TRMY_METKA
ID TRMY_METKA Reviewed; 203 AA.
AC Q8TWL5;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=tRNA (pseudouridine(54)-N(1))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00587};
DE EC=2.1.1.257 {ECO:0000255|HAMAP-Rule:MF_00587};
GN Name=trmY {ECO:0000255|HAMAP-Rule:MF_00587}; OrderedLocusNames=MK1018;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC -!- FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at
CC position 54 (Psi54) in tRNAs. {ECO:0000255|HAMAP-Rule:MF_00587}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00587};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00587}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.
CC {ECO:0000255|HAMAP-Rule:MF_00587}.
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DR EMBL; AE009439; AAM02231.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TWL5; -.
DR SMR; Q8TWL5; -.
DR STRING; 190192.MK1018; -.
DR EnsemblBacteria; AAM02231; AAM02231; MK1018.
DR KEGG; mka:MK1018; -.
DR HOGENOM; CLU_107018_0_0_2; -.
DR OMA; HADHCII; -.
DR Proteomes; UP000001826; 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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..203
FT /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT /id="PRO_0000157949"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT BINDING 179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ SEQUENCE 203 AA; 23033 MW; C292AB7DCE66BBBF CRC64;
MREFLVLFNH APTSPDRVRL KDLPGSGRFD LVCRVTTQAL LYSHGVRTDT VVHLLLRGPD
DPPKTITVTG RRVRRLYPDE RTTAIHLRRA LEADPDTEPH PGIFVRRADL EDLLGEMKGA
KLYYLSEDGR DLEEVEPEPD AVFVLGDHEG PTPEQDRLLR RHADAVISLG PIPYHADQCI
VILHRYLDVK RPPEYAHGPS NVM
