ID A0A1L9SK07_9EURO Unreviewed; 1234 AA.
AC A0A1L9SK07;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ASPZODRAFT_93802 {ECO:0000313|EMBL:OJJ47421.1};
OS Penicilliopsis zonata CBS 506.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ47421.1, ECO:0000313|Proteomes:UP000184188};
RN [1] {ECO:0000313|Proteomes:UP000184188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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}.
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DR EMBL; KV878340; OJJ47421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9SK07; -.
DR STRING; 1073090.A0A1L9SK07; -.
DR VEuPathDB; FungiDB:ASPZODRAFT_93802; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000184188; 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 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.
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:UP000184188};
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 1092..1209
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1218..1234
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 20..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 137958 MW; D4513B39E9677714 CRC64;
MSRSSAGFAD FFPTAPAVLQ QKRRRATQEQ QPPESQDDRV NTIESSSLST ELPLAVDNPV
VGVKTGGNTT TRSGEELSEG LGLGSTNFKS RGCSVPPGGV SVDGIHLDTL TPLTNGESSP
PRKAPSPSDA KMDDEFTEDG AHSGPQGDSK LALNQICAPP TPLSQSRHIE SAIKGWKVAY
DPDLDKRSSS KEKKKKVQYV SFVANEDNSP GSDPRLKIVN YNRGAACKQK SKYRPAPYLL
KPWPYDATTT IGPGPPTRIV ATGYDPLTPI APISALFASF GEISEINNRT DPITGSFLGI
CSIQYKDSLS FRGNGPVLAA SAARRAYLEC KKEQRIGTRR IRVEWDRDGT TSDRLVSRAI
TSQRAELRGN LQNGEERDTE TKAEKNEPPL TAPKGPSGRI SIRTAFPPPE GPRAALKPAV
PSLIEETPIL GQIKRDPYIF IAHCYVPVLS TTVPHLKKRL KLFKWKSIRC DKTGYYVLFE
NSRRGEEETE RCYKICHMKP LFTYIMNMES QPYGNPNYER SPSPERLQAE HKQRSEKERL
KKEAELDLEE EKRQRAIDLD PCKEVLSIII SELKDKLLDD VKSRIAAPAL YDYLDPDRHA
PKRRKLGLPD PEGTKRLSFQ IGIENSLGSH DSDIRLPHSR APFGASNMNI LALPRIRKAH
GLDRTDTVFL DERRKQSSRK TRVRPLYHRL QQLHEVEDSD EELQSPFGQD TDSRPPSRAT
SISSDSENDN DSGTETLDTS TTKGILAFEN EGDNDAPDSS VDGQSLSDFS NLLSTSNRKR
KRLNQELEAR KRQKDDSLFG LAQSPEDTDS DIQGRSANTL VSGSDTIDPG IIQEDLGIAS
TPLEQGKMEM VASEPLEDIK ELRKPVEDGF KETDQTTGLP SAVSYSNRKL ARPKEAKIGW
DVSYDEPRAT VEDDDTIIQD LDGWQCIVKD DEDLRFLREV LVDQLKFNIG NLAAWAWRQK
EIKALNRSGE RGIVRNETLI DGYYKSNIAG SARAEGKKRI LESEKSKYLP HRIKVQKARE
EREARAKNDP QATAAEAARI AAAKSISKST SRSTRVNNRR LIADINAQKQ ALPTQQGEGD
VLRFNQLKKR KKPVRFARSA IHNWGLYAEE NIAANDMIIE YVGEKVRQQV ADMRERRYLK
SGIGSSYLFR IDENTVIDAT KRGGIARFIN HSCTPNCTAK IIKVDGSKRI VIYALRDIER
DEELTYDYKF EREWDSDDRI PCLCGSTGCK GFLN
//
