TRMN6_SHESA
ID TRMN6_SHESA Reviewed; 241 AA.
AC A0L0I8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Shewana3_3333;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK49557.1; -; Genomic_DNA.
DR RefSeq; WP_011718136.1; NC_008577.1.
DR AlphaFoldDB; A0L0I8; -.
DR SMR; A0L0I8; -.
DR STRING; 94122.Shewana3_3333; -.
DR EnsemblBacteria; ABK49557; ABK49557; Shewana3_3333.
DR KEGG; shn:Shewana3_3333; -.
DR eggNOG; COG4123; Bacteria.
DR HOGENOM; CLU_061983_0_0_6; -.
DR OMA; NQYTEAF; -.
DR OrthoDB; 1027015at2; -.
DR Proteomes; UP000002589; 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..241
FT /note="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
FT /id="PRO_0000387428"
SQ SEQUENCE 241 AA; 27119 MW; 48EECDE26762E5BF CRC64;
MAFTFKQFHI DDLNCGMPVS TDGVILGAWA PLSRAKHILD IGAGSGLLSL MAAQRSQGQI
TAVELEEKAA AACQYNMTQS PWADRCKLIH GDIQHVCQQA EYQEYFDHII CNPPYFEHGP
KANEQHRAMA RHTDTLGFTP LLEAISQCLS HEGHASLILP IQSLTRFKAC LHQTQLYLVK
EVRVKSMENK DANRVLLLLA KILLTQSQDE PCQHTELTLR GEDGRYTEQM IALTKDFYLK
L