ID A0A1M4SW19_9BACE Unreviewed; 236 AA.
AC A0A1M4SW19;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=tRNA1(Val) (adenine(37)-N6)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01872};
DE EC=2.1.1.223 {ECO:0000256|HAMAP-Rule:MF_01872};
DE AltName: Full=tRNA m6A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01872};
GN ORFNames=SAMN05444405_101212 {ECO:0000313|EMBL:SHE36424.1};
OS Bacteroides luti.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHE36424.1, ECO:0000313|Proteomes:UP000184509};
RN [1] {ECO:0000313|EMBL:SHE36424.1, ECO:0000313|Proteomes:UP000184509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26991 {ECO:0000313|EMBL:SHE36424.1,
RC ECO:0000313|Proteomes:UP000184509};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the adenine in position 37 of
CC tRNA(1)(Val) (anticodon cmo5UAC). {ECO:0000256|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:0000256|HAMAP-Rule:MF_01872};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01872}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. tRNA
CC (adenine-N(6)-)-methyltransferase family. {ECO:0000256|HAMAP-
CC Rule:MF_01872}.
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DR EMBL; FQTV01000001; SHE36424.1; -; Genomic_DNA.
DR RefSeq; WP_073398654.1; NZ_FQTV01000001.1.
DR AlphaFoldDB; A0A1M4SW19; -.
DR STRING; 1297750.SAMN05444405_101212; -.
DR OrthoDB; 5383291at2; -.
DR Proteomes; UP000184509; Unassembled WGS sequence.
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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR47739; TRNA1(VAL) (ADENINE(37)-N6)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR47739:SF1; TRNA1(VAL) (ADENINE(37)-N6)-METHYLTRANSFERASE; 1.
DR Pfam; PF05175; MTS; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01872};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01872,
KW ECO:0000313|EMBL:SHE36424.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184509};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01872};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01872}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01872}.
FT DOMAIN 37..158
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 236 AA; 26629 MW; D9EB9B6938DD3AB3 CRC64;
MPNPYFSFKQ FTVWHDKCAM KVGTDGVLLG AWTDVSNANS VLDIGTGTGL VALMIAQRCN
ADIFAIEIDN NAVIQATDNK NRSPWSERIS IIQGDFKTFE SNTKFDVIVS NPPYFSNSLL
PPDIKRSTAR HTNELSYYEL IEGAAELLSP RGKFSLIIPA DVIDKIIEIA ANFDLYPIRQ
TNILPKQDSS PKRVLISFSN KKDTIFAKPN DLIIELARHQ YTPEYIDLTK EYYLNM
//
