ID E4ZVE6_LEPMJ Unreviewed; 1069 AA.
AC E4ZVE6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Lysine-specific histone demethylase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LEMA_P027240.1 {ECO:0000313|EMBL:CBX95572.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; FP929127; CBX95572.1; -; Genomic_DNA.
DR RefSeq; XP_003839051.1; XM_003839003.1.
DR AlphaFoldDB; E4ZVE6; -.
DR STRING; 985895.E4ZVE6; -.
DR EnsemblFungi; CBX95572; CBX95572; LEMA_P027240.1.
DR GeneID; 13281128; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR InParanoid; E4ZVE6; -.
DR OMA; WCAENPF; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR CDD; cd00084; HMG-box_SF; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 218..313
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 940..1020
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 940..1020
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 65..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 117447 MW; ED3DCAB1C8EC1982 CRC64;
MFSTSTFAST TDPSALDDGT YLFDQSHDDL LSVPMSSDSI HLKGGITPMT GLSNLEYGRE
STTSSVHYGE SHDTSELSTG HISGGDDHEA STPGAFINGY GHMYAHSPLQ DPFTPQSNMG
NGTNNVQAEP NMRTATHDPK RHPPLKNHQE DAGVMARTPQ SLDRVSHASS TPELPQMAGR
PSVHRRTNST PARGKVVELK ASSSIPTTIS WQEFGRQCIL AAENSRLNPF ALHPAEYRLL
REHINQAQVT IYLNIRNAIL RIWHRNPLVY VSLQEAAGCA RDKRHFGLAK VAYMWLLRNG
YINFGCVEIP NTAGPTPKSK AKAGLQRTII IVGAGMSGLG CARHLEGLFA QLGNQLTEAG
ERAPKIVILE ARPRVGGRVY SHPFLNQSSS SLPPGHRCTA EMGAQIVTGF EHGNPLITII
QRAAVYRNKP AVQRTVEGDR SFLLFGREPS DNGGPTIAQT EEADVSLLAN ADHAASTKEE
KPTTGVEKLA GRAYQLSAGF NPDITAAETM QSLGWKLKLG ASTSQSLDLD TIAKGSDFPT
LGQTMDEGFR QYQSILDMQP KDMRLLSWHH ANLEYANAVS VNQLSLSGWD QDIGNEFEGE
HSEVIGGFQQ VPRGLWQSPS RLDIRFNSPV RTVRYQTDGS QSGKAVKIEC SNGETYEADQ
IVLTTPLGVL KSGSVEFQPP LPDWKQDVIA RMGFGLLNKI ILVYEKAFWE PERDMFGLLN
EAEIDASMRP EDYSAKRGRF YLFWNCIKTS GKPVLVALMA GDAAHYAEAT SNDQLVKEVT
DRLDSMFAPN PVPLPSETIV TRWKRDPYAR GSYSYVGPQT QAGDYDVMAR PHGPLHFAGE
ATCGTHPATV HGAYLSGLRV AAEVAETILG PIQIPSPLVE KKMKVEASTT PTLDGKRRFE
PAVSPQKNAK PARVQRDEDY EAAIIGAILT EIGERPIKPG RTGVNPFLLY TKDFWYICKQ
EGDDARKAAT GNPEAKASKQ EIRNAIGLRW RMASEEVKKP YLEQASHARE DATAHAADFK
ERVATWDKEA ARIRREYIQA NPPEGGNEDL ILNSRTAIEL GASKRLRRL
//
