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   27-MAR-2024, entry version 168.
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; 13.
DR   IntAct; Q8TEA1; 1.
DR   STRING; 9606.ENSP00000366519; -.
DR   ChEMBL; CHEMBL5169179; -.
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; 9606-ENSP00000366519; -.
DR   PeptideAtlas; Q8TEA1; -.
DR   ProteomicsDB; 74429; -.
DR   Pumba; Q8TEA1; -.
DR   Antibodypedia; 25416; 154 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   AGR; HGNC:23529; -.
DR   CTD; 221078; -.
DR   DisGeNET; 221078; -.
DR   GeneCards; NSUN6; -.
DR   HGNC; HGNC:23529; NSUN6.
DR   HPA; ENSG00000241058; Tissue enhanced (liver).
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; 1077100at2759; -.
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 1156 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 147 other cell types or tissues.
DR   ExpressionAtlas; Q8TEA1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016428; F:tRNA (cytidine-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; IDA:FlyBase.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21150; PUA_NSun6-like; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
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; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF34; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE NSUN6; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
DR   Genevisible; Q8TEA1; HS.
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
//