ID A0A1C7M7D8_GRIFR Unreviewed; 1139 AA.
AC A0A1C7M7D8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=Kat7 {ECO:0000313|EMBL:OBZ72296.1};
GN ORFNames=A0H81_07717 {ECO:0000313|EMBL:OBZ72296.1};
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ72296.1, ECO:0000313|Proteomes:UP000092993};
RN [1] {ECO:0000313|EMBL:OBZ72296.1, ECO:0000313|Proteomes:UP000092993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9006-11 {ECO:0000313|EMBL:OBZ72296.1,
RC ECO:0000313|Proteomes:UP000092993};
RA Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT "Whole genome sequencing of Grifola frondosa 9006-11.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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:OBZ72296.1}.
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DR EMBL; LUGG01000009; OBZ72296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7M7D8; -.
DR STRING; 5627.A0A1C7M7D8; -.
DR OMA; FDIETWY; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000092993; Unassembled WGS sequence.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15526; PHD1_MOZ_d4; 1.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
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; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092993};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OBZ72296.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 100..158
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 155..205
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 453..750
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 71..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..972
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1139
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 631
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1139 AA; 126200 MW; 41F03B9A8F24DDC4 CRC64;
MRCSRCAAGH GPLIIFMVSE YLNTEFRAPY CTHRTASSKC CPTADFLPAT KSYAAAFASI
FPRTQGDPFA EPPPAYLPVE EPAPPPTKPL KRKRRPPPRE EECGFCHGDD TKNKTGVPEL
LVSCAECGRS GHPSCMQLPG LGDMMRSYPW KCAECKSCEV CQQKRDDSTM LICDFCDRGW
HMACLRPPLL EPPDGQWHCP ICPPFPPPSQ LEIATEPYFS EVMLQSPSLP QIPPRESSVA
SSSRIIQEQD ESQQHIAVSE NSDMDVDGTD LSPGKKRKSK KKSRWKGKEP MRDIPEEVED
PLSSSLPSKR MRIRLSSPVP PPDSSPAPLP KTVIRFRIPA RGKGKARDDG QEDGERSIFE
DILGTEDRDV TSTLITNGDK QRFERCRLAA EGKIFPPPAP ATPQVLDTTV AGPSSRPLRS
AAHHHPPPAA NPIPAFSTSP APSTPDPQNA ASPNGLRIRR IRFGEFDIET WYDAPFPEEY
ANIPDGRLWI CEFCLKYMKS RFSAGRHQMK CKTRHPPGDE IYRDGVISIF EVDGRKNKIY
CQNLCLLSKM FLDHKSLFYD VEPFLFYVMT EVDESGARFV GYFSKEKLSP KYYNVSCIMT
LPVRQRQGWG NLLIDFSYLL SKKEQRAGSP EKPLSALGAL GYKNYWTLSL MRYLHSAPPN
PRLEDISAAT SLTIEDIHTT LTQLRMIAIE DTTPLRGRFL GKPSSSQRDG RMALHASICS
WDPEDVAQYL AKWETKGYLK LKPEKLKWSP FIVARTKRME QLLSTDAAAN AADGEANGRT
TESAADPQTS RPEPALETAE SAGSPVCALF DDDNVEIVSA TAQAPSIVLP QTPQVRSPSA
EPEEQAQAEK GRTLAKKLAR SSPTSSRHLR NRGKSATPQP PRVEYLHEER PVNGDRRKST
HRMRSNAQVN GHNDSDSIAQ DAALAAKLAL EEGRPRRQLR SRSNTEQDTK RPISSPRSAS
PRKRRRGSRP LPKLNRAKST PSKVQRRSSR VANGSAVANN ISRPAAQVVR GGSAPRMRNL
HEKGEAAEIM ESEPPDEAER EHERPADPPT EDMKYEDADT PLTGLTSRHS APSDDTVIAL
EGITMKVSPV GPVNVAEVEP PPTEQDRALN DSGLDEGGDE DAEGEEDVDA EGEPDLETL
//
