ID A0A094CDR2_9PEZI Unreviewed; 910 AA.
AC A0A094CDR2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN ORFNames=V496_09660 {ECO:0000313|EMBL:KFY50003.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY50003.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY50003.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY50003.1}.
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DR EMBL; JPJY01001889; KFY50003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CDR2; -.
DR STRING; 1420909.A0A094CDR2; -.
DR HOGENOM; CLU_005327_1_0_1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000029302; 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 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; PF16866; PHD_4; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 179..238
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 497..774
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 673
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
FT NON_TER 910
FT /evidence="ECO:0000313|EMBL:KFY50003.1"
SQ SEQUENCE 910 AA; 101272 MW; D4641528FF4B3DD5 CRC64;
MPTSEDDAEY EEDYDQDVDM GANAEAFAAN NQLLNGVHQN HTEGSGYGEN GDENDEEEDE
EQRQDHEEDD LSDRDAEGED DYEQDHGDTI RISMAGDGTV DEEENEDDED GEGVGAVKIQ
PRDLEEDDGD AAFGQDDEEE SEDAADDASN GSSDESEVEA EAEWEAAVAQ DDEAEPIDPN
RCIFCHQDEE HDPSPEFEEY LACAVCGDNA HRQCARDSEA LEADEDAAKW RCPGCVSNAL
EPETVNQETP SRGAIKPDSH SVFNNLIVDD DPMDGSRLLR KRKTSSAEAE EGVLSSVGKR
RKRASDGSSN AIITDAEPAE NIDSHIVEPA ELFNDENKAA EPANSRPSRS LRPLKVSKPP
VAIEKHTRTS LIIRFRVNAA DLARVLANPP KPVKKRPRST AIARRASTSA PPPAYVPRIY
SQPFYSFHDK DMDELKSKPY GGILTEAQSD TSKTLPQADD RRMFDNARQK AEEEWALKTA
LEHAEAENVK KPRKVSGPAS QIECINFGGY EIDTWYAAPY PEEYSRNRVL HICEFCLKYM
NSEYVAWRHK MKCSAKHPPG DEIYREASIS VFEVDGRKNP VYCQNLCLLA KLFLGSKTLY
YDVEPFLFYV MTEYDEFGCH FVGYFSKEKR PSSQNNVSCI LTLPIHQRKG YGNLLIDFSY
LLTLVERKSG SPEKPLSDMG LVSYRNYWRL VLCYRLLDTK EEKKSISVVE LSEQTGMTAD
DIVSALEGLR ALVRDPVTGT YALRLDYDFY EEYIKKWEDK NYVRLNPHGL VWTPYIMGRN
NQNMIEHAPP MSAIAPREDE DEDDENPADS TQPALTNGDI PSEQTNGLTN GASFAASDAE
GQSVEPGDEM VLDPSLAGTS GKGPRPATDT TPTPASPPSS RPSLQPLANG GPHPDYPLTI
NTDNDFSPIP
//
