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Database: UniProt
Entry: A0A0F8DG84_CERFI
LinkDB: A0A0F8DG84_CERFI
Original site: A0A0F8DG84_CERFI 
ID   A0A0F8DG84_CERFI        Unreviewed;       964 AA.
AC   A0A0F8DG84;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   Name=SET1 {ECO:0000313|EMBL:KKF94994.1};
GN   ORFNames=CFO_g2635 {ECO:0000313|EMBL:KKF94994.1};
OS   Ceratocystis fimbriata f. sp. platani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF94994.1, ECO:0000313|Proteomes:UP000034841};
RN   [1] {ECO:0000313|EMBL:KKF94994.1, ECO:0000313|Proteomes:UP000034841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFO {ECO:0000313|EMBL:KKF94994.1,
RC   ECO:0000313|Proteomes:UP000034841};
RA   Belbahri L.;
RT   "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT   trees.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKF94994.1}.
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DR   EMBL; LBBL01000125; KKF94994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8DG84; -.
DR   Proteomes; UP000034841; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; IPR000504; RRM_dom.
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; 3.
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; PS50102; RRM; 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:UP000034841};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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          128..219
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          822..939
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          948..964
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  108555 MW;  5EF6F61A544EE988 CRC64;
     MTPSSEPHNI YNNKTTTTLP LSPSPAQTER IPARDTNRSI LGLRCIYDPS SDRSGSAKSA
     KRDLEPRFKE FGPNDDTPPA DPRLAKGGRL GYINVDFHLP KSRLRHAPYN LKPYQFDART
     SIGPSPPTQI VVSGFNPLMS FAKLTALFSQ FGDIAESSNK LDPEDGSYLG FATFRYRDSP
     PNAVRRIFVA AIDAARRAVR DANGRRIDTY RIKVEFDADG YFIIFESSNY GRIEAERCHR
     QCNEAELFTY HMTMELFVPA NLLNHIGSSS TRHRRPSTPE LKARAEQREK EEQEQLKREL
     EEDIEEEKRQ RAKNFDPVGE AVQVIRRELL EHLIRHIRVK VAAPAVLDFM EPANHVAKRR
     ELNLEIPEMH SAFLDDSEEP SRAGTPNSRA DPIENRTGKF DVSALPRIRK FKSAAPPASS
     LKANRKAPNR QNAIRSLHHR LYDSESDSDD DLQAPKQRSV TRDTEEYEPR PTSRMSTDED
     KEEGATWGGG EEDLMMERSF AATDGSQVRK RKLELLEEVV IKRQKKLDED PMETDSVAPT
     DDGNHDVDTD VQSRAETPVL QPATGKAAPK KKAAPKSKKK TKKQLAEEAE AAKRQAEAAA
     AVIAEPKAEP EPSAKPVVRE VKEKVVKNLD PKLFPSSPMP ALELSVDTII SDFRILNGLG
     LGAHDAPDVS RLLRRSKATT MEQPELWVWT RDRLRTLNAN KSSQDGSAMI EGYYVPNPTG
     CARTEGYKKI LNSEKSKYLP HHIKVQKARE ERQARVSKDG KDPTASAAEA AKLAAEKLIS
     QGNSRANRAN NRRYVADLND QKKTLGQDSD VFKFNQLKKR KKPVKFARSA IHNWGLYAME
     KIPKDDMIIE YVGEEVRQQI SEIREKRYLK SGIGSSYLFR IDEDTVIDAT KKGGIARFIN
     HSCMPNCTAK IIKVEGSKRI VIYALRDIAL NEELTYDYKF EREIGALDRI PCLCGTAACK
     GFLN
//
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