CTM1_YEAST
ID CTM1_YEAST Reviewed; 585 AA.
AC P38818; D3DL59; Q66R84;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytochrome c lysine N-methyltransferase 1;
DE EC=2.1.1.59;
GN Name=CTM1; OrderedLocusNames=YHR109W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=10791961; DOI=10.1074/jbc.m001891200;
RA Polevoda B., Martzen M.R., Das B., Phizicky E.M., Sherman F.;
RT "Cytochrome c methyltransferase, Ctm1p, of yeast.";
RL J. Biol. Chem. 275:20508-20513(2000).
RN [6]
RP DOMAIN.
RX PubMed=16096273; DOI=10.1074/jbc.m507672200;
RA Porras-Yakushi T.R., Whitelegge J.P., Miranda T.B., Clarke S.;
RT "A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in
RT yeast.";
RL J. Biol. Chem. 280:34590-34598(2005).
CC -!- FUNCTION: Methyltransferase which mediates trimethylation of 'Lys-78'
CC of cytochrome c (CYC1). {ECO:0000269|PubMed:10791961}.
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 ECO:0000269|PubMed:10791961};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10791961}.
CC -!- DOMAIN: The SET-like region, although related with the SET domain is
CC not detected by any prediction method. {ECO:0000269|PubMed:16096273}.
CC -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; U00059; AAB68855.1; -; Genomic_DNA.
DR EMBL; AY723824; AAU09741.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06803.1; -; Genomic_DNA.
DR PIR; S48951; S48951.
DR RefSeq; NP_011977.1; NM_001179239.1.
DR AlphaFoldDB; P38818; -.
DR BioGRID; 36542; 49.
DR DIP; DIP-5597N; -.
DR IntAct; P38818; 1.
DR STRING; 4932.YHR109W; -.
DR iPTMnet; P38818; -.
DR MaxQB; P38818; -.
DR PaxDb; P38818; -.
DR PRIDE; P38818; -.
DR EnsemblFungi; YHR109W_mRNA; YHR109W; YHR109W.
DR GeneID; 856509; -.
DR KEGG; sce:YHR109W; -.
DR SGD; S000001151; CTM1.
DR VEuPathDB; FungiDB:YHR109W; -.
DR eggNOG; ENOG502RXKP; Eukaryota.
DR HOGENOM; CLU_026942_0_0_1; -.
DR InParanoid; P38818; -.
DR OMA; NEHALMI; -.
DR BioCyc; YEAST:YHR109W-MON; -.
DR PRO; PR:P38818; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38818; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000277; F:[cytochrome c]-lysine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IDA:SGD.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..585
FT /note="Cytochrome c lysine N-methyltransferase 1"
FT /id="PRO_0000202911"
FT DOMAIN 18..273
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 186..288
FT /note="SET-like"
FT CONFLICT 256
FT /note="K -> R (in Ref. 3; AAU09741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 68284 MW; 353BCC6EF1425309 CRC64;
MEEVFRFYSN SRNIFIHKSL SLKPSTIDDP KSGYGLFVEP SKFKNDELKS ETIQLLRIPK
RCTFNINTLL ALLGDEDEFS SKEEFQRTND KIKIALREIM AHPNFSVFLT ETNLLIIYFM
IFQTIRSRYE IPENIQYYLE NVLMSIEVET AMDSIENLAT DYGHYPQIFG LRETLNLFKE
LFHDVLNLSD IKHLYSAIIS RCLEIPERAD TKSEEFTVHS TLVPIVDFAN HEGTQKNAYF
DIDPSNNDVL LLLDTKAVQS ELTKPIEVFI SYSPTEDLFS MLVTYGFTPD FRGNSQFWTV
SFDRCFLRNY DGPDKTTNLR LFYKWMHINP VVPLVKYEHN GKTRWFLNDT TPEFDMLLLP
FIPSIDDGKI ARWAYDSTCH LMFTKIHCLI NPEANEHALM IAENYRSLIK EKESNGDDFI
NLPPLAWSLR YKDTENDCVR QRHICSEDAV AVLKQEEMQD STKTKSQFTS FFRKFLEFRR
SKIIRPTSDS KVASILYQQE LEIIADLAKA IDSSSTIFFS DLNVTLDTEP ERLPPLRFLD
DYIEISADKQ EPSPICEDLS YYTPSRFTDF FQEEVSQYAA FFQDD
