SET10_SCHPO
ID SET10_SCHPO Reviewed; 547 AA.
AC O74738;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ribosomal lysine N-methyltransferase set10;
DE EC=2.1.1.-;
DE AltName: Full=SET domain-containing protein 10;
GN Name=set10; ORFNames=SPBC1709.13c;
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 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 [3]
RP FUNCTION.
RX PubMed=18292091; DOI=10.1074/jbc.m709211200;
RA Shirai A., Matsuyama A., Yashiroda Y., Hashimoto A., Kawamura Y., Arai R.,
RA Komatsu Y., Horinouchi S., Yoshida M.;
RT "Global analysis of gel mobility of proteins and its use in target
RT identification.";
RL J. Biol. Chem. 283:10745-10752(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that methylates ribosomal protein L23 (rpl23a and
CC rpl23b). {ECO:0000269|PubMed:18292091}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. RKM1 family. {ECO:0000255|PROSITE-ProRule:PRU00190,
CC ECO:0000305}.
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DR EMBL; CU329671; CAA21252.1; -; Genomic_DNA.
DR PIR; T39641; T39641.
DR RefSeq; NP_595446.1; NM_001021355.2.
DR AlphaFoldDB; O74738; -.
DR SMR; O74738; -.
DR BioGRID; 276370; 19.
DR STRING; 4896.SPBC1709.13c.1; -.
DR MaxQB; O74738; -.
DR PaxDb; O74738; -.
DR EnsemblFungi; SPBC1709.13c.1; SPBC1709.13c.1:pep; SPBC1709.13c.
DR GeneID; 2539820; -.
DR KEGG; spo:SPBC1709.13c; -.
DR PomBase; SPBC1709.13c; set10.
DR VEuPathDB; FungiDB:SPBC1709.13c; -.
DR eggNOG; KOG1337; Eukaryota.
DR HOGENOM; CLU_030667_1_0_1; -.
DR InParanoid; O74738; -.
DR OMA; ISCPFEY; -.
DR PhylomeDB; O74738; -.
DR PRO; PR:O74738; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:PomBase.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; ISO:PomBase.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; NAS:PomBase.
DR CDD; cd19180; SET_SpSET10-like; 1.
DR Gene3D; 3.90.1420.10; -; 1.
DR InterPro; IPR011219; Rubisco-cyt_methylase_MET.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR044432; Set10/Efm1_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF026986; MET_SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..547
FT /note="Ribosomal lysine N-methyltransferase set10"
FT /id="PRO_0000303949"
FT DOMAIN 17..235
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 547 AA; 62320 MW; 03F965BB7B70271A CRC64;
MEKLLHEALQ NGCKLHKSVE FIQSRDDNAC FGSYIAVAQN DIAPDQLLIS CPFEYAITYN
KAKEELKKLN PNFESCNPHI TLCTFLALES LKGIQSKWYG YIEYLPKTFN TPLYFNENDN
AFLISTNAYS AAQERLHIWK HEYQEALSLH PSPTERFTFD LYIWSATVFS SRCFSSNLIY
KDSESTPILL PLIDSLNHKP KQPILWNSDF QDEKSVQLIS QELVAKGNQL FNNYGPKGNE
ELLMGYGFCL PDNPFDTVTL KVAIHPDLPH KDQKAAILEN DCQFQLSNLV FFLPKSPDKE
IFQKILQCLA VVTASSLELR KLTAHLLTGD LASYVPSLRG QIKSLEVLLM YIDSRADLLL
KSNPQVSPTS ERQVWAKIYR DSQINILQDS ITYVKNYMEE SLQKTYKPLP NLLQYLILNS
ISIFLLQHPL FAPLSHAIES LYGSTDAEAL VATDEQDILM ILICVYCLSI SEKLPFSISM
LVEGYPAVAN PEGVEVFEIL DEMFFQQFTN VFGESKHFNK ENVSWALQLV NDESLDFSGF
TFIIAHN
