ID J4KPS1_BEAB2 Unreviewed; 1043 AA.
AC J4KPS1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=BBA_02840 {ECO:0000313|EMBL:EJP67944.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP67944.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP67944.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP67944.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; JH725155; EJP67944.1; -; Genomic_DNA.
DR RefSeq; XP_008596159.1; XM_008597937.1.
DR AlphaFoldDB; J4KPS1; -.
DR STRING; 655819.J4KPS1; -.
DR GeneID; 19885852; -.
DR HOGENOM; CLU_005327_1_2_1; -.
DR InParanoid; J4KPS1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000002762; 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:UP000002762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJP67944.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 166..225
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 464..745
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1006
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1043
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 640
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1043 AA; 116661 MW; B0BE8D6EBA80456F CRC64;
MASAQDMEEQ LQQSVMISED GAFESSSSGL GTANTISPNG DEEMSDRDAS GEEIEEGDED
AEGEEDNDLI QQQINAGHQS IVASAKPPSD DDDEVEGEDE EEEEEREESD DDDGVDLVKI
RPDSDGEGDS EASTHESEAE EDEGAAAWED EANEEDEEDE SAESPSNACI FCKQDEENDP
SEDFEAYLSC KRCGDHSHQQ CAREAAAMTE DNAAQNWKCP ECVDKSSDEE DDAEVGSVAA
SDAKGSQASD GTGTGTRAGR KRKSSPLQDE DEDDVITVRK RRRNISVDAN SAQDGIEGNE
PMRNRTARQK STRQSLVSVE KRSRHSLIMK FQVRPGNLKE FLSRRRRDRK RPSTTRPVRP
IIQQASSAGF DVPISAMPTP FSSDVYSQPF YSFFDKETDE VKGKPYGGIL TEAEADTSKT
FPTSDDRKRF DKAKQQAEDE WRARVLAMQA EQDMPVRRHK KNSEHASQIE CIEFGGWEIE
TWYAAPYPAE YSRNRVLYIC EFCLKYMNSD YVAWRHKLKC GTKHPPGDEI YRHDSISVFE
VDGRKHPVYC QNLCLLAKLF LGSKTLYYDV EPFLFYVLCE YDDCGYHFVG YFSKEKRASS
QNNVSCILTL PIHQRKGYGN LLIDFSYLLT RVEQKTGSPE KPLSDMGLVS YRNYWRLRLC
RYFLDIVESG EFKTNGLSIK KMSDDTGMTP DDVISALEGL RALVRDPETK LYAFRIDLEY
CRNYWEKWDS KGYVRLKSEA LVWTPYVMGR SNAVNFEFGP PINAIAPRED DEAKILEGPN
RVGTDKLRQT NGDDAHSTAD QSEPDPGPTA SIEKAESEEK PIKSEDEVMK DADEPSVQTW
DAAYKDIPAT RFEVFPAVGG ARRDRNRRRS STNNGVPRKR GRPPLSRVRS TSSRRKGGGT
GRGPGRYPKG TRKSDYGNAN SGPGLPPGWR SVTADAKANG DEAGAAIEEE SAQDEVQVQL
LTSNEGAAAA AEEESGADQE DEEEAQEAED DEEEEEEEEE DGERESEGRD DVAREVEAEA
EAEEDEDQEA QEEVDVDASG EEE
//
