ID A0A162LV62_9HYPO Unreviewed; 1220 AA.
AC A0A162LV62;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=BBO_03838 {ECO:0000313|EMBL:OAA45260.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA45260.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA45260.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA45260.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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}.
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 -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC {ECO:0000256|ARBA:ARBA00011755}.
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:OAA45260.1}.
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DR EMBL; AZHA01000009; OAA45260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162LV62; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000076863; 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 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 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:OAA45260.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAA45260.1}.
FT DOMAIN 1078..1195
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1204..1220
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1220 AA; 135989 MW; 2B0D265B77B7DBE1 CRC64;
MTRPPPGVSF AQFFPNAPKV RAEAQGRSDR DRIRQITDSA ESSTLSAVAH DNASDALSRS
QVNGGGVMPT HQGDDDSPLG DMPSTVDSTS SHASSSSSLF SNAAARLPTS GTPRVSHAPA
VSSPLHHSNS TTSLYKGSIS LKAELATNGA ESRSHSAPSD PLRIEREVAR EPGSSVKGRK
CTYDPILDRL RNKAVSKSAK PVYREFGLDD TPAPQDPRLA KGGRLGYINT DFYLPRSRFS
PAPENLKPYP YDPKTSIGPG PPTQIVVTRY NPLIPFNKVT AIFATFGDIA ESSNKMHPET
GSYLGFATIR YRDSKRADRP SISAIDAARR AVQARGLKVD SEMVKVEYDP EGRRSRRMLE
SHLRREREKL EREKIAQAAL SAKTSAEIKP SPVSFARPPP TGPKGPATSR PLQSPVSQAT
PPPPPANRAA NFESRDISAQ LANEPYIFID CQSVPLLTSI LPHMKKRLKN YAFDDIRIDK
TGYYVIFKNS FTGKMEAERC FRAVNHTEFF TYNMSMQLCL PRTRAITPVD RKRSPSPERN
SRRAEQLRAE EDANRRRRED EADIEEERKQ RAKNFDPVME AVQVVQREMM EHLIRHIRTQ
VAAPSLSDFL DPANHSAKRR QLNIDVAEEE DEAALTDAFD TSRMGTPNSR ADPIERRTGR
FEVGALPKIR KSKTKGAAYR STFVDPFSRK RASVSRPAFR SLHHRLKSFD SDFESDDDTD
AKTLAAAEAE GNASRPQSRM STDEDNWAPN EDDSMTEASL AVVDKSLSKK RKLVSAADIA
SKRHKKLDED AFGVRFDDAK TDLSEDVGAE ADVADDNDSS LSRSQTPLSI VPKGGKKKST
KPTSSIAKQA FEEQENWSQK ADDDETPEPQ SIPKKSIPTP REPQKYDERL FSTEPVSKAL
LLPDNFKPDI SALELLHLGA KDVPDMTKLG KRFQTADVGN ADLWLWQKQR IRQLNTSRSS
THKPISIGGY YVPNPTGCAR TEGVKKILNS EKSKYLPHHI KVQKVREERE ARVKNGKDSV
ASSVDASKIA ADKLIAKGNS RANRATNRRY VADLNDQKKT LGQDSDVFKF NQLKKRKKPV
KFARSAIHNW GLYTMEDIHK DDMIIEYVGE EVRQQISEIR ENRYLKSGIG SSYLFRIDEN
TVIDATKKGG IARFINHSCL PNCTAKIIKV EGSKRIVIYA LREITMNEEL TYDYKFEREI
GSLDRIPCLC GTAACKGFLN
//
