ID   CTM1_KLULA              Reviewed;         503 AA.
AC   Q6CMC0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Cytochrome c lysine N-methyltransferase 1;
DE            EC=2.1.1.59;
GN   Name=CTM1; OrderedLocusNames=KLLA0E21494g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Methyltransferase which mediates trimethylation of cytochrome
CC       c (CYC1). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[cytochrome c] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[cytochrome c] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:24312, Rhea:RHEA-COMP:9754, Rhea:RHEA-COMP:9755,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.59;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00943};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- DOMAIN: The SET-like region, although related with the SET domain is
CC       not detected by any prediction method. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190,
CC       ECO:0000255|PROSITE-ProRule:PRU00943}.
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DR   EMBL; CR382125; CAH00006.1; -; Genomic_DNA.
DR   RefSeq; XP_454919.1; XM_454919.1.
DR   AlphaFoldDB; Q6CMC0; -.
DR   STRING; 28985.XP_454919.1; -.
DR   EnsemblFungi; CAH00006; CAH00006; KLLA0_E21407g.
DR   GeneID; 2894625; -.
DR   KEGG; kla:KLLA0_E21407g; -.
DR   eggNOG; ENOG502RXKP; Eukaryota.
DR   HOGENOM; CLU_026942_0_0_1; -.
DR   InParanoid; Q6CMC0; -.
DR   OMA; NEHALMI; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000277; F:[cytochrome c]-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018022; P:peptidyl-lysine methylation; IEA:InterPro.
DR   InterPro; IPR025815; Ctm1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS51611; SAM_MT59; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..503
FT                   /note="Cytochrome c lysine N-methyltransferase 1"
FT                   /id="PRO_0000228983"
FT   DOMAIN          52..276
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          190..291
FT                   /note="SET-like"
SQ   SEQUENCE   503 AA;  58504 MW;  EFA5142927DCF82D CRC64;
     MEAATEWLLE NTPITKSECT TIRESVVDGD TGGYGVFVNF TKLRTLKGEK DSKFELLRIP
     RSATISMTSI RDILAKSTSE NAVTASIKGH LTAFLSDENH HAFINETNLI VIYLVLKAIL
     SDNKTYKLTG FASFYLNEVL LKTFVPLPCN TFQEDADKWN QYYKEYLNFP QQLFIEIINR
     FISARFLGMN YEKLISTVYC SVISRILEIP ESSGEDTDDF FVSPTLVPLL DFVNHDNDHR
     NAHFDIDLRT NDIVLYLELD DIDSTVEEAQ VFISYAPVEE LVHFEQIYGF LPKSNNVQVW
     CYRFDEDFLS TYHYNGINVS HFYKCMRVRP SFQILILPSE VLINDCIVEF GELLILFSQH
     LQDPKKISFQ LSETNDSYCS ILKDKCGTET TKLLDKEECL EEFFGEHDEI ENYEKTLKEF
     KSFLSKYITF RREKISSINL LSQNSSFTAF WQKEINLLDS LKGQFESKKE VMWYEKYGND
     EKIKIPTVPF PPPSWIDYEN MRV