ID   TRMN6_HISS2             Reviewed;         236 AA.
AC   B0UWL8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=HSM_0322;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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; CP000947; ACA31955.1; -; Genomic_DNA.
DR   RefSeq; WP_012341184.1; NC_010519.1.
DR   AlphaFoldDB; B0UWL8; -.
DR   SMR; B0UWL8; -.
DR   STRING; 228400.HSM_0322; -.
DR   EnsemblBacteria; ACA31955; ACA31955; HSM_0322.
DR   KEGG; hsm:HSM_0322; -.
DR   HOGENOM; CLU_061983_0_0_6; -.
DR   OMA; NQYTEAF; -.
DR   OrthoDB; 1027015at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..236
FT                   /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT                   /id="PRO_0000387388"
SQ   SEQUENCE   236 AA;  27012 MW;  9A31FE2F08D576A2 CRC64;
     MAKKQEFTFK QFHINQDQCA MKVGTDGILL GAWANINQAN TLLDLGTGTG LIALMLAQRS
     PEHCQISAVE LDQLAYLQAK DNIQQSPWAN KIKIFQQDII VFAQDCEHKF DVITANPPYF
     KQGVDCASKQ RNLARYTLTQ SHLDWLNAAE KLLNLTGEIH LILPFEEGKS LQKKCGLFCI
     RECKIITKAG KTPQRLLLSF SREERKCEES QLVIYDRNNQ YSTEFKTLTQ DFYLNF