ID A0A168D5Y1_9HYPO Unreviewed; 1072 AA.
AC A0A168D5Y1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=AAL_03357 {ECO:0000313|EMBL:KZZ97393.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ97393.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ97393.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ97393.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ97393.1}.
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DR EMBL; AZGY01000006; KZZ97393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168D5Y1; -.
DR STRING; 1081109.A0A168D5Y1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000078544; 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 Acyltransferase {ECO:0000313|EMBL:KZZ97393.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZZ97393.1}.
FT DOMAIN 467..748
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..173
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 643
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1072 AA; 114958 MW; ED575E2525806420 CRC64;
MTSAQAMEEE LQQSVLLSEE GAYDGGVIDE QSGATESQTP VKDGLSESQS DGEELSDRDA
SGEDLDEDAS GEEDDEMLDH QIVVGTTHAA DTGPSDEDGE GEDDADEGVG AVKVRPAGSE
SDDVDSDVSD AASAEEDEES DGDEEAAWEE GDAGDEEEEG DSDSDEDADD AEGSVDGSSS
TSHPSQRRKF ADDSVLAELA NGDADDHMDA DDSGLESSST IHSRPARKRK AVSAEPDDDL
PAVRKRRRNQ SNDTSDGGRS TRDSRSAEPS RGASSRSARL KSARPPPVTV EKRSRTSLVL
KIDVRPGNLK EILSRRKRDR RRAGGSGGGG DGDGDGDGDG DGDGDGDGDG DGGSSVRVQP
ARPAPARPPA AIVPAMMSTM PTPFTSESYS QPFYSFFDKE TDEMKGKPYG GILTETEADT
SKTLPSSDDR KKFEQAKQKA EDEWRSRVLA MQAEADLPIR KPKKASDNAS QIECIEFGGW
EIDTWYAAPY PAEYSRNRAL YICEFCLKYM NSDYVAWRHK LKCGTKHPPG DEIYRHESIS
IFEVDGRKHP VYCQNLCLLA KLFLGSKTLY YDVEPFLFYV LCEFDQTGYH FVGYFSKEKR
ASSQNNVSCI LTLPIHQRKG YGNLLIDFSY LLTKVERKTG SPEKPLSDMG LVSYRNYWRL
ELCRYFLNHM KGDRHVKEGL SIKKISDDTG MTADDVVSAL EGLRALVRDP QTQLYAFRVD
VDYCRHYVAK WESKGYYTLK PSALAWTPYV MGRSNVVNFE LGHAINTIAP REDDEVKVQE
GHARADGDAP AAKNGTDAGE GGQPSTDNPP GGAANSTSSS SGGGGGSERA VAPVKSIEKV
AAEDKENAEP DDGSMEDATP VAPRTAAEDD GEQGQEEREE EEEEGRAWVV PSSARRSTTT
TASRPKPTSS SARRKSGGTG RGPGRWPKGT KKSDYGNADS GPGLPPGWKE RQARLQGLAS
NDGTASQTTP ASAPAPAPAS APAPSTAAPA APAVKIPVPA EEEPAQDEVR VSMPPAPTAH
QKKAVNGNDD DDSDDDEGGS ASGSESDEQE ASASASASVS NADDVDAEGE DS
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