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Database: UniProt
Entry: M5W0X9_PRUPE
LinkDB: M5W0X9_PRUPE
Original site: M5W0X9_PRUPE 
ID   M5W0X9_PRUPE            Unreviewed;       239 AA.
AC   M5W0X9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN   ORFNames=PRUPE_6G278200 {ECO:0000313|EMBL:ONI03731.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI03731.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI03731.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
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; CM007656; ONI03731.1; -; Genomic_DNA.
DR   RefSeq; XP_007205807.1; XM_007205745.1.
DR   AlphaFoldDB; M5W0X9; -.
DR   SMR; M5W0X9; -.
DR   STRING; 3760.M5W0X9; -.
DR   EnsemblPlants; ONI03731; ONI03731; PRUPE_6G278200.
DR   GeneID; 18772751; -.
DR   Gramene; ONI03731; ONI03731; PRUPE_6G278200.
DR   KEGG; pper:18772751; -.
DR   eggNOG; KOG1632; Eukaryota.
DR   HOGENOM; CLU_058315_1_0_1; -.
DR   OMA; KFYSLCD; -.
DR   OrthoDB; 313735at2759; -.
DR   Proteomes; UP000006882; Chromosome g6.
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:SF39; PHD FINGER PROTEIN ALFIN-LIKE 3; 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:UP000006882};
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|RuleBase:RU369089}.
FT   DOMAIN          183..235
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
SQ   SEQUENCE   239 AA;  27123 MW;  7B4C5F5B4B89B408 CRC64;
     MEMASSPRNV EEIFKDYSAR RTAVVRALTY DVDEFYGLCD PDKENLCLYG HPNETWEVTL
     PAEEVPPELP EPALGINFAR DGMNRKDWLS LVAVHSDSWL LSVAFYFGAR LNRNERKRLF
     SLINDLPTVF EVVTERKPVK EKPSVDSGSK SRGSTKRSSD GIVKSNPKLP DESFEEEDDE
     HSETLCGSCG GNYNADEFWI GCDICERWFH GKCVKITPAK AENIKQYKCP SCSLKRGRQ
//
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