SET1_ASPFU
ID SET1_ASPFU Reviewed; 1241 AA.
AC Q4WNH8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9Y7R4};
DE AltName: Full=COMPASS component set1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=set1; ORFNames=AFUA_6G06335;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:Q9Y7R4}.
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:Q9Y7R4};
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; AAHF01000006; EAL88486.1; -; Genomic_DNA.
DR RefSeq; XP_750524.1; XM_745431.1.
DR AlphaFoldDB; Q4WNH8; -.
DR SMR; Q4WNH8; -.
DR STRING; 746128.CADAFUBP00007032; -.
DR EnsemblFungi; EAL88486; EAL88486; AFUA_6G06335.
DR GeneID; 3508771; -.
DR KEGG; afm:AFUA_6G06335; -.
DR VEuPathDB; FungiDB:Afu6g06335; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004391_1_0_1; -.
DR InParanoid; Q4WNH8; -.
DR OMA; CHMTALF; -.
DR OrthoDB; 1017537at2759; -.
DR Proteomes; UP000002530; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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 Gene3D; 3.30.70.330; -; 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; 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; PTHR45814; 1.
DR Pfam; PF11764; N-SET; 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; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1241
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269765"
FT DOMAIN 1099..1216
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1225..1241
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 139368 MW; 084B0B9578429E63 CRC64;
MSRTSAGFAD FFPTAPSVLQ QKRVRAPRDR PCPKDRPEDQ LHVQDDNGQS SCSPGTSAAN
VSTNGSPPSV SVSETGTGVE NSGCKLVGET NTDITGTDTS ILSASLAQCR ATQVNEARFD
NLTPVTNAES SPPRKLSPHQ SKSVEVAEYE SNKFATDESK LAATPLHTPP TPRSQTSRSG
VIKGCKLVYD PDLEKRSSKE KRRKPQYVDF VVNEQDGCSP DPRLSILNYT RGAGCKQKTK
YRPAPYRLKQ WPYDTATTIG PGPPVQIVVT GFDPLTPVAP INALFSSFGE ISEINNRTDP
ITGRFLGVCS VKYKDSTSFR GAGPVPAATA ARRAYVECKK EQRIGTRRIR VELDRDGAVS
DRIVARAIES QRMGHKKNIV GEEAKVEPQA KKNEPPPTAP KGPSRSSTRP VAAVPEGPRA
SFLKPAIPSL IEETPILAQI KRDPYIFIAH CYVPVLSTTI PHLKKRLKLF DWKDIRCDKT
GYYIIFENSR RGEEETERCF KVCHMKPLFT YIMNMESQPY GNPNYERSPS PERLQAERRE
RAERERLKKE ADLDLEEEKK QRAIDLDPCR EVLALIVRDL KDKLLEDVKS RIAAPTLYDY
LDPDRHAARR RALGIPDPEG IRRHTFRLDA DNFGSNNPRS FLPGDRSFSP YGLNILALPR
IRKARRLNRA NAAFLDERRK QPVRRKEVRP LYHRLQQLHD VDDSDEDQRT PFSRDIDEQD
SRPPSRMSSR SSISDDGEES EPLDGLAPQG KRHESRLLGL EYEDSGNTLN EAVDGYSRHD
SPGLSSTRKR KRVAEGIDVR KRPKEESERS QLNRSVEAGD TFYEESQHSE AAELGTVKPE
NLAGIGGKFL GRVEDRSINE DGEKENMERL HIESAIQGAN LGIQQPLPDE STTTKSHEDP
ITEIEWGVSN DEPRPTVVDD ETIILDLDGW QNLVKDEEDL CFLRHVLDGQ SRSKVGNLSA
WAWRQKEIKA LNRAGESGPV HQETRIPDYY VCNPTGAART EGRKRILESE KSKYLPHRIK
VQKAREEREA NAKSDPHASS AAEAARISAA KTISKSTSRS TRVNNRRLVA DINAQKQALP
MQGGDGDVLR FNQLKKRKKP VRFARSAIHN WGLYAEENIS ANDMIIEYVG EKVRQQVADM
RERQYLKSGI GSSYLFRIDE NTVIDATKRG GIARFINHSC TPNCTAKIIK VDGSKRIVIY
ALRDIGRDEE LTYDYKFERE WDSDDRIPCL CGSTGCKGFL N
