EFMT3_XENTR
ID EFMT3_XENTR Reviewed; 224 AA.
AC Q28IN4; Q5FVB9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=EEF1A lysine methyltransferase 3 {ECO:0000250|UniProtKB:Q96AZ1};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96AZ1};
DE AltName: Full=Methyltransferase-like protein 21B;
DE AltName: Full=Protein-lysine methyltransferase METTL21B {ECO:0000250|UniProtKB:Q96AZ1};
GN Name=eef1akmt3 {ECO:0000250|UniProtKB:Q96AZ1}; Synonyms=fam119b, mettl21b;
GN ORFNames=TNeu018k12.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-224 (ISOFORM 2).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively mono-,
CC di- and trimethylates 'Lys-165' of the translation elongation factors
CC EEF1A1 and EEF1A2 in an aminoacyl-tRNA and GTP-dependent manner. EEF1A1
CC methylation by EEF1AKMT3 is dynamic as well as inducible by stress
CC conditions, such as ER-stress, and plays a regulatory role on mRNA
CC translation. {ECO:0000250|UniProtKB:Q96AZ1}.
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:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+)
CC + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54197;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54200, Rhea:RHEA-COMP:13826, Rhea:RHEA-
CC COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61961, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54201;
CC Evidence={ECO:0000250|UniProtKB:Q96AZ1};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AZ1}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q96AZ1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q28IN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28IN4-2; Sequence=VSP_026272;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC family. {ECO:0000305}.
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DR EMBL; CR760304; CAJ82348.1; -; mRNA.
DR EMBL; BC090083; AAH90083.1; -; mRNA.
DR RefSeq; NP_001016660.1; NM_001016660.2. [Q28IN4-1]
DR AlphaFoldDB; Q28IN4; -.
DR SMR; Q28IN4; -.
DR PaxDb; Q28IN4; -.
DR DNASU; 549414; -.
DR Ensembl; ENSXETT00000021254; ENSXETP00000021254; ENSXETG00000009654.
DR GeneID; 549414; -.
DR KEGG; xtr:549414; -.
DR CTD; 25895; -.
DR Xenbase; XB-GENE-5830044; eef1akmt3.
DR eggNOG; KOG2793; Eukaryota.
DR HOGENOM; CLU_055721_4_0_1; -.
DR InParanoid; Q28IN4; -.
DR OMA; QFLEREC; -.
DR PhylomeDB; Q28IN4; -.
DR TreeFam; TF313206; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000009654; Expressed in gastrula and 12 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
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 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 Alternative splicing; Cytoplasm; Cytoskeleton; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..224
FT /note="EEF1A lysine methyltransferase 3"
FT /id="PRO_0000291851"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 84..86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96AZ1"
FT VAR_SEQ 86..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026272"
SQ SEQUENCE 224 AA; 25143 MW; B0D9155FB4A8FF58 CRC64;
MHPEAKEPDC GFSEVLPREL GSLFSDTYTE ESHYAFCGTE LRITQHYGAN LGVAAPVWDA
ALFLCGYFEE QKLDFKGKKV IELGAGTGIV GILVSLLGGH VTLTDLPHAL SQIQKNVSAN
VSSNNPPQVC ALSWGLDQEK FPQDYDFVLG ADIVYLHDTY PLLIQTLQYL CGPQTSIFLS
SKMRQEHGTM HFFQDILPQY FASELVKRNK DEEINIYKVT RYQN
