ID   TRM1_PYRFU              Reviewed;         381 AA.
AC   P81554;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=PF1871;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=9685492; DOI=10.1093/nar/26.16.3753;
RA   Constantinesco F., Benachenhou N., Motorin Y., Grosjean H.;
RT   "The tRNA(guanine-26,N2-N2) methyltransferase (Trm1) from the
RT   hyperthermophilic archaeon Pyrococcus furiosus: cloning, sequencing of the
RT   gene and its expression in Escherichia coli.";
RL   Nucleic Acids Res. 26:3753-3761(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [3]
RP   FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10438627; DOI=10.1006/jmbi.1999.2976;
RA   Constantinesco F., Motorin Y., Grosjean H.;
RT   "Characterisation and enzymatic properties of tRNA(guanine 26,N(2), N(2))-
RT   dimethyltransferase (Trm1p) from Pyrococcus furiosus.";
RL   J. Mol. Biol. 291:375-392(1999).
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, ECO:0000269|PubMed:10438627,
CC       ECO:0000269|PubMed:9685492}.
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         ECO:0000269|PubMed:10438627, ECO:0000269|PubMed:9685492};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10438627}.
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; AF051912; AAC31882.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81995.1; -; Genomic_DNA.
DR   PIR; T51778; T51778.
DR   AlphaFoldDB; P81554; -.
DR   SMR; P81554; -.
DR   IntAct; P81554; 1.
DR   STRING; 186497.PF1871; -.
DR   PRIDE; P81554; -.
DR   EnsemblBacteria; AAL81995; AAL81995; PF1871.
DR   KEGG; pfu:PF1871; -.
DR   PATRIC; fig|186497.12.peg.1941; -.
DR   eggNOG; arCOG01219; Archaea.
DR   HOGENOM; CLU_010862_5_1_2; -.
DR   OMA; VFYNPVM; -.
DR   PhylomeDB; P81554; -.
DR   Proteomes; UP000001013; 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   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..381
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_0000147689"
FT   DOMAIN          6..378
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ   SEQUENCE   381 AA;  43319 MW;  36F2C5125C9CC6EC CRC64;
     MSMELFEVHE GKAKVLVPKA KTIYDSPVFY NPRMAPNRDV VVLLLNVLKP KIVLDALSAT
     GIRGIRFALE TPAEEIWMND INELAYELMK KNVLLNFKGT LKENAKRAIF EGEKTIVINN
     DDANRLMAEK HRYFHFIDLD PFGSPMEFLD TALRSVKRKG ILGVTATDGA PLCGAHPKAC
     LRKYLAVPLR GELCHEVGTR ILVGVIARYA AKYDLGMEVL LAYYKDHYFR AFVKLKDGAK
     KGDETLENLG YVYFDEKTGR FEVEKSFLST RPNAYGPLWL GPLKNEKVVG EMLELLVSGF
     EVANYREVLK LLHMLHEELD IPLFYDTHAL GKRLKIEPKK LGEIIKELKS MGYEATRTHF
     SPTGIKTNAP YEVFVEVMRK N