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Database: UniProt
Entry: E3RPG7_PYRTT
LinkDB: E3RPG7_PYRTT
Original site: E3RPG7_PYRTT 
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
//
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