ID A0A100INM8_ASPNG Unreviewed; 1239 AA.
AC A0A100INM8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=ABL_07193 {ECO:0000313|EMBL:GAQ44532.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ44532.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ44532.1}.
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DR EMBL; BCMY01000012; GAQ44532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100INM8; -.
DR VEuPathDB; FungiDB:An18g06840; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1168483; -.
DR VEuPathDB; FungiDB:ATCC64974_106410; -.
DR VEuPathDB; FungiDB:M747DRAFT_150101; -.
DR OMA; CHMTALF; -.
DR Proteomes; UP000068243; 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 InterPro; IPR010916; TonB_box_CS.
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.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 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 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 1097..1214
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1223..1239
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 139234 MW; 9D08376A6F72A6ED CRC64;
MSRSSAGFAD FFPTAPSVLQ QKRKTIRERP RSEAHPEHDH SDEGRALPEE SKAILELTTG
LYAEEQNLPT VNGDGLASSD SVSVSAARPS THKHSTAYGN EARLDTLTPL TNAESSPAQR
LSPSHIRTAN GIEDSSGTIK TDDIKPAMTP LQTPPTPRSQ SRTSGNVRGW KLVYDPDSEK
RISSKEKRRK ARYVDIVPNG QDDRPADPRL KISNYSRGGG CKQKTKFRPA PYSLKHWPYD
ASTTIGPGPP VQIVVTGFDP LTPIAPINAL FSSFGEIAEI NNRTDPITGR FLGICSVKYK
DSASFRGGGP VLAANAARRA YYECKKEQRI GTRRIRVELD RDGIVSAKIV TRAVDSQRMG
DRNNLLSAEE PKTGVSAKNN EPPPTAPKGP SGRSQMRPTV PVPEGPRASF LKPVVPSLVE
EIPILSQIKR DPYIFIAHCY VPVLSTTVPH LKKRLKLFDW KDIRCDKTGY YIVFENSRRG
EEETERCYKM CHMKPLFTYI MNMESQPYGN PNYERSPSPQ RLQAEQRERA EKDRLKREAE
LDIEEEKRQR ALDLDPCREV VAIIIRDLRD KLLEDVKSRI AAPALYDYLD PVRHATKRER
LGIPEPEGAK RPMFRIDLDS SAGTPDSRSD LSTSRNPLGS SGLNILALPR IRKAHRLDRT
NAAFLDERRK QPLRKKEVRP LYHRLQQLHD VDDSDDEQRT PFTRDTEDLD SRAPSRMSSE
TSDSEEDSDR IGSETLEVPV AERQTDSDRS HDIDITRDDE SGVSPSEAPE QVPDRLQSSS
RKRKVDDDRA KARKKQKGGD ECFDMDDAAG SGEDQDMACS PSRSDTTQDV IAAADEPSVT
GTDPLVSHGQ LAGHGQKDDA VALMDSWGAD VEYKGLGKDH RHLVSQVGSF EHGKQTEEPR
TEIEWRVSND EPRSTVDDDE SIVLDLDGWQ NLVKDEEDLR FLRDVLREFS RSNVGNLSAW
AWRQKEIKAL NRPEESGPVR EETVIPGYYV SNTTGAARTE GRKRILESEK SKYLPHRIKV
QKAREEREAR AKSDPHAVAA EAARIAAAKT ISKSTSRSTR VNNRRLIADI NAQKQALPTQ
SGDGDVLRFN QLKKRKKPVR FARSAIHNWG LYAEENISAN DMIIEYVGEK VRQQVADMRE
RRYLKSGIGS SYLFRIDENT VIDATKRGGI ARFINHSCTP NCTAKIIKVD GSKRIVIYAL
RDIERDEELT YDYKFEREWD SDDRIPCLCG STGCKGFLN
//
