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RKM2_YEAST
ID   RKM2_YEAST              Reviewed;         479 AA.
AC   Q03942; D6VSI1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Ribosomal lysine N-methyltransferase 2 {ECO:0000303|PubMed:17005568};
DE            EC=2.1.1.- {ECO:0000269|PubMed:17005568};
GN   Name=RKM2 {ECO:0000303|PubMed:17005568};
GN   OrderedLocusNames=YDR198C {ECO:0000312|SGD:S000002606};
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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   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   [4]
RP   FUNCTION.
RX   PubMed=17005568; DOI=10.1074/jbc.m606578200;
RA   Porras-Yakushi T.R., Whitelegge J.P., Clarke S.;
RT   "A novel SET domain methyltransferase in yeast: Rkm2-dependent
RT   trimethylation of ribosomal protein L12ab at lysine 10.";
RL   J. Biol. Chem. 281:35835-35845(2006).
RN   [5]
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).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that trimethylates 60S ribosomal protein L12 (RPL12A
CC       and RPL12B) at 'Lys-4' and 'Lys-11'. {ECO:0000269|PubMed:17005568,
CC       ECO:0000269|PubMed:18957409}.
CC   -!- MISCELLANEOUS: Present with 768 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. RKM2 family. {ECO:0000255|PROSITE-ProRule:PRU00190,
CC       ECO:0000305}.
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DR   EMBL; Z48784; CAA88711.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12041.1; -; Genomic_DNA.
DR   PIR; S52705; S52705.
DR   RefSeq; NP_010484.1; NM_001180506.1.
DR   AlphaFoldDB; Q03942; -.
DR   BioGRID; 32250; 54.
DR   DIP; DIP-6397N; -.
DR   IntAct; Q03942; 3.
DR   STRING; 4932.YDR198C; -.
DR   MaxQB; Q03942; -.
DR   PaxDb; Q03942; -.
DR   PRIDE; Q03942; -.
DR   EnsemblFungi; YDR198C_mRNA; YDR198C; YDR198C.
DR   GeneID; 851779; -.
DR   KEGG; sce:YDR198C; -.
DR   SGD; S000002606; RKM2.
DR   VEuPathDB; FungiDB:YDR198C; -.
DR   eggNOG; KOG1337; Eukaryota.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; CLU_041939_0_0_1; -.
DR   InParanoid; Q03942; -.
DR   OMA; YWGDYTI; -.
DR   BioCyc; YEAST:G3O-29784-MON; -.
DR   PRO; PR:Q03942; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03942; protein.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:SGD.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:SGD.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:SGD.
DR   CDD; cd19177; SET_SETD4; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR016852; SET_MeTrfase.
DR   InterPro; IPR044429; SETD4_SET.
DR   PIRSF; PIRSF027158; Lys_MTase_YDR198C_prd; 1.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..479
FT                   /note="Ribosomal lysine N-methyltransferase 2"
FT                   /id="PRO_0000253809"
FT   DOMAIN          22..325
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   479 AA;  55950 MW;  4E19ADFADEE1A0A4 CRC64;
     MEGKVDVLLT WLKKSDKFYI APNISICESP ETGRGIVLSH GSIRKNDIIV SVPSSKQLNF
     HTILYHISKF NKELNIPGIT IDRKPINYED NIIEAENKAW ADPRYGLYSE LSKEFLLSLS
     SFQLVSFYIL VENFLLPKWT HNEIYSDWKP FFDVWPSMEE LRSIPAIWNC DPNSRYHSLI
     EYLPAASRKH MARISGLVRE DWETISEVVL KWNEIYGSLS CTKNSDKFTS DELFSLFVHV
     YFIINSRCLY AKIPLKIEDS PSNFTLVPYV DFMNHICESD LHCYPQLSPQ LRSEGENIIG
     IGQFTIRCGD HLYDNINEEL FLNYGAHSND FLLNEYGFVV DGNKWNYLDI SDEIIELIDD
     DKKEVKTFLL EHDYWGDYTI NETDISYRIF VALNYYVTRD ERRVRKFIEG YISEDYFKPK
     ISSVLKELLV SLTAKYTKTL SELTEKVSNL ENNLCLQNLI TIYKGYIKIL TQHLQDLQS
 
 
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