RKM4_SCHPO
ID RKM4_SCHPO Reviewed; 468 AA.
AC Q9P6L2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ribosomal lysine N-methyltransferase 4 {ECO:0000250|UniProtKB:Q12504};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q12504};
DE AltName: Full=SET domain-containing protein 13 {ECO:0000303|PubMed:20444689};
GN Name=set13 {ECO:0000303|PubMed:20444689};
GN ORFNames=SPAC688.14 {ECO:0000312|PomBase:SPAC688.14};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20444689; DOI=10.1074/jbc.m110.132274;
RA Shirai A., Sadaie M., Shinmyozu K., Nakayama J.;
RT "Methylation of ribosomal protein L42 regulates ribosomal function and
RT stress-adapted cell growth.";
RL J. Biol. Chem. 285:22448-22460(2010).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that monomethylates 60S ribosomal protein L42 (rpl42)
CC at 'Lys-55'. {ECO:0000269|PubMed:20444689}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:20444689}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000305}.
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DR EMBL; CU329670; CAB90780.2; -; Genomic_DNA.
DR RefSeq; NP_594072.2; NM_001019496.2.
DR AlphaFoldDB; Q9P6L2; -.
DR SMR; Q9P6L2; -.
DR BioGRID; 279768; 13.
DR STRING; 4896.SPAC688.14.1; -.
DR iPTMnet; Q9P6L2; -.
DR MaxQB; Q9P6L2; -.
DR PaxDb; Q9P6L2; -.
DR PRIDE; Q9P6L2; -.
DR EnsemblFungi; SPAC688.14.1; SPAC688.14.1:pep; SPAC688.14.
DR GeneID; 2543346; -.
DR KEGG; spo:SPAC688.14; -.
DR PomBase; SPAC688.14; set13.
DR VEuPathDB; FungiDB:SPAC688.14; -.
DR eggNOG; KOG1338; Eukaryota.
DR HOGENOM; CLU_621353_0_0_1; -.
DR InParanoid; Q9P6L2; -.
DR OMA; MFNGDDE; -.
DR PRO; PR:Q9P6L2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:PomBase.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IMP:PomBase.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR CDD; cd19178; SET_SETD6; 1.
DR InterPro; IPR011383; N-lys_methylase_SETD6.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044430; SETD6_SET.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF011771; RMS1_SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..468
FT /note="Ribosomal lysine N-methyltransferase 4"
FT /id="PRO_0000303948"
FT DOMAIN 22..302
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 188..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 468 AA; 54023 MW; F2934820771869BC CRC64;
MLKQAESMLK WAIEKDNYTT SEKIGLNDYR HVHESLGIGF IALEDIKEDE KLVSFKKDSV
LCLTNSDLAQ LPEVQSLPSW AALLLVMATE NASPNSFWRP YLSIFPTKER ITSPFYWDEN
KKDALLRGTV LESNEDCNEI TQLWIDRIEP IIKLYPNRFS QVSYEDFLRM SAVMLAYSFD
IEKTKSPISN ENEKSAAETS IKEDKNGDAA KKNEGSANQD DEKLHSQSLV GNNCEVNSED
EFSDLESEVD PDELEKAMCP ISDMFNGDDE LCNIRLYDIN GTLTMIATRD IKKGEQLWNT
YGELDNSELF RKYGFTKKKG TPHDFVLIKK EHWLPEYIEK LGFEEVEARL ELLCREELLY
NLEGDFTFSK ADLTFKEICL AFVLMEKEKE LISVPSKSDI KPKHYRKLLK IIEKRINMYP
KISDPKNFDE ENAKTLIEGE IDILQNLSAK VKEALTKNRP KKKQKVDH
