ID   METL2_XENTR             Reviewed;         337 AA.
AC   Q5M8E6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=tRNA N(3)-methylcytidine methyltransferase METTL2 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q8BMK1};
DE   AltName: Full=Methyltransferase-like protein 2;
GN   Name=mettl2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       mediates N(3)-methylcytidine modification of residue 32 of the tRNA
CC       anticodon loop of tRNA(Thr)(UGU) and tRNA(Arg)(CCU). N(3)-
CC       methylcytidine methylation by mettl2 requires the N6-
CC       threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as
CC       prerequisite. {ECO:0000250|UniProtKB:Q96IZ6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) +
CC         N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:50960, Rhea:RHEA-COMP:12850, Rhea:RHEA-COMP:12852,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC         Evidence={ECO:0000250|UniProtKB:Q8BMK1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50961;
CC         Evidence={ECO:0000250|UniProtKB:Q8BMK1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(32) in tRNA(Arg)(CCU) + S-adenosyl-L-methionine =
CC         H(+) + N(3)-methylcytidine(32) in tRNA(Arg)(CCU) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60912, Rhea:RHEA-COMP:15710, Rhea:RHEA-
CC         COMP:15712, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC         Evidence={ECO:0000250|UniProtKB:Q8BMK1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60913;
CC         Evidence={ECO:0000250|UniProtKB:Q8BMK1};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96IZ6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96IZ6}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC       {ECO:0000305}.
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DR   EMBL; BC088068; AAH88068.1; -; mRNA.
DR   RefSeq; NP_001011322.1; NM_001011322.1.
DR   AlphaFoldDB; Q5M8E6; -.
DR   SMR; Q5M8E6; -.
DR   STRING; 8364.ENSXETP00000017172; -.
DR   PaxDb; Q5M8E6; -.
DR   DNASU; 496782; -.
DR   GeneID; 496782; -.
DR   KEGG; xtr:496782; -.
DR   CTD; 55798; -.
DR   eggNOG; KOG2361; Eukaryota.
DR   HOGENOM; CLU_029724_0_2_1; -.
DR   InParanoid; Q5M8E6; -.
DR   OrthoDB; 987359at2759; -.
DR   PhylomeDB; Q5M8E6; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016427; F:tRNA (cytosine) methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR026113; MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22809; PTHR22809; 2.
DR   PIRSF; PIRSF037755; Mettl2_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..337
FT                   /note="tRNA N(3)-methylcytidine methyltransferase METTL2"
FT                   /id="PRO_0000328850"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         140
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         212
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
SQ   SEQUENCE   337 AA;  38717 MW;  8BF31C0EBDD2456E CRC64;
     MEGKRPQFGN RHLDDPSRVF QHNAWDNVQW SEEQESAAHK KVQENSVQPL PLEKQEEYEN
     KASNFWDDFY TIHENRFFKD RHWLFTEFPE LSSRSSTQTG TESQEGQVMQ LNGCQEETER
     ADVENPFPGA SATYRIMEVG CGVGNTVFPI LQNNTDPGLF VYCCDFSSTA VELVKSNELY
     SPSRCFAFVH DVSDEQSSFP MPEHSLDVIV LIFVLSAINP AKMQNVISRL SSLLKPGGCI
     LLRDYGRYDM AQLRFKKGRC LAENFYVRGD GTRVYFFTQD DLDTLFISAG LQKVQNTVDR
     RLQVNRGKQL TMYRVWIQCK YVKPQETELQ NGGCSSE