ID   TRMN6_ALIFM             Reviewed;         234 AA.
AC   B5F9T8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=tRNA1(Val) (adenine(37)-N6)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01872};
DE            EC=2.1.1.223 {ECO:0000255|HAMAP-Rule:MF_01872};
DE   AltName: Full=tRNA m6A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01872};
GN   OrderedLocusNames=VFMJ11_0445;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the adenine in position 37 of
CC       tRNA(1)(Val) (anticodon cmo5UAC). {ECO:0000255|HAMAP-Rule:MF_01872}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43160, Rhea:RHEA-COMP:10369, Rhea:RHEA-COMP:10370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.223;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01872};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01872}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. tRNA
CC       (adenine-N(6)-)-methyltransferase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01872}.
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DR   EMBL; CP001139; ACH65486.1; -; Genomic_DNA.
DR   RefSeq; WP_012533086.1; NC_011184.1.
DR   AlphaFoldDB; B5F9T8; -.
DR   SMR; B5F9T8; -.
DR   EnsemblBacteria; ACH65486; ACH65486; VFMJ11_0445.
DR   KEGG; vfm:VFMJ11_0445; -.
DR   HOGENOM; CLU_061983_0_0_6; -.
DR   OMA; NQYTEAF; -.
DR   Proteomes; UP000001857; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016430; F:tRNA (adenine-N6-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01872; tRNA_methyltr_YfiC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   InterPro; IPR022882; tRNA_adenine-N6_MeTrfase.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..234
FT                   /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT                   /id="PRO_0000387444"
SQ   SEQUENCE   234 AA;  26236 MW;  0D81DED3E8E30392 CRC64;
     MSKSFTFKQF HIDIGSCGMP VSTDGVLLGA WTNISECSQI LDIGAGTGLL SLMSAQRNSN
     AHIDAIELMP IAAEVARLNF SQSPWKERLV LIHQDFLSYQ TAYEYDAIIC NPPYFNNGEQ
     SLKGERSTAR HTDSLPFDKL LQHCKTLISS TGRASFILPV FEGEIFIKIA KGCDFHLTKI
     TKVKTTEKKS PTRLLIELSL FPHIYQESTL TIHDGNGYSD DFIKLTRMFY LNMG