ACKMT_CAEEL
ID ACKMT_CAEEL Reviewed; 190 AA.
AC Q9XX11;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=ATP synthase subunit C lysine N-methyltransferase;
DE EC=2.1.1.- {ECO:0000269|PubMed:30530489};
GN ORFNames=Y39A1A.21 {ECO:0000312|WormBase:Y39A1A.21a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30530489; DOI=10.1074/jbc.ra118.005473;
RA Malecki J.M., Willemen H.L.D.M., Pinto R., Ho A.Y.Y., Moen A.,
RA Kjoenstad I.F., Burgering B.M.T., Zwartkruis F., Eijkelkamp N.,
RA Falnes P.O.;
RT "Lysine methylation by the mitochondrial methyltransferase FAM173B
RT optimizes the function of mitochondrial ATP synthase.";
RL J. Biol. Chem. 294:1128-1141(2019).
CC -!- FUNCTION: Mitochondrial protein-lysine N-methyltransferase that
CC trimethylates ATP synthase subunit C. Trimethylation is required for
CC proper incorporation of the C subunit into the ATP synthase complex and
CC mitochondrial respiration. {ECO:0000269|PubMed:30530489}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC Evidence={ECO:0000269|PubMed:30530489};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000269|PubMed:30530489};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6P4H8}.
CC -!- SIMILARITY: Belongs to the ANT/ATPSC lysine N-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CAA21030.2; -; Genomic_DNA.
DR PIR; T26741; T26741.
DR RefSeq; NP_001022840.2; NM_001027669.4.
DR AlphaFoldDB; Q9XX11; -.
DR SMR; Q9XX11; -.
DR STRING; 6239.Y39A1A.21a; -.
DR EPD; Q9XX11; -.
DR PaxDb; Q9XX11; -.
DR PeptideAtlas; Q9XX11; -.
DR EnsemblMetazoa; Y39A1A.21a.1; Y39A1A.21a.1; WBGene00012658.
DR EnsemblMetazoa; Y39A1A.21a.2; Y39A1A.21a.2; WBGene00012658.
DR UCSC; Y39A1A.21a; c. elegans.
DR WormBase; Y39A1A.21a; CE50211; WBGene00012658; -.
DR eggNOG; KOG4058; Eukaryota.
DR GeneTree; ENSGT00390000014771; -.
DR HOGENOM; CLU_068443_4_0_1; -.
DR InParanoid; Q9XX11; -.
DR OMA; GVNTVWF; -.
DR OrthoDB; 1605787at2759; -.
DR PRO; PR:Q9XX11; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012658; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9XX11; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:UniProtKB.
DR GO; GO:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; IMP:UniProtKB.
DR GO; GO:1905706; P:regulation of mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026170; FAM173A/B.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13610; PTHR13610; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..190
FT /note="ATP synthase subunit C lysine N-methyltransferase"
FT /id="PRO_0000446890"
SQ SEQUENCE 190 AA; 20493 MW; E04442599C578DD7 CRC64;
MGMNTGLVIA GVAGATALAI SAAAIPFVAP ALRRVCIPYV PATTEQLANV SRALSLATSS
NSNKKGTLID LGSGDGRVVL QCAREGFNST GVELNSILVA YSKYRSIREG LGKETRFMRK
NIFKTDLNPY QTAVIFGAES LMGDLVPKLS EMRSNTNLLA CRFPLPENDA WKLEHQIGEG
IDAVWVYKRN