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Database: UniProt
Entry: R0G8F3_9BRAS
LinkDB: R0G8F3_9BRAS
Original site: R0G8F3_9BRAS 
ID   R0G8F3_9BRAS            Unreviewed;      1069 AA.
AC   R0G8F3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CARUB_v10025786mg {ECO:0000313|EMBL:EOA12824.1};
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:EOA12824.1, 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).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KB870812; EOA12824.1; -; Genomic_DNA.
DR   RefSeq; XP_006279926.1; XM_006279864.1.
DR   AlphaFoldDB; R0G8F3; -.
DR   STRING; 81985.R0G8F3; -.
DR   eggNOG; ENOG502QTVY; Eukaryota.
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; cd04301; NAT_SF; 1.
DR   CDD; cd20405; Tudor_Agenet_AtDUF_rpt1_3; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR008395; Agenet-like_dom.
DR   InterPro; IPR014002; Agenet_dom_plant.
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:SF12; GB|AAC80581.1; 1.
DR   PANTHER; PTHR46309; PHD FINGER PROTEIN 12; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF16135; TDBD; 1.
DR   SMART; SM00743; Agenet; 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          681..726
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          823..975
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          1011..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1069 AA;  122525 MW;  F505222DEDA1ABF5 CRC64;
     MKAAIVRSLE EGFLGSWYLG TVIAAKRRCR RCIRYANILS DDGTDYLVET VDVSDVVEGL
     NSDCTDVSDT FRGRLRPVPP KLEVDKSKLV YGICVDVFFS EAWWEGVLFD HENGSEKRRV
     FFPDLGDEMD ADLQYLRITQ DWNESTEMWK CRGRWLFLDL IETYKEDNYL PVSVKQLWYD
     IRDRIGFARI QEWTCSTRYL WEDLMLEVID DNLRITVNQF LHDYDAERFP QLKLLKEASQ
     AVSETNTCLS GVLVIAQKEQ QFSCTDKDYQ LASQICHSLS VLTSVSGIRS ETRYINRETE
     FSSKKSTAVD KKLILHKKTG NWHPFNCVAK SCPQAVSSFI RSMSPEMATH VRKHIKSMGW
     TIEHMVDEAG RQRFRYLSPN GRLTEHSLRQ VCFRLKQRDE SLTTPRMAKF PILSCDDQTY
     NTQKMRCIVL ALPARNRTVG PGEGRTPPAE TLLECDTQGN EEIFTEESRH FCPRNAFSGQ
     KKTLCVRLEP ETKAQGIQRL KSKRKQKHKL RYNSKKEEVI TGLRNVDMRM RRGNTSRMLM
     DIKNRVIGRG KTRVLRSSKR VQRVITPISR NHSPRSILSW LIDNNVVLPR ETIRCHNQKD
     DTLRKEGKLT REGIKCSCCR RIFTISGFEV HAGSGSCRAG ANIFLDDGRS LLECQIEAYE
     ARKKAQPPNI LKIKLRQGEN DVICSVCHYG GKLILCDGCP SAFHANCLGL EDVPDGDWFC
     ASCCCGACGQ TIVNATSKYA KEEYFISCKQ CELRYHPSCM RYDGAGDSLD IFLVDKWFCS
     KNCEKIFENL CELIGKPREV GVDNLTWRLL QSLEPNTCGI DASKIEDVAE NHCKLSVALD
     VMHELFEPVK RPHAGGDLAE DVIFGRWSKF KRLNFSGFYT VLLEKNDELV TVATVRIFGN
     KVAEMPFIGT RFQYRQRGMC RVLINELEKV LIELGVERLV LPAVPSVLNT WINSFGFTKI
     TLSKRKDFLK FAFLEFGRTI LCQKILSSVA DPFLSRVSLG EPHCDILGTE DNSASDDRSE
     VHQAEQHVDE SISTKNPPEE IKKDEQLLLK RNNILKCYTR RKSKCMRLT
//
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