ID E3RI88_PYRTT Unreviewed; 1665 AA.
AC E3RI88;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFQ94561.1};
GN ORFNames=PTT_07707 {ECO:0000313|EMBL:EFQ94561.1};
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:EFQ94561.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94561.1,
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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; GL533248; EFQ94561.1; -; Genomic_DNA.
DR RefSeq; XP_003297343.1; XM_003297295.1.
DR STRING; 861557.E3RI88; -.
DR EnsemblFungi; EFQ94561; EFQ94561; PTT_07707.
DR KEGG; pte:PTT_07707; -.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_0_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15519; PHD1_Lid2p_like; 1.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 97..138
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 162..255
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 478..528
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 620..786
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1347..1396
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 270..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1665 AA; 186962 MW; A8133F8FB1D8866B CRC64;
MVDFMPPGGP ATGATMTTFR VATDNGLAEG TSGTPKSRMG GAAMAAANAA QPNGAGSIPL
SARKAAPLDL ATVERRGHGA PNNQPPKQNR LFGLRESPTY RPTAEQFKDP VQYIQSIRDE
AQKYGIVKIV PPDSWNPPFA IDTERFHFRT RRQELNSVEG GTRANLNYLD QLSKFHKQHG
HSLTRFPSVD KRPLDLYKLK KAVEKRGGFE RVCKHKKWAE IGRDLGYSGK IMSSLSTSLK
NSYQKWLHPY EEYLRLVKPG VQQMLEFEHG GPFTPSPAHS PMKKSLQGTP IANTSAAESP
AMRASAALNA TLHTEAVPTP PPEPPRSSMP SGFTPVNAGG FTAVNAQKPS QSPTPTSFAA
VNVPNGMHRE VLESRTSTPL RNAGSPMLST DNTPDFRPSG AAFTPLSNGH HFNQLKRTLS
QDPDSSANDD ADEANGRRSK RLKKDPAPTV AGSHMTQPRQ STPGRSFPRV RAADERPGDR
CETCGTDNDP SNILLCDSCD SGYHGYCLDP PIKGIPAHDW HCPRCLVGTG EFGFEEGGIY
SLKQFQERAH LFKQNHFASK MPFDPITNAP KPVTEDDVER EFWHSVANVT ETVEVEYGAD
IHSTTHGSGF PTIEKNPRDP YSTDPWNLTV LPYAPDSLFR HIKSDISGMT VPWLYVGMVF
STFCWHAEDH YTYSANYQHF GATKTWYGVP AEDTDKFEQA MREAVPELFE SQPDLLFQLV
TLLTPEQLLK AGVRVYAIDQ RAGEFVITFP EAYHAGFNHG FNLNEAVNFA PSDWEPFGEH
GVQRLQDYRR QPCFSHDELL LAAASRKDTT IKTAKWLGPA MERMRDRELR LRSDFLEKHK
AVKAHTCKID GSGDVDATCE LEFIVDDADM HEDELMCAFC KSYGYLSRFY CRNAKKVLCL
QHAGSFECCP DTPEADRYSG AKGQHMLVYR MPEDALTSLV QRIVDKAGTP EAWEAKMDAL
LAEGPRPQLK TLRALLNEGE RIDWELKGLS DLKEFVDKCQ EVAEEAILYT TRKQQARRKA
ERPGRGRPSK SAIAEADEKE REYRNVENIQ KLLNQAKDLG FDSPEITTLR ERAESIVEFQ
TRARIALRDR PVEQSITRLD ELLEEGKGFN VDLPELESLE KVVQQLKWLQ EVQEFRLKPT
PTLIEVGDLI KNGTDVGMPE HHPELQFLQE KRRQGEFWDK KAKELMEVEN VHYQQLDTFS
KQATNLPVPP ETRAAMDAIL KKQRDAQELI MSLYERSKNP DFSQRPKYME VRNAMESLNA
LNCKPNGTTD LEKEQKRHED WMRRGKKLFG KANAPLHILH AHMKQVDERN RSCFDLSDQP
RMPVEPASRE QSPAEGEEVD GSGSSRDVFC ICRKPEAGMM IECELCHEWY HGKCLKIARG
KVKEDDKYTC PICDYRVKIP RDATRPKLED LQLWQDELPG LPFQPEEEET LESLIDHGTK
FRDYVAQYIN PLMSSPDELT TQRFYLRKLE GAEILLSNEI NFFRQELHKW APVAPSPPPI
LQVSLSTRKP RPTKQQKLMN QLGITNPEDL PQHLRTKTHQ FKRKEDVPKS SSLQPAPAEQ
SHTPPGEPRQ GQGDNDYFNT ATTTSTYTNS PTFATTAPLN FSGASSIAPI DPGLFETSGA
GPTSPIQDPF KSSGSAHEMF GEAMEMGGGQ AEEALAVTEG NNYEE
//
