ID A0A565CI38_9BRAS Unreviewed; 239 AA.
AC A0A565CI38;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN ORFNames=ANE_LOCUS23797 {ECO:0000313|EMBL:VVB13353.1};
OS Arabis nemorensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=586526 {ECO:0000313|EMBL:VVB13353.1, ECO:0000313|Proteomes:UP000489600};
RN [1] {ECO:0000313|EMBL:VVB13353.1, ECO:0000313|Proteomes:UP000489600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dittberner H.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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; CABITT030000008; VVB13353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A565CI38; -.
DR Proteomes; UP000489600; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:SF119; PHD FINGER PROTEIN ALFIN-LIKE 1; 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:UP000489600};
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 184..236
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 138..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 239 AA; 27027 MW; B4708550D4DDA972 CRC64;
MAAESSNPRT VEEIFKDFDG RRSGFLKALS VDVDKFYSLC DPEMENLCLY GHPNGTWEVN
LPAEEVPPEL PEPALGINFA RDGMERKDWL SLVAVHSDCW LLSVSSYFGA RLNRNERKRL
FSLINDLPTL FEVVTGRKPT KDKPSMDLGS KSRNGVKRSI EGQTKSTPKL MEESYEDEDD
EHGDTLCGSC GGNYTNDEFW ICCDVCERWY HGKCVKITPA KAESIKQYKC PSCCTKKGR
//
