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TRM1_SULIY
ID   TRM1_SULIY              Reviewed;         378 AA.
AC   C3NDZ5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=YG5714_1268;
OS   Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=439386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.G.57.14 / Yellowstone #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001403; ACP45534.1; -; Genomic_DNA.
DR   RefSeq; WP_012716131.1; NC_012622.1.
DR   AlphaFoldDB; C3NDZ5; -.
DR   SMR; C3NDZ5; -.
DR   EnsemblBacteria; ACP45534; ACP45534; YG5714_1268.
DR   GeneID; 7809173; -.
DR   KEGG; siy:YG5714_1268; -.
DR   HOGENOM; CLU_010862_5_1_2; -.
DR   OMA; VFYNPVM; -.
DR   Proteomes; UP000002308; 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   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..378
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_1000204872"
FT   DOMAIN          4..374
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ   SEQUENCE   378 AA;  42876 MW;  9DD9619844795CC6 CRC64;
     MKLKEVTEGK VRIFVPDPKE YMIEGKFDPS WAPVFYNPKM TFNRDLSVIV VSLLKPKIIL
     DALSATGIRG IRYYVESWKS EQLILNDKNS TAASLIQINV KNNGIENAKI YNKDANALLY
     EIKSEYIDID PFGSPVPFIL SSVNATIRNG IVAFTATDLS PLEGSSRTSC RRKYDAINYK
     LSSSKELGLR ILIGKIIREA ATLEKTVHPL FSFYADYYYR LFAIVESGAR KADENINKNL
     KYFGECPRCG FQTFVDENCK TKCPICGENF IIIGPLYIGP LHNMEFLKRM IDTYSDFNYL
     SSFNRIQKLL NVIEKEAKYK SVFYNISKLA SKLKVSAIPP IDSILECLGD ASKTHFAPTG
     IRTDKGYEEI IRCVKSLR
 
 
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