ID B9SB99_RICCO Unreviewed; 1937 AA.
AC B9SB99;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS51805};
GN ORFNames=RCOM_0649850 {ECO:0000313|EMBL:EEF39107.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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DR EMBL; EQ973912; EEF39107.1; -; Genomic_DNA.
DR RefSeq; XP_002523268.1; XM_002523222.2.
DR STRING; 3988.B9SB99; -.
DR eggNOG; KOG0732; Eukaryota.
DR InParanoid; B9SB99; -.
DR OrthoDB; 553033at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:UP000008311};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 442..562
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1937 AA; 215082 MW; A88029E2F042D98C CRC64;
MQLKSSSPKG RDYSPKSGSR VKQKHKRLDA ICENVYNQNH QSESKPLDDA NSELRRSSRV
RRAPVVLDVS PPPVKKRKKL DKNVKNVNLS VVNRRSGSGR GLRGVEIKEG NEQLGFLDTP
GSWRSRLRSR GRVRNLVSRE RGETSRKRKL FDEEVEMVES EEEEEEEEEE GEEEEEELKE
EFDDDEKLMV LKLKRLGRVK AVNGLGNEMK NDEDNVSGKD DGKESVGKDE IEGVEEGMPV
FGSEIDGGNE MEVVRDEVEE CVPVLVDAVD GGNEREEVDD DGDAVQLRLD KQEEKDRLDG
LELEKNINEN YNVENVEQGD RKMEEVDTRM DVENEGDVEV DETPMNDVED PNKEGNVVEI
DETLMNEVKD PNNEGDIEVN EIPLEVEKVA KAEKSKHDSH TLGRPQVKQG RWCGLCGCAN
DGKPPKKLIQ DAGDSENETY SGSSASEEPN YDIWDGFGDE PSWLGRLLGP INDRHGIAGI
WVHQHCAVWS PEVYFAGLGC LKNVRAALCR GRALKCTRCG RPGATIGCRV DRCPKTYHLP
CARANGCIFY HRKFLIACTD HRHLFQPYGN QNLMRIKKLK ARKMKLEVRK RSNDAWRKDI
EAEEKWLENC GEDEEFLKRE SKRLHRDLLR IAPAYIGGSD SESLKLFEGW DSVAGLKDVI
QCMKEVVILP LLYPEFFNNL GITPPRGVLL HGYPGTGKTL VVRALIGSCA RGDKRIAYFA
RKGADCLGKY VGDAERQLRL LFQVAEKCQP SIIFFDEIDG LAPCRTRQQD QTHSSVVSTL
LALMDGLKSR GSVVVIGATN RPEAVDPALR RPGRFDREIY FPLPSIEDRA AILSLHTRRW
PKPVTGSLLH WVASRTVGFA GADLQALCSQ AAIIALKRNF PLHEMLSAAE KKAPGANCVP
LPAFTVEERD WLEALACAPP PCSRREAGIA ANDLITCPLP VHLIPCLLCP LTKLLVSLHL
DERLWLPPPL SKAATMVKSV IISTLAKKNL PSNQWWFHVD NLLKQTEVAN EIQRRLSVAG
ILIEENSYTH AHAIDENDDD GVQFEPSVCS KRLSTSFLRG ISLTSRKKGY RILVAGGPRS
GQRHVASCML NCFLGNVEVQ KVDLATISQE GHGDLVLGIT QLLMKCASFQ SLVIFMPRID
LWAVEACRQV TKENGASSTD QLSEKTECYS PSLQDVGKEN ASEKAESCYK PIQDVGQEKV
SEKTESYSTP IEVNDKENET FAHKCRESEM QQPQNATLIA SHSWCSFVEQ VENISVSTSL
IILATSEIPY LELPQEIMQF FESDVSNSTE LTPLEHTVPR FSVHVGDDFN RDLVVSLSAA
KLLGDITQLF VLLIHQKAHI HTTSVQYKFC DSVQTCATEN QFKKNGSGVE NDFGKAFPHD
HSKVAPPPSN KSLKGKSSLL LAISAFGYQI LRCPHFAELC WVTSKLKEGP CADFNGPWKG
WPFNSCFIHP GNMDNVPATY STGNIKSKDK YSLVRGLIAV GLSAYRGVYK SLREVSFEVR
KVLELLVGQV NEKIQAGKDR YQYIRLLSQV AYLEDMVNSW AHALQSLELD NQIKLANAGQ
STPDFPCDYA SVENSIQNEE CRGVIPNKSA QESEGSPVKL APGNVEGVQL IEGENGFGLS
GSDIRGVLSE DLSPKQNVHC DHTNLDKNLQ SFTSDNQLVD KNTDEQNGIT LGQREPKNTS
ALKVVTGLDN GSLKHSNGLT VADIGVHSEG GVCNSSEQCT NKFAGPSKPC DRIDGMVATE
EGAKCKDNQP NCSDFSPGKD TSHFADCEVV CSYICCYGCL HMLQKMIQEV LVHKWELNNS
HWRVDDVHDV VSSLSVDLLS AVRKADVTSD SIHGNLRCAN PDILSESSEM QNCRCQSSGN
SLALAAECSC HSMAGFATAK ANGSPNSDLR IELEFIFRDG VLVPVDTNKN ISFHCKYETL
CLCSIIKSVV MMKQPSD
//