ID A0A0D9XP30_9ORYZ Unreviewed; 1889 AA.
AC A0A0D9XP30;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
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:LPERR11G02640.2, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR11G02640.2, 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:LPERR11G02640.2, 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:LPERR11G02640.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR EnsemblPlants; LPERR11G02640.2; LPERR11G02640.2; LPERR11G02640.
DR Gramene; LPERR11G02640.2; LPERR11G02640.2; LPERR11G02640.
DR HOGENOM; CLU_002742_1_0_1; -.
DR Proteomes; UP000032180; Chromosome 11.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
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; 2.
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:UP000032180};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 339..399
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 553..600
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1462..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1889 AA; 206428 MW; 553A1CBD98BFA276 CRC64;
MEEPQGVSDR MLHDASPAAA IAPAPAEDDV REAEIGGDIA VAAAGEEPPA AAPSGSEAAG
DGVIAVEHEH AAANPVSDTK MEVDEGEGGV VDAEQTAAPS PGEVKAEVNG GSTLDKGEYV
VALACVPKEE KMEVCENGVP EQLHTVAAVA SEVKIEGCEG GLVVDQQSST PAGGGCQMKK
EGECLVGRYI SRSVTGHGRI LLGKVASYDS STGVYSVVFE DGQGEDFELA QLQLLLVGEE
NGAFGMKVSC RKRKLDLLVS SGGATEVKGP PCTRQRVNES EVSTKPDESQ QSGSGSDASE
DVESSSNSSN HAKELPEEHC PPVQILELPP SSGDIAVPEE AISYLFSVYN FLRSFSVQLF
LSPFGLDDFV SSINCTTQNT LLDAVHVSLL RALRRHLETK SSEGSKLASN CLKYLDWALL
DSLTWPAFLL EYLYLMGVIK DLGGRRFGRS VLAIEYYKLP VTLKLRILQL LCDHVTDSEE
LKTELEDREG YSEEMEYEMD SSTSAEVGPR SISTRGSKAS AYKKLNALEN LENDQNGNNP
EAAPAHASQD DNSDDCRICG MDGTLVCCDG CPWAYHSRCI GQNKAFLPQG DWFCPECVVN
KLGPTSSRIE RGARGAQFFG IDMCGRSFLG CCNYLLVVGT SPDAEFCARY YNHLDVAKVL
QILASSDAHI DICRRMTEYW SHLLDIFQNE RSKIGKEVCG SLTPQSNILL TVTPVKANNG
SVQATLKDGG DSKSAVLSQT NVCLENQFTT CSANSSEAFT QTPLAQNYVD NTYRNGAFGP
SGTSSISHQS ASMATAMPNI TQAQPAHGLI RPDLCGSVIG NGTSRENIKS SSARKDLICP
SYQSKPPVQL VTENMSSGKT AKFSSFRPQA YMNLYIHGNV AASAAANLAV LKSDEGKAPT
SHLTTNQRKK LAADCALQMK AFSSAALQFV WPSTEKKVME VPRDRCGWCL ACQSSAGGTK
KACFLNMATA NASKGSARIL SGMRIIKNCE SHFPSILTYL THMEESLRGL LVGPLQDLQR
REQWYNQLKG ASNCRNLIPL LLELESNIRG VTFSASWLKL IDDWPMESPS ASVGASRPAA
YQKRGTGGRR GRKRSMASES GPVTDDDNSW KEVNWWSGGN VSKRILQRGA IPILTLRKAA
RQGGKKRMPG LSYHEGSNCP RRTRQFAWRA CVGLCQNSSQ LALQVRYLDA HIRWKEFIPP
DQVPSDGKSL DSDFSVLRNA VICDKKIVDN KIRYALKFPN QKHLPVRVTK NILEAEDNQD
GDGKFWFSEN HIPLYLLRDF EQKAGASSLS TPGMLDSNYF ANFYRRRVKA FVGDVFFYLL
HKDDVYPCTS CKKDVAFRSV GSKEGNAAPS LTCKLCLQKR NLMLTNYNTN ASFILPQQKS
NVHQAVAAPK IIFKVGSSHS AEPVAKVEAH PIAKVEAQPV VKKETCPIVK METQPAANVE
AHPTAKVEAQ PIVNSATQNI AGAQAQPKAK SKKPKPEKPR KPKKVQDIKY FGLVWKKNTV
DKNSNDNGDE FRAKDVILKG KDGIGSPIKP TCCLCSKAYC PDFLYVRCER CQKWFHGDAL
QLKEEQIFQV VQYRCCRCRR RAIPKCPHSD DYKKPEPEFS EQTITTSSQS TMLSSEENFA
VADQDPLLAS YGRVEPGEQT MDADLSMDMV NFNTGINQKL SVRRGHNKNC EYVDQASIPM
DEYYIQNQSQ GNANINFSHS NEFSLSEADG VDPSDLLGWD FSQGNACAAP SDFAANCPWN
ETSCGSVADE YEPQTYFSFT ELLEADDTQF DNTFGMSSSL QDDGTGSLDQ QGIGFDEMSF
MLEDGASNMH FPAIDSASDE DVTSARILSH HLISNAQYVD CRFIVIAHLG RKVKNQQMVP
VGVVVLVGSG DDELQTFYLR YAHMQSAAV
//
