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Database: UniProt
Entry: A0A0D9XYX7_9ORYZ
LinkDB: A0A0D9XYX7_9ORYZ
Original site: A0A0D9XYX7_9ORYZ 
ID   A0A0D9XYX7_9ORYZ        Unreviewed;      1236 AA.
AC   A0A0D9XYX7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:LPERR12G08750.2, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR12G08750.2, 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:LPERR12G08750.2, 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:LPERR12G08750.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   AlphaFoldDB; A0A0D9XYX7; -.
DR   EnsemblPlants; LPERR12G08750.2; LPERR12G08750.2; LPERR12G08750.
DR   Gramene; LPERR12G08750.2; LPERR12G08750.2; LPERR12G08750.
DR   Proteomes; UP000032180; Chromosome 12.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; PTHR33304; RING_FYVE_PHD ZINC FINGER SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR33304:SF9; RING_FYVE_PHD ZINC FINGER SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
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          116..167
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1236 AA;  135673 MW;  6BF37A6B453BC45A CRC64;
     MVVKKKRGRR APSSSRRFSG NNVVGIEDAV GNCNHAKEEG QAGDSSDVAL SPSCRKTEDR
     DQSTKQDSLN TKTTGKGVSA SEASEKSSTL KKTSVGQAAS RSVNPEDNFL EPMDKVKVCD
     ICGDVGEEER LAVCSRCNDG AEHIYCMRVM MEEVPEGEWL CEECETQLVL EKDKKKLEKS
     QLKVGTPKGQ SFEGKADKLA NTLKSSSSGN EASQAFEGKV NKLDTALKSR SSFKNELEDE
     NGDNKELNST NQCNNITAKK KEEAAGIISS IRQSLPERCG LSMGAESRKR LPLSRESSFR
     LDVEKGKPST TQVPTPLTFD ATKNLAPSLR GQISKSTSFN NSKVPKVKQL VNEVPQKPNN
     LKDHSSFITK KEVPVGILAK SPFFKKPKPC EPANKAKSSI LPPTESKVMN PPAGQNATND
     RDTSILGCPS VTASMTTQAS CKEESKAQCL TVDNDMADSN NLSITQGQGG MNSLGYSEVN
     KQPLAKAPGS TTVSGAEKSS GILGSGSQRK NTDAVHRDDK VKDPTSLRPG VFSSNRTLRC
     QRCNEAGHST QFCSVDKLSL SAVKPISERT MKESSAKRNK TSEVTNMIAA DTAASRPANQ
     SEHIVKCGPY RNPTYRPKDL LSTSFGHVKK PSQLYGQTNE QDMRNTSNSR ASTDCSNLKP
     KECQTMPDMA GRFIDDSSTM PDALMDKSNK VLLPGHGPTV ATVPELNFIW QGGFELRRTG
     RSPELCDGFQ AHLSCSASPK VLEVAKKFPS KVQLEELPRQ NSWPTQFQGN GPSYENIGLF
     FFAKDTDSYE NHYSKLVQNM LKNDLALRGN IETAELLIFP SNILSNNFQR WNMFYFLWGV
     FRVRKKDQMN IPPDVPFSTC EPNLNSDPMD VDQSISVLTA GHSSSEDQNN GAKSDHDLVK
     PVPCADYQFP WTIETNHQGC LNGEHISNQP MSRNESEDHH HISITASCST NNSTDLATEQ
     QNISCSEDQD TKDSSNSNVC KAMLDVKTVP VTCSISSVHE KGKDSRAFNL NDVDNLVDVD
     INNCEVNSGK VDPVSHFTAS PHKRNVEVAN WVDEVNGKLE QKRIKLDNVG SANSSLSENT
     SDGRLSSKVH PLLSSSFDDS VDQSLAGSSK CNGKRVLLDL NTVDDDATGN VVDILSSDDE
     DMPERHVPEH EQHGDNKSPR KTMFSFLPPK RQLPEMSNRN KDYPEYECTY MILLQCANRG
     VIHGVVLTDV QHPAELLHWK EQNYFAETVS CIPEGL
//
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