METL2_BOVIN
ID METL2_BOVIN Reviewed; 378 AA.
AC Q0P5B2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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. Interacts with DALRD3.
CC {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; BC120275; AAI20276.1; -; mRNA.
DR RefSeq; NP_001068714.1; NM_001075246.2.
DR AlphaFoldDB; Q0P5B2; -.
DR SMR; Q0P5B2; -.
DR STRING; 9913.ENSBTAP00000012443; -.
DR PaxDb; Q0P5B2; -.
DR PRIDE; Q0P5B2; -.
DR Ensembl; ENSBTAT00000012443; ENSBTAP00000012443; ENSBTAG00000009458.
DR GeneID; 506221; -.
DR KEGG; bta:506221; -.
DR CTD; 339175; -.
DR VEuPathDB; HostDB:ENSBTAG00000009458; -.
DR eggNOG; KOG2361; Eukaryota.
DR GeneTree; ENSGT00940000156059; -.
DR HOGENOM; CLU_029724_0_2_1; -.
DR InParanoid; Q0P5B2; -.
DR OMA; PAKWWNL; -.
DR OrthoDB; 987359at2759; -.
DR TreeFam; TF323232; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000009458; Expressed in caput epididymis and 104 other tissues.
DR ExpressionAtlas; Q0P5B2; baseline and differential.
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; 1.
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..378
FT /note="tRNA N(3)-methylcytidine methyltransferase METTL2"
FT /id="PRO_0000328846"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
SQ SEQUENCE 378 AA; 43485 MW; DB258FAF0FEEAE33 CRC64;
MDCSFPEGDP AAVCGKRQQF GSRFLSDPAR VFHHNAWDNV EWSEEQAAEA ERKVQENSTQ
RVCQEKQADY EINANKYWNN FYKIHENGFF KDRHWLFTEF PELAPSQNHL KNLLSENKRS
EVYEYYRSGE DGPDLTIEEQ HRCSSVSLGD KTQPPLTEES VTQKLHHLEI CANEFPGSSA
TYRILEVGCG VGNTVFPILQ TNNDPSLFVY CCDFSSTAVE LVQTNSAYDP SRCFAFVHDL
CDEDKSYPMP ENSLDVIILI FVLSAIVPDK MQNAINRLSR LLKPGGIMLL RDYGRYDMAQ
LRFKKGQCLS ENFYVRGDGT RVYFFTQDEL DTLFTTAGLE KVQNLVDRRL QVNRGKQLTM
YRVWIQCKYR KPLGSSTG
