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 27-MAR-2024, entry version 112. 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). Has higher activity on tRNA(Asp) modified with queuosine at CC position 34. {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PhosphoSitePlus; Q4G073; -. DR PaxDb; 10116-ENSRNOP00000038279; -. DR Ensembl; ENSRNOT00000038651.6; ENSRNOP00000038279.4; ENSRNOG00000026132.6. DR GeneID; 291324; -. DR KEGG; rno:291324; -. DR UCSC; RGD:1306292; rat. DR AGR; RGD:1306292; -. 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; HYAFKYA; -. DR OrthoDB; 197881at2759; -. DR PhylomeDB; Q4G073; -. DR TreeFam; TF300024; -. DR PRO; PR:Q4G073; -. DR Proteomes; UP000002494; Chromosome 17. DR Bgee; ENSRNOG00000026132; Expressed in thymus and 19 other cell types or tissues. 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 (cytidine-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:0030488; P:tRNA methylation; ISS:UniProtKB. DR GO; GO:0036416; P:tRNA stabilization; ISS:UniProtKB. DR CDD; cd00315; Cyt_C5_DNA_methylase; 1. DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00675; dcm; 1. DR PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1. DR PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. DR Genevisible; Q4G073; RN. 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 //