ID A0A0M9ETW8_FUSLA Unreviewed; 1253 AA.
AC A0A0M9ETW8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=FLAG1_07563 {ECO:0000313|EMBL:KPA39560.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA39560.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA39560.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA39560.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
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}.
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:KPA39560.1}.
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DR EMBL; JXCE01000185; KPA39560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9ETW8; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000037904; 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: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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000037904};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1111..1228
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1237..1253
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 139686 MW; 1F8659F7BE2DCB7C CRC64;
MTRPPGASFA EFFPTAPKVK AQAQTRADQV RDRDRFKTAS TPASINGTID STTGTAVLEA
DANIGPNGIV SASDTMPAQP DDNESPFTDI PNTVDSASSY SSAASSIFST STRHGAAATT
ASSRLPTSSL TPSAFKESPN SAPAAAKPDM STYQTPDRAA RQSSRNSPAS GPNVSISNGL
TSNERIPARD PLPSAKGLKC TYDPLLDRVH NKSVSKSAKP TYQEFGREDD VPPKDPRLAR
SDGRLGYINT DYYLPKSRLR TAPENIKPYP YDPKTSIGPG PPTQIVVTRY NPLIPFSKVT
AIFASFGEIA ESSNKMHPET GSYLGFATIR YRDSKRPDRP PVSAIDAARR AVRARGIKVD
ADIVRVEYDA EGRRSRRMLE EHLKREKEKF EKIEQERLAL AAKAPPTGPK SGTAPGFTRP
PPTAPKGPSA QRQSIPPGTP QIPLLGTPAK PLNLEPSNLA QKLADDPYIY VTGDSVPVLP
SILPHMKKRL KSYGFEEIRV DKSGYFIVFR NSFTGSSEAE RCFRAVNHTE FFNYDMTMQL
CLPRSRRDGA PDRQTHAEPR YRDEKDRRRR EEEADLEEEK KQRAKNFDPV IQAVEVVRRE
MMEHLIRHIR TKVAAPALSD FLDPTNHVAK RRKLNIEHPD DIQEIPSIED GNDSSRVGTP
NSRADPIERR TGRLEPKALP RIRKTKVKGQ AQKSAFVDPF ARKRPPVARN AFRSLHHRLR
SLDSDAESDD DTDTRALLAR ETEEAESRPR SRMSTDDEAS KDDFVPWEQG EDDSMTEASF
AIADTATSRK RKLVASLETV FKRQKKSDEE LFGVNLETLD SEFKGREDSV DIIPEPETGD
DVESRVSRSE TPASAIGKPL KKRPGKVKKT KKASFEEPET SKTQPETESQ RDDEATEPSK
VKQEKAEKSS MEELIPEKFD DKLFATEPLT PALELPDGVK PDLPIFQGLT VSIQDIPDLA
KLARRFNTKD IGNAELWLWT RNRIRELNSA RRTLDSPVTI GGYYVPNPTG CARTEGVKKI
LNSEKSKYLP HHIKVQKARQ EREARNKLGR DAAADAADAA RIAAEKLVAK GNSRANRATN
RRYVADLNDQ KKTLGQDSDV FKFNQLKKRK KPVKFARSAI HNWGLYAMEN IAKDDMIIEY
VGEQVRQQIS EIRENRYLKS GIGSSYLFRI DDNTVIDATK KGGIARFINH SCMPNCTAKI
IKVEGSKRIV IYALRDIALN EELTYDYKFE REIGSTDRIP CLCGTAACKG FLN
//
