SET11_SCHPO
ID SET11_SCHPO Reviewed; 381 AA.
AC O74405;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ribosomal lysine N-methyltransferase set11;
DE EC=2.1.1.-;
DE AltName: Full=Meiotically up-regulated gene 76 protein;
DE AltName: Full=SET domain-containing protein 11;
GN Name=set11; Synonyms=mug76; ORFNames=SPCC1223.04c;
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
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, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 189-ASN--PRO-192 AND
RP 216-GLY--TYR-224.
RX PubMed=18195021; DOI=10.1074/jbc.m709429200;
RA Sadaie M., Shinmyozu K., Nakayama J.;
RT "A conserved SET domain methyltransferase, Set11, modifies ribosomal
RT protein Rpl12 in fission yeast.";
RL J. Biol. Chem. 283:7185-7195(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that trimethylates 60S ribosomal protein L12 (rpl1201
CC and rpl1202) at 'Lys-4' and may dimethylate L12 also at 'Lys-40' and
CC 'Lys-41'. Overexpression causes a severe growth defect. Has a role in
CC meiosis. {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:18195021}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
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; CU329672; CAA20873.1; -; Genomic_DNA.
DR PIR; T40864; T40864.
DR RefSeq; NP_588349.1; NM_001023340.1.
DR AlphaFoldDB; O74405; -.
DR SMR; O74405; -.
DR BioGRID; 275802; 37.
DR STRING; 4896.SPCC1223.04c.1; -.
DR PaxDb; O74405; -.
DR EnsemblFungi; SPCC1223.04c.1; SPCC1223.04c.1:pep; SPCC1223.04c.
DR GeneID; 2539232; -.
DR KEGG; spo:SPCC1223.04c; -.
DR PomBase; SPCC1223.04c; set11.
DR VEuPathDB; FungiDB:SPCC1223.04c; -.
DR eggNOG; KOG1337; Eukaryota.
DR HOGENOM; CLU_041939_3_2_1; -.
DR InParanoid; O74405; -.
DR OMA; YYGNYQV; -.
DR PhylomeDB; O74405; -.
DR PRO; PR:O74405; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; TAS:PomBase.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR016852; SET_MeTrfase.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF027158; Lys_MTase_YDR198C_prd; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Meiosis; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..381
FT /note="Ribosomal lysine N-methyltransferase set11"
FT /id="PRO_0000116804"
FT DOMAIN 23..224
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT MUTAGEN 189..192
FT /note="Missing: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18195021"
FT MUTAGEN 216..224
FT /note="Missing: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18195021"
SQ SEQUENCE 381 AA; 44080 MW; 3EE7D5A3DD364169 CRC64;
MSNKQNIESE VSWVKSKGAF VHPSLEFSVI PDAGSCVLAN NDINENTVLL KLPPNILINK
RTCSRYSFRD KLTSFQFLSW LISEDVHSNL EISPYYTKAL PQGFSFHPVT LTSDHPLWSI
LPDEVRNSLL ERKNVMAFDY EQVKKFVSVD QPTFQWGWLC VNTRCLYYDT GSKNTEDHLT
LAPIFEYFNH SPEAQTALIN TRGTITIKST RRIDKGEQIF LCYGPHGNDK LFTEYGFCLS
NNPNISIQLD RFIEFDKWQQ SFLQDHGYWN DYTCSLHGAS FRTLVGVRTL LVSPSEKLND
ASYDQTRRVL QYINGFSDGS RDRQDVEDYL KKVLQELLCE AEECKEKVKG ISDGSYVFIC
AEQLWKDRIM CCQYLMEHSF E
