SET1_ASPOR
ID SET1_ASPOR Reviewed; 1229 AA.
AC Q2UMH3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9Y7R4};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=set1; ORFNames=AO090003000002;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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:0000250|UniProtKB:Q9Y7R4}.
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:0000250|UniProtKB:Q9Y7R4};
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AP007155; BAE57242.1; -; Genomic_DNA.
DR RefSeq; XP_001819244.1; XM_001819192.1.
DR AlphaFoldDB; Q2UMH3; -.
DR SMR; Q2UMH3; -.
DR STRING; 510516.Q2UMH3; -.
DR EnsemblFungi; BAE57242; BAE57242; AO090003000002.
DR GeneID; 5992596; -.
DR KEGG; aor:AO090003000002; -.
DR VEuPathDB; FungiDB:AO090003000002; -.
DR HOGENOM; CLU_004391_1_0_1; -.
DR OMA; CHMTALF; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IEA:InterPro.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 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; PTHR45814; 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; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1229
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269766"
FT DOMAIN 1087..1204
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1213..1229
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 22..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 137590 MW; C1F3AB36366980C0 CRC64;
MSRSSAGFAD FFPTAPSVLQ QKRFKVTRER PRPKAQIDSE HSDESSACPT ETRAILNLSN
GGASLDSGQI SSTDLKKTSP ESSVEGSASS TAGDRSALSL SVAQHGANSH EARLDTLTPL
TNAESSPPQK ANSPRNKIAE GIVANTTIDT KSGINPLHTP PTPQSQGRRT GSIRGYKLVY
DPDTEKRSSS KEKRRKPRYV DIILSEQNNC PPDPRLGIPN YMRGAGCKQK RKYRPAPYTL
KPWPYDASST IGPGPPAQIV ITGFDPLTPI APISALFSSF GDIGEINNRT DPITGRFLGI
CSVKYKDSAS FRGGGPVLAA SAARRAYYEC RKEQRIGTRR IRVDLDRDGV VSERFVARTI
ESQRMGQKSN LQSTEEVKSD SETKKNEPPP TAPKGPSGKT SVRPIVAIPE GPRANFLKPV
MPSLVEEVPI LGQIKRDPYI FIAHCYVPVL STTVPHLKKR LKLFNWKDIR CDKTGYYIIF
ENSRRGEEET ERCYKMCHMK PLFTYIMNME SQPYGNPSYE RSPSPERCRA EQRERAERER
LKREVGLDIE EEKRQRAVDL DPCQEVLTII IRDLKDKLLE DVKSRIAAPA LYDYLDPDRH
ALKRKTLGIA DPEGIKRPMF RIDDSFGTPD SRSGLSDARR PFSGSTPNIL ALPRIRKARH
LGRTDTAFLD ERRKQPLRRR EVRPLYHRLQ QLHDVDDSDD EQRTPKDTDE QDSRPPSRMS
SGTSESDDGD GFVSEALGLP VVELAGSGQN KEPDEILKDN QSVGESSQLE SNEISPELRK
RKRASEELEA RKRQKEDDEL FGINPIAEAE VEGTQIIATP IAVDINLEVS EAALSILPKE
SNDNRQETGE ANHLDFDGID VTSSTIEKDR RGILDPLDDI DNAAAREESR TEVGWRVSND
EPRPIVDDDD AIIMDLDGWQ NLIKDDEDLH FLRDILVGYS ESNVGNLSAW AWRQKEIKAL
NHPGDVGPLR GGTGIAGYYV PNTTGAARTE GRKRILESEK SKYLPHRIKV QKAREEREAR
AKNDPHTAAV EAARVAAAKN ISKSTSRSTR VNNRRLIADI NAQKQALPTQ SGDGDVLRFN
QLKKRKKPVR FARSAIHNWG LYAEENISAN DMIIEYVGEK VRQQVADMRE RQYLKSGIGS
SYLFRIDENT VIDATKRGGI ARFINHSCTP NCTAKIIKVD GSKRIVIYAL RDIERDEELT
YDYKFEREWD SDDRIPCLCG STGCKGFLN
