ID TRMY_ARCFU Reviewed; 288 AA. AC O29206; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 24-JAN-2024, entry version 102. DE RecName: Full=tRNA (pseudouridine(54)-N(1))-methyltransferase; DE EC=2.1.1.257; GN Name=trmY; OrderedLocusNames=AF_1056; OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC OS 100126 / VC-16). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; OC Archaeoglobus. OX NCBI_TaxID=224325; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16; RX PubMed=9389475; DOI=10.1038/37052; RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., RA Smith H.O., Woese C.R., Venter J.C.; RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing RT archaeon Archaeoglobus fulgidus."; RL Nature 390:364-370(1997). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 95-288 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE. RG Midwest center for structural genomics (MCSG); RT "Crystal structure of APC86534.1."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at CC position 54 (Psi54) in tRNAs. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) + CC N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:55292, Rhea:RHEA-COMP:14140, Rhea:RHEA-COMP:14141, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:65314, ChEBI:CHEBI:74890; EC=2.1.1.257; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family. CC {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; AE000782; AAB90184.1; -; Genomic_DNA. DR PIR; H69381; H69381. DR PDB; 2QMM; X-ray; 1.85 A; A/B=95-288. DR PDBsum; 2QMM; -. DR AlphaFoldDB; O29206; -. DR SMR; O29206; -. DR STRING; 224325.AF_1056; -. DR PaxDb; 224325-AF_1056; -. DR EnsemblBacteria; AAB90184; AAB90184; AF_1056. DR KEGG; afu:AF_1056; -. DR eggNOG; arCOG01239; Archaea. DR HOGENOM; CLU_965053_0_0_2; -. DR PhylomeDB; O29206; -. DR EvolutionaryTrace; O29206; -. DR Proteomes; UP000002199; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule. DR CDD; cd18087; TrmY-like; 1. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00587; tRNA_methyltr_TrmY; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR007158; TrmY. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR PANTHER; PTHR40703; TRNA (PSEUDOURIDINE(54)-N(1))-METHYLTRANSFERASE; 1. DR PANTHER; PTHR40703:SF1; TRNA (PSEUDOURIDINE(54)-N(1))-METHYLTRANSFERASE; 1. DR Pfam; PF04013; Methyltrn_RNA_2; 1. DR SUPFAM; SSF75217; alpha/beta knot; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1..288 FT /note="tRNA (pseudouridine(54)-N(1))-methyltransferase" FT /id="PRO_0000157945" FT REGION 1..94 FT /note="Unknown" FT REGION 95..288 FT /note="Methyltransferase" FT BINDING 221..223 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 242 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|Ref.2" FT BINDING 265..270 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 275 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|Ref.2" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:2QMM" FT TURN 115..119 FT /evidence="ECO:0007829|PDB:2QMM" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 142..148 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:2QMM" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:2QMM" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:2QMM" FT HELIX 205..215 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:2QMM" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 235..242 FT /evidence="ECO:0007829|PDB:2QMM" FT HELIX 249..256 FT /evidence="ECO:0007829|PDB:2QMM" FT STRAND 260..264 FT /evidence="ECO:0007829|PDB:2QMM" FT HELIX 272..287 FT /evidence="ECO:0007829|PDB:2QMM" SQ SEQUENCE 288 AA; 32192 MW; 02CD364BC26A45A8 CRC64; MENPDSAFLL FRNAPRLPLA TMHTPLCGDS HQPDFAFRKP ARDALLRPWN GRNHRCGLQD GREICQGQLP AHQKSYWSDC AALPRLFRAY GGAVVRGFLI VGNKAFTQPF SLNDLPGAGR MDVLCRCTSQ ALFISHGIRR DVEVYLLLLG PPSPPKSILI KGDEVRRMSP DERNVAGHIK KALAVECGKS WKKVHSGVYV SRKGLEELIE ELSEKYSIIY LKEDGVDISN AQLPPNPLFV IGDHEGLTEE QEKVVERYAA LKLSLSPLSL LAEQCVVIAH HHLDRLQF //