TRMN6_ECOL6
ID TRMN6_ECOL6 Reviewed; 245 AA.
AC Q8FF14;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=c3099;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN81548.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN81548.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000083664.1; NC_004431.1.
DR AlphaFoldDB; Q8FF14; -.
DR SMR; Q8FF14; -.
DR STRING; 199310.c3099; -.
DR EnsemblBacteria; AAN81548; AAN81548; c3099.
DR KEGG; ecc:c3099; -.
DR eggNOG; COG4123; Bacteria.
DR HOGENOM; CLU_061983_0_0_6; -.
DR Proteomes; UP000001410; 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; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..245
FT /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT /id="PRO_0000387372"
SQ SEQUENCE 245 AA; 27273 MW; 0EEFA66A800C1745 CRC64;
MSQSTSVFRR NGFTFKQFFV AHDRCAMKVG TDGILLGAWA PVAGVKRCLD IGAGSGLLAL
MLAQRTDDSV MIDAVELESE AAAQAQENIN QSPWAERINV HTADILQWIT QQTVRFDLII
SNPPYYQQGV ECATPQREQA RYTTTLDHPS LLTCAAECIT EEGFFCVVLP EQIGNGFTEL
ALSMGWHLRL RTDVAENEAR LPHRVLLAFS PQAGECFSDR LVIRGPDQNY SEAYTALTQA
FYLFM