ID   CMKMT_XENLA             Reviewed;         318 AA.
AC   Q6GQ33;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Calmodulin-lysine N-methyltransferase;
DE            Short=CLNMT;
DE            Short=CaM KMT;
DE            EC=2.1.1.60;
GN   Name=camkmt; Synonyms=clnmt;
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20975703; DOI=10.1038/ncomms1044;
RA   Magnani R., Dirk L.M., Trievel R.C., Houtz R.L.;
RT   "Calmodulin methyltransferase is an evolutionarily conserved enzyme that
RT   trimethylates Lys-115 in calmodulin.";
RL   Nat. Commun. 1:43-43(2010).
CC   -!- FUNCTION: Catalyzes the trimethylation of 'Lys-116' in calmodulin.
CC       {ECO:0000269|PubMed:20975703}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[calmodulin]-L-lysine + S-adenosyl-L-methionine =
CC         [calmodulin]-N(6)-methyl-L-lysine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:21556, Rhea:RHEA-COMP:11360, Rhea:RHEA-COMP:11361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.60;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00942,
CC         ECO:0000269|PubMed:20975703};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7Z624}. Nucleus
CC       {ECO:0000250|UniProtKB:Q7Z624}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. CLNMT methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00942}.
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DR   EMBL; BC072915; AAH72915.1; -; mRNA.
DR   RefSeq; NP_001085547.1; NM_001092078.1.
DR   AlphaFoldDB; Q6GQ33; -.
DR   SMR; Q6GQ33; -.
DR   PRIDE; Q6GQ33; -.
DR   DNASU; 443973; -.
DR   GeneID; 443973; -.
DR   KEGG; xla:443973; -.
DR   CTD; 443973; -.
DR   Xenbase; XB-GENE-5848447; camkmt.L.
DR   OrthoDB; 1161502at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 443973; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018025; F:calmodulin-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025800; CaM-Lys-N-MeTrfase.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13539; PTHR13539; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51610; SAM_CLNMT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..318
FT                   /note="Calmodulin-lysine N-methyltransferase"
FT                   /id="PRO_0000300117"
SQ   SEQUENCE   318 AA;  35880 MW;  2D5F472806EBFABC CRC64;
     MESSVPLGNS VRTGAACGRI MAVPSKAAQG DARARWKLLG QALRKERLDD SLQKVSVRRF
     NSFRLFSVVE MKEIKREADC QTWFQYTCVF CPQYSLCLRH NSGISNVADI LTSFDNTGNV
     CVWPSEEVMA YYCLKHKDIF RGLAVCELGG GMTCLAGLMV AISADVKEVL LTDGNEKAIK
     NVSDIIRRPQ NEEMFKDRLV SSRVLRWDNE TDVSQLEGHF DIVICADCLF LDQYRACLVD
     AIKRLLKPSG KAMVFAPPRG NTLSQFCNLA EAAGFSIQRH ENYDEHISNF HSKLKEKEAA
     VYDENLHYPF LLVLCKTR