NSUN6_HUMAN
ID NSUN6_HUMAN Reviewed; 469 AA.
AC Q8TEA1; B0YJ54;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=tRNA (cytosine(72)-C(5))-methyltransferase NSUN6 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:26160102, ECO:0000269|PubMed:27703015, ECO:0000269|PubMed:28531330};
DE AltName: Full=NOL1/NOP2/Sun and PUA domain-containing protein 1;
DE AltName: Full=NOL1/NOP2/Sun domain family member 6;
GN Name=NSUN6 {ECO:0000312|HGNC:HGNC:23529}; Synonyms=NOPD1;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-419, 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 [7]
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 [8]
RP MUTAGENESIS OF CYS-373, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=26160102; DOI=10.1261/rna.051524.115;
RA Haag S., Warda A.S., Kretschmer J., Guennigmann M.A., Hoebartner C.,
RA Bohnsack M.T.;
RT "NSUN6 is a human RNA methyltransferase that catalyzes formation of m5C72
RT in specific tRNAs.";
RL RNA 21:1532-1543(2015).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27703015; DOI=10.1074/jbc.m116.742569;
RA Long T., Li J., Li H., Zhou M., Zhou X.L., Liu R.J., Wang E.D.;
RT "Sequence-specific and Shape-selective RNA Recognition by the Human RNA 5-
RT Methylcytosine Methyltransferase NSun6.";
RL J. Biol. Chem. 291:24293-24303(2016).
RN [10] {ECO:0007744|PDB:5WWQ, ECO:0007744|PDB:5WWR, ECO:0007744|PDB:5WWS, ECO:0007744|PDB:5WWT}
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH TRNA AND
RP S-ADENOSYL-L-METHIONINE, DOMAIN, MUTAGENESIS OF ARG-126; TYR-131; LYS-159;
RP LYS-160; ARG-181; LEU-218; ASN-220; SER-223; LYS-248; ASP-266; LYS-271;
RP ASP-293; ASP-323 AND PHE-458, S-ADENOSYL-L-METHIONINE BINDING, ACTIVE SITE,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28531330; DOI=10.1093/nar/gkx473;
RA Liu R.J., Long T., Li J., Li H., Wang E.D.;
RT "Structural basis for substrate binding and catalytic mechanism of a human
RT RNA:m5C methyltransferase NSun6.";
RL Nucleic Acids Res. 45:6684-6697(2017).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the C5 position of cytosine 72 in
CC tRNA(Thr)(TGT) and tRNA(Cys)(GCA) (PubMed:26160102, PubMed:27703015,
CC PubMed:28531330). In vitro also methylates tRNA(Thr)(AGT)
CC (PubMed:27703015, PubMed:26160102). Methylation requires, in the
CC acceptor stem region, the presence of the 3'-CCA terminus, the target
CC site C72, the discriminator base U73, and the second and third base
CC pairs (2:71 and 3:70) in the tRNA substrates (PubMed:26160102,
CC PubMed:27703015). {ECO:0000269|PubMed:26160102,
CC ECO:0000269|PubMed:27703015, ECO:0000269|PubMed:28531330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(72) in tRNA(Thr) + S-adenosyl-L-methionine = 5-
CC methylcytidine(72) in tRNA(Thr) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:21124, Rhea:RHEA-COMP:15877, Rhea:RHEA-COMP:15878,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:26160102, ECO:0000269|PubMed:27703015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21125;
CC Evidence={ECO:0000269|PubMed:26160102, ECO:0000269|PubMed:27703015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(72) in tRNA(Cys) + S-adenosyl-L-methionine = 5-
CC methylcytidine(72) in tRNA(Cys) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61584, Rhea:RHEA-COMP:15875, Rhea:RHEA-COMP:15876,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:26160102, ECO:0000269|PubMed:27703015,
CC ECO:0000269|PubMed:28531330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61585;
CC Evidence={ECO:0000269|PubMed:26160102, ECO:0000269|PubMed:27703015,
CC ECO:0000269|PubMed:28531330};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.02 uM for tRNA(Thr)(TGT) {ECO:0000269|PubMed:27703015};
CC KM=1.58 uM for tRNA(Thr)(AGT) {ECO:0000269|PubMed:27703015};
CC KM=0.89 uM for tRNA(Cys)(GCA) {ECO:0000269|PubMed:27703015};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26160102}.
CC -!- DOMAIN: The PUA domain plays a role in tRNA recognition through
CC precisely recognizing the CCA end and the D-stem region of tRNA.
CC {ECO:0000269|PubMed:28531330}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; AK074323; BAB85051.1; -; mRNA.
DR EMBL; EF445003; ACA06032.1; -; Genomic_DNA.
DR EMBL; EF445003; ACA06033.1; -; Genomic_DNA.
DR EMBL; AL512641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86191.1; -; Genomic_DNA.
DR EMBL; BC035778; AAH35778.1; -; mRNA.
DR CCDS; CCDS7130.1; -.
DR RefSeq; NP_872349.1; NM_182543.3.
DR PDB; 5WWQ; X-ray; 2.81 A; A/B=1-469.
DR PDB; 5WWR; X-ray; 3.10 A; A/B=1-469.
DR PDB; 5WWS; X-ray; 3.25 A; A/B=1-469.
DR PDB; 5WWT; X-ray; 3.20 A; A/B=1-469.
DR PDBsum; 5WWQ; -.
DR PDBsum; 5WWR; -.
DR PDBsum; 5WWS; -.
DR PDBsum; 5WWT; -.
DR AlphaFoldDB; Q8TEA1; -.
DR SMR; Q8TEA1; -.
DR BioGRID; 128682; 6.
DR IntAct; Q8TEA1; 1.
DR STRING; 9606.ENSP00000366519; -.
DR CarbonylDB; Q8TEA1; -.
DR iPTMnet; Q8TEA1; -.
DR PhosphoSitePlus; Q8TEA1; -.
DR SwissPalm; Q8TEA1; -.
DR BioMuta; NSUN6; -.
DR DMDM; 74751440; -.
DR EPD; Q8TEA1; -.
DR jPOST; Q8TEA1; -.
DR MassIVE; Q8TEA1; -.
DR MaxQB; Q8TEA1; -.
DR PaxDb; Q8TEA1; -.
DR PeptideAtlas; Q8TEA1; -.
DR PRIDE; Q8TEA1; -.
DR ProteomicsDB; 74429; -.
DR Antibodypedia; 25416; 135 antibodies from 25 providers.
DR DNASU; 221078; -.
DR Ensembl; ENST00000377304.7; ENSP00000366519.4; ENSG00000241058.4.
DR GeneID; 221078; -.
DR KEGG; hsa:221078; -.
DR MANE-Select; ENST00000377304.7; ENSP00000366519.4; NM_182543.5; NP_872349.1.
DR UCSC; uc010qcp.2; human.
DR CTD; 221078; -.
DR DisGeNET; 221078; -.
DR GeneCards; NSUN6; -.
DR HGNC; HGNC:23529; NSUN6.
DR HPA; ENSG00000241058; Tissue enhanced (liver).
DR MalaCards; NSUN6; -.
DR neXtProt; NX_Q8TEA1; -.
DR OpenTargets; ENSG00000241058; -.
DR PharmGKB; PA134986220; -.
DR VEuPathDB; HostDB:ENSG00000241058; -.
DR eggNOG; KOG1122; Eukaryota.
DR GeneTree; ENSGT00940000155370; -.
DR HOGENOM; CLU_005316_1_1_1; -.
DR InParanoid; Q8TEA1; -.
DR OMA; YQGAMLY; -.
DR OrthoDB; 1040075at2759; -.
DR PhylomeDB; Q8TEA1; -.
DR TreeFam; TF324225; -.
DR BRENDA; 2.1.1.202; 2681.
DR PathwayCommons; Q8TEA1; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q8TEA1; -.
DR BioGRID-ORCS; 221078; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; NSUN6; human.
DR GenomeRNAi; 221078; -.
DR Pharos; Q8TEA1; Tbio.
DR PRO; PR:Q8TEA1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8TEA1; protein.
DR Bgee; ENSG00000241058; Expressed in oviduct epithelium and 145 other tissues.
DR ExpressionAtlas; Q8TEA1; baseline and differential.
DR Genevisible; Q8TEA1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0002946; P:tRNA C5-cytosine methylation; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Methyltransferase;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..469
FT /note="tRNA (cytosine(72)-C(5))-methyltransferase NSUN6"
FT /id="PRO_0000263114"
FT DOMAIN 111..203
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000269|PubMed:28531330, ECO:0007744|PDB:5WWS"
FT BINDING 242..248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000269|PubMed:28531330, ECO:0007744|PDB:5WWS"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000269|PubMed:28531330, ECO:0007744|PDB:5WWS"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000269|PubMed:28531330, ECO:0007744|PDB:5WWS"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 126
FT /note="R->A: Decreases substantially tRNA methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 131
FT /note="Y->A: Abolishes methylation of tRNA (Cys)."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 159
FT /note="K->A: Decreases tRNA methyltransferase activiry.
FT Abolishes tRNA methyltransferase activiry; when associated
FT with A-181."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 160
FT /note="K->A: Decreases tRNA methyltransferase activiry.
FT Abolishes tRNA methyltransferase activiry; when associated
FT with A-181."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 181
FT /note="R->A: Decreases subtantially tRNA methyltransferase
FT activiry."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 218
FT /note="L->A: Decreases substantially tRNA methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 220
FT /note="N->A: Decreases substantially tRNA methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 223
FT /note="S->A: Dose not affect tRNA methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 248
FT /note="K->A: Abolishes tRNA methyltransferase activity.
FT Does not affect S-Adenosylmethionine binding."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 266
FT /note="D->A: Loss of S-Adenosylmethionine binding. Loss of
FT tRNA methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 271
FT /note="K->A: Loss of S-Adenosylmethionine binding. Loss of
FT tRNA methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 293
FT /note="D->A: Loss of S-Adenosylmethionine binding. Loss of
FT tRNA methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 323
FT /note="D->A: Abolishes tRNA methyltransferase activity.
FT Abolishes S-Adenosylmethionine binding."
FT /evidence="ECO:0000269|PubMed:28531330"
FT MUTAGEN 373
FT /note="C->A: Does not impair target RNA binding. Abolishes
FT tRNA (cytosine-5-)-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26160102,
FT ECO:0000269|PubMed:28531330"
FT MUTAGEN 458
FT /note="F->A: Abolishes tRNA methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28531330"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5WWQ"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:5WWQ"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5WWQ"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5WWQ"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5WWS"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:5WWQ"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5WWR"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 362..373
FT /evidence="ECO:0007829|PDB:5WWQ"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 415..419
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:5WWQ"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:5WWR"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:5WWQ"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:5WWQ"
SQ SEQUENCE 469 AA; 51770 MW; EB6D383915547CF6 CRC64;
MSIFPKISLR PEVENYLKEG FMNKEIVTAL GKQEAERKFE TLLKHLSHPP SFTTVRVNTH
LASVQHVKNL LLDELQKQFN GLSVPILQHP DLQDVLLIPV IGPRKNIKKQ QCEAIVGAQC
GNAVLRGAHV YAPGIVSASQ FMKAGDVISV YSDIKGKCKK GAKEFDGTKV FLGNGISELS
RKEIFSGLPE LKGMGIRMTE PVYLSPSFDS VLPRYLFLQN LPSALVSHVL NPQPGEKILD
LCAAPGGKTT HIAALMHDQG EVIALDKIFN KVEKIKQNAL LLGLNSIRAF CFDGTKAVKL
DMVEDTEGEP PFLPESFDRI LLDAPCSGMG QRPNMACTWS VKEVASYQPL QRKLFTAAVQ
LLKPEGVLVY STCTITLAEN EEQVAWALTK FPCLQLQPQE PQIGGEGMRG AGLSCEQLKQ
LQRFDPSAVP LPDTDMDSLR EARREDMLRL ANKDSIGFFI AKFVKCKST
