ID   TRMN6_FLAB3             Reviewed;         231 AA.
AC   C6X2D2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=FIC_02159;
OS   Flavobacteriaceae bacterium (strain 3519-10).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=531844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3519-10;
RX   PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA   Raymond J.A., Christner B.C., Schuster S.C.;
RT   "A bacterial ice-binding protein from the Vostok ice core.";
RL   Extremophiles 12:713-717(2008).
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; CP001673; ACU08595.1; -; Genomic_DNA.
DR   RefSeq; WP_015806879.1; NC_013062.1.
DR   AlphaFoldDB; C6X2D2; -.
DR   SMR; C6X2D2; -.
DR   STRING; 531844.FIC_02159; -.
DR   EnsemblBacteria; ACU08595; ACU08595; FIC_02159.
DR   KEGG; fba:FIC_02159; -.
DR   eggNOG; COG4123; Bacteria.
DR   HOGENOM; CLU_061983_0_0_10; -.
DR   OMA; NQYTEAF; -.
DR   OrthoDB; 1027015at2; -.
DR   Proteomes; UP000001512; Chromosome.
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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..231
FT                   /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT                   /id="PRO_0000387379"
SQ   SEQUENCE   231 AA;  26032 MW;  F9DC5679B3A4077B CRC64;
     MKPFRFKKFT VQQHKEVFRV GTDGVLLGAL ADVSDAKNIL EVGTGTGLVA LMTAQRNPTS
     NITAIDVNPV AAELAAKNFL ESHFGHRMRA MHCDYKTFGT QKKFDLIISN PPYFETNPSE
     KDATARQQRE LSFKTLISKT AEILATEGRF CVIIPFPAGP TFEKTCEENK LFLLRRITVY
     GNANVEPKRL ILEFSSNKNI SVSEEIFVTE KAPRVYSEQY LKATADFHEF E