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Database: UniProt
Entry: A0A0E0BFB3_9ORYZ
LinkDB: A0A0E0BFB3_9ORYZ
Original site: A0A0E0BFB3_9ORYZ 
ID   A0A0E0BFB3_9ORYZ        Unreviewed;      1884 AA.
AC   A0A0E0BFB3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM11G02760.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM11G02760.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM11G02760.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   STRING; 40148.A0A0E0BFB3; -.
DR   EnsemblPlants; OGLUM11G02760.1; OGLUM11G02760.1; OGLUM11G02760.
DR   Gramene; OGLUM11G02760.1; OGLUM11G02760.1; OGLUM11G02760.
DR   eggNOG; KOG1473; Eukaryota.
DR   HOGENOM; CLU_002742_1_0_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15532; PHD2_CHD_II; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR047365; Tudor_AtPTM-like.
DR   InterPro; IPR028942; WHIM1_dom.
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; PTHR46508; PHD FINGER FAMILY PROTEIN; 1.
DR   PANTHER; PTHR46508:SF1; PHD FINGER FAMILY PROTEIN; 1.
DR   Pfam; PF02791; DDT; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF21743; PTM_DIR17_Tudor; 1.
DR   Pfam; PF15612; WHIM1; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00249; PHD; 4.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          330..390
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          544..591
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1472..1498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1603..1622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1884 AA;  206094 MW;  2B2C077C207D9A79 CRC64;
     MEVSDRMLHA SPAAAAAAPA TADDARETEI AGGIASASAA VEDPPASAPP ASEAAGEGVI
     AVEHERAAAH PVSETKMDVD EVGTADAEQA VAPAAGEVKA EVNGGSIPDK EQDAAACTPT
     QVKTEVYENG VQEQVHTVAA VASEVKMEGC EGGVVDQKPT TTPADGCQMK EEGECLVGRY
     ISRSVAGHGR ILLGKVASYD GSTGIYSVVF EDGQGEDLEL AQLQSQLVGE ENGAFGMKVS
     CRKRKLDLLV SSGGATEVKG PPITRQRVNE SEVSTRPDES QESGSGSDAS EDVESSSNSS
     NCTKELPVEH YPPVQVLELP PSSGDIAVPE EAISYLFSVY NFLRSFSVQL FLSPFGLDDF
     VSSVNCTTQN TLLDAVHVSL LRALRRHLET KSSEGLKLAS NCLKYLDWTL LDSLTWPAFL
     LEYLYVMGII KDLGGRRFGR SVLAIEYYKL PVTLKLRILQ LLCDHVIDSE ELKTELEERE
     GYSEEMEYEM DSSTFAEVGS RSVLTRGSKA SACKKLDALQ NLETAPNGNN PESASTHASQ
     DGNSDDCRIC GMDGTLVCCD GCPWAYHSRC IGQNKAFLPQ GDWFCPECVV NKLGPTSSRI
     ERGARGAQLF GIDMCGRSFL GCCNYLLVIG TSSDVEFCAR YYNHCDVVKV VQILASSDAY
     TDICRRMTEY WSHLLDIFQN ERSKISKEVG GSLMSQSNIL STATPVKANN GSVQATLKDG
     QDSKMAVLSQ INAHQVMDNQ FTLCSANNNE AFRQTPLAKT YVDNAYRNGA FGPSGTSSIS
     HQSTSMVTVM PNRTQAQPAH GLIRPDLSCG SVIGNGMSRE NIRSSISARA DLISPPYKSK
     PPVQLITENM SGGKPAKFSS FRPQAYMNLY NHGNVAASAA ANLAILKSDE GKAPTSHLTT
     NQRKKLAADC ALQVKAFSSA ALQFVWPSTE KKVMEVPRDR CGWCLACQSS AGGTKKACFL
     NMATANASKG SARILSGMRL IKNSDSHFPS IVTYLSHMEE SLRGLLVGSL QDVQRRQQWY
     NQLKDASNCG NIIPLLLELE SNIRGVAFST SWLKLIDDWP VESPSASAGA SRPAAYQKRG
     TGGRRGRKRS MASESAPVTD DDNSWKEVNW WSGGNVSKRI LQRGALPILT IRKAARQGGK
     KRMFSVSYHE GSNFPRRTRQ LAWRACVGLS QSSSQLALQV RYLDAHIRWK EFIPPDQIPS
     EGKSVDSDYS VLRNAVVCDK KIVDNKIRYA LKFPNQKHLP VRVTKNILEA EDNQDGDGKF
     WFSENHIPLY LLREFEQKAG VSSLPTPGML DSNCFANFYQ RRVKSSIGDV FFYLLHKGDV
     YPCTSCKKDV SFRDIIKCSS CQGNCHKECT LRSVGSKEGN AASSLTCKLC LQKRSLMLTN
     YNTNASFILP QQKSNVHHAV AAPKIIFKVG SSHSAEPATK VEAPPIVKAE AQPVVKKETW
     PVVKMETQPT ANVEAQPTAK VEAFPISNLA TQNNAGAQVQ PKTKSKKPKP EKPRKSKKTE
     EIKYFGLVWK KSTNDKNNNE NSGEVFRAND VILKGKDGVG SSIKPTCCLC NKPYCPDFLY
     VRCERCKKWF HGDALQLEEE KIFELVSYRC CRCRRRAIPK CPHSDDYKKP EPEYSEQTVA
     TSSQSTMLSS EENFAVADQD PLLASYGRVE PFGAQTMDAD LSMNMMSFNP GNQKLSVRRG
     QNKNCEYVDQ SSIHVDDYYI QNQPQGNANI NFSHSNEFSL SEADGVDASE LLGWDFSQGN
     TSAAPSDFAA NCPWNDISCG SVAGDEYEPQ TYFSFTELLE ADDTQFDNTF GMSNSVQDDG
     DQQGIGFDEM AFMMEDGASN MPFPAIDSAS DEVACDRCKN PQPPPDLKCA VCGLQMHRHC
     SPWEDGEQPS DSADWSCGAC REWR
//
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