EFMT4_BOVIN
ID EFMT4_BOVIN Reviewed; 255 AA.
AC P0DPE1; A5PJH8; G3N1Q4; Q10711; Q547G8; Q865C4;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=EEF1A lysine methyltransferase 4 {ECO:0000250|UniProtKB:P0DPD7};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P0DPD7};
GN Name=EEF1AKMT4 {ECO:0000250|UniProtKB:P0DPD7};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-lysine methyltransferase that efficiently catalyzes
CC three successive methylations on 'Lys-36' in eukaryotic translation
CC elongation factor 1 alpha (EEF1A1 or EEF1A2).
CC {ECO:0000250|UniProtKB:P0DPD7}.
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:P0DPD7};
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:P0DPD7};
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:P0DPD7};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=EEF1AKMT4-1;
CC IsoId=P0DPE1-1, Q10711-5;
CC Sequence=Displayed;
CC Name=EEF1AKMT4-ECE2-1; Synonyms=ECE-2a-1;
CC IsoId=P0DPE2-1, Q10711-1;
CC Sequence=External;
CC Name=EEF1AKMT4-ECE2-2; Synonyms=ECE-2a-2;
CC IsoId=P0DPE2-2, Q10711-2;
CC Sequence=External;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; DAAA02001884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC142117; AAI42118.1; -; mRNA.
DR RefSeq; NP_001300993.1; NM_001314064.1. [P0DPE1-1]
DR AlphaFoldDB; P0DPE1; -.
DR SMR; P0DPE1; -.
DR Ensembl; ENSBTAT00000064633; ENSBTAP00000055807; ENSBTAG00000051586. [P0DPE1-1]
DR GeneID; 281134; -.
DR KEGG; bta:281134; -.
DR CTD; 9718; -.
DR VEuPathDB; HostDB:ENSBTAG00000051586; -.
DR GeneTree; ENSGT00940000164140; -.
DR OMA; INMFHEE; -.
DR OrthoDB; 1163024at2759; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000051586; Expressed in rumen papilla and 104 other tissues.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..255
FT /note="EEF1A lysine methyltransferase 4"
FT /id="PRO_0000443292"
FT MOTIF 129..134
FT /note="Required for methyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 88..89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 113..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT MOD_RES 39
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DPD7"
FT CONFLICT 76
FT /note="I -> L (in Ref. 2; AAI42118)"
SQ SEQUENCE 255 AA; 28396 MW; 8E7563A80258990C CRC64;
MACLGPSAQV PELPEKNCGY REVQYWDQRY QGAADSAPYE WFGDFSCFRD LLEPELRPLD
RILVLGCGNS ALSYEIFLGG FPDVTSVDYS SVVVAAMRAR YAHVPTLRWE TMDVRALGFP
SGSFDVVLEK GTLDALLTGE QDPWTVSSEG VHTVDQVLNE VSRVLVPAGR FISLTSAAPH
FRTRHYAQAH YGWSLRHATY GNGFQFHFYL MQKGKELSVA QLAVGAQILS PPRPPTPSCF
LQDSDHEDFL SAIQL
