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SET5_SCHPO
ID   SET5_SCHPO              Reviewed;         319 AA.
AC   O74467;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=SET domain-containing protein 5;
DE            EC=2.1.1.-;
GN   Name=set5; ORFNames=SPCC1739.05;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND THR-318, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC         methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR   EMBL; CU329672; CAA20779.1; -; Genomic_DNA.
DR   PIR; T41113; T41113.
DR   RefSeq; NP_588413.1; NM_001023404.2.
DR   AlphaFoldDB; O74467; -.
DR   SMR; O74467; -.
DR   BioGRID; 275434; 22.
DR   STRING; 4896.SPCC1739.05.1; -.
DR   iPTMnet; O74467; -.
DR   MaxQB; O74467; -.
DR   PaxDb; O74467; -.
DR   PRIDE; O74467; -.
DR   EnsemblFungi; SPCC1739.05.1; SPCC1739.05.1:pep; SPCC1739.05.
DR   GeneID; 2538853; -.
DR   KEGG; spo:SPCC1739.05; -.
DR   PomBase; SPCC1739.05; set5.
DR   VEuPathDB; FungiDB:SPCC1739.05; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   HOGENOM; CLU_028281_0_0_1; -.
DR   InParanoid; O74467; -.
DR   OMA; DAFQMMA; -.
DR   PhylomeDB; O74467; -.
DR   PRO; PR:O74467; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000785; C:chromatin; IC:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:PomBase.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:PomBase.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.170.270.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..319
FT                   /note="SET domain-containing protein 5"
FT                   /id="PRO_0000317700"
FT   DOMAIN          4..141
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         318
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   319 AA;  36499 MW;  B0A26AF8F546B1CB CRC64;
     MNPYETEIYK VVPIPNKGMG MIAKVKIPVG TRIFAETPLI RTKSDAKEIE EALSTKTKEE
     QEAFHRLFNA HPDTMGPFLG PFYSNALTID ETKGGMFLLG SRMNHDCSPN VKHTWNPRLD
     QVTVHAVRDI EAGEEILTTY IDLHKSHTER QKILLEHFGF KCYCSVCSVE ERKIRKISDL
     RRKQLAYYDR TMAKMCIVNP RGALRALRHR IHIAHEELLF GRLDIIALLD AFRLCVIHGD
     FERASIFAKK GTKAISLYEG TDSEKYLKIS KYVENPRSHA LAEGVPALPL FLEEDDELSD
     LEDNLWGCKL EEDVYSDTD
 
 
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