MT21A_DANRE
ID MT21A_DANRE Reviewed; 218 AA.
AC Q5BLD8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
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; ORFNames=zgc:110528;
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;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2005) 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}.
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DR EMBL; BC090479; AAH90479.1; -; mRNA.
DR RefSeq; NP_001013584.1; NM_001013566.2.
DR RefSeq; XP_009294375.1; XM_009296100.2.
DR AlphaFoldDB; Q5BLD8; -.
DR SMR; Q5BLD8; -.
DR STRING; 7955.ENSDARP00000026757; -.
DR PaxDb; Q5BLD8; -.
DR Ensembl; ENSDART00000025198; ENSDARP00000026757; ENSDARG00000012051.
DR GeneID; 541441; -.
DR KEGG; dre:541441; -.
DR CTD; 151194; -.
DR ZFIN; ZDB-GENE-050320-145; mettl21a.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000157249; -.
DR HOGENOM; CLU_055721_4_2_1; -.
DR InParanoid; Q5BLD8; -.
DR OMA; AQDWKKL; -.
DR OrthoDB; 1588190at2759; -.
DR PhylomeDB; Q5BLD8; -.
DR TreeFam; TF313206; -.
DR Reactome; R-DRE-8876725; Protein methylation.
DR PRO; PR:Q5BLD8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000012051; Expressed in early embryo and 21 other tissues.
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..218
FT /note="Protein N-lysine methyltransferase METTL21A"
FT /id="PRO_0000292036"
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 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8WXB1"
SQ SEQUENCE 218 AA; 24445 MW; 4F254331E0605CC8 CRC64;
MALVPYDENV LPALSKLHQS SAEFTLANHR IRLSQDWKRL GVAAVVWDAA VVLCMFLEMG
KVDLKGKRVI ELGAGTGLVG IVAALLGANV TITDREPALE FLTANVHENI PQGRQKAVQV
SELTWGENLD LYPQGGYDLI LGADIVYLEE TFPALLQTLE HLSSGDTVVL LSCRIRYERD
ERFLTELRQR FSVQEVHYDS QRDIHVYRAV KNKSNTEL
