ID F8MWF8_NEUT8 Unreviewed; 1135 AA.
AC F8MWF8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=NEUTE1DRAFT_68475 {ECO:0000313|EMBL:EGO54100.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO54100.1};
RN [1] {ECO:0000313|EMBL:EGO54100.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO54100.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; GL891307; EGO54100.1; -; Genomic_DNA.
DR RefSeq; XP_009854098.1; XM_009855796.1.
DR AlphaFoldDB; F8MWF8; -.
DR GeneID; 20829322; -.
DR KEGG; nte:NEUTE1DRAFT68475; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_68475; -.
DR HOGENOM; CLU_005327_0_0_1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
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 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 PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 526..807
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..128
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 702
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1135 AA; 125451 MW; E7D0DC94BC9A00DC CRC64;
MADEQLRAEE LQQSVMMSEH QAEASTADGD VAMVDQVTIT SEMSNIIAKP EPSEADEDQE
MHDAQEENDH HDEEMGEGDD AEHSDQGSHD GHDDHDHHED SGDEHGEEEE HDGEDPEGFD
EDAEGDEGDS VHSEEHTSQQ HLPSVEEDHD DDEDDDDEGV GAVKIKPGDT DHSESESGEE
EDDHSKTKTT TRPRNSRSIL HVLDVETTCA REANALPSDQ ALDAWKCPNC ASEEGSQTAA
GKNHEPTQVN GTETITHPTT RRASAPKLAR DLLPPQKHTN PDSHSVFNQL VLDEDPMDGS
RVLRKRKTSS VEPPEHIISL RKRRRNTVGT EEEPDESTAG HDEQARPTSA RSLRIKISNP
AAPVNIVKKT RSSILLRMRV DPTKLQQITS QPPKGNSKRS SRSARSGRSG RSGRSGRKTL
GRSGRSRRAA AAADAMEPST APFASTSYTQ PFYSFYDKET DELKGKPYGG ILTDAEADTS
KTLPQPEDRR RFDEAKQMAE EEWRQRLLKM QAEIEAPVKK SKKTAGPASQ IECIEFGGWE
IDTWYAAPYP EEYSRNRVLY ICEFCLKYMN SDYVAWRHKL KCPAKHPPGD EIYRHGSISV
FEVDGRKNPV YCQNLCLLAK LFLGSKTLYY DVEPFLFYVL CEYDQYGYHF VGYFSKEKRA
SSQNNVSCIL TLPIHQRKGY GNLLIDFSYL LTRVEQKTGS PEKPLSDMGL VSYRNYWRLV
MCKYLLEHCS SDPKEKKGLS IKKISDDTGL TPDDVISSLE GLRCLVRDPQ TQLYAFRVDL
PYCREYVAKW EAKKYVQLEP KALTWTPYVM GRSNATNFEL GPALNAIAPR EDDETKPTVE
EGTVLNGDAS QPDGLANQVE KMEIDTSAPT ILESTEPNEL GIIQPEVISP RSVLKTNGLF
PNGSVHGSVH PNDDHDRKAK TEPDADGEDK ENPDDWMAQY EGIPPTRFEV VPPVNTSRRG
AGVDRIRNTV ARLPAVRTNS GSAARPRNPR RTSGVRRVSS AIKPRSSSSS KRKAGGTGRG
PGRWPKGTKK SDYGNAESGP GFPPGWLAKQ KSLDSTTPKK EGEEGMRDTV HVTPTAESAA
GYNMSGSGSG SGSRSANSSG ANGNGEDAGS ADNGDSFNGG GEDEQADITM KDDDN
//
