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Database: UniProt
Entry: A0A0D2IZ12_9EURO
LinkDB: A0A0D2IZ12_9EURO
Original site: A0A0D2IZ12_9EURO 
ID   A0A0D2IZ12_9EURO        Unreviewed;       999 AA.
AC   A0A0D2IZ12;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Lysine-specific histone demethylase 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z518_09597 {ECO:0000313|EMBL:KIX01870.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX01870.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX01870.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX01870.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
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DR   EMBL; KN847481; KIX01870.1; -; Genomic_DNA.
DR   RefSeq; XP_013269006.1; XM_013413552.1.
DR   AlphaFoldDB; A0A0D2IZ12; -.
DR   STRING; 1442369.A0A0D2IZ12; -.
DR   GeneID; 25297668; -.
DR   VEuPathDB; FungiDB:Z518_09597; -.
DR   HOGENOM; CLU_004498_1_2_1; -.
DR   OrthoDB; 5402444at2759; -.
DR   Proteomes; UP000053617; Unassembled WGS sequence.
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   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; 2.
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   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:UP000053617}.
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..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   999 AA;  111944 MW;  E70A788C09362BCD CRC64;
     MEEDDDDDDA SSSGPASILR SLQLESENRD SPNSSMTSGS VASSVAEQKA KIALKMEAKP
     ETSKNVSPYM FLKAPTTCRA KSSIPPRLSP SEYASQCVAA AEASRLNPYA LHEDEHKLLQ
     DKLCYSHVSV YLNIRNGILR LWTRNPSVSV SLEEAIGCAR DERWTRLACF AYEWLLRRGY
     INFGCVEPPI VTKSASRGRK KETSRETIVV IGGGMAGLST ARQLTNLFQH YPDRVPPKII
     VLEARDRIGG RIYSHPLSSM RSSILSPDQR PTAEMGAHII VGFERGNPLD AIVRGQLALD
     YHLLRDLSTL YDIDGTPVNG VNDAMIERLY NDVLDRTGHY RLKHTVKKTA QGDKDLIDAG
     RDPPDEESLT IKQFEEATAL GTIDQLLPNK KSRRRGAGHR AAKGDKSSEE VDTSMETKIQ
     LPAAQAAKEF GFLLRKTTQM HETLELDDLA TQLNQSLGVV MNAGIDQYQK FLDLKPYALR
     LINWHFANLE YANAANVDKL SLRGWDQDIG NEFEGEHAQV VGGYQQVPRA LWRHPEPLDV
     RTRKSVRSIR YSAAGSRGRA TVTCEDGQSI EADKIVLTAP LGVLKEQSIQ FDPPLPQWKR
     DAIRRMGFGL LNKLILVFEK PFWDVERDMF GLLRAPRNGS GVNQRDYKEG RGQFYLFWNC
     IDTTGLPMLI ALMAGEAAHE AEKVSDEVLV GQCMEQLRNV FGAMNVPMPV ESIVTRWGLD
     RFARGTYSYV AAEARPGDYD LIAAPIQNLF FAGEATIATH PATVHGAYLS GLRAAYEVFE
     SMVGPIPIPP TLVPSSVMKK PSSGSVELTQ MDTHMVQGGK RKGDELLPAG TFTRPVKEKD
     NSLQEAWDAA MWVRIYDDLG PPPVKPPKAN VNSFLLYSGE HWEEVKARLA EERKKTGKRT
     KQSERDQVRV ELGKMWAALS EEEKKPYTDK TNKNREENDK AMKEWSIKAA EWDRRTWEVK
     DVWIKEGNSF EEFCKRKRED DALMDAEVAK RAKIQGHHG
//
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