TRMY_HALLT
ID TRMY_HALLT Reviewed; 207 AA.
AC B9LP86;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=Hlac_1588;
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
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; CP001365; ACM57174.1; -; Genomic_DNA.
DR RefSeq; WP_015910314.1; NC_012029.1.
DR AlphaFoldDB; B9LP86; -.
DR SMR; B9LP86; -.
DR STRING; 416348.Hlac_1588; -.
DR EnsemblBacteria; ACM57174; ACM57174; Hlac_1588.
DR GeneID; 7399536; -.
DR KEGG; hla:Hlac_1588; -.
DR eggNOG; arCOG01239; Archaea.
DR HOGENOM; CLU_107018_0_0_2; -.
DR OMA; HADHCII; -.
DR Proteomes; UP000000740; Chromosome 1.
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; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..207
FT /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT /id="PRO_1000197959"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ SEQUENCE 207 AA; 22599 MW; D186CEBC8168D0AA CRC64;
MRQFVVIGHD VPTDPDAISL SDIPGAGRLD LLCRCVAAGV FLSHGIRERV RVHLVVADEF
TVTFDADSLR HLHPDERNVA ARIRDALDAQ DDAIGHMPAD VSPGVELRRM GLEATLDRVL
DTPGTSSASA DPTLVQLHED GDPLVDAAPP TDPVFVLSDH NDFAPAERDL LADRAERRVR
VGPELLHADH TVSVVHNWLD TDGYESY
