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Database: UniProt
Entry: R0HWE2_9BRAS
LinkDB: R0HWE2_9BRAS
Original site: R0HWE2_9BRAS 
ID   R0HWE2_9BRAS            Unreviewed;      1189 AA.
AC   R0HWE2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CARUB_v10012838mg {ECO:0000313|EMBL:EOA29750.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA29750.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
RN   [2] {ECO:0000313|EMBL:EOA29750.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., Wright S.;
RT   "Genome sequencing of Capsella rubella.";
RL   Nat. Genet. 0:0-0(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KB870807; EOA29749.1; -; Genomic_DNA.
DR   EMBL; KB870807; EOA29750.1; -; Genomic_DNA.
DR   RefSeq; XP_006296851.1; XM_006296789.1.
DR   RefSeq; XP_006296852.1; XM_006296790.1.
DR   AlphaFoldDB; R0HWE2; -.
DR   STRING; 81985.R0HWE2; -.
DR   GeneID; 17893734; -.
DR   KEGG; crb:17893734; -.
DR   eggNOG; ENOG502QTVY; Eukaryota.
DR   OrthoDB; 1222616at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15539; PHD1_AIRE; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR032308; TDBD.
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; PTHR46309:SF7; OS04G0433900 PROTEIN; 1.
DR   PANTHER; PTHR46309; PHD FINGER PROTEIN 12; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF16135; TDBD; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          727..772
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          861..1025
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          569..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1074..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..594
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1189 AA;  131998 MW;  B0F33C98CD190250 CRC64;
     MMLGGAEIEM FGGDCFEGSY EDHKIFREVF FGTDPENTTK RCLVTGVINF ECDSTKNVNS
     SLSSNNDNSV ITSGYLEGFE ASASKDGSDF NNRAKRVKLS GNKHLDVRDE KGSALNGFPN
     SDIARETVPL HLVESSNSGV LTSSYLLKQS IEKGREVYLG GIVSERFKSQ NLDRSDGKEF
     KAIASPVSQE SFATRMICAG ASTPHSEKQA FSLQLNNGSK VSPNELVMSQ TCLKIDPKED
     PRPLLYKYAC KLLNAARWKI EKRARSGRKY LETFYISPEG RRFREFGSAW KSLGRILLAD
     HKLMDTSTKK WTGINDFWSD LSLTLLDIEE NMKNINLANT RALWWSALEP FVIAVFISKQ
     VGSLRRGNKV EVARNTVIDK FKKDDATCLN MISGCPESVL TLSEGSHLVC DVDASQEIHS
     DLEVQTKIVR RKVSTGLERQ NIIGKEISGA DEQEVSKGVV ASKLIAEDML ESVMRKKLHR
     RSKKISDIKL APLDQHDSLD SNSLDNLEGQ DKEMGSIHLI SKRSRDERLR NEKMKNSFCN
     SKKGRKKARK HYSQDDDLMV SSVIRKKGKV WRSSQKKKTH KPKARTKKRN NKGGCRLLPR
     STSNAENQNF QGNWSILGPR TVLSWLIATK VISRDEVIQL RDPDDDTVVK TGLVTKDGVV
     CTCCNRTVSL SEFKNHAGFN QNCPCLNLFM GSGKPFASCQ LEAWSAEYRA RRTGWRSVEA
     SDDDPNDDSC GVCGDGGELI CCDNCPSTFH QACLSMQMLP EGSWYCSSCT CWICSELVSD
     NAERSQDFKC SQCAHKYHGI CLQGASKRRK LFPETYFCGK GCEKVYTGLS SRVGVINPSA
     DGLSWSILKC FQEDGSVHSA RRIALKAECN SKLAVALSIM EESFQSMVDP RTGIDMIPHV
     LYNWGSKFAR LDFDGFYTVV VEKDDVMISV ASIRVHGVTI AEMPLVATCS KYRRQGMCRI
     LVAAIEEILM SLKVEKLVVA ALPSLVDTWT QGFGFKPMDD EERDALNRIN LMVFPGTILL
     KKTLYESTNT NTVKGVCLSE DHSKPSNKEA DVEPGVDKAG FPMNTQIESC DQMVPAGSDE
     EPAPGFPVPL GAKETEPTSE TENRSGESNA DDRPNKTTIS MGEEEGLQEE VSKFSEEGKE
     MARASSTSAA LEEVSDVGVV VVNNVSDDML LCFDEQLDSD SSEEEENSE
//
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