ID   ETKMT_XENLA             Reviewed;         246 AA.
AC   Q4V7W8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Electron transfer flavoprotein beta subunit lysine methyltransferase;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q80ZM3, ECO:0000250|UniProtKB:Q8IXQ9};
DE   AltName: Full=ETFB lysine methyltransferase;
DE            Short=ETFB-KMT;
DE   AltName: Full=Protein N-lysine methyltransferase METTL20;
DE   Flags: Precursor;
GN   Name=etfbkmt; Synonyms=mettl20;
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=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC       trimethylates the flavoprotein ETFB in mitochondria. Thereby, may
CC       negatively regulate the function of ETFB in electron transfer from
CC       Acyl-CoA dehydrogenases to the main respiratory chain.
CC       {ECO:0000250|UniProtKB:Q8IXQ9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IXQ9}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IXQ9}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. ETFBKMT
CC       family. {ECO:0000305}.
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DR   EMBL; BC097686; AAH97686.1; -; mRNA.
DR   RefSeq; NP_001090037.1; NM_001096568.1.
DR   AlphaFoldDB; Q4V7W8; -.
DR   SMR; Q4V7W8; -.
DR   DNASU; 735110; -.
DR   GeneID; 735110; -.
DR   KEGG; xla:735110; -.
DR   CTD; 735110; -.
DR   Xenbase; XB-GENE-5901000; etfbkmt.S.
DR   OMA; ILNCELN; -.
DR   OrthoDB; 1585716at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 735110; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:1904733; P:negative regulation of electron transfer activity; ISS:UniProtKB.
DR   GO; GO:1904736; P:negative regulation of fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Mitochondrion; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..246
FT                   /note="Electron transfer flavoprotein beta subunit lysine
FT                   methyltransferase"
FT                   /id="PRO_0000318713"
SQ   SEQUENCE   246 AA;  27598 MW;  EF4E92CA7BEBFBCF CRC64;
     MLRTARFLQR SISATSRPNC IVQPQRTSAT CPRSFILQHT EATSDPLTPE IRLRLLTPRC
     DFWRQKPELW PYGDPYWAIY WPGGQALSRF LLDNPQIVRG GRVLDLGCGC GAAAIAAWMG
     GASYVLANDI DPVAGEAFRL NCELNNMKPL DFQAENLIGR ETGPWSLIVL GDMFYDAELA
     DLLCDWLRRS IRSHGTKVLI GDPGRAQFSS HPVLRHLQPL AQYSLSDSTK EENYGLTDST
     VWSFEP