ID A0A2A9M7Y7_9APIC Unreviewed; 475 AA.
AC A0A2A9M7Y7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Inhibitor of growth protein {ECO:0000256|RuleBase:RU361213};
GN ORFNames=BESB_022750 {ECO:0000313|EMBL:PFH31783.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH31783.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH31783.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH31783.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of an histone acetyltransferase complex.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SUBUNIT: Component of an histone acetyltransferase complex. Interacts
CC with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU361213}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000256|ARBA:ARBA00010210,
CC ECO:0000256|RuleBase:RU361213}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFH31783.1}.
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DR EMBL; NWUJ01000013; PFH31783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9M7Y7; -.
DR STRING; 94643.A0A2A9M7Y7; -.
DR VEuPathDB; ToxoDB:BESB_022750; -.
DR OrthoDB; 217724at2759; -.
DR Proteomes; UP000224006; Chromosome xii.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd16857; ING_ING1_2; 1.
DR CDD; cd15522; PHD_TAF3; 1.
DR Gene3D; 6.10.140.1740; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028651; ING_fam.
DR InterPro; IPR024610; ING_N_histone-binding.
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; PTHR10333; INHIBITOR OF GROWTH PROTEIN; 1.
DR PANTHER; PTHR10333:SF42; INHIBITOR OF GROWTH PROTEIN 3; 1.
DR Pfam; PF12998; ING; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM01408; ING; 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:RU361213};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361213};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361213};
KW Reference proteome {ECO:0000313|Proteomes:UP000224006};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361213};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 419..471
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 148..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..46
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 253..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 47407 MW; C72E3CCB5CF158AD CRC64;
MGDPVEQWLE DCLTLPGKLH RALRLMAHLE QEASRIETQF RSREKEFLLR LRQSQQQGTA
WPAAEQEEEI VAIKFLHAKC RALLREKVAV NKQIASFIHY EQQRLVKERD KLLHSMHGLG
AAATLKAHGV AGQELGAVTA AGPGGVPGGH LPGVGAPSAV GGTPGAGPLG ATGTHGGTGS
AGGSTVGRSA LRRRAAERGG SSILGTAGDV SSGLPGDGAG ADRGGGAGLG LDADGSGFYV
RGADRTALNG DYQAHQDQGA SASRHPSSQS STVTAGPQGA GGPPHAASGA DARGQAGLAV
PAAPAGVHHP SGSKSSGGGR SRNQPSHGSR SRHDGSGSKG GAAAGPLASS GSASPAPSYG
SGHRMGASPG AYYPPGGGSA DPAGHAGGGA SSGSGAGVPG GAGATTRSGG QSESADAWEG
ICPVCHKGES SECNNMVACD ACNQWFHFEC VGYSAETQED DAWFCPQCYQ HGLVP
//
