ID A0A225AFJ3_9EURO Unreviewed; 1107 AA.
AC A0A225AFJ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=UA08_04716 {ECO:0000313|EMBL:OKL60091.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL60091.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL60091.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL60091.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) 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:OKL60091.1}.
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DR EMBL; LFMY01000006; OKL60091.1; -; Genomic_DNA.
DR RefSeq; XP_020120212.1; XM_020267017.1.
DR AlphaFoldDB; A0A225AFJ3; -.
DR STRING; 1441469.A0A225AFJ3; -.
DR GeneID; 31004471; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000214365; 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:UP000214365};
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 162..221
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 476..750
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..968
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 652
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1107 AA; 122037 MW; 2958BF540F53D60A CRC64;
MAAVMTAPHD ELGVNPQTDL LDSDQDAEGE EDTDLYQLDQ ELQSAVQKAD AGHAAEDDEA
TAESDFAEEI RSGDESAEDA ASRDDENDEE FEGSRRLRRG RRGAVFSKSD DEESDPDVAF
ENGLDAHSGS DSNSNVSDAE PEDWDAESNG KEDEHDGEKI SRGNCIFCGQ DEDHDPSEDF
EEYLTCAVCG DHSHRQCARE QSAFSDTEDA ESWRCVTCVQ NNFEPDPGED SAALRRSTAQ
NIARDLLAAS TGTQGPSSHS IFTNLIVDDD PMDGTRSLRK RKISSADPDE HVPVLRKRQR
RTPSQGATDS ADGSFDTDGL PRTRPRRKRK SDKKLCRVVE SDIGKCVIAL HLNFVKMAKI
LNSRPRPLKA RRRRQQPKPP PIEDEPLTHF APIVPAYTTA PFYSFHDREV DELKSKPYGG
ILSEADADTS RTLPTQADRE KFESARRKAE EDWQRKVMES EPIGEVNHRA SQKVSGPPSK
IKWINFGGYE IETWYAAPYP EEYSRNKVLY ICEFCLKYMN SDFVAWRHKL KCPAKHPPGD
EIYRDGSVSI YEVDGRKNPV YCQNLCLLAK LFLGSKTLYY DVEPFLFYVM TEFDELGCHF
VGYFSKEKRP SSSNNVSCIL TLPIHQRKGY GNLLIDFSYL LTRVEKKTGS PEKPLSDMGL
VSYRNYWRLV LSYQLRNQKT PVSIAELSDR TGITADDIVS GLEGLRALVR DPVTKTYALR
LNYPYFEEYI QNWEAKGYVK LNPNALVWTP YIMGRSNQSH YDRAQLHTVA PREDLNDEDD
MDTDEVGAMH IDGNGSAKTN GDLASKGGIS SYAPAGPPTT AFSSFGEEST SLSQTNGDTG
AVDPAANIPP TRFEIYPPVQ PPVFKRRPGR PWGSKTNYNR TSYNTTPRGP RSAPRRTSTS
MFGIGSQASA GADAVSSARR SRSGLASELL PGAESLSVSM GMNSNHDYDP DNDEPTLPDA
DEEEGEQIEG FTNGTSISES AMPESNHALS PLPADADADA DADAEVETNQ SGTNGIDVPT
DPNSNNESIT ATAVSNNVTA TSTNSTGNLT PRRTRRSAAD EEKKTIKLSS TTRASINGNG
TATANASANG DSDVDADGEV DEDVQMS
//
