ID A0A074WP41_9PEZI Unreviewed; 767 AA.
AC A0A074WP41;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN ORFNames=M436DRAFT_46528 {ECO:0000313|EMBL:KEQ73364.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ73364.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ73364.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ73364.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; KL584709; KEQ73364.1; -; Genomic_DNA.
DR RefSeq; XP_013427526.1; XM_013572072.1.
DR AlphaFoldDB; A0A074WP41; -.
DR STRING; 1043004.A0A074WP41; -.
DR GeneID; 25410542; -.
DR HOGENOM; CLU_005327_1_2_1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000027730; 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:UP000027730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 127..188
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 484..756
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 677
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
FT NON_TER 767
FT /evidence="ECO:0000313|EMBL:KEQ73364.1"
SQ SEQUENCE 767 AA; 86368 MW; CF700E05F2CBECBE CRC64;
MRSSSIDAEG EEDDLDMPET QSPSLQNDAP EDQDDDEDEE DDEEDEDADA DQDDDDSEIV
GAVKRAPTRT RTLRARKSRD MESSEDDDSA SDGENDSDSS DESAATQAPW EKESDTAQEQ
DQDVVTDSIC VYCGQDEEND PSDEYEEYLE CGHCGDHAHK QCARNANSLS SDQDKNPRTW
MCHDCVGNGF ELQQDVDKMT INDGSQRRSS VPKLARDLLP AVRGGIKPNS HSVFNNLILD
DDPMDGSRSL RKRRISSVEA DESTQRATSR KRRRSTASES QTNINVTPRD AVKEQNTSTR
SSGSAESEKS SNTRANRLRK QPQSGTNARI VSAETYDDQP KSLVVAIPIS AAALENIERN
AQRKARRRER DRARRALMGG RKKKSGAQGD VSEVVETTSS HYPAVATTLY DNPYYPFPDR
ELDTVQGKPF GGILTDAEAD TTKTFPQQAD RDLFEESRRQ ADEARKAEQE ANPIELPSRS
KQSGLPTKIK YIHFGGWEIE TLHAAPYPEE YNRNPILCIC EFCLKYMSSS YVAFRHKLKC
PHKHPPGDEI YRDDIIDADG NKKSISFFEV DGRRSPLYCQ NLCLLAKLFL GSKTLYYDVE
PFLFYVMTEN DEFGCHFVGY FSKEKRDWAG ANSIDPPGNN VSCILVFPVH QRHGFGRTLI
EFSYLLTRVE GRTGSPEKPL SDLGLVSYRS YWRGVMCRLL LGYKEAPRGS YDISFLSMAR
ATGMTIDDVV SSLEALRAIV KDPVTNKYAL RCDWAYMAEY LEKHDKK
//
