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Database: UniProt
Entry: N1QHT8_SPHMS
LinkDB: N1QHT8_SPHMS
Original site: N1QHT8_SPHMS 
ID   N1QHT8_SPHMS            Unreviewed;      1500 AA.
AC   N1QHT8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=PLU-1-domain-containing protein {ECO:0000313|EMBL:EMF12019.1};
DE   Flags: Fragment;
GN   ORFNames=SEPMUDRAFT_46716 {ECO:0000313|EMBL:EMF12019.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF12019.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF12019.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF12019.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR   EMBL; KB456265; EMF12019.1; -; Genomic_DNA.
DR   RefSeq; XP_016760140.1; XM_016909009.1.
DR   STRING; 692275.N1QHT8; -.
DR   GeneID; 27906146; -.
DR   eggNOG; KOG1246; Eukaryota.
DR   HOGENOM; CLU_000991_0_0_1; -.
DR   OMA; GFDQVCK; -.
DR   OrthoDB; 48111at2759; -.
DR   Proteomes; UP000016931; 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   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:UP000016931};
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          58..99
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          123..216
FT                   /note="ARID"
FT                   /evidence="ECO:0000259|PROSITE:PS51011"
FT   DOMAIN          434..484
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          577..743
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          1302..1351
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          228..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1269..1298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1453..1472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1480..1500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1500
FT                   /evidence="ECO:0000313|EMBL:EMF12019.1"
SQ   SEQUENCE   1500 AA;  171487 MW;  9A7A12BF223FA465 CRC64;
     MPAVPGTLNG PPSGNNHAIP LSARRAEALD LSTVERRGQP NQRSYPTRKS RLFDIPNAPI
     YRPTEEEFRD PMEYMRKIAP EGSKYGIVKV VPPENWNPPF AINTERFHFR TRRQELNSVE
     GGNRVNNDYL DQLAKFHKQN GHNLNRFPSV DKRPLDLYRL KKTVERKGGF EQVCKGKRWA
     EVGRDLGYSG KIMSSLSTSL KNSYQKWLLP YEEYLRLAKP GVHHHIEMMN GGPYTPSPGP
     SPVKRPPGAT PGEHTSTKHA SAALHASLNG HSPHPTFSGN HEILHPVQQH ETPQQPHYAA
     PQPHIAPITG GFTPVNAGGF TPVNALPPPP PTQSGFTAVN GMNGMHHTNS GHPPHPMEGN
     SKHMSQHAAP SPNGVSTLKR PHAELTPDEV SQLERRSKRM RNDVPTVAGS NMHHSRMGPK
     QLQANRERGN YSPGEVCENC LTPNEPHKQL KCESCGDAYH MYCLEPPLKQ APAHEWHCPR
     CLVGTNEYGF EEGDVYSLSG FQRKANEFKE HHFNTMPRQY SPFNETKHHL EEDDVEREFW
     RLVEDMSDAT EVEYGADIHS TTHGSGFPTI EKHPRDPYST DPWNLNILPL DKESLFRHIK
     SDVSGMTVPW LYVGMVFSTF CWHNEDHYTY SANYQHFGET KTWYGIPGED SYKFEETMKQ
     EVPELFETQP DLLFQLVTLA KPEKLRRAGV KVYAIDQHAG EFVITFPRAY HAGFNQGFNF
     NEAVNFAPHD WEPFGQEGVR RLRDYRKQPC FSHDEMLLTA ASRDNSIRTS KWLAPAMERM
     RDDELSTRQH FMGSLEPETG TQQQDPYTGP RYGREPEAID PATEEEEVIC TFCKAYCHLS
     RYQCKKTKKV LCLLHAGSYE CCDALESERY SGQNGEHAVY YRMTDDVLTA TVQKVVDKAN
     IPEAWAVKVA KELEDSARPS LKHLRTLLTE GDKIQYELPQ LPDLRRFVDR CNEWVEEATN
     YITRKQTNRR KSEKVWRKGT KAAEQEERDK ELRKISNIYN LLESAEKIGF DCPEIVTLRE
     RAVNIEEFQK DANAALGNIL AKKTEDFEEL LERAKDFHVD MPEIESIERV LKRLRWNDTA
     KAKRPSQETG KQGQTLSDIE KFLSEGAEIG VPDTNPDVAF FKEHKAQGEL WEQKAKELMA
     VEQVHYQQLD ALSRQASTLP VTVETLAAVD AILKKQREIQ EKIVSLVDRS KDPDFRKRPH
     YNEMKEVMDA LDELQSKPNG TIDLEKESKR HEDWMRRGKK LFGKANAPLH ILQQHMHIVD
     MRNQACFDIE DKPRGPVEPS SRAGSPTEGD APITEGSTSS RDVFCICRKS EAGMMIECEI
     CHEWYHGKCL KIARGKVKED DKYTCPICDW RVKIPRDAAR PKLEDLQAWF DELETLPFQP
     VEEKTLSNIC ESGQVFRDFI RPYVEPSMEP TPEEVSILRF YLRKVEGADI LLAHETNYLR
     QQLHRLAKVA PEAPPLTDAS HSTRKPRPTK QQKLMAQLGI TNPEDLPTQY KMKPHVAKRK
//
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