ID   TRMY_HALVD              Reviewed;         198 AA.
AC   D4GTL8;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
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=HVO_1989;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=22274954; DOI=10.1261/rna.028498.111;
RA   Wurm J.P., Griese M., Bahr U., Held M., Heckel A., Karas M., Soppa J.,
RA   Woehnert J.;
RT   "Identification of the enzyme responsible for N1-methylation of
RT   pseudouridine 54 in archaeal tRNAs.";
RL   RNA 18:412-420(2012).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND GENE NAME.
RX   PubMed=22274953; DOI=10.1261/rna.030841.111;
RA   Chatterjee K., Blaby I.K., Thiaville P.C., Majumder M., Grosjean H.,
RA   Yuan Y.A., Gupta R., de Crecy-Lagard V.;
RT   "The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with
RT   pseudouridine synthase Pus10, catalyze the formation of 1-
RT   methylpseudouridine at position 54 of tRNA.";
RL   RNA 18:421-433(2012).
CC   -!- FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at
CC       position 54 (Psi54) in tRNAs. {ECO:0000255|HAMAP-Rule:MF_00587,
CC       ECO:0000269|PubMed:22274953, ECO:0000269|PubMed:22274954}.
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         ECO:0000269|PubMed:22274953, ECO:0000269|PubMed:22274954};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- DISRUPTION PHENOTYPE: Deletion leads to the absence of 1-
CC       methylpseudouridine at position 54 of tRNA, but does not lead to any
CC       obvious phenotype. {ECO:0000269|PubMed:22274953,
CC       ECO:0000269|PubMed:22274954}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.
CC       {ECO:0000255|HAMAP-Rule:MF_00587}.
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DR   EMBL; CP001956; ADE02260.1; -; Genomic_DNA.
DR   RefSeq; WP_004041871.1; NZ_AOHU01000038.1.
DR   AlphaFoldDB; D4GTL8; -.
DR   SMR; D4GTL8; -.
DR   STRING; 309800.C498_05231; -.
DR   EnsemblBacteria; ADE02260; ADE02260; HVO_1989.
DR   GeneID; 8926438; -.
DR   KEGG; hvo:HVO_1989; -.
DR   eggNOG; arCOG01239; Archaea.
DR   HOGENOM; CLU_107018_0_0_2; -.
DR   OMA; HADHCII; -.
DR   OrthoDB; 126445at2157; -.
DR   BRENDA; 2.1.1.257; 2561.
DR   Proteomes; UP000008243; 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; IMP:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; IMP:UniProtKB.
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   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..198
FT                   /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT                   /id="PRO_0000416524"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ   SEQUENCE   198 AA;  21946 MW;  0204035BBD28A769 CRC64;
     MRQFIVTGHD APTTPDFSLD DIAGGAGRLD VLCRCVNSAF FLSHDIREDV RVHLVLGDEY
     TVRFEGSELR RLNPDERSTA ALIRKALEKR EEAIGHMPAE SSPGVSIRRM GFETTLEEAA
     SDATVVELHE DGDPVVQVEP PENPLFVLSD HHDFTDEEAE LLAAAADERV RLGPEILHAD
     HSITVAHNYL DTAGYSRY