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Database: UniProt
Entry: A0A0M8N0F1_9HYPO
LinkDB: A0A0M8N0F1_9HYPO
Original site: A0A0M8N0F1_9HYPO 
ID   A0A0M8N0F1_9HYPO        Unreviewed;       524 AA.
AC   A0A0M8N0F1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839};
DE            EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
DE   AltName: Full=SET domain-containing protein 1 {ECO:0000256|ARBA:ARBA00030093};
GN   ORFNames=ESCO_002547 {ECO:0000313|EMBL:KOS18004.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS18004.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS18004.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KOS18004.1}.
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DR   EMBL; LGSR01000022; KOS18004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8N0F1; -.
DR   STRING; 150374.A0A0M8N0F1; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000053831; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd20072; SET_SET1; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR044570; Set1-like.
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   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KOS18004.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOS18004.1}.
FT   DOMAIN          382..499
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          508..524
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  59023 MW;  1779CCE0314160D4 CRC64;
     MEAVEARRKL NILPPEADDD DLSDDGDNGA FRADTPNSRA DPIERRTSRF EPKALPKIRK
     SKIKESAAET ALKRQKKSDE ELFGVRMGHL DASSKATEDS EDQWQEPEAV EDSALSRSET
     PSSLSIPTKA PKKKPPKAKK KTKKQIFEER EALKRQQEAQ TQEDETDDLK TEIVDIVAEE
     EPEPVVVEKY DEKLFSTEPL TVALSLPEGF RPDIASLTDL SLGPNDMPDL AKLQKRFHIG
     DIGDPELWLW KRNRIRELNS HGASNKPVCI EGYYVPNSTG CARTEGVKKI LNSEKSKYLP
     HHIKVQKARE EREASYKRTG KDAAAAANEA AKIAAEKLIA KGNSRANRVT NRRFVADLND
     QKKTLGQDSD VFKFNQLKKR KKPVKFARSA IHNWGLYAME NIGKDDMIIE YVGEEVRQQI
     AEIREARYLK SGIGSSYLFR IDDNTVIDAT KKGGIARFIN HSCMPNCTAK IIKVEGSKRI
     VIYALRDIAL NEELTYDYKF EREIGSTDRI PCLCGTAACK GFLN
//
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