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Database: UniProt
Entry: E9DWC5_METAQ
LinkDB: E9DWC5_METAQ
Original site: E9DWC5_METAQ 
ID   E9DWC5_METAQ            Unreviewed;       718 AA.
AC   E9DWC5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=MAC_01923 {ECO:0000313|EMBL:EFY91975.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY91975.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY91975.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC       {ECO:0000256|ARBA:ARBA00010107}.
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DR   EMBL; GL698478; EFY91975.1; -; Genomic_DNA.
DR   RefSeq; XP_007808263.1; XM_007810072.1.
DR   AlphaFoldDB; E9DWC5; -.
DR   STRING; 655827.E9DWC5; -.
DR   GeneID; 19246234; -.
DR   KEGG; maw:MAC_01923; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_0_0_1; -.
DR   InParanoid; E9DWC5; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
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   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF180; HISTONE ACETYLTRANSFERASE SAS2; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
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   Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFY91975.1}.
FT   DOMAIN          270..636
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          1..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..182
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..265
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..639
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        530
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   718 AA;  77427 MW;  9CAD45E79BC4B350 CRC64;
     MPQKRRRLEE PAQPALAEQS SSLRRTTRQT PVLPPLPPTS AAVAKVAQAP AVADPTAMAT
     TTVTATASAS APAPATATGA NGPGSAVSGR PQLQPTGPAT TASTATTTTV SNAIATSQTP
     VPIPTPLGSG QQPNRSRERP QSTIPPPPFP PTYSPPVKTP VPVPVVTPIS PPSIPRRPLP
     SLGSNPPAGR SMSAVSVTDN ARPSDLVAPE ISYHVPQPAV PGRVQSSLLR PHGPSALPPR
     LDRRPAPPVV TPVPPPKPPT LPVNDRGPPR ADRNIDKVVL GDLCFRTWYP SYYGKEILGD
     TSGNSRNGGG SKDGSNEASS KASKRDKDNQ PMLERLYVCP SCFKYAKELV AWRGHVRVCE
     RKAFIPGKKI YRHPRGRRKV LVAFEGKGPG PKRRRGDSGI RYTEEIVHDE GEWSIWEVDG
     EKHGLFCQNL SLFAKLFLDN KSVFFDVTGF NYFLLVYTPP ASPVAPETEP IQTRPPQVCG
     FFSKEKMSWD NNNLACILVF PPWQRKGLGA LLMGASYEIS RREGILGGPE KPISDLGKKG
     YKRFWSGEIA RWLLSLESTA PQPQPQSPQV AGGPVITQEL IVDVNDCSRD TWIAAEDCLG
     VLRDMGVLED AGMGFGKPEK KADAAAEEDE SRELLPEGGD GAAHKQQDLV SRSAEEKRSL
     SVKVVPRVRI DKEVVRRYVA THRISLERTC DPDGFVQGYA MKVDSSGNDG DKTGVETA
//
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