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Database: UniProt
Entry: A0A5D2YWG0_GOSMU
LinkDB: A0A5D2YWG0_GOSMU
Original site: A0A5D2YWG0_GOSMU 
ID   A0A5D2YWG0_GOSMU        Unreviewed;       252 AA.
AC   A0A5D2YWG0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN   ORFNames=E1A91_A06G125100v1 {ECO:0000313|EMBL:TYJ30359.1};
OS   Gossypium mustelinum (Cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=34275 {ECO:0000313|EMBL:TYJ30359.1, ECO:0000313|Proteomes:UP000323597};
RN   [1] {ECO:0000313|EMBL:TYJ30359.1, ECO:0000313|Proteomes:UP000323597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1408120.09 {ECO:0000313|EMBL:TYJ30359.1};
RA   Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA   Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA   Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA   Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA   Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT   "WGS assembly of Gossypium mustelinum.";
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; CM017641; TYJ30359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5D2YWG0; -.
DR   SMR; A0A5D2YWG0; -.
DR   Proteomes; UP000323597; Chromosome a06.
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: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:UP000323597};
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          196..248
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          145..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..197
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   252 AA;  28395 MW;  18993BC63EC14C84 CRC64;
     MEGMPHPIPR TVEEVFNDFK GRRSGLIKAL TTDVDKFYQQ CDPEKENLCL YGLPNETWEV
     NLPVEEVPPE LPEPALGINF ARDGMQEKDW LSLVAVHSDS WLLAVAFYFG ARFGFGKNER
     KRLFQMINDL PTIFEVVTGN VKQLKDQSAN HNGSSKSKSS AKSRQSEPQG KMVKMSPPSK
     DEDESGEEDE EDDEQGATCG ACGDSYGTDE FWICCDICER WFHGKCVKIT PAKAEHIKQY
     KCPSCSSKRA RV
//
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