TRMN6_BACTN
ID TRMN6_BACTN Reviewed; 237 AA.
AC Q8A9H7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=BT_0838;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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=AAO75945.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015928; AAO75945.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_809751.1; NC_004663.1.
DR RefSeq; WP_048692148.1; NZ_UYXG01000019.1.
DR AlphaFoldDB; Q8A9H7; -.
DR SMR; Q8A9H7; -.
DR STRING; 226186.BT_0838; -.
DR PaxDb; Q8A9H7; -.
DR PRIDE; Q8A9H7; -.
DR EnsemblBacteria; AAO75945; AAO75945; BT_0838.
DR GeneID; 60926807; -.
DR KEGG; bth:BT_0838; -.
DR PATRIC; fig|226186.12.peg.855; -.
DR eggNOG; COG4123; Bacteria.
DR HOGENOM; CLU_061983_0_0_10; -.
DR InParanoid; Q8A9H7; -.
DR Proteomes; UP000001414; 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..237
FT /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT /id="PRO_0000387343"
SQ SEQUENCE 237 AA; 26748 MW; 8DD5E8AEDAEA9C48 CRC64;
MANPFFQFKQ FTVWHDKCAM KVGTDGVLLG AWASVQGAHR ILDIGTGTGL VALMLAQRSL
PDANIVALEI DEAAAGQAKE NVARSPWKDR IEVVKQDFLF YQSPDKFDVI VSNPPYFVDS
LSCPDQQRSM ARHNDSLTYE KLLKGVADLL KKEGTFTIVI PTDVADRVKT AASEYHLYAT
RQLNVITKPG GTPKRMLITF TFNNEGCIKE ELLTEVARHQ YSEEYKELTR EYYLHLK