyladenosine transferase 2, mitochondrial" FT /id="PRO_0000273179" FT REGION 44..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 330..331 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:29149603, FT ECO:0007744|PDB:6ERP, ECO:0007744|PDB:6ERQ" FT BINDING 75 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026" FT BINDING 124 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026" FT BINDING 150 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026" FT VARIANT 48 FT /note="S -> F (in dbSNP:rs148620105)" FT /evidence="ECO:0000269|PubMed:18980857" FT /id="VAR_071249" FT VARIANT 64 FT /note="A -> T (in dbSNP:rs143880306)" FT /evidence="ECO:0000269|PubMed:18980857, FT ECO:0000269|PubMed:19096125" FT /id="VAR_071250" FT VARIANT 156 FT /note="P -> L (in dbSNP:rs11585481)" FT /id="VAR_030097" FT VARIANT 264 FT /note="H -> Y (in dbSNP:rs12037377)" FT /evidence="ECO:0000269|PubMed:19096125" FT /id="VAR_030098" FT MUTAGEN 105 FT /note="G->A: Abolishes methyltransferase activity." FT /evidence="ECO:0000269|PubMed:17031457" FT MUTAGEN 330 FT /note="R->A: Impairs transcription initiation; when FT associated with A-331." FT /evidence="ECO:0000269|PubMed:29149603" FT MUTAGEN 331 FT /note="R->A: Impairs transcription initiation; when FT associated with A-330." FT /evidence="ECO:0000269|PubMed:29149603" FT CONFLICT 200..201 FT /note="EK -> GR (in Ref. 2; BAB15441)" FT /evidence="ECO:0000305" FT HELIX 78..89 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 108..115 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 120..125 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 130..139 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 169..176 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 200..213 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 216..220 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 224..230 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 231..237 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 249..257 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 258..267 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 295..303 FT /evidence="ECO:0007829|PDB:6ERO" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:6ERO" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 317..329 FT /evidence="ECO:0007829|PDB:6ERO" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 335..339 FT /evidence="ECO:0007829|PDB:6ERO" FT TURN 340..342 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 347..353 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 362..364 FT /evidence="ECO:0007829|PDB:6ERO" FT HELIX 367..379 FT /evidence="ECO:0007829|PDB:6ERO" SQ SEQUENCE 396 AA; 45349 MW; C13DC398974BB88F CRC64; MWIPVVGLPR RLRLSALAGA GRFCILGSEA ATRKHLPARN HCGLSDSSPQ LWPEPDFRNP PRKASKASLD FKRYVTDRRL AETLAQIYLG KPSRPPHLLL ECNPGPGILT QALLEAGAKV VALESDKTFI PHLESLGKNL DGKLRVIHCD FFKLDPRSGG VIKPPAMSSR GLFKNLGIEA VPWTADIPLK VVGMFPSRGE KRALWKLAYD LYSCTSIYKF GRIEVNMFIG EKEFQKLMAD PGNPDLYHVL SVIWQLACEI KVLHMEPWSS FDIYTRKGPL ENPKRRELLD QLQQKLYLIQ MIPRQNLFTK NLTPMNYNIF FHLLKHCFGR RSATVIDHLR SLTPLDARDI LMQIGKQEDE KVVNMHPQDF KTLFETIERS KDCAYKWLYD ETLEDR //