ID A0A078I5B4_BRANA Unreviewed; 204 AA.
AC A0A078I5B4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN Name=BnaA06g09370D {ECO:0000313|EMBL:CDY45267.1};
GN ORFNames=GSBRNA2T00081709001 {ECO:0000313|EMBL:CDY45267.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY45267.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY45267.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- FUNCTION: Histone-binding component that specifically recognizes H3
CC tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription
CC start sites of virtually all active genes.
CC {ECO:0000256|RuleBase:RU369089}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000256|RuleBase:RU369089}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU369089}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000256|RuleBase:RU369089}.
CC -!- SIMILARITY: Belongs to the Alfin family.
CC {ECO:0000256|ARBA:ARBA00010445, ECO:0000256|RuleBase:RU369089}.
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DR EMBL; LK032619; CDY45267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078I5B4; -.
DR STRING; 3708.A0A078I5B4; -.
DR PaxDb; 3708-A0A078I5B4; -.
DR EnsemblPlants; CDY45267; CDY45267; GSBRNA2T00081709001.
DR Gramene; CDY45267; CDY45267; GSBRNA2T00081709001.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd15613; PHD_AL_plant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045104; Alfin.
DR InterPro; IPR021998; Alfin_N.
DR InterPro; IPR044104; PHD_AL_plant.
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; PTHR12321; CPG BINDING PROTEIN; 1.
DR PANTHER; PTHR12321:SF132; PHD FINGER PROTEIN ALFIN-LIKE; 1.
DR Pfam; PF12165; Alfin; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|RuleBase:RU369089};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369089}; Nucleus {ECO:0000256|RuleBase:RU369089};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU369089};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU369089};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369089};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 145..198
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 99..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 22634 MW; 789B1F4805FD7C1A CRC64;
MCAANENLCL YGLPNGSWEL NLPVDEVPPE LPEPALGINF SRDGMPEENW VSLIAVHSDS
WLIAVAFYFG ARFSFDKNER LFKMINDLPT IFEVVTGNAK QSKDQSANSG RSKSGGAAKR
SPPPPPTREE SESGDDDGEE DEGQGEFCGV CGESDDGEEE FWIWCDTCER WFHGKCVKIT
PARAEHIKHY KCPSCCGSNK KHRA
//
