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
//