TRM1_PYRAR
ID TRM1_PYRAR Reviewed; 356 AA.
AC A4WMB7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Pars_1987;
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-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; CP000660; ABP51534.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WMB7; -.
DR SMR; A4WMB7; -.
DR STRING; 340102.Pars_1987; -.
DR PRIDE; A4WMB7; -.
DR EnsemblBacteria; ABP51534; ABP51534; Pars_1987.
DR KEGG; pas:Pars_1987; -.
DR HOGENOM; CLU_010862_5_1_2; -.
DR OMA; VFYNPVM; -.
DR PhylomeDB; A4WMB7; -.
DR Proteomes; UP000001567; 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; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..356
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_1000114980"
FT DOMAIN 5..352
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ SEQUENCE 356 AA; 39542 MW; D9EA406724020681 CRC64;
MSRIVLRREG TVEFYAPDPR AYGSIYSAPV FYNPAMEKNR TLSVLFLKAY GATGLTVCEP
LSGTGVRGIR YAVETGAVGR LILNDISREA VELIKKNLEV NGVDAEVYNE DANVLLHRLR
DKCDVVDIDP FGSPAPFLQA GFRALREEGV ICVTATDTAV LVGRYPKKCL RRYGAVMFKT
PFYIEAGLRN LTGYVARVAA SEDYGFEPLF AYWEGHYFRL CARAVRGARD ADSNFNFIGY
VEYKKPSRKV VRRPGERSLG PLWVGPMGDP ILVNKMAEYG PYGDFLQLLS EEYSVAAPWF
FKVPEFALGG VSRGIEEALN ALKKGGIYAV RTHMAPDGFK TEVSAGEVER VLRIVI