EFMT1_DANRE
ID EFMT1_DANRE Reviewed; 166 AA.
AC Q6NYP8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=EEF1A lysine methyltransferase 1 {ECO:0000250|UniProtKB:Q8WVE0};
DE EC=2.1.1.-;
DE AltName: Full=N(6)-adenine-specific DNA methyltransferase 2;
DE AltName: Full=Protein-lysine N-methyltransferase n6amt2;
GN Name=eef1akmt1 {ECO:0000250|UniProtKB:Q8WVE0}; Synonyms=n6amt2;
GN ORFNames=zgc:77010;
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=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively catalyzes
CC the trimethylation of EEF1A at 'Lys-79'.
CC {ECO:0000250|UniProtKB:Q8WVE0}.
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:Q8WVE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q8WVE0};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53200}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM5 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an N(6)-adenine-specific DNA
CC methyltransferase based on primary sequence and predicted secondary
CC structure. {ECO:0000250|UniProtKB:P53200}.
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DR EMBL; BC066508; AAH66508.1; -; mRNA.
DR RefSeq; NP_996970.1; NM_207087.1.
DR AlphaFoldDB; Q6NYP8; -.
DR SMR; Q6NYP8; -.
DR STRING; 7955.ENSDARP00000059401; -.
DR PaxDb; Q6NYP8; -.
DR DNASU; 404619; -.
DR GeneID; 404619; -.
DR KEGG; dre:404619; -.
DR CTD; 221143; -.
DR ZFIN; ZDB-GENE-040426-2551; eef1akmt1.
DR eggNOG; KOG3350; Eukaryota.
DR InParanoid; Q6NYP8; -.
DR OrthoDB; 1272987at2759; -.
DR PhylomeDB; Q6NYP8; -.
DR Reactome; R-DRE-8876725; Protein methylation.
DR PRO; PR:Q6NYP8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISS:UniProtKB.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR019369; Efm5/EEF1AKMT1.
DR InterPro; IPR041370; Mlase_EEF1AKMT1/ZCCHC4.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13200; PTHR13200; 1.
DR Pfam; PF10237; N6-adenineMlase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Reference proteome; Transferase.
FT CHAIN 1..166
FT /note="EEF1A lysine methyltransferase 1"
FT /id="PRO_0000311297"
SQ SEQUENCE 166 AA; 18915 MW; 2202901E04F5D66C CRC64;
MSQFWYSEET ASRLAEELLQ QAGEHGRIAC LSAPSVYQKL KQLESVRSDG VSAVLLEFDR
RFAAYGDEFV FYDYNNPLCL PEDLLPQSFD IVIADPPYLS EECLSKVTLT VKHLTKGKIL
LCTGAIMEEH AGKLLDLKMC SFLPRHNHNL ANEFRCYVNY ESRLLS