ID A0A367L1X7_9HYPO Unreviewed; 917 AA.
AC A0A367L1X7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
GN ORFNames=L249_8932 {ECO:0000313|EMBL:RCI08449.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI08449.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI08449.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI08449.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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:RCI08449.1}.
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DR EMBL; LKCN02000019; RCI08449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367L1X7; -.
DR STRING; 1330021.A0A367L1X7; -.
DR Proteomes; UP000253664; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46462; UPSET, ISOFORM A; 1.
DR PANTHER; PTHR46462:SF3; UPSET, ISOFORM A; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 274..402
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 121..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 100050 MW; 1216121FA1C1F44C CRC64;
MTEKPSPLPT QTAVPSQPLL AAPATPHVKK EVVASAAETV EEEPYTIKCI CNFSDDDGNT
IYCETCDTWQ HIDCFYPDNR EEAIREDFSH SCAECKPRPL NRQKAIERTL RLRNVVVKEE
LVDKKPKRPP KKKAKPSDLQ TSVPHAPSEA GKHGSPGEQP PSSKKSKPSH RQSHSVSSQP
SKRSPPNPAH PPSPATTPPD LPVDFQIHHY SAGFCSLYSE QDVPDTLSNA FASLAIPTAL
SRWLREPDTM KHEVGHSHSD VFQTLPPNAG EKRPRLEIKD STRSLSPGTL LRWRSVKSTT
PIDKDVPLIE LNGEIGFQKD YCADPDNLWA HLSSPLPLVF FHPVLPLYID TRKEGSLARY
VRRSCKPNAQ LDTYLSDGSE YHFWLVSDRY ISASEQITLP WDFRLERSVH VRWLHLLGLS
DDDSSVQDEP ELDASEYTAI SNWIDRILSE YGGCACDLEN NCAFARFHRH YLFGKSNGRL
SKKKSRKSRN RTISPTSTSH ATNSRAASES QANDVADNDA RNESNPSRSK PPSRDRTPLL
GQFDQLGILT EPTDRDKRKV AMVEDSFRRM EQQQPPRKKK RVSDSASNPP STAKPKSRNG
SAAPPGRYAD AGTSSRSNPD SPTSARSPSL TNTIGPASAR SVCTSRSRQP STGLRPAYVD
ASVQTDVVEG EWFSEPCKPR TPMRRIISLP RRLLNSKLRN RAGDEERERR SLSGPTAGSA
ASELGSPTGE SKPPLAVTPS DPLSPVVAQN PDGLAPGLLQ APTLMTTTAA ATTTAATSRA
MPEQVKSKVP DLRVQMPPVP AFDGSTTVTT PLSSATSTTT VYSPVVTNLP SPFAPPAVNG
IAINPSPIKK KLSLSDYTKS RLNKAAGKAA NATAAAHRPG LMSPEETKPD VTMTEPPPVN
DKAEDGISPT AGANGFG
//
