ID M3XUF1_MUSPF Unreviewed; 237 AA.
AC M3XUF1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=EEF1A lysine methyltransferase 2 {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
DE AltName: Full=Methyltransferase-like protein 10 {ECO:0000256|HAMAP-Rule:MF_03188};
DE AltName: Full=Protein-lysine N-methyltransferase METTL10 {ECO:0000256|HAMAP-Rule:MF_03188};
GN Name=EEF1AKMT2 {ECO:0000256|HAMAP-Rule:MF_03188,
GN ECO:0000313|Ensembl:ENSMPUP00000002701.1,
GN ECO:0000313|RefSeq:XP_004751803.1};
GN Synonyms=METTL10 {ECO:0000256|HAMAP-Rule:MF_03188};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000002701.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000002701.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004751803.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004751803.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively catalyzes
CC the trimethylation of EEF1A at 'Lys-318'. {ECO:0000256|HAMAP-
CC Rule:MF_03188}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03188}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03188}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000256|HAMAP-Rule:MF_03188}.
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DR EMBL; AEYP01029832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004751803.1; XM_004751746.3.
DR STRING; 9669.ENSMPUP00000002701; -.
DR Ensembl; ENSMPUT00000002757.1; ENSMPUP00000002701.1; ENSMPUG00000002730.1.
DR GeneID; 101692432; -.
DR KEGG; mpuf:101692432; -.
DR CTD; 399818; -.
DR eggNOG; KOG1271; Eukaryota.
DR GeneTree; ENSGT00390000013399; -.
DR HOGENOM; CLU_044783_2_1_1; -.
DR OMA; YWEDAYQ; -.
DR OrthoDB; 609682at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR12843:SF5; EEF1A LYSINE METHYLTRANSFERASE 2; 1.
DR PANTHER; PTHR12843; PROTEIN-LYSINE N-METHYLTRANSFERASE METTL10; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03188};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03188}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03188};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03188}.
FT DOMAIN 82..210
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 25793 MW; 97C91E9D66079E3F CRC64;
MNSGTGDGGG GAGAAEPSRS GSPGEDGFAP SALGTREHWD AVYERELQTF QEYGDTGEIW
FGEESMDRLI RWMQNRKIPL DASVLDIGTG NGVFLVELAK FGFSDITGID YSPSAIQLSG
SIIEKEGLSN IKLKVEDFLN LSTKLSGFHI CIDKGTFDAI SLNPDNAIEK RKQYVKSLSG
ALNVKGFFLI TSCNWTKEEL LDEFSEGFEL FEELPTPTFS FGGRSGNSVT ALVFQKT
//
