ID A0A1Q5SXY0_9EURO Unreviewed; 1061 AA.
AC A0A1Q5SXY0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative lysine-specific histone demethylase 1 {ECO:0000313|EMBL:OKO92715.1};
GN ORFNames=PENSUB_12700 {ECO:0000313|EMBL:OKO92715.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO92715.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO92715.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO92715.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKO92715.1}.
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DR EMBL; MNBE01000740; OKO92715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5SXY0; -.
DR STRING; 1316194.A0A1Q5SXY0; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000186955; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 2.
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 Methyltransferase {ECO:0000313|EMBL:OKO92715.1};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW Transferase {ECO:0000313|EMBL:OKO92715.1}.
FT DOMAIN 183..278
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 945..1025
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 945..1025
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 116994 MW; C917BC96F27B3B2D CRC64;
MHATSSILIP PLTGIPPNQR PFIHQVGPNG FSNTAVHETM DSSQSESSEP PVKRIRTDNG
HAASFAYPPP SVLLEYHHKP AVYQALSQKM MSNGIHETQS PSSSYIGEET QILNASTTST
SITSSMEPRK SSTPPSTPAQ SLQTASAVSG VSVLDSNRVD LSKCRPRSSI PSKLTPSVYG
QQCVAAAYAS RLDPYALHEK EQEILQDHLC HMHVTTYLNI RNGILRLWTR NPMVGVTREE
ALGCTKDYRW MNLASLAYDW LARHGYINFG CVEVPMPLVA PRRGRRKEGP VILVVGAGVG
GLGCARQLEG LFKHYRDSDT EPRVIVIEGR PRIGGRVYSH PLHSLQSDML PEGLVPKAEM
GAQIIIGFDH GNPLDQIVRG QLALHHHLLH DLSTIYDFDG SPVPNTQDEM VNKLYEDVSE
RAFAYRHKKL VRQTAEGDRE MIDDGKETTV DDGITVRQWE EARAAGTTDS LVPTKRVRRR
RGVGHKTGDI AAANAAAPKL EGETEDHPAA LAAQAAGWKL NAGYTANDTL ELDRVAYAAE
AQSLGAVMDE GVKQYRDMLP LTSRDMRLLN WHFANLEYSF AANPKKLSLT LADQDSGNEF
EGLHSMVVGG YNQLPYGLYS VPNKLNVHTN KIVTKIAYDT NGGGNRKAVV YCENGEKFVG
DHVVYTGSLG TLQHRTVQFD PPLPDWKQGA VDRLGFGLLN KVVLVFDEPF WDTERDFFGL
LRTPDNPESM VQEEYAANRG RYYLFWNCIR TTGLPVLVGL MAGDAAHQAE QMPDAEIVEE
VTTQLRNVFK HTVIPDPLET IVTRWASDPF TRGSYSFVAA GAKPEDYDLM ARKVGNLHFA
GEATCGTHPA TVHGAYLSGL RAASEVIEAT IGPIEIPMPL VPEKPAASVI TPPTAGIIAG
TPKRPAPATT SRSPNVADKQ RRDTYEQAMW TAIYAELGPT PTAPAKAGRN PFLLYQKDFW
AKCKEQCDEA RRVAANNPNA KASRDDIRAA LGLMWRNAPP EEKQPYIDQV EANRIANDEA
FEKFKAVGAE WNRRSFEVRD KWCAENPFED WQVPAGSTVA N
//
