ID   MT21A_XENTR             Reviewed;         215 AA.
AC   A4IGU3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Protein N-lysine methyltransferase METTL21A;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q8WXB1};
DE   AltName: Full=Methyltransferase-like protein 21A;
GN   Name=mettl21a; Synonyms=Fam119a;
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].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC       trimethylates residues in heat shock protein 70 (HSP70) family members.
CC       {ECO:0000250|UniProtKB:Q8WXB1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         Evidence={ECO:0000250|UniProtKB:Q8WXB1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC         Evidence={ECO:0000250|UniProtKB:Q8WXB1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WXB1}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC       family. {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; BC135248; AAI35249.1; -; mRNA.
DR   RefSeq; NP_001090861.1; NM_001097392.1.
DR   AlphaFoldDB; A4IGU3; -.
DR   SMR; A4IGU3; -.
DR   STRING; 8364.ENSXETP00000029481; -.
DR   PaxDb; A4IGU3; -.
DR   DNASU; 100038275; -.
DR   GeneID; 100038275; -.
DR   KEGG; xtr:100038275; -.
DR   CTD; 151194; -.
DR   Xenbase; XB-GENE-5860641; mettl21a.
DR   eggNOG; KOG2793; Eukaryota.
DR   HOGENOM; CLU_055721_4_2_1; -.
DR   InParanoid; A4IGU3; -.
DR   OMA; AQDWKKL; -.
DR   OrthoDB; 1588190at2759; -.
DR   PhylomeDB; A4IGU3; -.
DR   TreeFam; TF313206; -.
DR   Reactome; R-XTR-8876725; Protein methylation.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
DR   GO; GO:0006479; P:protein methylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..215
FT                   /note="Protein N-lysine methyltransferase METTL21A"
FT                   /id="PRO_0000292037"
FT   BINDING         47
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT   BINDING         73..75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXB1"
FT   BINDING         141
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXB1"
SQ   SEQUENCE   215 AA;  24579 MW;  BB01F5EE593F70CC CRC64;
     MALVPYTDSG VQSLKRFHDS SASFKFVNHN IEIKQDWKQL GVAAVVWDAA LVLCMYLESE
     GIHLQNSSVI ELGAGTGLVG IVAALLGAQV TITDRDLAME FLRMNVRDNI PKDSLHRVSV
     RALNWGKSLE EFSTYDFILG ADIIYLEETF PDLLQTFLHL SSQQSVILLS SRLRYQRDHD
     FLEMMKLHFT IADVYYDKNT DVHIFRAQLR QRKEL