TRMY_ARCFU
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 03-AUG-2022, entry version 98.
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}.
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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 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 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; PTHR40703; 1.
DR Pfam; PF04013; Methyltrn_RNA_2; 1.
DR SUPFAM; SSF75217; SSF75217; 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
