ID E3RPG7_PYRTT Unreviewed; 1109 AA.
AC E3RPG7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Lysine-specific histone demethylase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PTT_10530 {ECO:0000313|EMBL:EFQ92361.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ92361.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ92361.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GL534338; EFQ92361.1; -; Genomic_DNA.
DR RefSeq; XP_003299522.1; XM_003299474.1.
DR AlphaFoldDB; E3RPG7; -.
DR STRING; 861557.E3RPG7; -.
DR EnsemblFungi; EFQ92361; EFQ92361; PTT_10530.
DR KEGG; pte:PTT_10530; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000001067; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR CDD; cd00084; HMG-box_SF; 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 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT DOMAIN 216..311
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 980..1060
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 980..1060
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 52..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 122266 MW; E1F953140F300782 CRC64;
MFSIESTAAS TALDDGSYIF DQTQDDIIMP MSNDTIHLKS AIAPTPGISD LGYGRESSAS
SVHYGDSHDT SEPSIGQEGE GSTPGACVGG YVANYTPSPL QHPFTPNSAV YGVTNIQSNQ
PLQSESFQHK LTSEKDTKAH LSLKDQRGDG VFIARTPQSL SRESQASSTP ELQQSSEQPK
KHRRTNSLPS KGRTVEMKAS SSIPAELSWP EFGRQCILAA ESSRLNPFTL HPAEYKLLRE
HVTLAQVTIY LNIRNAILRL WHRNPLVYVS LEEAAGCARD RRYFGLARVA YLWLMRHGYI
NFGCVEVPST VGTIAKSKAK NTTRRTIIVV GAGMSGLGCA RHLEGLFAQL GDQLTDMGER
PPKIIILEAR PRVGGRVYSH PFLNQKDSTL PPGHRCTAEM GAQIVTGFEH GNPLNAIIRG
QLAIPYHGLR DNTILYDYDG TVVEMGQDIL VEKLYNDVLE RAAVYRNKPA AHTTVEGNRD
QMNFGRDPAD NGGPTIAELE DSGSSLSGNT TSIASTKQEK PTTGVEKLAG RAYQLSAGFN
PDITAAATVQ RMGWKLKAGA TDAQSLDLDT IAKASEYPTL GQTMDEGLRQ YQSLVDLKPR
DMRLLSWHHA NLEYANAVSV NQLSLSGWDQ DIGNEFEGEH SEVIGGYQQV PRGLWQCPSK
LDVRFNTPIK TVHYDTEERQ VGKAVRIECT NGEVYEADQV ILTTPLGVLK SGSIKFEPPL
PDWKQDVIER MGFGLLNKII LVYEKAFWEP DRDMFGLLNE AEHAASMRPE DYSEKRGRFY
LFWNCIKTSG KPVLVALMAG DAAHWAENTS NNELVKDVTD RLDAMFAPNH VPLPTETIVT
RWKKDPFARG SYSYVGPKTQ TGDYDVMARP HGPLHFAGEA TCGTHPATVH GAYLSGLRVA
AEVAETVLGP IKVPSPLVEK KVVKMEPSSA ISGGEKRRFE PAVGPQRDSK SSRIQRDEDY
EAAIIGAILD QIGERPIKPG RAGVNPFLLF TKDFWYICKQ ECDDAHKAKT GNPEAKAPKQ
EIRNAVGLRW RTAEQEVKQP YLDQASNARD DASANAADFK ERVATWDVEA ARIRREYIQA
NPPEGGNEEL ILNSRTAIEL GAGKRLRRQ
//