TRDMT_SPOFR
ID TRDMT_SPOFR Reviewed; 332 AA.
AC A0A2H1VE33; K0A166; L7MTK8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
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 {ECO:0000303|PubMed:23103599};
DE Short=Dnmt2 {ECO:0000303|PubMed:23103599};
DE EC=2.1.1.37 {ECO:0000269|PubMed:23103599};
GN Name=TRDMT1 {ECO:0000250|UniProtKB:O14717};
GN Synonyms=DNMT2 {ECO:0000303|PubMed:23103599};
GN ORFNames=SFRICE_001256 {ECO:0000312|EMBL:SOQ38672.1};
OS Spodoptera frugiperda (Fall armyworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7108 {ECO:0000312|EMBL:SOQ38672.1};
RN [1] {ECO:0000312|EMBL:AFS64716.1, ECO:0000312|PDB:4H0N, ECO:0007744|PDB:4H0N}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN
RP COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-230 AND CYS-231.
RX PubMed=23103599; DOI=10.1093/jmcb/mjs057;
RA Li S., Du J., Yang H., Yin J., Ding J., Zhong J.;
RT "Functional and structural characterization of DNMT2 from Spodoptera
RT frugiperda.";
RL J. Mol. Cell Biol. 5:64-66(2013).
RN [2] {ECO:0000312|EMBL:SOQ38672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rice {ECO:0000312|EMBL:SOQ38672.1};
RA Bretaudeau A.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of
CC tRNA(Asp) (By similarity). Also has DNA (cytosine-5)-methyltransferase
CC activity (PubMed:23103599). Shows affinity for both tRNA(Asp) and DNA
CC substrates (PubMed:23103599). {ECO:0000250|UniProtKB:O14717,
CC ECO:0000269|PubMed:23103599}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000269|PubMed:23103599};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23103599}. Nucleus
CC {ECO:0000269|PubMed:23103599}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016, ECO:0000255|RuleBase:RU000416}.
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DR EMBL; JX428898; AFS64716.1; -; mRNA.
DR EMBL; ODYU01001870; SOQ38672.1; -; Genomic_DNA.
DR PDB; 4H0N; X-ray; 2.71 A; A/B/C/D=1-332.
DR PDBsum; 4H0N; -.
DR AlphaFoldDB; A0A2H1VE33; -.
DR SMR; A0A2H1VE33; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Methyltransferase; Nucleus;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..332
FT /note="tRNA (cytosine(38)-C(5))-methyltransferase"
FT /id="PRO_0000451456"
FT DOMAIN 3..332
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT BINDING 12..14
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:23103599,
FT ECO:0007744|PDB:4H0N"
FT BINDING 33..34
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:23103599,
FT ECO:0007744|PDB:4H0N"
FT BINDING 55..56
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:23103599,
FT ECO:0007744|PDB:4H0N"
FT BINDING 75
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:4H0N"
FT BINDING 79
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:4H0N"
FT BINDING 97
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:4H0N"
FT BINDING 316..317
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:23103599,
FT ECO:0007744|PDB:4H0N"
FT MUTAGEN 230
FT /note="C->Q: Significantly reduced DNA methyltransferase
FT activity. Significantly reduced DNA methyltransferase
FT activity; when associated with Q-231."
FT /evidence="ECO:0000269|PubMed:23103599"
FT MUTAGEN 231
FT /note="C->Q: No effect on DNA methyltransferase activity.
FT Significantly reduced DNA methyltransferase activity; when
FT associated with Q-230."
FT /evidence="ECO:0000269|PubMed:23103599"
FT CONFLICT 101
FT /note="I -> L (in Ref. 1; AFS64716)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="G -> R (in Ref. 1; AFS64716)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..212
FT /note="DKI -> EKM (in Ref. 1; AFS64716)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="N -> K (in Ref. 1; AFS64716)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="S -> G (in Ref. 1; AFS64716)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4H0N"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:4H0N"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:4H0N"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:4H0N"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:4H0N"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:4H0N"
SQ SEQUENCE 332 AA; 38406 MW; B79EDF2A71442763 CRC64;
MSHKILELYS GIGGMHCAWK ESGLDGEIVA AVDINTVANS VYKHNFPETN LLNRNIQQLT
PQVIKKWNVD TILMSPPCQP FTRNGKYLDD NDPRTNSFLY IIGILDQLDN VDYILMENVK
GFENSTVRNL FIDKLKECNF IYQEFLLCPS TVGVPNSRLR YYCTARRNNL TWPFKRGDEI
ITRLPKDFGV PHSLESIIEE DVDEKFLVPD KILRCAKVFD ICYKTSKRSC CFTKAYTHYA
DGTGSIFTDK PREVVQKCYE EANQNEIGSE KFVELFKELK LRYFTPKEVL MIMCFPKSYN
LPTNISMKQC YRLLGNSVNV KVISELLKIL FE
