ID   TRMN6_PECCP             Reviewed;         248 AA.
AC   C6DC08;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=PC1_3079;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT14102.1; -; Genomic_DNA.
DR   RefSeq; WP_015841250.1; NC_012917.1.
DR   AlphaFoldDB; C6DC08; -.
DR   SMR; C6DC08; -.
DR   STRING; 561230.PC1_3079; -.
DR   EnsemblBacteria; ACT14102; ACT14102; PC1_3079.
DR   KEGG; pct:PC1_3079; -.
DR   eggNOG; COG4123; Bacteria.
DR   HOGENOM; CLU_061983_0_0_6; -.
DR   OMA; NQYTEAF; -.
DR   OrthoDB; 1027015at2; -.
DR   Proteomes; UP000002736; 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..248
FT                   /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT                   /id="PRO_0000387394"
SQ   SEQUENCE   248 AA;  27882 MW;  6BE6952426CC8575 CRC64;
     MSHQADNKLT LRRDGFTFKQ FFVAHDRCAM KVGTDGILLG AWAPLSSVTR ILDIGSGSGL
     LALMLAQRSD THVRIDAVEL DSAASQQAKE NISASPWADR IAVYAEDIID FADTRSADYS
     LIISNPPYFP PGIACGSAER EQARYTTLLT HETLLRCAHQ LLMPDGLFCV VLPIQVAENF
     IPLAQQHNWY VHQQLRVSEQ EDKPAHRVLL ALSRQKKECV NASLAIRDEE RRYSTAFQQL
     TKDFYLFM