RKM3_YEAST
ID RKM3_YEAST Reviewed; 552 AA.
AC P38222; D6VQ31;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ribosomal lysine N-methyltransferase 3 {ECO:0000303|PubMed:18957409};
DE EC=2.1.1.- {ECO:0000269|PubMed:18957409, ECO:0000269|PubMed:24517342};
GN Name=RKM3 {ECO:0000303|PubMed:18957409};
GN OrderedLocusNames=YBR030W {ECO:0000312|SGD:S000000234}; ORFNames=YBR0314;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=18957409; DOI=10.1074/jbc.m806006200;
RA Webb K.J., Laganowsky A., Whitelegge J.P., Clarke S.G.;
RT "Identification of two SET domain proteins required for methylation of
RT lysine residues in yeast ribosomal protein Rpl42ab.";
RL J. Biol. Chem. 283:35561-35568(2008).
RN [7]
RP FUNCTION.
RX PubMed=24517342; DOI=10.1021/pr401251k;
RA Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.;
RT "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights
RT into non-histone protein lysine methyltransferase activity.";
RL J. Proteome Res. 13:1744-1756(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that monomethylates 60S ribosomal protein L42 (RPL42A
CC and RPL42B) at 'Lys-40'. {ECO:0000269|PubMed:18957409,
CC ECO:0000269|PubMed:24517342}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7880 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z35899; CAA84972.1; -; Genomic_DNA.
DR EMBL; X76078; CAA53686.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07151.1; -; Genomic_DNA.
DR PIR; S45886; S45886.
DR RefSeq; NP_009586.1; NM_001178378.1.
DR AlphaFoldDB; P38222; -.
DR BioGRID; 32732; 106.
DR IntAct; P38222; 4.
DR MINT; P38222; -.
DR STRING; 4932.YBR030W; -.
DR MaxQB; P38222; -.
DR PaxDb; P38222; -.
DR PRIDE; P38222; -.
DR EnsemblFungi; YBR030W_mRNA; YBR030W; YBR030W.
DR GeneID; 852318; -.
DR KEGG; sce:YBR030W; -.
DR SGD; S000000234; RKM3.
DR VEuPathDB; FungiDB:YBR030W; -.
DR eggNOG; KOG1337; Eukaryota.
DR GeneTree; ENSGT00940000153577; -.
DR HOGENOM; CLU_033565_1_0_1; -.
DR InParanoid; P38222; -.
DR OMA; FIYETTV; -.
DR BioCyc; YEAST:G3O-29008-MON; -.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
DR PRO; PR:P38222; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38222; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:SGD.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IMP:SGD.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 2.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..552
FT /note="Ribosomal lysine N-methyltransferase 3"
FT /id="PRO_0000202472"
FT DOMAIN 26..335
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 399..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 334
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 552 AA; 62594 MW; E7460154E683D7B0 CRC64;
MSVTFKDDVH RILKFVANCN GRFEDSKCDI RESPLGGLGV FAKTDIAEGE SILTLNKSSI
FSASNSSIAN LLCDSSIDGM LALNIAFIYE TTVFRNSSHW YPFLRTIRIR DDEGHLNLPP
SFWHADAKRL LKGTSFDTLF DSLAPEEEIM EGFEIAVDLA HKWNDEFGLE IPKGFLDVSE
ENHEEDYNLK LEKFISVAYT LSSRGFEIDA YHETALVPIA DLFNHHVSDP DLKFVSLYDV
CDKCGEPDMC KHLIAEEYLE AENLDKNMPK VASMETRVID EDLIKSLEND LEKEYSNVTA
NIEDDDGGIE NPDECVDLVL KNDVAQGQEI FNSYGELSNV FLLARYGFTV PENQYDIVHL
GPDFMKILKK EEKYQEKVKW WSQVGHGLFS AWYAQMRQED EEDEDGQAKS DNLSDDIESE
EEEEEEEGDD SLESWLSQLY IDSSGEPSPS TWALANLLTL TAVQWESLFS KKATPHISDS
IVNEEKLPFL AKKDNPHSKK LLSNLLKEKQ LPCIKGDNSS KITSATKSML QNARTLVQSE
HNILDRCLKR LS
