TRMN6_ECO5T
ID TRMN6_ECO5T Reviewed; 245 AA.
AC C6UQY1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=ECSP_3521;
OS Escherichia coli O157:H7 (strain TW14359 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=544404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW14359 / EHEC;
RX PubMed=19564389; DOI=10.1128/iai.00198-09;
RA Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C.,
RA Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H.,
RA Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K.,
RA Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.;
RT "Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-
RT associated outbreak isolate indicates candidate genes that may enhance
RT virulence.";
RL Infect. Immun. 77:3713-3721(2009).
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; CP001368; ACT73287.1; -; Genomic_DNA.
DR RefSeq; WP_000083666.1; NC_013008.1.
DR AlphaFoldDB; C6UQY1; -.
DR SMR; C6UQY1; -.
DR KEGG; etw:ECSP_3521; -.
DR HOGENOM; CLU_061983_0_0_6; -.
DR OMA; NQYTEAF; -.
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_0000387368"
SQ SEQUENCE 245 AA; 27215 MW; 4E79CA35A7CE03EB CRC64;
MSQSTSVLRR NGFTFKQFFV AHDRCAMKAG TDGILLGAWA PVAGVKRCLD IGAGSGLLAL
MLAQRTSDSV IIDAVELESE AATQAQENVA QSPWLERINV HTADIQQWVT QQTARFDLII
SNPPYYEQGV ECATPQREQA RYTTSLDHQT LLTCAAECIT EEGFFCVVLP EQIGNSFTEL
ALSMGWHLRL RTDVAENEAR LPHRVLLAFS PQAGECFSDR LVIRGPDQNY SEAYTALTQA
FYLFM