TRM1_METS5
ID TRM1_METS5 Reviewed; 382 AA.
AC A4YHH9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Msed_1726;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP95881.1; -; Genomic_DNA.
DR RefSeq; WP_012021668.1; NC_009440.1.
DR AlphaFoldDB; A4YHH9; -.
DR SMR; A4YHH9; -.
DR STRING; 399549.Msed_1726; -.
DR EnsemblBacteria; ABP95881; ABP95881; Msed_1726.
DR GeneID; 5105089; -.
DR GeneID; 59457156; -.
DR KEGG; mse:Msed_1726; -.
DR eggNOG; arCOG01219; Archaea.
DR HOGENOM; CLU_010862_5_1_2; -.
DR OMA; VFYNPVM; -.
DR Proteomes; UP000000242; Chromosome.
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 PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..382
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_1000197032"
FT DOMAIN 4..370
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ SEQUENCE 382 AA; 42812 MW; 3DBBDEF9A5E509A6 CRC64;
MKLTEVIEGK ARLVIPDPSE FSREGKFDPA WSPVFYNPRM VFNRDVSVLA VSVISPPSVL
DAMSATGVRG IRYVKESGVK GEVLFNDKNP VSVELISKNL ELNGITGKVL RSDANSLMHQ
VKVGYTDLDP FGSPAPYLFS AISSLRRKGV LGVTATDLSA LEGKSRTSSK RKYGVQGSRL
SYSKEAGLRV LLGKIVKEAS VQEKGIRPLM GFYHDYYYRL FVKMEDGAKR ADRSLESLGT
LYECDRCGYS FMSSDECERK CPVCGGELKY YGPAWIGEFN DLEFLKEMKN RLTEFSYLSN
SVKISELLEY LERENRFGPY YRVDVLASRL KVNMPPMNSL LGCLGDAVRT HFDPRGFKSF
REFSEILECV KGSSATYETS GR