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Database: UniProt
Entry: P38222
LinkDB: P38222
Original site: P38222 
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   10-APR-2019, entry version 137.
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};
GN   ORFNames=YBR0314;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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
RT   chromosome II from Saccharomyces cerevisiae reveals 16 open reading
RT   frames, including ten new open reading frames, five previously
RT   identified genes and a 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;
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.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Dephoure N., 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.,
RA   Wilkins M.R.;
RT   "Stoichiometry of Saccharomyces cerevisiae lysine methylation:
RT   insights 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
CC       (RPL42A 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
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
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   ProteinModelPortal; P38222; -.
DR   BioGrid; 32732; 105.
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_mRNA; YBR030W.
DR   GeneID; 852318; -.
DR   KEGG; sce:YBR030W; -.
DR   EuPathDB; FungiDB:YBR030W; -.
DR   SGD; S000000234; RKM3.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; HOG000142026; -.
DR   InParanoid; P38222; -.
DR   OMA; FIYETTV; -.
DR   BioCyc; YEAST:G3O-29008-MONOMER; -.
DR   PRO; PR:P38222; -.
DR   Proteomes; UP000002311; Chromosome II.
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   Pfam; PF00856; SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    552       Ribosomal lysine N-methyltransferase 3.
FT                                /FTId=PRO_0000202472.
FT   DOMAIN       26    335       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   COMPBIAS    418    427       Poly-Glu.
FT   BINDING     334    334       S-adenosyl-L-methionine.
FT                                {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
//
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