ID   SET1_SCHPO              Reviewed;         920 AA.
AC   Q9Y7R4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE            EC=2.1.1.354 {ECO:0000269|PubMed:12589755};
DE   AltName: Full=COMPASS component set1;
DE   AltName: Full=Lysine N-methyltransferase 2;
DE   AltName: Full=SET domain-containing protein 1;
DE   AltName: Full=Set1 complex component set1;
DE            Short=Set1C component set1;
DE   AltName: Full=Spset1;
GN   Name=set1 {ECO:0000312|EMBL:CAB41652.1}; Synonyms=kmt2;
GN   ORFNames=SPCC306.04c;
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] {ECO:0000312|EMBL:CAB41652.1}
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.
RX   PubMed=12193658; DOI=10.1073/pnas.182436399;
RA   Noma K., Grewal S.I.S.;
RT   "Histone H3 lysine 4 methylation is mediated by Set1 and promotes
RT   maintenance of active chromatin states in fission yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16438-16445(2002).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND IDENTIFICATION IN 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   [4] {ECO:0000305}
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12589755; DOI=10.1016/s0022-2836(03)00030-5;
RA   Kanoh J., Francesconi S., Collura A., Schramke V., Ishikawa F.,
RA   Baldacci G., Geli V.;
RT   "The fission yeast spSet1p is a histone H3-K4 methyltransferase that
RT   functions in telomere maintenance and DNA repair in an ATM kinase Rad3-
RT   dependent pathway.";
RL   J. Mol. Biol. 326:1081-1094(2003).
RN   [5] {ECO:0000305}
RP   IDENTIFICATION IN 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: Catalytic component of the COMPASS (Set1C) complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3 (PubMed:12589755, PubMed:12488447). Binds RNA which might
CC       negatively affect its histone methyltransferase activity (By
CC       similarity). COMPASS recognizes ubiquitinated H2B on one face of the
CC       nucleosome which stimulates the methylation of H3 on the opposing face
CC       (By similarity). Methylation promotes maintenance of active chromatin
CC       states at euchromatic chromosomal domains and is present throughout the
CC       cell cycle (PubMed:12193658). Plays a role in telomere maintenance and
CC       DNA repair in an ATM kinase rad3-dependent pathway (PubMed:12589755).
CC       Required for efficient telomeric and centromeric silencing
CC       (PubMed:12589755). {ECO:0000250|UniProtKB:P38827,
CC       ECO:0000269|PubMed:12193658, ECO:0000269|PubMed:12488447,
CC       ECO:0000269|PubMed:12589755}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC         COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC         Evidence={ECO:0000269|PubMed:12589755};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC         = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC         COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000250|UniProtKB:P38827};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3]
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-
CC         COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:P38827};
CC   -!- SUBUNIT: Component of the Set1C/COMPASS complex composed of ash2, sdc1,
CC       set1, shg1, spp1, swd1, swd2 and swd3. {ECO:0000269|PubMed:12488447,
CC       ECO:0000269|PubMed:14617822}.
CC   -!- INTERACTION:
CC       Q9Y7R4; Q9HDV4: lid2; NbExp=2; IntAct=EBI-2106005, EBI-2105919;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC   -!- DOMAIN: A construct containing set1 C-terminal fragment of 692-920 is
CC       able to form H3K4me.
CC   -!- DOMAIN: The RxxxRR motif forms an adapter helix that bridges the
CC       nucleosome and ubiquitin. {ECO:0000250|UniProtKB:P38827}.
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; CAB41652.1; -; Genomic_DNA.
DR   PIR; T41282; T41282.
DR   RefSeq; NP_587812.1; NM_001022805.2.
DR   AlphaFoldDB; Q9Y7R4; -.
DR   SMR; Q9Y7R4; -.
DR   BioGRID; 275345; 365.
DR   ELM; Q9Y7R4; -.
DR   IntAct; Q9Y7R4; 1.
DR   STRING; 284812.Q9Y7R4; -.
DR   iPTMnet; Q9Y7R4; -.
DR   MaxQB; Q9Y7R4; -.
DR   PaxDb; 4896-SPCC306-04c-1; -.
DR   EnsemblFungi; SPCC306.04c.1; SPCC306.04c.1:pep; SPCC306.04c.
DR   GeneID; 2538762; -.
DR   KEGG; spo:SPCC306.04c; -.
DR   PomBase; SPCC306.04c; set1.
DR   VEuPathDB; FungiDB:SPCC306.04c; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_1_0_1; -.
DR   InParanoid; Q9Y7R4; -.
DR   OMA; ERLPCLC; -.
DR   PhylomeDB; Q9Y7R4; -.
DR   Reactome; R-SPO-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   PRO; PR:Q9Y7R4; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000785; C:chromatin; IC:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IDA:PomBase.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IDA:PomBase.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; ISM:PomBase.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IC:PomBase.
DR   CDD; cd00590; RRM_SF; 1.
DR   CDD; cd12303; RRM_spSet1p_like; 1.
DR   CDD; cd20072; SET_SET1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR044570; Set1-like.
DR   InterPro; IPR017111; Set1_fungi.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF11767; SET_assoc; 1.
DR   PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS51572; SAM_MT43_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW   Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..920
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT                   specific"
FT                   /id="PRO_0000186085"
FT   DOMAIN          94..179
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          781..898
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          904..920
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          205..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           749..754
FT                   /note="RxxxRR motif"
FT                   /evidence="ECO:0000250|UniProtKB:P38827"
FT   COMPBIAS        205..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         897
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   920 AA;  105038 MW;  C4AD7E6C3ECFF8BC CRC64;
     MDFNTSTRSK SQPVQRNNYK VLYDPELGIK ENLGRKIIYR FNGVSKPPLV VRDPRLKNPI
     YARGIPKSGR PFLKSLQTIN YDYNENSLGP EPPTQVFVSN ISPLVTSEQL RYHFKSFGEV
     FDLDLKLNPY TGTSLGLCCI SFDKRSSISV AAHSAKIAVQ QANGLRFSGK PLSVVLDRDG
     SLCEEAFKKA LNAVEKQFQE ETLQKQRFER EDESSRQKLS AAMNEDIPPW RQPSKNSQTL
     SNGDLQHSKV QNVDQKSGFL TSSETDVPKN INDYIYLLID DRFVPPDRVY YTDIKHHFRK
     FLYEKIYMNK DGFYITFNNY REASNCYRAL DRTYVQNCRI KLKFHDIPSR TKEDGKKSAV
     RRVVLPPEEA YAEATSVVLR DLEAALLRDV KSKIIGPAIF KYLHSMPKPS VKEELQENLL
     VSSTSVPDVP LKIESTVGKL PSLPKFKKRV DSSKMNLSAG SKTKSKLQRR RRRRHEARPL
     HYQLNQMYNS SASEAESDQE LLLSSGDERV ERGKIGSIKS VKSDEATPVF SDTSDENDKF
     HRFRTKSKIS KKKYEKMEVD YTSSSETESD ASILSPSAAI PKSGSAIKDE LISPKKEIDE
     VLALAPKWRI NEFDETGSVY YGALPYNYPE DDVLLDLDGL QYLVKNDEDY SYLQEALKDE
     PLMDINDPNF WAYERKSCKF KNGDVKYGDT AILPEPKGYF RSNTSGSAKS EGYYIIPTTE
     KSLYLPLRNR STIDTISHST SRITSRMNRV NNRRLAAGVE KSQLPAEADL LRFNALKARK
     KQLHFGPSRI HTLGLFAMEN IDKNDMVIEY IGEIIRQRVA DNREKNYVRE GIGDSYLFRI
     DEDVIVDATK KGNIARFINH SCAPNCIARI IRVEGKRKIV IYADRDIMHG EELTYDYKFP
     EEADKIPCLC GAPTCRGYLN
//