SET1_USTMA
ID SET1_USTMA Reviewed; 1468 AA.
AC Q4PB36; A0A0D1C6X9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:P38827};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=SET1; ORFNames=UMAG_02677;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC specifically mono-, di- and trimethylates histone H3 to form
CC H3K4me1/2/3, which subsequently plays a role in telomere length
CC maintenance and transcription elongation regulation.
CC {ECO:0000250|UniProtKB:P38827}.
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:0000250|UniProtKB:P38827};
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; CM003145; KIS69337.1; -; Genomic_DNA.
DR RefSeq; XP_011389058.1; XM_011390756.1.
DR AlphaFoldDB; Q4PB36; -.
DR SMR; Q4PB36; -.
DR STRING; 5270.UM02677P0; -.
DR PRIDE; Q4PB36; -.
DR EnsemblFungi; KIS69337; KIS69337; UMAG_02677.
DR GeneID; 23563368; -.
DR KEGG; uma:UMAG_02677; -.
DR VEuPathDB; FungiDB:UMAG_02677; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004532_0_0_1; -.
DR InParanoid; Q4PB36; -.
DR OMA; KQYERQG; -.
DR OrthoDB; 1017537at2759; -.
DR Proteomes; UP000000561; Chromosome 6.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF11767; SET_assoc; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1468
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269777"
FT DOMAIN 1327..1444
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1453..1468
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 164530 MW; 7CC6632973149DF9 CRC64;
MPYSSQQNGY TSASTSRLSE QTSSHSRSSR EDRHLTEKGR RPPSPEARHR SDRDYDRRRS
TEYVRDDDYR RSSRSSHDSR YADAYDHWRS ARSAYSPTPR DDRRDEARND LSSTKRHRSP
EHSTSRLRHR SPESAHRRQN GTANRLDSKP DRGGDRKTGE ALDSGRSRWS QRAYEYDDWR
NERPSARYER YRHDREPHRS RREDEYETKR SRDDSNGNSI YAPTRRSRSR SRSRSRSRDR
YRSRDHSRER RRERSRDRSN GTYSSRDDRR PKADRSAHTI KRDEHSTRLN GTSEDSKDLR
HESQRRVSAS VQSASEGPAS TPVARAVYIK HAEVDQEAPA PPTTRDYHSC PQRWPDQADS
AVRASSAPNG SATAPSRSDR PPANGSSGRH SPRSLPTREK AEEARTSSTR RPSSQTNDNV
NNSRDPLTQR KATSERSFGH VLLPHELPVE CRGKNYMATA TYKEGVKSIY KSAADKHLVD
VDTRDPRRLG KKSSRYRESL HSASFRWDSN SRGKKPLPPP RNLVLTNLSG LLQPHQILLH
ILPHGRIESS KLEIDPKIGQ SLGIFRVTFA HDFDEHGKPL ESMPAGQNPQ HGAKVAKAAC
LALNGRMIGQ TRAQAFLDRD GEVIAERIKA KLAENEHKLR PTIVPPAPPA AASSSPATPS
TTKQSMPPPQ VPRGPKVFMP AAPSPSYASS PASARANTDR YEYSATSHSR YRSSYEESRK
LASSETYHRR RGTEEYDTYN RSKPYADAQV PAGSRSETRK DIKRPDEEIL NELRDKKRPY
VHIPRPKNCD IDVTSVEAQL RSTAPIWVRE GQKGFYAAFH TSKEANQCKV VNETLTIGGY
TLQVDVRSAP SQHAPSQQIR TPSGKHASVP LSMPAPPKQE RKAIDTGLRP PTADEKLKVD
WSAAELQDAV FRMLQKELAD TFVRDVKSRV VGPYLTAYLK PDGEGGKMLA KATMKKPVIP
TSINDHGTTL FEATGEARLP SFRKLAGAHP KKKASDADTT TSQAKRDQTD AKKKRGHTHR
SKVHRDRDVS SSENESDDME RGMVVAARRN SYTRSKSSTK RRGAAAWLLE ASDAEAGTDD
VDSTETDALS RSVSASVEPT GEEQIEVDVG AKAKKIPKVK AATVSKKKGT TAARKKLDVA
PPEAVVEADQ GSETATPETD VPIKTAAAKA KVKPAKTSAK AKSALVDPFE AGLVEDSEDC
HYLRLALEHL SRTGELASEH TLPDEIELEV EAEEQAMAAG GIPKHSTGSA RTEGYYRIPP
EQKAMHLPDR NKATEDVDTS SNAQILQSAR NNRADSRRLV LGIEQHKRET ATDTDIFKFN
QLRTRKKQLK FAKSPIHDWG LYAMELIPAG DMVIEYVGEV VRQQVADERE KQYERQGNFS
TYLFRVDDDL VVDATHKGNI ARLMNHCCTP NCNAKILTLN GEKRIVLFAK TAIRAGEELT
YDYKFQSSAD DEDAIPCLCG SPGCRRFL
