ID   A1DM29_ASPF1            Unreviewed;      1241 AA.
AC   A1DM29;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   02-SEP-2026, entry version 120.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839, ECO:0000256|PIRNR:PIRNR037104};
DE            EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182, ECO:0000256|PIRNR:PIRNR037104};
GN   ORFNames=NFIA_051950 {ECO:0000313|EMBL:EAW15850.1};
OS   Aspergillus fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Neosartorya fischeri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW15850.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3. Binds RNAs which might negatively affect its histone
CC       methyltransferase activity. COMPASS recognizes ubiquitinated H2B on one
CC       face of the nucleosome which stimulates the methylation of H3 on the
CC       opposing face. {ECO:0000256|ARBA:ARBA00044492}.
CC   -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3. COMPASS recognizes ubiquitinated H2B on one face of the
CC       nucleosome which stimulates the methylation of H3 on the opposing face.
CC       {ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine =
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine + 3 H(+); Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537,
CC         Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         EC=2.1.1.354; Evidence={ECO:0000256|ARBA:ARBA00047571,
CC         ECO:0000256|PIRNR:PIRNR037104};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = N(6)-methyl-L-
CC         lysyl-[histone] + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00905};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         methionine = N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + S-
CC         adenosyl-L-homocysteine + H(+); 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:0000256|ARBA:ARBA00049129};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC         = N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         homocysteine + H(+); Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540,
CC         Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000256|ARBA:ARBA00047583};
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC       {ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- SUBUNIT: Component of the Set1C/COMPASS complex.
CC       {ECO:0000256|ARBA:ARBA00044515}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|PROSITE-ProRule:PRU00905}.
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DR   EMBL; DS027698; EAW15850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1DM29; -.
DR   STRING; 331117.A1DM29; -.
DR   KEGG; nfi:NFIA_051950; -.
DR   VEuPathDB; FungiDB:NFIA_051950; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_1_0_1; -.
DR   OMA; CHMTALF; -.
DR   OrthoDB; 308383at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; 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; 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; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 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 {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|PIRNR:PIRNR037104};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037104}.
FT   DOMAIN          1099..1216
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1225..1241
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          19..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..421
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..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..723
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..734
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1037
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1062
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   1241 AA;  139380 MW;  5410637BC4667BFE CRC64;
     MSRTSAGFAD FFPTAPSVLQ QKRVRAPRDR SRSKDRPEDQ LQVQDGNGQL ACSSGASAAN
     VSTNGSPPSV SVSETGTGVE KPGCKLVEET NTDITGTDTS ILSASLAQCR ATQVNEARFD
     NLTPVTNAES SPPRKLSPHQ SKSVSVAEYE SNKFATDELK LAATPLHTPP TPRSQTSRSG
     VIKGCKLVYD PDLEKRSSKE KRRKPQYVDF VVNEQDGCSP DPRLSILNYT RGAGCKQKTK
     YRPAPYRLKQ WPYDTATTIG PGPPVQIVVT GFDPLTPVAP INALFSSFGE ISEINNRTDP
     ITGRFLGVCS VKYKDSTSFR GAGPIPAATA ARRAYVECKK EQRIGTRRIR VELDRDGAVS
     DRIVARAIES QRMGHKKNTV GEEAKIEPQA KKNEPPPTAP KGPSRSSTRP AAAVPEGPRA
     SFLKPAMPSL IEETPILGQI KRDPYIFIAH CYVPVLSTTI PHLKKRLKLF DWKDIRCDKT
     GYYIIFENSR RGEEETERCF KVCHMKPLFT YIMNMESQPY GNPNYERSPS PERLQAERRE
     RAERERLKKE ADLDLEEEKK QRAIDLDPCR EVLALIVRDL KDKLLEDVKS RIAAPTLYDY
     LDPDRHAARR RALGIPDPEG IRRHTFQLDV DIFGSNNPQS SLPGGRSFSP YGLNILALPR
     IRKARRLNRA HAAFLDERRK QPVRRKEVRP LYHRLQQLHD VDDSDEDQRT PFSRDIDEQD
     SRPPSRMSSR SSISDDGEES EPLDGLASQD KRHEARLLGL EYGDSGTTLN ETVDGYSRHD
     SPGLSSTRKR KRLAEGIEVR KRPKEESERS ELNRSVETEN TLFYEESQHS EAAELGAVKP
     ENLAGIGGKF LGRLEDRSIK EDGEKENVER LQIKSAIQGA DLDVQPPLPD ESTIAKSHED
     PITEIEWGVS NDEPRPTVDD DETIILDLDG WQNLVKDEED LCFLRHVLDG QSRSKVGNLS
     AWAWRQKEIK ALNRPGESGP VHQETRIPDY YVCNPTGAAR TEGRKRILES EKSKYLPHRI
     KVQKAREERE ANAKSDPHAS AAEAARISAA KTISKSTSRS TRVNNRRLVA DINAQKQALP
     MQGGDGDVLR FNQLKKRKKP VRFARSAIHN WGLYAEENIS ANDMIIEYVG EKVRQQVADM
     RERQYLKSGI GSSYLFRIDE NTVIDATKRG GIARFINHSC TPNCTAKIIK VDGSKRIVIY
     ALRDIGRDEE LTYDYKFERE WDSDDRIPCL CGSTGCKGFL N
//