ID Q8WZU5_NEUCS Unreviewed; 823 AA.
AC Q8WZU5;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Chromatin modification-related protein {ECO:0000256|RuleBase:RU361213};
GN Name=B8J24.070 {ECO:0000313|EMBL:CAD21110.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAD21110.1};
RN [1] {ECO:0000313|EMBL:CAD21110.1}
RP NUCLEOTIDE SEQUENCE.
RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA Nyakatura G., Mewes H.W., Mannhaupt G.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAD21110.1}
RP NUCLEOTIDE SEQUENCE.
RA German Neurospora genome project;
RL Submitted (JAN-2002) 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}.
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DR EMBL; AL669990; CAD21110.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WZU5; -.
DR VEuPathDB; FungiDB:NCU03461; -.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
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; cd17016; ING_Pho23p_like; 1.
DR CDD; cd15505; PHD_ING; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR628651-51};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361213};
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 766..817
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 769
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 771
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 782
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 787
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 793
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 796
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT SITE 768
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 779
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 783
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 791
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
SQ SEQUENCE 823 AA; 86812 MW; 9F3B443EEB064C5E CRC64;
MKTAKPPAAE APSGPSGSNR RAQPVRQTRI NPPRTSSLNR TNSFPNGPTP EQPIDIFPAV
THFTDAITAL PKELVRHFTL LKEVDAKIFA PEATLFELVD AALKAPVPDR TRSVTDGNNS
VAPASTPMSA QNSTSGRVAS NANPATVPPS ITDSAHAAVF DPTNLPRRHL FRQAAWKIQE
MLVSLEEKNH VISTANDALH KQLSRIEEIW PHLENEFSDE AKWGSTTHWA YAENRVPKTN
HKEAERSRRE GAATLSAAAQ QIAEEAAARS SDRKQALAAK KNNKGQATEP EADSKAQETT
KKGPGTGKSR KHQAEATPVG LGIANGTPTN GTGPSKRRKV EKEPKANGSA PMERAMSSVF
GNGTAKSKTT ASPRGSPAPD GATPTGPTTK KRKALPSGST QAKKRTNAAN SPSVAASPLL
GSLPDTKAGR NSPVPLPPRP ASSRARGNST ASTTLPIQQR PATATTNKPN GITPAVAEAV
PQSKSTSDAK APKEADPPAP TPAKTEAAKP ETEIKPPVPP EPVANASTSK KENSKAVTAP
AEEPETKKRT NSIVSQTAIL PPPISTTVTT TKSGRASKPS TPATGTFAEA ANATTTTARS
RPSRNSTNQS DKDSNSTSGK DTFGNSTTTT SGTTTSKRSH KKGASSVSAV AVSVALQDEK
PGKSAAASDE KKDAASDENS GRPTTSGRGK GSAAAHRDSK AERGSERDRG GERDTKTETN
HGHGHGRRGT ATAAAARAQQ QQPQHQQRQE EEDDDDDDDD VDADEQRYCF CNGISYGEMV
ACDGDGCPRE WFHLECVGLK VAPKGNAKWY CEDCKKRLRA SGR
//
