ID A0A0F0IDX1_ASPPU Unreviewed; 1082 AA.
AC A0A0F0IDX1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=P875_00010375 {ECO:0000313|EMBL:KJK65371.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK65371.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK65371.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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:KJK65371.1}.
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DR EMBL; JZEE01000366; KJK65371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IDX1; -.
DR STRING; 1403190.A0A0F0IDX1; -.
DR Proteomes; UP000033540; 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:UP000033540};
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 162..221
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 479..753
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 655
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1082 AA; 120145 MW; 1776E95F04CE906C CRC64;
MAATAPPADD DTEMRLPPDL VDSDQDAEGE EETDLYQMDQ QLQDAVHRAY SGEVAEESNS
ASREDDKDAE GEPDSDLDSN GENDETEPVG AVKLPKGKSS LDNEDAADAE GDAAFENQSD
SDQDASGSSS SSRGSDEEDD DEEWDGESND HDDAEVDNNT VRGNCIFCGQ DEDHDPSEDF
EEYLTCTVCG DHSHRQCARE QSALNDAEDA STWRCPTCVR EKLEPNAEGN NSSHRRLGSK
NMRKELLPAH TGEEGSGFHS IFNTVDIDDD NLLNSSRSLR KRKTLSADVQ EHTPVLRKRQ
RQTSLRSERA ESRDHLGDAS DALSPVRTRS RRVRGGEKEN CRVVLRQFGR LVLAFQLNET
KLSKILSSRS RSQQRGRRTP KPPPVAHEPP AHFAPIVPVS YVSPFYSFND REMDESKSKP
YGGILSEADA DTTKTLPTQP DRERFEVARQ KAEEEWQRRV MEAESGGEPV QHAAQKVSGP
PSRIKYINFG GYEIETWYAA PYPEEYSRNR VLYICEFCLK YMNSDYVAWR HKLKCPAKHP
PGDEIYRDGS ISIFEVDGRK NPVYCQNLCL LAKLFLGSKT LYYDVEPFLF YIMTEFDDLG
CHFVGYFSKE KRPSSANNVS CILTLPIHQR KGYGNLLIDF SYLLTRIEGK TGSPEKPLSD
MGLVSYRNYW RLILSYQLHK QKAPLSIVEL SERTGMTADD IVSGLEALRA LVRDPVTKTY
ALRLDYKYFE ECIQSWESKG YVQLNPDALV WTPYIMGRSN QSQFDRAPLH AVAPREGLED
EEVEDVKDSG NEEEQQLSEN LGKVNGDDNP QPTINGVAQA VSGELSAEPA GPPSTELLTN
GAGLHRTQLA ADSNPTEANT VQDIPAWRFE VYPPVQAPVV KRRPGRPFGS KTTYNKVAVT
PTTARTSGRN TPRRSSALAS MTPTANAYSV RRGRSAKLLD SPAVESTGTE ANGVENDDQL
PDHEDDKGGE QDPAQPDGLS ETDVQNNHKG DHDAPSQLNG INGVETVGTE LHVTEQVTPT
KEVSAENTAK LTRSVNRKAV VEKLEFVIPA EDHGTTNHNA VVEEHTDGPN GVDKDGDAIM
ET
//
