ID A0A0F4GJM2_9PEZI Unreviewed; 1934 AA.
AC A0A0F4GJM2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=PLU-1-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TI39_contig478g00016 {ECO:0000313|EMBL:KJX97581.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97581.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX97581.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97581.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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:KJX97581.1}.
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DR EMBL; LAFY01000470; KJX97581.1; -; Genomic_DNA.
DR STRING; 1047168.A0A0F4GJM2; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000033647; 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; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR CDD; cd15543; PHD_RSF1; 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); 2.
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:UP000033647};
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 100..141
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 165..258
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 538..588
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 681..847
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1410..1459
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1934 AA; 216182 MW; C8D60B0283594000 CRC64;
MVVPPSVGGP PPQMMAARDS PTAAVAGPSS MSAPKALNKN ATPSAPGTLN GPPSGNNHAI
PLSARRAEPL DMTTVERRGH PKRRADEKPR SHRLFDIPNA PVFRPTEEEF RDPMEYMRKI
APEGSKYGIV KIIPPDAWNP PFAINTERFH FRTRRQELNS VEGGNRVNND YLDQLAKFHK
QNGHNLNRFP SVDKRPLDLY RLKKTVERKG GFDLVCKSKR WAEVGRDLGY SGKIMSSLST
SLKNSYQKWL FPYEEYLRLA KPGVQHQMEM MNGGPYTPSP GPSPAKRPPG SASHEHTPTL
QASAALNASL NGHSHSPSQS PFAFGQPQFA PMQHHPAQHM PQQHHVPQHM QQHHTQQPMP
QHQTHQHTTP HHTPQSMPPP HSSQPHPNQP MSHQPQPPTT GGFTPVNAGG FTPVNAGGFT
SVNAHPPPPA PTPSFMPVNG MNGFQPSNGT PQPSHQAHQH PENGPSSNPQ LIAPNPTGLA
ALKRQHSELT PDEVDLMNRR SKRLRKDVPT VAGSNMHHSR MSAARFQAVR DRVDFRPGEM
CETCGKGDDP HRLLKCESCD NVYHMACLDP PRTHAPEHEW HCPRCLVGTN EYGFEEGDVY
SLAGFQRRAN EFKNYHFSTI PRQFTPFNEN KNFLVEDDVE REFWRLVDDL SDATEVEYGA
DIHSTTHGSG FPTIEKHPRD PYSIDPWNLN TLPLDKESLF RHIKSDISGM TVPWLYVGMV
FSTFCWHNED HFTYSANYQH FGETKTWYGI PGEDTAKFEQ ALKDDMPELF ETQPDLLFQL
VTLAKPDKLR KAGVRVYAID QHAGEFVVTF PKAYHAGFNH GFNFNEAVNF APADWEPFGE
EGVKRLRDYR KQPCFSHDEL LLTAASRDQT IRTAKWLAPA LERMRDDELG MRQQFLSASA
SIEGGTSAEE PYQGPRYQGK PETIDPATEE EEVICTFCKS YCYLSRYICK RSGKVLCLLH
AGSYECCEAN EADRYSGGAY KDHVLYYRMG DEPLKTIVRK AVDKANIPET WAAKVDSELD
ENDRPSLKHL RTLLAEGEKI QYELPQLADL RRFVDRCNEW VEEATSYITR KQTNRRKSEK
PARKSTAKMV EAEERDKELR KVSNIQNLLA SADKIGFDCP EINTLRERAE NIEEFQKDAN
AAIGDILSRT TADFEELAER GRDFHVDMPE MDMLERVLKR LRWNDSGKEK RPNPETGRQE
QTLGEIEKHI KEGEELLVPD TNPDMAFFRE HKAQGELWEQ KSKELMAVEQ VHYQQLDALS
RQASTLPVTP ETLAAVDAIL KKQREVQDKI QSLVERSKDP EFRNRPHYRE MKEVMDALDE
LQSKPNGTID LEKESKRHED WMRRGKKLFG KANAPLHILH QHMITVDKRN ESCFDLTDKP
RGPVEPSSRA ATPEEGEGAP QTEGSSSSRD VFCICRRSEA GMMIECELCH EWYHGKCLKI
ARGKVKEDDK YTCPICDWRV KIPRDAARPR LEDLQAWQDE LETLPFQPEE EKTLANICNY
GQNFREFIKP YVEPAMPPTA DEVGVLRFYL RKIEGADILL AEETNYLRRE LHKFAPVAPV
PPPVIAASGS TRKPRPTKQQ KLMASLGITN PDHLPTQYKM KPHVAKRKQS NTMGSQMPGS
NASASPPGSA TPGPSGSSSH QNGASQPLGE TPPRKFKHMT ALALHVLEGL AGNAIVDHFL
ASEPHANRDR LLKVKAVLEM NDPTAVVDLE TFKARMASLP APAAHNPGHG YETPSERTTM
VNNVYGNQFT TAAANDSFAA TTGEACMGSP GQFSYPAPPG GSPPPNNFDP NLFDTGSGDM
FETPAPTRPE GKDSNARSSA SPEFSSRPAG NTISSGMPAD MFDSPKHSQL EVPTSHAGFA
TSAGASSPGF GGSQQSAGAM DNVFADLVHD QDEGMGAMVN AQHDDAVHPT TEARSSDAHA
DPQQDVAQPE AQRS
//
