TRMN6_PROMH
ID TRMN6_PROMH Reviewed; 252 AA.
AC B4F055;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=PMI1896;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(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; AM942759; CAR43937.1; -; Genomic_DNA.
DR RefSeq; WP_012368142.1; NC_010554.1.
DR AlphaFoldDB; B4F055; -.
DR SMR; B4F055; -.
DR STRING; 529507.PMI1896; -.
DR EnsemblBacteria; CAR43937; CAR43937; PMI1896.
DR GeneID; 6802808; -.
DR KEGG; pmr:PMI1896; -.
DR PATRIC; fig|529507.6.peg.1848; -.
DR eggNOG; COG4123; Bacteria.
DR HOGENOM; CLU_061983_0_0_6; -.
DR OMA; NQYTEAF; -.
DR Proteomes; UP000008319; 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..252
FT /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT /id="PRO_0000387400"
SQ SEQUENCE 252 AA; 28864 MW; B3001C0E18C23175 CRC64;
MKQKKVKKAG LRKGGFTFKQ FFVAHDKCEM KVGTDGVLLG AWAPITKAKT VLDIGTGSGL
IALMLAQRAP QVERIDGIEL DEDAALQASE NAQQSQWSSL IHIYHHDIYQ YAQQAPTRYD
LIVSNPPYFE PAVACRNQER EQARYTKTLT HEGLLDSAQQ LITDEGLFCV VLPYLIGEQF
IEISQRKGWN VVQRVNIKDS ADKPYHRILL AFQRQYQGET KPCNIEELII RNNDGHYTTQ
FQSWVTDFYL YY