ID K7VSQ7_PHAVU Unreviewed; 240 AA.
AC K7VSQ7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=PHD finger protein ALFIN-LIKE {ECO:0000256|RuleBase:RU369089};
GN ORFNames=PHAVU_008G103200g {ECO:0000313|EMBL:ESW12323.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:AFW90529.1};
RN [1] {ECO:0000313|EMBL:AFW90529.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pod {ECO:0000313|EMBL:AFW90529.1};
RA Amelia K., Bhore S.J., Shah F.H.;
RT "Phaseolus vulgaris (BAT93) Pods Tissue cDNA Library Construction and
RT Random Isolation of cDNA Clones for Gene Discovery.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESW12323.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; JX869964; AFW90529.1; -; mRNA.
DR EMBL; CM002295; ESW12323.1; -; Genomic_DNA.
DR RefSeq; XP_007140329.1; XM_007140267.1.
DR AlphaFoldDB; K7VSQ7; -.
DR STRING; 3885.K7VSQ7; -.
DR EnsemblPlants; ESW12323; ESW12323; PHAVU_008G103200g.
DR GeneID; 18622443; -.
DR Gramene; ESW12323; ESW12323; PHAVU_008G103200g.
DR KEGG; pvu:PHAVU_008G103200g; -.
DR eggNOG; KOG1632; Eukaryota.
DR OMA; CTLKRSR; -.
DR OrthoDB; 313735at2759; -.
DR Proteomes; UP000000226; Chromosome 8.
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: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 2: Evidence at transcript level;
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:UP000000226};
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 184..236
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 140..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 240 AA; 27127 MW; FED32CEDA559F40D CRC64;
MDMASSPRTV EEIFKDYSAR RTAVIRALTH DVDEFYGLCD PDKDNLCLYG HPNEAWEVTL
PAEEVPPELP EPALGINFAR DGMNRRDWLS LVAVHSDSWL VSVAFYLGAR LNRNERKRLF
SLINDLPSVF EVVTERKPVK DKPTVDSGSK SRGSTKRAND GQVKSTPKFA ADEGYEEDED
EHNETLCGSC GGNYNADEFW ICCDICERWF HGKCVKITPA KAESIKQYKC PSCSLRRGRP
//
