ID   METL6_PONAB             Reviewed;         282 AA.
AC   Q5RDV8;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=tRNA N(3)-methylcytidine methyltransferase METTL6 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q8BVH9};
DE   AltName: Full=Methyltransferase-like protein 6;
GN   Name=METTL6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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(Ser), including tRNA(Ser)(UGA) and
CC       tRNA(Ser)(GCU). Interaction with SARS1/SerRS is required for N(3)-
CC       methylcytidine methylation. {ECO:0000250|UniProtKB:Q8TCB7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) +
CC         N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:50956, Rhea:RHEA-COMP:12849, Rhea:RHEA-COMP:12851,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC         Evidence={ECO:0000250|UniProtKB:Q8BVH9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50957;
CC         Evidence={ECO:0000250|UniProtKB:Q8BVH9};
CC   -!- SUBUNIT: Monomer. Interacts with SARS1/SerRS; interaction is mediated
CC       via tRNA(Ser) and is required for N(3)-methylcytidine methylation.
CC       {ECO:0000250|UniProtKB:Q8TCB7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TCB7}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8TCB7}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC       {ECO:0000305}.
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DR   EMBL; CR857786; CAH90049.1; -; mRNA.
DR   RefSeq; NP_001124980.1; NM_001131508.1.
DR   AlphaFoldDB; Q5RDV8; -.
DR   SMR; Q5RDV8; -.
DR   STRING; 9601.ENSPPYP00000015764; -.
DR   GeneID; 100171853; -.
DR   KEGG; pon:100171853; -.
DR   CTD; 131965; -.
DR   eggNOG; KOG2361; Eukaryota.
DR   InParanoid; Q5RDV8; -.
DR   OrthoDB; 987359at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR026113; MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22809; PTHR22809; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   PIRSF; PIRSF037755; Mettl2_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..282
FT                   /note="tRNA N(3)-methylcytidine methyltransferase METTL6"
FT                   /id="PRO_0000240313"
FT   BINDING         45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         49
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT   BINDING         157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TCB7"
SQ   SEQUENCE   282 AA;  32959 MW;  6B22A5C51D669759 CRC64;
     MASLQRKGLQ ARILTSEEEE KLKRDQTLVS DFKQQKLEQE AQKNWDLFYK RNSTNFFKDR
     HWTTREFEEL RSCREFEDQK LTMLEAGRGV GNCLFPLLEE DPNIFAYACD FSPRAVEYVK
     QNPLYDTERC KVFQCDLTKD DLLDHVPPES VDVVMLIFVL SAVHPDKMHL VLQNIYKVLK
     PGKSVLFRDY GLYDHAMLRF KAGSKLGENF YVRQDGTRSY FFTDEFLAQL FMDTGYEEVV
     NEYVFRETVN KKEGLCVPRV FLQSKFLKPP KNPSPVVPGP GS