ID A0A087HJN8_ARAAL Unreviewed; 1302 AA.
AC A0A087HJN8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN OrderedLocusNames=AALP_Aa2g243600 {ECO:0000313|EMBL:KFK42340.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42340.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- SIMILARITY: Belongs to the SBNO family.
CC {ECO:0000256|ARBA:ARBA00006992}.
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DR EMBL; CM002870; KFK42340.1; -; Genomic_DNA.
DR EnsemblPlants; KFK42340; KFK42340; AALP_AA2G243600.
DR Gramene; KFK42340; KFK42340; AALP_AA2G243600.
DR eggNOG; KOG1513; Eukaryota.
DR OMA; ARHSHKR; -.
DR OrthoDB; 3541637at2759; -.
DR Proteomes; UP000029120; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:EnsemblPlants.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:EnsemblPlants.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:EnsemblPlants.
DR GO; GO:0010286; P:heat acclimation; IEA:EnsemblPlants.
DR GO; GO:1900036; P:positive regulation of cellular response to heat; IEA:EnsemblPlants.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR026937; SBNO_Helicase_C_dom.
DR InterPro; IPR026741; SNO.
DR InterPro; IPR039187; SNO_AAA.
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; PTHR12706:SF13; PROTEIN FORGETTER 1; 1.
DR PANTHER; PTHR12706; STRAWBERRY NOTCH-RELATED; 1.
DR Pfam; PF13872; AAA_34; 1.
DR Pfam; PF13871; Helicase_C_4; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 688..738
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..686
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 144439 MW; 3D12A912A74D2C7D CRC64;
MTQSPVQPPP PLPPPPHSAA GNVSRGDVQV RCAGCRVILR VKTGVVEFSC PTCQLPQMLP
PELLSRSRQQ FSQPPPPPPQ SIPPIQQQLK SPPINLPRPP VPAHGIDPTK MQLPCANCQA
ILNVPHGLTR FSCPQCHVEL AVDVSKLNRS LTAPQSTPPI SGAAPPVPPP PPPEEVNEEA
IEVEREEDEG GTAGETFMDY RPPKLSIGPP HPDPIVETSS LSAVQPPEPT YDLRIKEELE
RTKALSCLQI ETLVYACQRH LQHLADGTRA GFFVGDGAGV GKGRTIAGLI WENWKHGRRK
ALWISIGSDL KYDARRDLDD VGASSVGVNP LNKLPYSKLD SKNVGVKDGV VFLTYNSLIA
SSEKGRSRLQ QLVQWCGPEF DGLLIFDECH KAKNLVPEAG SQPTRIGQAV VDIQDKIPQA
RVLYCSATGA SEPRNMGYMV RLGLWGAGTS FSDFNKFLGA LDKGGVGALE LVAMDMKARG
MYVCRTLSYK GAEFEIVEAR LEAGMEAMYN KSAEFWAELR IELLSASAFL PNEKPNPSQL
WRLYWSSHQR FFRHLCMSAK VPVTVRLAKK ALSTNKCVVI GLQSTGEART EEAVTKYGLE
LDDFVSGPRE LLLKFVEENY PLPEEPEPLS EDDNPKELHR KRHSASPGVS IRGRVRKMAK
RKPESDDESD LQSEAESADD SNDSDDEFQI CQICSGEDER KKLLHCSECD KLFHPDCVIP
PVTDLPSEAW VCYSCKEKTE EYIQARRIYI ADMQKRYDAA LERKSKIIDI IRSLNLPNNP
LDDIVDQLGG PDKVAEITGR RGMLVRASNG KGVTYQARNT KDITMEMVNM HEKQQFMDGK
KFVAIISEAG SAGVSLQADR RAANQRRRVH LTLELPWSAD RAIQQFGRTH RSNQTSAPEY
RLLFTNLGGE RRFASIVAKR LETLGALTQG DRRKVMLLSK PFLSCLAGPS LSAYNYDSNF
GKKSLMVMYR GIMEQEKLPV VPPGCSTDEP ETIKEFLTKA RAALIAVGIV RDSVLANGKD
VGKLSGRIID SDMHDVGRFL NRLLGLPPDI QNRLFELFTS ILDVLVHNAR IEGSFDSGIV
DMKANSVELL TPPKTVHVDH MSGASTMLFT FTLDRGVTWE SASSMLEGKR RDGLGSASDG
FYESKREWLG RRHFILAFES AASGLFKIVR PAVGESIREM SLSELKTKYR KLSSLEKARN
GWEDEYEVSS KQCMHGRKCK LGEYCTVGRR IQEVNVVGGL ILPIWGTIEK ALSKQARHSH
KRIRVIRIET TTDNQRIVGL SIPNAAVETV LQDLAWVQEI DD
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