ID   TRM1_CAEEL              Reviewed;         526 AA.
AC   Q23270;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase;
DE            EC=2.1.1.216;
DE   AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase;
DE   AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase;
DE   AltName: Full=tRNA(m(2,2)G26)dimethyltransferase;
GN   Name=trm-1; Synonyms=trm1; ORFNames=ZC376.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND MUTAGENESIS OF ARG-246.
RC   STRAIN=Bristol N2;
RX   PubMed=10048958; DOI=10.1016/s0378-1119(98)00550-2;
RA   Liu J.M., Zhou G.Q., Straby K.B.;
RT   "Caenorhabditis elegans ZC376.5 encodes a tRNA
RT   (m2/2G(26))dimethyltransferance in which (246)arginine is important for the
RT   enzyme activity.";
RL   Gene 226:73-81(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Dimethylates a single guanine residue at position 26 of most
CC       tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
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|PROSITE-ProRule:PRU00958};
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
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DR   EMBL; AF059608; AAD13737.1; -; mRNA.
DR   EMBL; Z77136; CAB00881.1; -; Genomic_DNA.
DR   PIR; T43053; T43053.
DR   RefSeq; NP_506513.1; NM_074112.5.
DR   AlphaFoldDB; Q23270; -.
DR   SMR; Q23270; -.
DR   BioGRID; 44926; 3.
DR   STRING; 6239.ZC376.5.1; -.
DR   EPD; Q23270; -.
DR   PaxDb; Q23270; -.
DR   PeptideAtlas; Q23270; -.
DR   EnsemblMetazoa; ZC376.5.1; ZC376.5.1; WBGene00006613.
DR   EnsemblMetazoa; ZC376.5.2; ZC376.5.2; WBGene00006613.
DR   UCSC; ZC376.5; c. elegans.
DR   WormBase; ZC376.5; CE15201; WBGene00006613; trm-1.
DR   eggNOG; KOG1253; Eukaryota.
DR   GeneTree; ENSGT00530000063646; -.
DR   HOGENOM; CLU_010862_4_1_1; -.
DR   InParanoid; Q23270; -.
DR   OMA; YRVSYSH; -.
DR   OrthoDB; 1414511at2759; -.
DR   PhylomeDB; Q23270; -.
DR   BRENDA; 2.1.1.216; 1045.
DR   PRO; PR:Q23270; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00006613; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central.
DR   Gene3D; 3.30.56.70; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
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..526
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_0000147673"
FT   DOMAIN          22..441
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         246
FT                   /note="R->G: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10048958"
SQ   SEQUENCE   526 AA;  58400 MW;  5CF69A2BA917D3A0 CRC64;
     MTENVNSSGD SAIKSEDKEE VTVIQEGQAK VGFHGPVFYN PVQEFNRDLT VTVLRQFSAD
     HQKWAEEQKQ LKTEEEPPKK KNKLAINEDG KIRILDALSA SGLRALRFSK EVPNVGFIMA
     NDFSDNAVAS IQENVKLNGV EDIVEAHFGD AVMTMMEHRG IDKRFHAVDL DPYGTASTFL
     DSAVQCVADR GILMVTCTDM AVLCGNTPEA CYNKYDAVTT RMKCCHEVGL RILLRAIDSA
     ANRYTRYIEP LVSISVDFYV RVFVRVHTGA FQAKQSGTKV GTVLVCSGCH SMEPLVLLKR
     GEGNQQSKYS IPTVRHSISG PGNRCIHCLL PLHQIGPIYL APIHSKPFVT SLLERLKSTP
     EAERLGTHGR LQGVLTMVNE ELDDVLYYEH NQMANVVKVS VPKSQSVRSA ILNAGFKVSG
     SHCNPRAIKT NAPMHLLWDI YRQVAKDTSV DREKRLAKES AGYHILGQPI TNTVNFTLHP
     GAIEQAKKEN LVRFQCNKGK NWGPRQKAKG SVNSTKAGFQ LTEHKE