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Database: UniProt
Entry: Q5ZKT6
LinkDB: Q5ZKT6
Original site: Q5ZKT6 
ID   EFMT1_CHICK             Reviewed;         213 AA.
AC   Q5ZKT6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
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}; ORFNames=RCJMB04_9d5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719998; CAG31657.1; -; mRNA.
DR   RefSeq; NP_001006277.1; NM_001006277.1.
DR   RefSeq; XP_015133532.1; XM_015278046.1.
DR   AlphaFoldDB; Q5ZKT6; -.
DR   SMR; Q5ZKT6; -.
DR   STRING; 9031.ENSGALP00000074055; -.
DR   PaxDb; 9031-ENSGALP00000027624; -.
DR   Ensembl; ENSGALT00000101742; ENSGALP00000074055; ENSGALG00000017133.
DR   Ensembl; ENSGALT00010013193.1; ENSGALP00010007755.1; ENSGALG00010005514.1.
DR   Ensembl; ENSGALT00015041842; ENSGALP00015024405; ENSGALG00015017131.
DR   GeneID; 418951; -.
DR   KEGG; gga:418951; -.
DR   CTD; 221143; -.
DR   VEuPathDB; HostDB:geneid_418951; -.
DR   eggNOG; KOG3350; Eukaryota.
DR   GeneTree; ENSGT00390000016366; -.
DR   HOGENOM; CLU_074410_2_1_1; -.
DR   InParanoid; Q5ZKT6; -.
DR   OMA; CNFRPEH; -.
DR   OrthoDB; 6014at2759; -.
DR   PhylomeDB; Q5ZKT6; -.
DR   TreeFam; TF106153; -.
DR   Reactome; R-GGA-8876725; Protein methylation.
DR   PRO; PR:Q5ZKT6; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000017133; Expressed in spermatid and 14 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:RHEA.
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   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:SF0; EEF1A LYSINE METHYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR13200; UNCHARACTERIZED; 1.
DR   Pfam; PF10237; N6-adenineMlase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..213
FT                   /note="EEF1A lysine methyltransferase 1"
FT                   /id="PRO_0000311296"
SQ   SEQUENCE   213 AA;  24079 MW;  BDDC0CAA4B2A1FA4 CRC64;
     MDDDDDDIPQ LSSHTLAALQ EFYLEQQQRE GMKTSQGFNQ YSVGSIEEDW QLSQFWYSDE
     TASCLANEAI VAAGKGGRIA CVSAPSVYQK LREQGGADFS VCILEYDRRF SVYGEEFIFY
     DYNNPLNLPE HLLPHSFDIV VADPPYLSEE CLQKTAETIK YLTKGKILLC TGAIMEEQAA
     KHLGVKICKF IPKHSRNLAN EFRCYVNYAS GLD
//
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