TRM1_METM7
ID TRM1_METM7 Reviewed; 373 AA.
AC A6VIL5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE EC=2.1.1.216 {ECO:0000255|HAMAP-Rule:MF_00290};
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
GN Name=trm1 {ECO:0000255|HAMAP-Rule:MF_00290}; OrderedLocusNames=MmarC7_1228;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of a
CC number of tRNAs using S-adenosyl-L-methionine as donor of the methyl
CC groups. {ECO:0000255|HAMAP-Rule:MF_00290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00290};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|HAMAP-Rule:MF_00290}.
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DR EMBL; CP000745; ABR66291.1; -; Genomic_DNA.
DR RefSeq; WP_011977601.1; NC_009637.1.
DR AlphaFoldDB; A6VIL5; -.
DR SMR; A6VIL5; -.
DR STRING; 426368.MmarC7_1228; -.
DR EnsemblBacteria; ABR66291; ABR66291; MmarC7_1228.
DR GeneID; 5327960; -.
DR KEGG; mmz:MmarC7_1228; -.
DR eggNOG; arCOG01219; Archaea.
DR HOGENOM; CLU_010862_5_1_2; -.
DR OMA; VFYNPVM; -.
DR OrthoDB; 70865at2157; -.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.56.70; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00290; tRNA_dimethyltr_TRM1; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR022923; TRM1_arc_bac.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR PANTHER; PTHR10631; PTHR10631; 1.
DR Pfam; PF02005; TRM; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00308; TRM1; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 3: Inferred from homology;
KW Methyltransferase; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..373
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_1000114979"
FT DOMAIN 2..365
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ SEQUENCE 373 AA; 41936 MW; 3150299C693044D5 CRC64;
MKIISEGETK LMVPEESTLS KKDTVFYNPV METNRDISVS VVQSFLDNFK RDEFLMCDPL
GGSGARGIRY ANELKFNGEL KVSIGDINPS AVKMIKENLK LNELENVEVF HEDANVLLSK
NFKIFNVVDL DPFGSPVPYL DSGIRASLTK GGLLCMTATD TAVLCGAYRK TCIRKYNAIP
LKGDKELAVR LMIGYAVKMA SKYDIGLKPI FSHVTDHYAR TFMVTERGAG KADSAIENLG
YIRQDSEQKS FKTFEEGYEK GYAGPFYLGE ISDKNIVQNS LETAKNRNYS KRAIDILELI
SKESKIEQVG CFDIHELCSF IKKLVPPVND IMENLKENGF KVSRVHYNPY GLKTDAELSD
LVVLISEYHS KKY