ID   TRMN6_ECOSM             Reviewed;         245 AA.
AC   B1LP88;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   04-NOV-2026, entry version 95.
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   Name=yfiC {ECO:0000255|HAMAP-Rule:MF_01872};
GN   OrderedLocusNames=EcSMS35_2727;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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 = N(6)-
CC         methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine + H(+);
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; CP000970; ACB15596.1; -; Genomic_DNA.
DR   RefSeq; WP_001295363.1; NC_010498.1.
DR   AlphaFoldDB; B1LP88; -.
DR   SMR; B1LP88; -.
DR   KEGG; ecm:EcSMS35_2727; -.
DR   HOGENOM; CLU_061983_0_0_6; -.
DR   OMA; AACFQFK; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:7770054; F:tRNA(Val) (adenine(37)-N6)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 3.40.50.150:FF:000087; tRNA1(Val) (adenine(37)-N6)-methyltransferase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR050210; tRNA_Adenine-N(6)_MTase.
DR   InterPro; IPR022882; tRNA_adenine-N6_MeTrfase.
DR   NCBIfam; NF047853; tRm6a37MtseTrmN; 1.
DR   PANTHER; PTHR47739; TRNA1(VAL) (ADENINE(37)-N6)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR47739:SF1; TRNA1(VAL) (ADENINE(37)-N6)-METHYLTRANSFERASE; 1.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..245
FT                   /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT                   /id="PRO_0000387362"
SQ   SEQUENCE   245 AA;  27270 MW;  CEB4F1E3A849B7E3 CRC64;
     MSQSTSVLRR NGFTFKQFFV AHDRCAMKVG TDGILLGAWA PVAGVKRCLD IGAGSGLLAL
     MLAQRTDDSV MIDAVELESE AAAQAQENIN QSPWAERINV HTADIQQWIT QQTVRFDLII
     SNPPYYQQGV ECSTPQREQA RYTTTLDHPS LLTCAAECIT EEGFFCVVLP EQIGNGFTEL
     ALSMGWHLRL RTDVAENEAR LPHRVLLAFS PQAGECFSDR LVIRGPDQNY SEAYTALTQA
     FYLFM
//