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Database: UniProt
Entry: A0A0D9W982_9ORYZ
LinkDB: A0A0D9W982_9ORYZ
Original site: A0A0D9W982_9ORYZ 
ID   A0A0D9W982_9ORYZ        Unreviewed;      1302 AA.
AC   A0A0D9W982;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR04G20340.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR04G20340.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR04G20340.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR04G20340.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SBNO family.
CC       {ECO:0000256|ARBA:ARBA00006992}.
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DR   EnsemblPlants; LPERR04G20340.1; LPERR04G20340.1; LPERR04G20340.
DR   Gramene; LPERR04G20340.1; LPERR04G20340.1; LPERR04G20340.
DR   eggNOG; KOG1513; Eukaryota.
DR   HOGENOM; CLU_000212_2_1_1; -.
DR   Proteomes; UP000032180; Chromosome 4.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR026937; SBNO_Helicase_C_dom.
DR   InterPro; IPR026741; SNO.
DR   InterPro; IPR039187; SNO_AAA.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PTHR12706:SF13; PROTEIN FORGETTER 1; 1.
DR   PANTHER; PTHR12706; STRAWBERRY NOTCH-RELATED; 1.
DR   Pfam; PF13872; AAA_34; 1.
DR   Pfam; PF13871; Helicase_C_4; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          725..775
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          45..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..67
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..174
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1302 AA;  142539 MW;  C7EE70477B687A49 CRC64;
     MAGGSSPSPS AAPVQVRCAG CRGVLAVAPG MTEFICPKCG MAQRLPPQLM PPKPTPPPPP
     TSSSSSPSPA PPKSSSASAP APARRGAAPA PAPTPQAQGV DPTKIQLPCA NCQAVLNVPH
     GLARFRCPQC GAELAVDLAK LHNFLASSNN NSAAPPPPTD PASRPALRAP PSVPVPPPQA
     PFLPAPTPGM TQAPQLVPGA LIPMVLPITD PPEEINEVAI DVEREEDEGG TVGETFTDYR
     PPKLSLGLPH PDPIVETSSL SAVQPPEPTY SLNIMDELDE TKALSCLQIE TLVYACQRHL
     YHLPTGDRAG FFIGDGAGVG KGRTIAGLIW ENWQQGRHKA VWVSIGSDLK YDARRDLDDV
     GAKCVQVHPL NKLPYSKLDS KAIGIKNGVI FVTYSSLIAS SERGRSRLQQ LVQWCGNEFD
     GLLVFDECHK AKNLVPDAGS QPTRTGKAVL EIQEKLPEAR VVYCSATGAS EPRNLGYMVR
     LGLWGDGTSF QNFAQFLGSL EKGGVGALEL VAMDMKARGM YVCRTLSYKG VDFDIVEAPL
     EERMMNMYGK AAEFWAEFRL ELLSAGDLVT EGISNQIWRL YWASHQRFFR HMCMSAKVPG
     VVRLAKEALA ENKCVVVGLQ STGEARTEEA ITKYGVEMED FVSGPRELLL KLVEENYPLP
     PKPDSFQQGE EKVTEIHRKR HSAQDVSFKG RVRKVAKVVE VSDDDSDDYS PSESDHGSTE
     SDEEFHMCQI CNTEEEKSLL LHCSGCSRHV HPACLTPPWT GILTDDWSCY TCKKLEGDEN
     EQDAHVADFS QRYDAAVERK MKILDMIRSL DLPNNPLDDI IDQLGGPDNV AEITGRRGML
     IRASDGKGVV YQARNAKEVS MEMINMHEKQ QFMDGKKLIA IISEAGSAGV SLHADRRAKN
     QRRRVHITLE LPWSADRAIQ QFGRTHRSNQ TSAPQYRLLF TNLGGEKRFA SIVAKRLETL
     GALTQGDRRA GPSLSAFNYD SNYGKKALTI MYRGIMEQDS FPVVPPGCFD NETSIQEFIA
     EAKAALVSVG IIRDAVVCNG KVAVKLSGRI VDSDMHDVAR FLNRLLGLAP KIQNSILDVV
     LHNARIEGQL DSGIVDIKAK NTVHIDSLSG ASTVLFTFTI DRGVTWESAK AMLDERQRDG
     ASSSNDGFYE SKREWMGRRH FTLAFEGSIE GMYKIIRPAV GEALREMPLT ELKSKYRKVS
     SIEKVNKGWQ DEYDASSKQC MHGSKCKVGS YCTVGRRLQE VNILGGLILP VWGTIEKALA
     KQVRQSHKRV RVVRLETTND NKRIVGLLIP NSAVESVLTG LF
//
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