EFMT2_DANRE
ID EFMT2_DANRE Reviewed; 233 AA.
AC Q5D013;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=EEF1A lysine methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03188};
DE AltName: Full=Methyltransferase-like protein 10 {ECO:0000255|HAMAP-Rule:MF_03188};
DE AltName: Full=Protein-lysine N-methyltransferase mettl10 {ECO:0000255|HAMAP-Rule:MF_03188};
GN Name=eef1akmt2 {ECO:0000255|HAMAP-Rule:MF_03188};
GN Synonyms=mettl10 {ECO:0000255|HAMAP-Rule:MF_03188}; ORFNames=zgc:110805;
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 catalyzes
CC the trimethylation of EEF1A at 'Lys-318'. {ECO:0000255|HAMAP-
CC Rule:MF_03188}.
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:Q5JPI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q5JPI9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03188}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03188}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000255|HAMAP-Rule:MF_03188}.
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DR EMBL; BC090299; AAH90299.1; -; mRNA.
DR RefSeq; NP_001013345.1; NM_001013327.1.
DR AlphaFoldDB; Q5D013; -.
DR SMR; Q5D013; -.
DR STRING; 7955.ENSDARP00000108342; -.
DR PaxDb; Q5D013; -.
DR GeneID; 503749; -.
DR KEGG; dre:503749; -.
DR CTD; 399818; -.
DR ZFIN; ZDB-GENE-050306-30; eef1akmt2.
DR eggNOG; KOG1271; Eukaryota.
DR InParanoid; Q5D013; -.
DR OrthoDB; 1422013at2759; -.
DR PhylomeDB; Q5D013; -.
DR Reactome; R-DRE-8876725; Protein methylation.
DR PRO; PR:Q5D013; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISS:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03188; Methyltr_EFM4; 1.
DR InterPro; IPR026635; Efm4/METTL10.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..233
FT /note="EEF1A lysine methyltransferase 2"
FT /id="PRO_0000325884"
SQ SEQUENCE 233 AA; 26033 MW; 35CC7A0742F04D1C CRC64;
MNSSVSTHGT GDCPVNCTKS EDFAPSKLGT KEYWDGAYKR ELQTYKDIGD VGEIWFGEES
MHRVIRWMEA QNISENAAIL DIGTGNGMFL VELARHGFSN LTGIDYSKAA LELTTNILVE
EGLKNINIQV EDFLNPSTEL KGFDVCIDKG TFDAISLNPE DREEAKKHYV TSLRAVMRPN
GFFIITSCNW TKEQLLEIFK PGFELVRELP TPNFQFGGVT GNSVTALVFK QTD
