ID   TRDMT_RAT               Reviewed;         391 AA.
AC   Q4G073;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=tRNA (cytosine(38)-C(5))-methyltransferase;
DE            EC=2.1.1.204 {ECO:0000250|UniProtKB:O14717};
DE   AltName: Full=DNA (cytosine-5)-methyltransferase-like protein 2;
DE            Short=Dnmt2;
GN   Name=Trdmt1; Synonyms=Dnmt2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of
CC       tRNA(Asp). {ECO:0000250|UniProtKB:O14717}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42956, Rhea:RHEA-COMP:10299, Rhea:RHEA-COMP:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.204;
CC         Evidence={ECO:0000250|UniProtKB:O14717};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42957;
CC         Evidence={ECO:0000250|UniProtKB:O14717};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14717}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; BC098700; AAH98700.1; -; mRNA.
DR   RefSeq; NP_001026813.1; NM_001031643.1.
DR   AlphaFoldDB; Q4G073; -.
DR   SMR; Q4G073; -.
DR   STRING; 10116.ENSRNOP00000038279; -.
DR   PaxDb; Q4G073; -.
DR   PRIDE; Q4G073; -.
DR   Ensembl; ENSRNOT00000038651; ENSRNOP00000038279; ENSRNOG00000026132.
DR   GeneID; 291324; -.
DR   KEGG; rno:291324; -.
DR   UCSC; RGD:1306292; rat.
DR   CTD; 1787; -.
DR   RGD; 1306292; Trdmt1.
DR   eggNOG; KOG0919; Eukaryota.
DR   GeneTree; ENSGT00390000016416; -.
DR   HOGENOM; CLU_049101_0_0_1; -.
DR   InParanoid; Q4G073; -.
DR   OMA; VMDIIHP; -.
DR   OrthoDB; 1519639at2759; -.
DR   PhylomeDB; Q4G073; -.
DR   TreeFam; TF300024; -.
DR   PRO; PR:Q4G073; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000026132; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q4G073; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; ISO:RGD.
DR   GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR   GO; GO:0002946; P:tRNA C5-cytosine methylation; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR   GO; GO:0036416; P:tRNA stabilization; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..391
FT                   /note="tRNA (cytosine(38)-C(5))-methyltransferase"
FT                   /id="PRO_0000249870"
FT   DOMAIN          4..391
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   BINDING         13..15
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O14717"
FT   BINDING         34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O14717"
FT   BINDING         57..58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O14717"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O14717"
FT   BINDING         376
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O14717"
SQ   SEQUENCE   391 AA;  44070 MW;  58768BA5BBD4E37C CRC64;
     MEPLRVLELY SGIGGMHHAL RESRVPAHVV AAIDVSTVAN EVYKHNFPHT HLLAKTIEGI
     SLEEFDKLSF NMILMSPPCQ PFTRIGLQGD MSDRRTNSFL YILDILPRLQ KLPKYILLEN
     VKGFEVSSTR GLLIQTMEAC GFQYQEFLLS PSSLGIPNSR LRYFLIAKLQ SEPLCFQAPG
     QILMEFPNSG TVQPQEYAVV EEGKLRVRTR EPDVCLDSSS TQCSGQDSIL FKHETAADID
     RKRQQDSDLS VQMLKGFLED GDTAQYLLPA KSLLRYALLL DIVKPTSRRS MCFTKGYGSY
     IEGTGSVLQT AEDVQIENIY KSLPDLPPEE KIAKLSMLKL RYFTPKEIAN LLGFPPEFGF
     PEKTTVKQRY RLLGNSLNVH VVSKLLTVLC E