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Database: UniProt
Entry: A0A565CI91_9BRAS
LinkDB: A0A565CI91_9BRAS
Original site: A0A565CI91_9BRAS 
ID   A0A565CI91_9BRAS        Unreviewed;       145 AA.
AC   A0A565CI91;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN   ORFNames=ANE_LOCUS23799 {ECO:0000313|EMBL:VVB13355.1};
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:VVB13355.1, ECO:0000313|Proteomes:UP000489600};
RN   [1] {ECO:0000313|EMBL:VVB13355.1, 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|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|RuleBase:RU369089}.
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DR   EMBL; CABITT030000008; VVB13355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A565CI91; -.
DR   Proteomes; UP000489600; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   InterPro; IPR045104; Alfin.
DR   InterPro; IPR021998; Alfin_N.
DR   PANTHER; PTHR12321; CPG BINDING PROTEIN; 1.
DR   PANTHER; PTHR12321:SF39; PHD FINGER PROTEIN ALFIN-LIKE 3; 1.
DR   Pfam; PF12165; Alfin; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|RuleBase:RU369089};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU369089};
KW   Nucleus {ECO:0000256|RuleBase:RU369089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000489600};
KW   Transcription {ECO:0000256|RuleBase:RU369089};
KW   Transcription regulation {ECO:0000256|RuleBase:RU369089};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU369089};
KW   Zinc-finger {ECO:0000256|RuleBase:RU369089}.
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..140
FT                   /note="Alfin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12165"
SQ   SEQUENCE   145 AA;  16829 MW;  2995972E89443B26 CRC64;
     MYRTTHPPPN TNPSTVEEIF ADINGRRSGF LQAFFVDVDS VFALCNPEEE ELCLYAYPNE
     RWNVSPPHLQ VPPDIPEPVL GINFVRDGMP RKAWLQFVAG HCDSWLLYLA FFFGCRLNRH
     ERTRLFDLID AQPTLYEQVT NRPSE
//
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