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ETKMT_DANRE
ID   ETKMT_DANRE             Reviewed;         258 AA.
AC   A3KP85;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Electron transfer flavoprotein beta subunit lysine methyltransferase {ECO:0000305};
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 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=etfbkmt {ECO:0000250|UniProtKB:Q8IXQ9}; Synonyms=mettl20;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI34210.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC134209; AAI34210.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001154967.1; NM_001161495.1.
DR   AlphaFoldDB; A3KP85; -.
DR   SMR; A3KP85; -.
DR   STRING; 7955.ENSDARP00000103806; -.
DR   PaxDb; A3KP85; -.
DR   GeneID; 100005455; -.
DR   KEGG; dre:100005455; -.
DR   CTD; 254013; -.
DR   ZFIN; ZDB-GENE-111107-1; etfbkmt.
DR   eggNOG; ENOG502QUSY; Eukaryota.
DR   InParanoid; A3KP85; -.
DR   OrthoDB; 1585716at2759; -.
DR   PhylomeDB; A3KP85; -.
DR   Reactome; R-DRE-8876725; Protein methylation.
DR   PRO; PR:A3KP85; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
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           ?..258
FT                   /note="Electron transfer flavoprotein beta subunit lysine
FT                   methyltransferase"
FT                   /id="PRO_0000318712"
SQ   SEQUENCE   258 AA;  28950 MW;  69EA4F65B5F88FA1 CRC64;
     MYRRIIMCFR SRATLNSFQR GMCCSTRRYV SSTGSEDDIK NFIIDNTEIV NSQSLTPEIS
     LRLFTPTCRF WTENPEFWPF PDPYWAIYWP GGQALARYLL NNPEVSAGRK VLDLGCGCGA
     SAIAARLSGA SCVVANDIDP IAAIATKMNC ELNNLAPLPC VTDNMIGSET DGWDLILLGD
     MFYDEALADG LHQWLQTCTN THGTQVLIGD PGRAQFEDHN IRRSLHRLAH FQLPDSVKEE
     NYGLTSSAVW RYNCKPDH
 
 
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