ID   EF2KT_BOVIN             Reviewed;         340 AA.
AC   Q1JPJ9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Protein-lysine N-methyltransferase EEF2KMT {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q96G04};
DE   AltName: Full=eEF2-lysine methyltransferase;
DE            Short=eEF2-KMT;
GN   Name=EEF2KMT; Synonyms=FAM86A;
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=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-340.
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Catalyzes the trimethylation of eukaryotic elongation factor
CC       2 (EEF2) on 'Lys-525'. {ECO:0000250|UniProtKB:Q96G04}.
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:Q96G04};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC         Evidence={ECO:0000250|UniProtKB:Q96G04};
CC   -!- SUBUNIT: Interacts with FAM86B2 and FAM86C1P.
CC       {ECO:0000250|UniProtKB:Q96G04}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96G04}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EEF2KMT family. {ECO:0000305}.
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DR   EMBL; AAFC03051150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BT025354; ABF57310.1; -; mRNA.
DR   RefSeq; NP_001157410.1; NM_001163938.1.
DR   AlphaFoldDB; Q1JPJ9; -.
DR   SMR; Q1JPJ9; -.
DR   STRING; 9913.ENSBTAP00000037316; -.
DR   PaxDb; Q1JPJ9; -.
DR   PRIDE; Q1JPJ9; -.
DR   Ensembl; ENSBTAT00000037485; ENSBTAP00000037316; ENSBTAG00000008222.
DR   GeneID; 531984; -.
DR   KEGG; bta:531984; -.
DR   CTD; 196483; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008222; -.
DR   eggNOG; KOG2497; Eukaryota.
DR   GeneTree; ENSGT00510000047003; -.
DR   InParanoid; Q1JPJ9; -.
DR   OMA; TGFFHST; -.
DR   OrthoDB; 958308at2759; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000008222; Expressed in oocyte and 105 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029426; FAM86_N.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
DR   Pfam; PF14904; FAM86; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..340
FT                   /note="Protein-lysine N-methyltransferase EEF2KMT"
FT                   /id="PRO_0000332111"
FT   BINDING         139
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         165..167
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         238
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         257
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96G04"
SQ   SEQUENCE   340 AA;  37952 MW;  587BF0CCBCC093CF CRC64;
     MAPEERADAA RLLRGFERRF LAARALRSFP WQSLEEKLRD SSGSELLLDI LQKTVKHPLC
     VKHPPSVKYS RSFLSELIRK HEAVHTEPLD ELYQALAEVL TAEDPTHCHR SYLLPSGDSV
     TLCESTAIVS HGTTGLVTWN AALYLAEWAV ENPAVFAHRM VLELGSGAGL TGLAICKTCR
     PRAYIFSDCH SHVLEQLRGN VLLNGFSLEP SIDTWAQHPG PHTPEAERPW VTVARLDWDT
     VTAPQLAAFQ PDVVLAADVL YCPETVLSLV GVLRKLSTCR KDQRAPDAYI AFTVRNPETC
     QLFTTELGQA GIPWEEVPCH DQKLFPYEEH SEMAILKLTL