METL6_RAT
ID METL6_RAT Reviewed; 287 AA.
AC Q6AXU8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079309; AAH79309.1; -; mRNA.
DR RefSeq; NP_001007624.1; NM_001007623.1.
DR AlphaFoldDB; Q6AXU8; -.
DR SMR; Q6AXU8; -.
DR STRING; 10116.ENSRNOP00000026413; -.
DR PaxDb; Q6AXU8; -.
DR DNASU; 290564; -.
DR Ensembl; ENSRNOT00000084645; ENSRNOP00000074466; ENSRNOG00000052391.
DR GeneID; 290564; -.
DR KEGG; rno:290564; -.
DR UCSC; RGD:1359565; rat.
DR CTD; 131965; -.
DR RGD; 1359565; Mettl6.
DR eggNOG; KOG2361; Eukaryota.
DR GeneTree; ENSGT00390000018500; -.
DR HOGENOM; CLU_029724_2_2_1; -.
DR InParanoid; Q6AXU8; -.
DR OMA; PEFKANK; -.
DR OrthoDB; 987359at2759; -.
DR PhylomeDB; Q6AXU8; -.
DR TreeFam; TF321001; -.
DR PRO; PR:Q6AXU8; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000057372; Expressed in thymus and 19 other tissues.
DR Genevisible; Q6AXU8; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; ISO:RGD.
DR GO; GO:0030488; P:tRNA methylation; ISO:RGD.
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..287
FT /note="tRNA N(3)-methylcytidine methyltransferase METTL6"
FT /id="PRO_0000240314"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 287 AA; 33381 MW; 4282D866E296DE1A CRC64;
MTSLQRKGPQ TRILSTGEEE KLKRDQALVS AFKQQKLEKE AQKNWDLFYK RNSTNFFKDR
HWTTREFEEL RSCREYEGQK LTLLEAGCGV GNCLFPLLEE DSNIFAYACD FSPRAVDYVK
QHPLYNAERC KVFQCDLTRD DLLDHIPPES VDAVTLIFVL SAVHPEKMHL VLLNVYKVLK
PGRSVLFRDY GLNDHAMLRF KAGSKLGENF YVRQDGTRSY FFTDEFLAKL FVDAGYEEVV
NEYVFRETVN KKEGLCVPRV FLQSKFRKPP KDPAPTTDSA SLLRKEF
