ID SWD2_SCHPO Reviewed; 357 AA.
AC O60137;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 24-JAN-2024, entry version 137.
DE RecName: Full=Set1 complex component swd2;
DE Short=Set1C component swd2;
DE AltName: Full=COMPASS component swd2;
DE AltName: Full=Complex proteins associated with set1 protein swd2;
GN Name=swd2 {ECO:0000312|EMBL:CAA18403.1};
GN Synonyms=swd2.1 {ECO:0000303|PubMed:14617822}; ORFNames=SPBC18H10.06c;
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] {ECO:0000312|EMBL:CAA18403.1}
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] {ECO:0000305}
RP FUNCTION, AND COMPOSITION OF THE SET1 COMPLEX.
RX PubMed=12488447; DOI=10.1074/jbc.m209562200;
RA Roguev A., Schaft D., Shevchenko A., Aasland R., Shevchenko A.,
RA Stewart A.F.;
RT "High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation
RT in budding and fission yeasts.";
RL J. Biol. Chem. 278:8487-8493(2003).
RN [3] {ECO:0000305}
RP COMPOSITION OF THE SET1 COMPLEX.
RX PubMed=14617822; DOI=10.1074/mcp.m300081-mcp200;
RA Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
RA Shevchenko A.;
RT "A comparative analysis of an orthologous proteomic environment in the
RT yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL Mol. Cell. Proteomics 3:125-132(2004).
CC -!- FUNCTION: The Set1 complex specifically methylates 'Lys-4' of histone
CC H3. {ECO:0000269|PubMed:12488447}.
CC -!- SUBUNIT: Component of the Set1 complex composed of ash2, sdc1, set1,
CC shg1, spp1, swd1, swd2 and swd3. {ECO:0000269|PubMed:12488447,
CC ECO:0000269|PubMed:14617822}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat SWD2 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA18403.1; -; Genomic_DNA.
DR PIR; T39770; T39770.
DR RefSeq; NP_595730.1; NM_001021628.2.
DR AlphaFoldDB; O60137; -.
DR SMR; O60137; -.
DR BioGRID; 277307; 179.
DR STRING; 284812.O60137; -.
DR iPTMnet; O60137; -.
DR MaxQB; O60137; -.
DR PaxDb; 4896-SPBC18H10-06c-1; -.
DR EnsemblFungi; SPBC18H10.06c.1; SPBC18H10.06c.1:pep; SPBC18H10.06c.
DR GeneID; 2540788; -.
DR KEGG; spo:SPBC18H10.06c; -.
DR PomBase; SPBC18H10.06c; swd2.
DR VEuPathDB; FungiDB:SPBC18H10.06c; -.
DR eggNOG; KOG1446; Eukaryota.
DR HOGENOM; CLU_044117_3_0_1; -.
DR InParanoid; O60137; -.
DR OMA; EISMATI; -.
DR PhylomeDB; O60137; -.
DR Reactome; R-SPO-9772755; Formation of WDR5-containing histone-modifying complexes.
DR PRO; PR:O60137; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IC:PomBase.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR037867; Swd2/WDR82.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19861:SF0; WD REPEAT-CONTAINING PROTEIN 82; 1.
DR PANTHER; PTHR19861; WD40 REPEAT PROTEIN SWD2; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..357
FT /note="Set1 complex component swd2"
FT /id="PRO_0000051252"
FT REPEAT 24..65
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 110..149
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 199..241
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 247..289
FT /note="WD 4"
FT /evidence="ECO:0000255"
SQ SEQUENCE 357 AA; 39813 MW; B7B901D7F3063C9D CRC64;
MTTVSITFDL LSSMQPRKWL KNQNFVGEIT SLSFDDSGEL CLASCTDDTL QLYNCISGKF
VKSLASKKYG AHLGRFTHHS NSLIHASTKE DNTVRYLDVV TNRYLRYFPG HKQTVTSIDV
SPADETFLSA SLDNTIRLWD LRSPNCQGLL NVSSPVVAAF DATGLIFASV SERKYKISLY
NIKSFDARPF QDIPLTFLPP HVRIANVEFS TDGKYLLLTT GNDFHYVIDA YSGSELLRVP
SKVSTKTQDG NLTYYASACM SPDSKFLFTS YDNEHLCMYQ LPELKQTVNS DHIVNSFTEM
GLASTTPTSN SHSTENPLAI IPSSTSKNLL PETPSIVRFN PRFSQLVTAH SGVIFWT
//
