ID A0A067DET6_CITSI Unreviewed; 141 AA.
AC A0A067DET6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN ORFNames=CISIN_1g032409mg {ECO:0000313|EMBL:KDO41353.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO41353.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO41353.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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; KK785653; KDO41353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067DET6; -.
DR STRING; 2711.A0A067DET6; -.
DR PaxDb; 2711-XP_006470806-1; -.
DR eggNOG; KOG1632; Eukaryota.
DR Proteomes; UP000027120; 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:SF60; PHD FINGER PROTEIN ALFIN-LIKE 7; 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:UP000027120};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..54
FT /note="Alfin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12165"
FT REGION 54..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 141 AA; 15369 MW; 6C5106E4DBD3C860 CRC64;
MQEKDWLSLV AVHSDSWLLA VAFYFGARFG FGKNERKKLF QMINDLPTIF EVVTGNAKQP
KDQSANHNSS KSKSSGKSRP AESQTKAVKM SPPPKDDDDS GMKKRKMMNR APPVEHAGIT
MALTNSGSAA ISVRNGSTAN V
//
