ID   EFNMT_DROPS             Reviewed;         673 AA.
AC   Q29LW1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=eEF1A lysine and N-terminal methyltransferase homolog {ECO:0000305};
DE   Includes:
DE     RecName: Full=eEF1A lysine methyltransferase homolog {ECO:0000305};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
DE   Includes:
DE     RecName: Full=eEF1A N-terminal methyltransferase homolog {ECO:0000305};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
GN   ORFNames=GA15401;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Dual methyltransferase. It catalyzes N-terminal methylation
CC       of target proteins via its C-terminus. It catalyzes dimethylation on
CC       lysine residues of target proteins via its N-terminus.
CC       {ECO:0000250|UniProtKB:Q8N6R0}.
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:Q8N6R0};
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:Q8N6R0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal glycyl-L-lysyl-L-glutamyl-[protein] + 3 S-adenosyl-
CC         L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-glycyl-L-lysyl-L-
CC         glutamyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:58440, Rhea:RHEA-COMP:15140, Rhea:RHEA-COMP:15143,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:142597, ChEBI:CHEBI:142600;
CC         Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH379060; EAL33934.1; -; Genomic_DNA.
DR   RefSeq; XP_001356868.1; XM_001356832.3.
DR   AlphaFoldDB; Q29LW1; -.
DR   SMR; Q29LW1; -.
DR   STRING; 7237.FBpp0279800; -.
DR   EnsemblMetazoa; FBtr0281362; FBpp0279800; FBgn0075420.
DR   GeneID; 4816930; -.
DR   KEGG; dpo:Dpse_GA15401; -.
DR   eggNOG; KOG2352; Eukaryota.
DR   HOGENOM; CLU_010025_1_0_1; -.
DR   InParanoid; Q29LW1; -.
DR   OMA; GEYCVEN; -.
DR   PhylomeDB; Q29LW1; -.
DR   Proteomes; UP000001819; Chromosome 4.
DR   Bgee; FBgn0075420; Expressed in female reproductive system and 3 other tissues.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
PE   3: Inferred from homology;
KW   Methyltransferase; Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN           1..673
FT                   /note="eEF1A lysine and N-terminal methyltransferase
FT                   homolog"
FT                   /id="PRO_0000310765"
SQ   SEQUENCE   673 AA;  76198 MW;  1BFA4E10ECED0E65 CRC64;
     MNLLPKTREE FAQTDYWNEF FKKRGEKAFE WYGEYLDLCD HIHKYIKPVD KILMLGCGNS
     KLSMDMYDSE YRDITNIDIS PVAVKKMLEQ NARTRPDMKF LQMDATAMTF PDESFSVALD
     KGTLDALFVD DAPETKAVVE NYFKEILRTM RNGGRYFCVS LLQEHILNFL VEFLPRHNCM
     LRIVHCLGVE QANKEKNADD AMKMPVFVVI ATKFKSLPMP ILEFGLGNDK MQRFTESSEL
     SNAVRSVQKA ALVFNGLARS SIAGHDEVTL DLYRPSENTP RYSIYILDQA AARGLNKYAA
     FIVPQGREIE WLFGTPSGRK KLQASAKFQR LAVVTLHRDQ VYNTLEEVQA ELGDTVFSLA
     PHGHIKQIPY LSLGSDVGKR ETLISGFSKI SGEFRIEEVE AGGKTLRRLI FLSNQFVVQS
     EALVKTIKIK GKKERKKIDF GYLACQHHLY MSVGVQLATT LQNPKKDVQK DVLVIGLGGG
     GLCSFLHAAL PQSRITAVEI DPIMLEVAEQ YFELKQDKRF HVVIDDGLAF VERCRNEDIH
     FDAVLFDVDS KDLSLGMSCP PQGFLAHDVL LHIKEIIGPK GLFMLNLVCR DETLKTEAIA
     NLQKVFPAVC SYKLEEDINE VVYCANDEKY KTVEHWQKAM GTAGRGLNTT IKEHKLASED
     PLEVAEFLSE LKL