ID H6C741_EXODN Unreviewed; 995 AA.
AC H6C741;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Lysine-specific histone demethylase 1 {ECO:0000313|EMBL:EHY59537.1};
GN ORFNames=HMPREF1120_07525 {ECO:0000313|EMBL:EHY59537.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY59537.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY59537.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY59537.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JH226135; EHY59537.1; -; Genomic_DNA.
DR RefSeq; XP_009159998.1; XM_009161750.1.
DR AlphaFoldDB; H6C741; -.
DR STRING; 858893.H6C741; -.
DR GeneID; 20312164; -.
DR VEuPathDB; FungiDB:HMPREF1120_07525; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR InParanoid; H6C741; -.
DR OMA; WCAENPF; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
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; PF09011; HMG_box_2; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00398; HMG; 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 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Methyltransferase {ECO:0000313|EMBL:EHY59537.1};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Transferase {ECO:0000313|EMBL:EHY59537.1}.
FT DOMAIN 97..192
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 867..946
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 867..946
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 111266 MW; 3D2FC7678B92FC7D CRC64;
MEEDDDEDYS SSSGPASILR NLQHESENRD SPNSSLTSVS TASSVTEQKV KVTVKQEVKP
ETPEKAIPYM FLKAPATCRA KSSIPSRLSP SEYANQCVAA AEASRLNPYA LHEDEHKLLQ
DKLCYSHVTV YLNIRNGILR LWTRNPSVSV TLEEAIGCAR DERWTRLACF AYEWLLRRGY
INFGCVEPAA IPKATGRGRK KEPQRETIVV IGGGVAGLST ARQLTNLFHH YPDRAAPRII
VLEGRDRIGG RIYSHPLTSM RTSKLAPGQR PTAEMGAHII VGFERGNPLD AIVRGQLALD
YHLLRDLSTL YDIDGTPVNG ANDAMIERLY NDILDRTGHY RLKHTVKKTA QGDKDYIDAG
RDPPDEESIT IKQYEEATAL GTIDQLLPKK KSRRRGAGHR AAKGDKSSEE VDTNMDTKMQ
LPAAQAAKEF GFMLRKTTQM HETLELDDLA RQLNQSLGAV MDAGVDQYQQ FLDLKPYALR
LLNWHFANLE YANAANVDKL SLRGWDQDIG NEFEGEHAQV VGGYQQVPRA LWRHPEPLDV
RTRKVVKSIK YSAAGSQTKA TVTCEDGQSI EADRVVFTAP LGVLKNQSIQ FDPPLPQWKR
DAIRRMGFGL LNKVVLVFER PFWDVHRDMF GLLRGPRNGP GLQQSDYKEG RGQFYLFWNC
IETTGLPVLI ALMAGEAAHE AEKIPDEELV GQCLGQLRNV FGPTNVPMPI ESIVTRWGSD
RFARGTYSFV AAEARPGDYD LIAAPIQNLF FAGEATIATH PATVHGAYLS GLRAAHEVFE
SMVGPIAIPP TLVPPATASK GCSASAELTL MDTHMAVGGK RKGDELLPAG TFTRPVKEKD
NSLQEAWDAA MWVRIYDDLG PPPVKPAKLT VNAFLLYSGE HWDEVKNRLG GERKKTGRKS
KHSERDQVRI ELGKMWAALS EEEKKPYTDR IQQNREENER AMKEWAAKAA EWDRRTWEVK
DVWIKEGNSF EEFCRRKRED DALMDAAAGA KRAKL
//