SET7_SCHPO
ID SET7_SCHPO Reviewed; 147 AA.
AC Q9Y7Q6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-37 specific;
DE EC=2.1.1.- {ECO:0000269|PubMed:30773398};
GN Name=set7 {ECO:0000312|PomBase:SPCC297.04c};
GN ORFNames=SPCC297.04c {ECO:0000312|PomBase:SPCC297.04c};
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 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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-20; TYR-59; TYR-61; ASN-79; HIS-80; TRP-88 AND TYR-115.
RX PubMed=30773398; DOI=10.1016/j.str.2019.01.011;
RA Shen Y., Mevius D.E.H.F., Caliandro R., Carrozzini B., Roh Y., Kim J.,
RA Kim S., Ha S.C., Morishita M., di Luccio E.;
RT "Set7 Is a H3K37 Methyltransferase in Schizosaccharomyces pombe and Is
RT Required for Proper Gametogenesis.";
RL Structure 27:631638.e8-631638.e8(2019).
CC -!- FUNCTION: Histone lysine methyltransferase that specifically mono-,
CC di-, and trimethylates 'Lys-37' of histone H3 to regulate sporulation.
CC {ECO:0000269|PubMed:30773398}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(37)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:67112, Rhea:RHEA-COMP:17189, Rhea:RHEA-COMP:17190,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000269|PubMed:30773398};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67113;
CC Evidence={ECO:0000269|PubMed:30773398};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67116, Rhea:RHEA-COMP:17190, Rhea:RHEA-
CC COMP:17191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000269|PubMed:30773398};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67117;
CC Evidence={ECO:0000269|PubMed:30773398};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(37)-[histone H3] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(37)-[histone H3]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67120, Rhea:RHEA-
CC COMP:17191, Rhea:RHEA-COMP:17192, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:30773398};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67121;
CC Evidence={ECO:0000269|PubMed:30773398};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30773398}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:30773398}. Nucleus {ECO:0000269|PubMed:30773398}.
CC -!- DISRUPTION PHENOTYPE: Abnormal sporulation resulting in asci with fewer
CC than four spores and with abnormal spore wall morphology.
CC {ECO:0000269|PubMed:30773398}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAB40784.1; -; Genomic_DNA.
DR PIR; T41271; T41271.
DR RefSeq; NP_588361.1; NM_001023352.2.
DR PDB; 5H6Z; X-ray; 2.00 A; A/B=1-147.
DR PDB; 5WW0; X-ray; 2.10 A; A/B=1-147.
DR PDBsum; 5H6Z; -.
DR PDBsum; 5WW0; -.
DR AlphaFoldDB; Q9Y7Q6; -.
DR SMR; Q9Y7Q6; -.
DR BioGRID; 275699; 2.
DR STRING; 4896.SPCC297.04c.1; -.
DR iPTMnet; Q9Y7Q6; -.
DR MaxQB; Q9Y7Q6; -.
DR PaxDb; Q9Y7Q6; -.
DR PRIDE; Q9Y7Q6; -.
DR EnsemblFungi; SPCC297.04c.1; SPCC297.04c.1:pep; SPCC297.04c.
DR GeneID; 2539127; -.
DR KEGG; spo:SPCC297.04c; -.
DR PomBase; SPCC297.04c; set7.
DR VEuPathDB; FungiDB:SPCC297.04c; -.
DR eggNOG; ENOG502S3RW; Eukaryota.
DR HOGENOM; CLU_124044_0_0_1; -.
DR InParanoid; Q9Y7Q6; -.
DR OMA; ATYEINF; -.
DR PhylomeDB; Q9Y7Q6; -.
DR PRO; PR:Q9Y7Q6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0062122; F:histone methyltransferase activity (H3-K37 specific); IDA:PomBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR009207; SET7_MeTrfase.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF022536; A612L_SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Sporulation; Transferase.
FT CHAIN 1..147
FT /note="Histone-lysine N-methyltransferase, H3 lysine-37
FT specific"
FT /id="PRO_0000317701"
FT DOMAIN 8..116
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT MUTAGEN 20
FT /note="R->A: Decreases activity."
FT /evidence="ECO:0000269|PubMed:30773398"
FT MUTAGEN 59
FT /note="Y->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:30773398"
FT MUTAGEN 61
FT /note="Y->A: Severely decreases activity."
FT /evidence="ECO:0000269|PubMed:30773398"
FT MUTAGEN 79
FT /note="N->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:30773398"
FT MUTAGEN 80
FT /note="H->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:30773398"
FT MUTAGEN 88
FT /note="W->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:30773398"
FT MUTAGEN 115
FT /note="Y->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:30773398"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:5H6Z"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:5H6Z"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:5H6Z"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:5H6Z"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:5H6Z"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:5H6Z"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:5H6Z"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:5H6Z"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5H6Z"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5H6Z"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5WW0"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:5H6Z"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:5H6Z"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5H6Z"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:5H6Z"
SQ SEQUENCE 147 AA; 17209 MW; 44FBC2EBC2ED3E3D CRC64;
MRIPVIRSPL EIRDTERKGR GVFALEPIPA QTCIEISPVL MFSKEEYEQH GQYTVLNEYT
YVWSEGKQGL ALGLGSMFNH DRHPNVYWKK DNRNNYISYY TLREIKTNEE LCISYGDHLW
FEDEASSASR ISPNEENEDF PLQNISL
