MET2A_DANRE
ID MET2A_DANRE Reviewed; 353 AA.
AC A8KBL7; Q568A6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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-A;
GN Name=mettl2a; Synonyms=mettl2; ORFNames=zgc:110598;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2007) 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 mettl2a 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; BC092943; AAH92943.1; -; mRNA.
DR EMBL; BC154164; AAI54165.1; -; mRNA.
DR RefSeq; NP_001017902.1; NM_001017902.1.
DR AlphaFoldDB; A8KBL7; -.
DR SMR; A8KBL7; -.
DR STRING; 7955.ENSDARP00000006586; -.
DR PaxDb; A8KBL7; -.
DR PeptideAtlas; A8KBL7; -.
DR DNASU; 100006618; -.
DR Ensembl; ENSDART00000180956; ENSDARP00000150100; ENSDARG00000113100.
DR GeneID; 100006618; -.
DR KEGG; dre:100006618; -.
DR CTD; 339175; -.
DR ZFIN; ZDB-GENE-050417-462; mettl2a.
DR eggNOG; KOG2361; Eukaryota.
DR InParanoid; A8KBL7; -.
DR OrthoDB; 987359at2759; -.
DR PhylomeDB; A8KBL7; -.
DR PRO; PR:A8KBL7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR Bgee; ENSDARG00000113100; Expressed in multicellular organism.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016427; F:tRNA (cytosine) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; IBA:GO_Central.
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..353
FT /note="tRNA N(3)-methylcytidine methyltransferase METTL2"
FT /id="PRO_0000328849"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 97
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 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT CONFLICT 17
FT /note="P -> T (in Ref. 1; AAH92943)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="R -> L (in Ref. 1; AAH92943)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="V -> A (in Ref. 1; AAH92943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 40488 MW; 866CC07B9229CDD5 CRC64;
MAAPVVAADS PVIENMPETA GGATENSAEA QKRPQFGTRF LTDPRQVFQH NAWDNVEWSA
EQEEAALKKV QENSQPLPAE KQEEFDNRAN EYWNDFYTIH ENRFFKDRHW LFTEFPELAP
QQKHLRGAEE KESLEHMLNG EDISLNPTHD EFPGASASYR ILEVGCGVGN TVFPILKTNN
DPGLFVYCCD FSSTAVDLVK SNPEYDPSRC HAFVHDMSDE SGEYPMPDHS LDVIVLIFVL
SALHPEKMQK SINRLGRLLK PGGVLLLRDY GRYDMAQLRF KKGRCLSENF YVRGDGTRVY
FFTQDELHDL FSSAGLEKLQ NLVDRRLQVN RGKQLTMYRV WVQCKYRKVL APT
