ID   TRM1_ENCCU              Reviewed;         432 AA.
AC   Q8SR99;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=TRM1; OrderedLocusNames=ECU08_1450;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
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       {ECO:0000250}.
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   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
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; AL590448; CAD26449.1; -; Genomic_DNA.
DR   RefSeq; NP_597273.1; NM_001041882.1.
DR   AlphaFoldDB; Q8SR99; -.
DR   SMR; Q8SR99; -.
DR   STRING; 284813.Q8SR99; -.
DR   GeneID; 859695; -.
DR   KEGG; ecu:ECU08_1450; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_1450; -.
DR   HOGENOM; CLU_010862_5_0_1; -.
DR   InParanoid; Q8SR99; -.
DR   OrthoDB; 1414511at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:InterPro.
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   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   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..432
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_0000383120"
FT   DOMAIN          9..382
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
SQ   SEQUENCE   432 AA;  48235 MW;  03D962CFF580815B CRC64;
     MESKDGARET ISEESTVITK NEWTFFNPAQ KFNRDISIEV VKECFKDRAS IRVLDAMSAT
     GLRGIRYLKE IGNSIVYLND ISQSSVDTIR SNVLLNGIED AEYFGSDLQG IKESGNARAN
     VVKSDCNVLM TSLPCFFDVI DIDPFGSCSE YIDSALRAIR HKGILCLTAT DKGVLCSNER
     KCLIKYSTSI MKGMGMNEVP LRTIVSLVSR QASKFDCSVE PVMSLSIDFY VRIFLRIVRR
     NPRSVVERNS HVLMCVCHNL AEIRSGQREI DSRCSNCSRR MRLCGPFWNG PLHDVKVIQG
     VLGGMNGGNK RLLGILRYLE QEIPTMFYYE IPRLCSLLGI STIKQSRLMH ALANMGYQVS
     YTHSELNAIK TNAPIASINK VLILSGAGDQ ERMEELGVEF NGNEGVKALE SIEFFKGLLK
     SGMGPLPLPR KH