ID   A1DM29_NEOFI            Unreviewed;      1241 AA.
AC   A1DM29;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 112.
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   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. 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, which subsequently plays a role in telomere length
CC       maintenance and transcription elongation regulation.
CC       {ECO:0000256|ARBA:ARBA00002789, ECO:0000256|PIRNR:PIRNR037104}.
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:0000256|ARBA:ARBA00000944,
CC         ECO:0000256|PIRNR:PIRNR037104};
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC       {ECO:0000256|ARBA:ARBA00011755, ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037104}.
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DR   EMBL; DS027698; EAW15850.1; -; Genomic_DNA.
DR   RefSeq; XP_001257747.1; XM_001257746.1.
DR   AlphaFoldDB; A1DM29; -.
DR   STRING; 331117.A1DM29; -.
DR   EnsemblFungi; EAW15850; EAW15850; NFIA_051950.
DR   GeneID; 4584262; -.
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; 950362at2759; -.
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   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 2.
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   4: Predicted;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037104};
KW   Chromosome {ECO:0000256|PIRNR:PIRNR037104};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR037104}; Nucleus {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        23..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..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        765..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//