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Database: UniProt
Entry: A0A061GH66_THECC
LinkDB: A0A061GH66_THECC
Original site: A0A061GH66_THECC 
ID   A0A061GH66_THECC        Unreviewed;       253 AA.
AC   A0A061GH66;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN   ORFNames=TCM_027993 {ECO:0000313|EMBL:EOY26404.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY26404.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY26404.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(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; CM001884; EOY26404.1; -; Genomic_DNA.
DR   RefSeq; XP_007023782.1; XM_007023720.2.
DR   RefSeq; XP_017979207.1; XM_018123718.1.
DR   AlphaFoldDB; A0A061GH66; -.
DR   SMR; A0A061GH66; -.
DR   STRING; 3641.A0A061GH66; -.
DR   EnsemblPlants; EOY26404; EOY26404; TCM_027993.
DR   EnsemblPlants; Tc06v2_t005390.2; Tc06v2_p005390.2; Tc06v2_g005390.
DR   EnsemblPlants; Tc06v2_t005390.3; Tc06v2_p005390.3; Tc06v2_g005390.
DR   GeneID; 18595661; -.
DR   Gramene; EOY26404; EOY26404; TCM_027993.
DR   Gramene; Tc06v2_t005390.2; Tc06v2_p005390.2; Tc06v2_g005390.
DR   Gramene; Tc06v2_t005390.3; Tc06v2_p005390.3; Tc06v2_g005390.
DR   KEGG; tcc:18595661; -.
DR   eggNOG; KOG1632; Eukaryota.
DR   InParanoid; A0A061GH66; -.
DR   OMA; PSKMVKM; -.
DR   OrthoDB; 313735at2759; -.
DR   Proteomes; UP000026915; Chromosome 6.
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:SF60; PHD FINGER PROTEIN ALFIN-LIKE 7; 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:UP000026915};
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          197..249
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          141..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..198
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   253 AA;  28399 MW;  DE0A8123C74D65F4 CRC64;
     MEGTPHPIPR TVEEVFNDFK GRRAGLIKAL TAEVDKFYQQ CDPEKENLCL YGLPNETWEV
     NLPVEEVPPE LPEPALGINF ARDGMQEKDW LSLVAVHSDS WLLAVAFYFG ARFGFGKNER
     KRLFQMINDL PTIFEVVTGN VKQPKEQSAN HNSSGKSKSS AKVSRQSEPP SKMVKMSPPS
     KDEDESGEED EEDDEQGATC GACGDSYGAD EFWICCDICE RWFHGKCVKI TPAKAEHIKQ
     YKCPSCSSKR ARV
//
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