TRDMT_BOVIN
ID TRDMT_BOVIN Reviewed; 391 AA.
AC Q7YS61; Q58D29;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=tRNA (cytosine(38)-C(5))-methyltransferase {ECO:0000250|UniProtKB:O14717};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12971987; DOI=10.1016/s1567-133x(03)00121-2;
RA Golding M.C., Westhusin M.E.;
RT "Analysis of DNA (cytosine 5) methyltransferase mRNA sequence and
RT expression in bovine preimplantation embryos, fetal and adult tissues.";
RL Gene Expr. Patterns 3:551-558(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7YS61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7YS61-2; Sequence=VSP_020573;
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; AY244708; AAP20550.1; -; mRNA.
DR EMBL; BT021768; AAX46615.1; -; mRNA.
DR RefSeq; NP_861528.1; NM_181812.2. [Q7YS61-1]
DR AlphaFoldDB; Q7YS61; -.
DR SMR; Q7YS61; -.
DR STRING; 9913.ENSBTAP00000027378; -.
DR PaxDb; Q7YS61; -.
DR PRIDE; Q7YS61; -.
DR Ensembl; ENSBTAT00000027378; ENSBTAP00000027378; ENSBTAG00000020546. [Q7YS61-1]
DR GeneID; 353353; -.
DR KEGG; bta:353353; -.
DR CTD; 1787; -.
DR VEuPathDB; HostDB:ENSBTAG00000020546; -.
DR eggNOG; KOG0919; Eukaryota.
DR GeneTree; ENSGT00390000016416; -.
DR HOGENOM; CLU_049101_0_0_1; -.
DR InParanoid; Q7YS61; -.
DR OMA; VMDIIHP; -.
DR OrthoDB; 1519639at2759; -.
DR TreeFam; TF300024; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000020546; Expressed in spermatid and 107 other tissues.
DR ExpressionAtlas; Q7YS61; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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 Alternative splicing; Cytoplasm; Methyltransferase; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..391
FT /note="tRNA (cytosine(38)-C(5))-methyltransferase"
FT /id="PRO_0000247560"
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"
FT VAR_SEQ 360..391
FT /note="FPEMTTVKQRYRLLGNSLNVHVVAKLIKILCD -> MWDTRGPQLSFINGLR
FT T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_020573"
SQ SEQUENCE 391 AA; 44570 MW; FDB6EE432C98265C CRC64;
MEPLRALELY SGIGGMHQAL RESCIPAQVV AAVDVNTVAN EVYKYNFPHT QLLAKTIEGI
TLEEFDRLSF NMILMSPPCQ PFTRIGLQGD VTDPRTNSFL HILDILPRLQ KLPKYILLEN
VKGFEMSSTR DLLIQTIENC GFQYQEFLLS PTSLGIPNSR LRYFLIAKLQ PEPFPFQAPG
QVLMEFPKTE SEHPPKYAIN AEKKTEEKKT GPKICFDSST QCSGKEAILF KLETAGEIDR
KHQQDSDLSV RMLKDFLEDD IDKHSFFLPP KSLLRYALLL DIVKPTSRRS MCFTKGYGRY
IEGTGSVLQT TEDVQIENIY KSLTSLSQEE KIMRLSMLQL RFFTPKEIAN LLGFPPEFGF
PEMTTVKQRY RLLGNSLNVH VVAKLIKILC D
