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Database: UniProt
Entry: M2LHI9_BAUPA
LinkDB: M2LHI9_BAUPA
Original site: M2LHI9_BAUPA 
ID   M2LHI9_BAUPA            Unreviewed;       668 AA.
AC   M2LHI9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
DE   Flags: Fragment;
GN   ORFNames=BAUCODRAFT_95505 {ECO:0000313|EMBL:EMC93632.1};
OS   Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS   (Baudoinia compniacensis (strain UAMH 10762)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX   NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC93632.1, ECO:0000313|Proteomes:UP000011761};
RN   [1] {ECO:0000313|EMBL:EMC93632.1, ECO:0000313|Proteomes:UP000011761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC93632.1,
RC   ECO:0000313|Proteomes:UP000011761};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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DR   EMBL; KB445560; EMC93632.1; -; Genomic_DNA.
DR   RefSeq; XP_007679696.1; XM_007681506.1.
DR   AlphaFoldDB; M2LHI9; -.
DR   STRING; 717646.M2LHI9; -.
DR   GeneID; 19117495; -.
DR   KEGG; bcom:BAUCODRAFT_95505; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   HOGENOM; CLU_009510_0_0_1; -.
DR   OMA; ECACEDK; -.
DR   OrthoDB; 124870at2759; -.
DR   Proteomes; UP000011761; 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:UP000011761};
KW   Transferase {ECO:0000256|ARBA:ARBA00022603};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          283..414
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          105..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         668
FT                   /evidence="ECO:0000313|EMBL:EMC93632.1"
SQ   SEQUENCE   668 AA;  75129 MW;  69EBCB1098D5C086 CRC64;
     MTESFYPVTA ITGHIGLHAA HANHQAHLDR LHHGAPSVDT AQEDDGEISC FCGFGDDDGN
     TVACDVCSRW QHIICYYPEY EGQGLPADLQ HFCVECRPRP VDAHAAHGRQ RTVREHHQLS
     YNGVKRPPAK SHKKKVKESP SAPYTNGWPV DKVRHDRNSA SPRDQPPPAK RPKTSHRTSD
     SNAFAPVKGN PRKRNLSNMH HRSISQSPDS PTAMYSEEFL RSHQEDDWTY SEANVMDALQ
     VTNHLSRWLQ LSNEDFYDEI QVEKGNVLNR WDKGTPDDIP GKPQIEVVEQ PDITCTDSEG
     NNPSWKAVIS HDALHAGAYI GELRGRIGLK DEYKRDPVNR WSKVRHPEPF VFFHPSLPIY
     IDARHEGTDL RFVRRSCQPN ARLQVLVTKG TDYHFCFMAS TLIESGTEIS IGWDTAEMHR
     QRDSTIPRSV ESIDDINMDE LRDWVSSVLS NCGPCACQRS YPDCAMSRFD RRRMLEEQDD
     VPQPVKASKL KKKRLGQHIS PLNTHSVNSR SGSEARKVGP DEDIVDSRSV SESVDRASAS
     RDNTPNTYYS ANGSLTLEPK ISERERKKLA KEEEMFRRQE EEKSGKIGKK KRNSAGSNVT
     TPSVTSSKQL GLHALPPRTA DAGTPQQPAL ISAKSVNGKR PRASTNKTPV KSAIKNVKRQ
     KPLYVESE
//
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