ID T1GQQ8_MEGSC Unreviewed; 399 AA.
AC T1GQQ8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Inhibitor of growth protein {ECO:0000256|RuleBase:RU361213};
OS Megaselia scalaris (Humpbacked fly) (Phora scalaris).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC Phoridae; Megaseliini; Megaselia.
OX NCBI_TaxID=36166 {ECO:0000313|EnsemblMetazoa:MESCA005971-PA, ECO:0000313|Proteomes:UP000015102};
RN [1] {ECO:0000313|Proteomes:UP000015102}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Durham, NC isolate 2 -- Noor lab
RC {ECO:0000313|Proteomes:UP000015102};
RA Hughes D.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:MESCA005971-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR EMBL; CAQQ02065370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1GQQ8; -.
DR STRING; 36166.T1GQQ8; -.
DR EnsemblMetazoa; MESCA005971-RA; MESCA005971-PA; MESCA005971.
DR HOGENOM; CLU_031900_0_0_1; -.
DR OMA; YEWFHWK; -.
DR Proteomes; UP000015102; Unassembled WGS sequence.
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; cd16858; ING_ING3_Yng2p; 1.
DR CDD; cd15585; PHD_ING3; 1.
DR Gene3D; 6.10.140.1740; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042020; ING3_PHD.
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; 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 Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR628651-51};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361213};
KW Reference proteome {ECO:0000313|Proteomes:UP000015102};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR628651-51};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 342..391
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 109..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT SITE 344
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 355
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 359
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 367
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
SQ SEQUENCE 399 AA; 44412 MW; DAC25763C80E8568 CRC64;
MDSLDRRSKH FFSECKRGDL KDQDADNEFQ NLRKDYYKVL EEADEKVALS TQMHELVERY
LRRLDNELFK FKCELEADNN GITEILEKRS LELDGGSSMS HLGTQKENRY FGSIGNNHHQ
SGSSSMSLQQ KEHRYRHRAE KRRDSGSNAV PAQHTSTPNY PTSAPSTPSI VRTASAASTN
ANANHAQPPN VAQNINAPVF NSNIAIAAAA SQAIVATQQM QQGRRTASLK ASYEATMGGA
VNGPHEIIIG RELAGATHNA IQAVERDHQR KKKKIPSIAS NQHPSTSAAA IQQPAPIQTA
NLAIPQVVTN PHIEVVNTRI ENGLVIEQTA DGEEWSYDPN EPRYCICNQV SFGDMVACDN
DTCPLEWFHY SCVGITQPPK GKWYCPKCTQ SMKRRNRKN
//
