ID   EFMT1_XENLA             Reviewed;         220 AA.
AC   Q6GN98;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=EEF1A lysine methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03187};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03187};
DE   AltName: Full=N(6)-adenine-specific DNA methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03187};
DE   AltName: Full=Protein-lysine N-methyltransferase n6amt2 {ECO:0000255|HAMAP-Rule:MF_03187};
GN   Name=eef1akmt1 {ECO:0000255|HAMAP-Rule:MF_03187};
GN   Synonyms=n6amt2 {ECO:0000255|HAMAP-Rule:MF_03187};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein-lysine methyltransferase that selectively catalyzes
CC       the trimethylation of EEF1A at 'Lys-79'. {ECO:0000255|HAMAP-
CC       Rule:MF_03187}.
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:0000255|HAMAP-Rule:MF_03187}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EFM5 family. {ECO:0000255|HAMAP-Rule:MF_03187}.
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:0000255|HAMAP-Rule:MF_03187}.
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DR   EMBL; BC073617; AAH73617.1; -; mRNA.
DR   RefSeq; NP_001085966.1; NM_001092497.1.
DR   AlphaFoldDB; Q6GN98; -.
DR   SMR; Q6GN98; -.
DR   DNASU; 444395; -.
DR   GeneID; 444395; -.
DR   KEGG; xla:444395; -.
DR   CTD; 444395; -.
DR   Xenbase; XB-GENE-6255370; eef1akmt1.S.
DR   OrthoDB; 1272987at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 444395; Expressed in heart and 19 other tissues.
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   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03187; Methyltr_EFM5; 1.
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; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..220
FT                   /note="EEF1A lysine methyltransferase 1"
FT                   /id="PRO_0000311298"
SQ   SEQUENCE   220 AA;  24748 MW;  4E0A165503F292CD CRC64;
     MEGSDDDDGV PQLSSHALAA LQEFYAEQQQ REAQKLGPDH EKFSVGSVEE DWQLSQFWYS
     DETALSLAKE AIEVCGENGR IACISAPSIY QKLRGLAGES VYIRLLEYDN RFAVYGDDFV
     FYDYNEPLKL PESLEPSSFD IVIADPPYLS EECLQNTAQT IKHLSRGKII LCTGAVMEDL
     AAQKLGLKKC KFIPEHTRNL ANEFRCYSNY ELALDKQGLA