CTM1_CANGA
ID CTM1_CANGA Reviewed; 551 AA.
AC Q6FR37;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cytochrome c lysine N-methyltransferase 1;
DE EC=2.1.1.59;
GN Name=CTM1; OrderedLocusNames=CAGL0I01210g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380955; CAG60244.1; -; Genomic_DNA.
DR RefSeq; XP_447307.1; XM_447307.1.
DR AlphaFoldDB; Q6FR37; -.
DR STRING; 5478.XP_447307.1; -.
DR EnsemblFungi; CAG60244; CAG60244; CAGL0I01210g.
DR GeneID; 2889115; -.
DR KEGG; cgr:CAGL0I01210g; -.
DR CGD; CAL0132300; CAGL0I01210g.
DR VEuPathDB; FungiDB:CAGL0I01210g; -.
DR eggNOG; ENOG502RXKP; Eukaryota.
DR HOGENOM; CLU_026942_0_0_1; -.
DR InParanoid; Q6FR37; -.
DR OMA; NEHALMI; -.
DR Proteomes; UP000002428; Chromosome I.
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..551
FT /note="Cytochrome c lysine N-methyltransferase 1"
FT /id="PRO_0000228982"
FT DOMAIN 46..273
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 184..288
FT /note="SET-like"
SQ SEQUENCE 551 AA; 63533 MW; 639D2E7A75853C0E CRC64;
MELANICNAT IAKGIAVQKD SYGGYGVYIV DPGALVGCND PKLGGDKIEL LRVSSVFNVK
NLMEAMNALE GEYAEDGQRA ADMFKSIIGS SIEELSAVSE TCLLVYFMMV IYLMGEQGYA
VPMKISRYID TVLLGTTVNN ASNCIESMLI HYEHVALFHE LDNNLQKLHK TLISKMPSKK
NYSIELLRQI YSATVSRVLE IPQELHEENY MDNYVVTPSL VPILDYVNHG DKTSRNAYYD
VDRRKGDIIL YLDLTVVNPG KLKPNTEVLI TYKDIEDSLA MITKYGFDPA NYTTTGTKIF
SCTFDKMYLS TNKFDNEIDI RNFYQWFSIN PSLQFVLNSE NEWLINDSLA EFERLLVPFA
TSSQRNEHYW IYSDGDDARK RFMEYFDIDE VEDEDEAWAQ LETQFKWFES SENDLMPFPP
CVWTVKSKFL KEKEATGYEL EKVIQNKLEN SRALYNETTN QFQAYLENYL DYRIDVLQEY
SPEDTENENA VSQLIARELS VLLKIRDRIN NNKSIFLNSE DKKYAKLPLL PTKNVERPPW
LSEGDDDFDQ D