TRM1_PYRIL
ID TRM1_PYRIL Reviewed; 352 AA.
AC A1RV26;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Pisl_1656;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) 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; CP000504; ABL88808.1; -; Genomic_DNA.
DR RefSeq; WP_011763383.1; NC_008701.1.
DR AlphaFoldDB; A1RV26; -.
DR SMR; A1RV26; -.
DR STRING; 384616.Pisl_1656; -.
DR PRIDE; A1RV26; -.
DR EnsemblBacteria; ABL88808; ABL88808; Pisl_1656.
DR GeneID; 4616909; -.
DR KEGG; pis:Pisl_1656; -.
DR eggNOG; arCOG01219; Archaea.
DR HOGENOM; CLU_010862_5_1_2; -.
DR OMA; VFYNPVM; -.
DR OrthoDB; 70865at2157; -.
DR Proteomes; UP000002595; 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..352
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_1000114982"
FT DOMAIN 4..350
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ SEQUENCE 352 AA; 39968 MW; FBCEEEA7C8CFF6CB CRC64;
MKLILNKEGA VEFYIPDPQT YRSIYSAPVF YNPSMEKNRT LSVLLLKTYG SGLTVCEPLS
GTGIRGIRYA IESNAVGRLI LNDISKEAVE LIKKNLELNG VEGEVYNEDA NVLLHKLRNT
CDVVDIDPFG SPAPFLHAAF RALRDEGLIC VTATDTAVLV GRYPRKCFRR YNSVIRRTPF
YIELGLRNLV GYVARVAASE DFSIQPVFSY WENHYFRTCA LATRGAREAD DSLNNLGYIW
YLKKRRKIVQ TLDEHSSGPL WIGPLGDPLV VHKMSQYGVY SVFLQTLEME YSIQAPWYFR
LPEFAVDGKS PTLEKTLELL RRGGIYATRT HMSYDGFKAE ANYDEIARIL SI