ID   CMKMT_RAT               Reviewed;         323 AA.
AC   B0K012;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA   Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA   Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=3700427; DOI=10.1016/s0021-9258(19)62721-3;
RA   Rowe P.M., Wright L.S., Siegel F.L.;
RT   "Calmodulin N-methyltransferase. Partial purification and
RT   characterization.";
RL   J. Biol. Chem. 261:7060-7069(1986).
RN   [4]
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, ECO:0000269|PubMed:3700427};
CC   -!- SUBUNIT: Monomer (Probable). Interacts with HSP90, probably as a client
CC       (By similarity). {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3700427}. 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; BC159411; AAI59412.1; -; mRNA.
DR   EMBL; CH473947; EDM02674.1; -; Genomic_DNA.
DR   RefSeq; NP_001127935.1; NM_001134463.1.
DR   AlphaFoldDB; B0K012; -.
DR   SMR; B0K012; -.
DR   STRING; 10116.ENSRNOP00000048187; -.
DR   PaxDb; B0K012; -.
DR   PRIDE; B0K012; -.
DR   Ensembl; ENSRNOT00000048550; ENSRNOP00000048187; ENSRNOG00000030629.
DR   GeneID; 299521; -.
DR   KEGG; rno:299521; -.
DR   UCSC; RGD:1310453; rat.
DR   CTD; 79823; -.
DR   RGD; 1310453; Camkmt.
DR   eggNOG; KOG3201; Eukaryota.
DR   GeneTree; ENSGT00390000002168; -.
DR   HOGENOM; CLU_057006_3_1_1; -.
DR   InParanoid; B0K012; -.
DR   OrthoDB; 1161502at2759; -.
DR   PhylomeDB; B0K012; -.
DR   TreeFam; TF316589; -.
DR   Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-RNO-8876725; Protein methylation.
DR   PRO; PR:B0K012; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Proteomes; UP000234681; Chromosome 6.
DR   Genevisible; B0K012; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0018025; F:calmodulin-lysine N-methyltransferase activity; ISO:RGD.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0018022; P:peptidyl-lysine methylation; ISO:RGD.
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..323
FT                   /note="Calmodulin-lysine N-methyltransferase"
FT                   /id="PRO_0000403786"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   323 AA;  35883 MW;  3A34ED60C4038F1A CRC64;
     MESQVAVAGD GETEAEAGKG PMIDSASQGS LVSAPKGAVR WKLLRQVLKQ KQLDDGLRHV
     SVRRFESFNL FSVTEAKNRG TEKEAGAWVQ YTSIFYPEYS ISLRRNSGSL SVEDVLTSFD
     NTGNVCIWPS EEVLAYYCLK HSHLFRDLAV CELGGGMTCL AGLMVAISAD VKEVLLTDGN
     EKAIRNVNSI IASNKKTGVF KTQKISSCVL RWDNKTDVSQ LEGHFDIVMC ADCLFLDQYR
     ASLVDAIKRL LQPSGKALVF APRRGNTFNQ FCNLAEKAGL SLQRHENYDE RISNFHSKLK
     KEGSDVYEEN LHYPLLLILT KTG