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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//