ID   EFNMT_XENLA             Reviewed;         693 AA.
AC   Q6NTR1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=eEF1A lysine and N-terminal methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE   AltName: Full=Methyltransferase-like protein 13 {ECO:0000250|UniProtKB:Q8N6R0};
DE   Includes:
DE     RecName: Full=eEF1A lysine methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
DE   Includes:
DE     RecName: Full=eEF1A N-terminal methyltransferase {ECO:0000250|UniProtKB:Q8N6R0};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
GN   Name=mettl13; Synonyms=eef1aknmt {ECO:0000250|UniProtKB:Q8N6R0};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dual methyltransferase that catalyzes methylation of
CC       elongation factor 1-alpha (eef1a1 and eef1a2) at two different
CC       positions, and is therefore involved in the regulation of mRNA
CC       translation. Via its C-terminus, methylates the N-terminus of eef1a1
CC       and eef1a2. Via its N-terminus dimethylates lysine residues of eef1a1
CC       and eef1a2. {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; BC068895; AAH68895.1; -; mRNA.
DR   RefSeq; NP_001084718.1; NM_001091249.1.
DR   AlphaFoldDB; Q6NTR1; -.
DR   SMR; Q6NTR1; -.
DR   DNASU; 414682; -.
DR   GeneID; 414682; -.
DR   KEGG; xla:414682; -.
DR   CTD; 414682; -.
DR   Xenbase; XB-GENE-965492; mettl13.S.
DR   OrthoDB; 912165at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 414682; Expressed in oocyte and 19 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   2: Evidence at transcript level;
KW   Methyltransferase; Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN           1..693
FT                   /note="eEF1A lysine and N-terminal methyltransferase"
FT                   /id="PRO_0000310763"
SQ   SEQUENCE   693 AA;  78325 MW;  7F825F42EFD1C29A CRC64;
     MDLLPKSSKE FAAPEYWEQF FRRRGERAFE WYGGYLELCG LLHKYIKPRD KVFVVGCGNS
     ELSEQLYDAG CQNLTNIDVS EVVIRQMNER NSNRRPNMTF QVMDATQTTF DDSCFQAVLD
     KGTLDAIMTD TDKGTLETAD KLMSEIGRVL TCGGRFLCVS LAQAHVLEKL VRHFSQGGWM
     VRVHQVMQGS TSETGSQFPM PVFVFVMTKV RQISGFPTVL EMMPDEEGGK PVRWGSPEEF
     MEAVKERQRY ALIRNRLNQN QSSQEVSLDL CDGDSRKSRY TFYIVDSPAV RLSHSNHFAI
     FIIPHGRETE WLFGSEQGRK QLAGSVGFNR LIIVALHRDQ QYTDMKAIQS ELSAKVLELA
     PPGLPDNQQI PFLSAGEDIG SRTIQHRGKS EFSGEYVVED VRGDGNSSYR RLIFLSNQNV
     VQSEARLLPI STHIGQKKRK DKKKQQKPVK DLEQPTITRI DKSYLCCEHH KAMISGLALL
     PNPGLLPECQ ASVLVIGLGG GSLSLFIHDY FPGSRVEVVE IDPSVLDVAS NWFNFCQDER
     MKVHLADGLV HINSLADNGE ACYDVIMFDV DSKDPSVGMS CPPPAFVEKM FLQNVHNILN
     ANGVFILNLV CRDTDLRLKV LNVLHEVFPL IYAQKIDEEV NEILFCRPNS ERKFSSLELK
     ESAKNLEKKL RKPGVQWDST YSLAEMLKSV QIV