ID S8AIP0_DACHA Unreviewed; 1128 AA.
AC S8AIP0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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=H072_3273 {ECO:0000313|EMBL:EPS42754.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS42754.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS42754.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS42754.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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:EPS42754.1}.
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DR EMBL; AQGS01000101; EPS42754.1; -; Genomic_DNA.
DR RefSeq; XP_011109255.1; XM_011110953.1.
DR AlphaFoldDB; S8AIP0; -.
DR STRING; 1284197.S8AIP0; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_005327_1_2_1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000015100; 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; 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 SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51726; MYST_HAT; 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:UP000015100};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 497..771
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..985
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"
SQ SEQUENCE 1128 AA; 123845 MW; 52C971282136E720 CRC64;
MAVTADRSNR KKRKRDTDDE GDESSSSYSS DSDTPDTPVP RGAVTAASSA TDGTSGSESG
SDSGSGSGSG SESGSDSGSG SDSESGSGSE SGSGSETKSR GKSRSRSISV SGDDRGGPGD
SGSDENGSTD DSNSGSSSSS SSDEDSSSGE EVWDGQSDND EAVETSSNTC IFCGGEEDED
PSETYEEPLE CKICSNTAHR QCARNHNGPG KLSSDTEESV LNWRCSTCAG LNFDVADEIG
ERTTPRLKLK LKNTSGNTQI RTSREKGSPS ASTAHDNDPS SRRLRTRHSD EFKTPHEARP
QRQIRRTNYL QLQTTLGLDD AMEGDNDPNA TPIRISSRQR RARFPDGGSG TAIIYKMNQR
PILKLKFKPE KLAYAIATAS SILAQYPKRG QRSSAQPWMT PGQINTFQPP PQVQLSHYSL
AYYESVTDDR DGKPYGGILS EAEYDTSKTL PLAGDKSRFD KARQEADEEK AQREAMLAAA
APTPNRKKQD QSMRASSHAS MIKCVHFGNY QIDTWYAAPY PEEYSRNRNL YLCEFCLKYM
NSEFVQWRHR LKCPHKHPPG DEIYRDGTIS IFEVDGRKQP AYCQNLCLLA KLFLGSKTLY
YDVDQFLFYV MTEYNETGCH FVGYFSKEKR STSSNNVSCI LTLPIHQRKG YGNLLIDFSY
LLTRTEGRLG SPEKPLSDLG LVSYRNYWKL TLCYLLRDFD GSTSVQAMCE QTGMTPDDVI
SALENLHALI RDPITKTYAF RIDRALMQAI IDKWEDKGYV KLNPHALVWV PFVMGRQSFF
YSALPTIAPR EDEPTLEEGI LVDQTVASTP AATSVNTPKD IMDHEDSSSS GKTGDPMDVD
SNGPQRFTMQ KGLRSPPGNN LTPPEDPPSA FKRGTSFIRL GDDPFRRASS TPAKELPTRV
AVDPNYIPPT RFQLVSATQG SGLKKPKFTR SPSAASSTSK TSQPSRVVSA PPGASRAQSV
SDLKTASTRK SHSHSTPQQQ VRKARSSLFE EAREPHNMTI IRQSSRKSTR VSLAPRGLVP
SPAPSREGQI TVITNGGNGG NGGYDSTDQM SDSVKSRLVI VTEPESLEML LIDDTSLQQD
APEIPRVRIF RGKRETLQQH KVYFGSVAFL RGEKPVEDEQ TNIVNQVP
//
