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