ID A0A0E0JM72_ORYPU Unreviewed; 1889 AA.
AC A0A0E0JM72;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS51805};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC01G25810.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC01G25810.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC01G25810.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR STRING; 4537.A0A0E0JM72; -.
DR EnsemblPlants; OPUNC01G25810.1; OPUNC01G25810.1; OPUNC01G25810.
DR Gramene; OPUNC01G25810.1; OPUNC01G25810.1; OPUNC01G25810.
DR eggNOG; KOG0732; Eukaryota.
DR HOGENOM; CLU_001894_1_0_1; -.
DR OMA; QSICTQA; -.
DR Proteomes; UP000026962; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR045199; ATAD2-like.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23069:SF7; P-LOOP CONTAINING NUCLEOSIDE TRIPHOSPHATE HYDROLASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS51805; EPHD; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 412..550
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1889 AA; 208194 MW; 1A22B465E60237D2 CRC64;
MPPSRPKRRR GGSARSRGRK KQKRLDAIHD VAAVSAPPAG VVVVVGGGGE SEDSDAEGPR
RSTRVRRAPA LLDTSPLPSP RRKRARGGGG GGGVAGSSGG SSRRGSRGRV RGEAGPAREI
GEEEEEDDEA GSVVWRSRLR DRVKGKAKLD KRVRSLWFDE DYEVELKEEE VEEEEEGDEE
EEEEEQARTL VVDLREGAEE ERMGEGSGGL PMRGREVRDR EINLTIDLNV EEHEAVEGVN
VVEEEDEGKG GESDAEKGEA IGTENDLDEG EHEEVGDKEE GFHGKERTEE LGSAVLEGRN
GDELPCNENN AEDGTGSSHE YEHLDVQNEQ TVEESNLYVE QQMELDDSCP SEQLKEVQQD
GQTDGVPNVV LPEEAPKEGV RKFPVSEEKQ GIMEIKEGRR CGLCGGGTDG RPPKVALHDT
VDSDNEAYEG ALPSEDPNYD MWDGFGDDPG WLGRLLGPIH DQFGIARVWV HQNCAVWSPE
VYFAGLGCLK NVRAALCRGR LLKCSRCGRP GATIGCRVDR CPKTYHLPCS RAEACIFDHR
MFLIACNDHR HYFQPQGDKY VELLRKMKTK KMKADITKVS HDAWRKDIEA EEKWLENCGE
DEEFLKREGK RLNRDLSRIA PVYIGGTSEN EKAYCGWESV AGLSNVIQSM KEVVILPLLY
PEFFSSLGLT PPRGVLLHGH PGTGKTLIVR ALIGACSQGN RRIAYFARKG ADCLGKYVGD
AERQLRLLFQ VAERCQPSII FFDEIDGLAP SRSRRQDQTH NSVVATLLSL LDGLKSRGSV
IVIGATNRPD AIDPALRRPG RFDREIYFPL PTFEDRSAIL SLHTKKWPSP ISGAFLSVIA
SQTVGYAGAD LQSICTQAAI NALKRTCPLE EILRSAEKGF EHGRLPLPSI LVEERDWLAA
LAAAPPPCSQ REAGIAANDL VSSPLVSYLV PCLLKPLLHL FISLYLDERI WLPSSLLKAF
ASIKQVIFSS MEKNNVPHTF WSSYLPSLIQ QKDIAKRIAS ILSSYGLIAS QLGNHDSVLN
HNEQHEKFDA HRLNSTGSHT KGGFAHKLSG FRALAAGAPR SGQQHLIRCL LHGFVGQTVI
HKLDLATMAQ EGNGDILSGL TQILLKCLNL GRCIIYMPRI DLWAIDKVHE QEAEDHVLNV
GTSKLGSTAT KYIQKCSEVW NALVDQMGSL LASVSISVLA TSELKFQDLP SGVRHFFSTH
VVDQCLASSE HTIPRFSVNV DSYFSWDEVI DACCLRISHD LVQQHVQLLH DRAHNNHDEQ
KEVFVPMEIS APGEHRSSGS KEASMFTKYP LNMDKHPSCG VSSREHPTQL GTCSAQQEPP
TSNVEDKEDN TEKIDFNEKV ATNRSNRIVK DNESLAIMAF GIQILQHPQF SKLCWVTSKL
REGPCTDING PWKGWPFNSC LLQSTTADKS LSGGNNVLKG KEKIPSVRGL IAVGLLAYRG
AYASILEVCS EVRKVLELLV GQVRTKILEK RSRYRYFHIL SQVAYLDDIM SSWAYTFQRL
HSDNRRVKTG PNITVGKSST RECQGDRNTA ETNTFGAPAG CSEDQCTPGQ HTDDLQVVPA
RCPSEMQENS VQHAPDHLEI HDVVCDLDND NVTSISSINA VEPDLIHSAS LDVHTDSLTP
ADAVINDGES CGVDNDGQMS RVINGEENPI SNIERPESHT VSVADFNELQ RKNSVASSIS
TDSAGTSRNM VSSEAHGSGN ERNTDFPVDD VKLGHLVNPQ SQDTMKSLSV LKPPCLYKCC
PVCFNAVYKM VHDILSNSVR PSLHCLAVDD MHDLLSSWSV NLLATVRKRY SSQGIVGSEE
NSGEGHCVCC SDIGCVPREC TCHLESNEDA GTIKDESYYL SGQPLSFFFK DGVLIPPDIT
AVTTLHCSYM RLCVCSIPGS ISMFNRILS
//
