ID R9ASE5_WALI9 Unreviewed; 1017 AA.
AC R9ASE5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-NOV-2023, entry version 54.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=J056_000338 {ECO:0000313|EMBL:EOR04975.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR04975.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; KE007224; EOR04975.1; -; Genomic_DNA.
DR RefSeq; XP_009266011.1; XM_009267736.1.
DR AlphaFoldDB; R9ASE5; -.
DR STRING; 1299270.R9ASE5; -.
DR GeneID; 20373290; -.
DR KEGG; wic:J056_000338; -.
DR eggNOG; KOG1244; Eukaryota.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_011557_0_0_1; -.
DR OMA; PEHESEM; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000014064; 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 CDD; cd15526; PHD1_MOZ_d4; 1.
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; PF00628; PHD; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 2.
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; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EOR04975.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 158..218
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 215..265
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 635..953
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 23..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 813
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1017 AA; 115828 MW; 84599810E0353EB8 CRC64;
MNNDDNSDYW AYIAGIRDLG VGGSTSTHPT QHITQSSTSK QDNSESDASG EDDVELDLDL
DLDYTRVTQQ PAHLAHPHHP PTQMSHNDVE SRNQRESRIR SDLTTASASY INETLNQRTK
RDKQGSNPKR DAGSSGDADN GVDNAGNNRN TSTNSGHSLR CAYCLGDYAY NNKTQRQEAM
VTCARCASSA HPTCLHFTPT LTQNAQAYDW CCVDCKGCEV CRHKGNEDDI IFCDLCDRGW
HMHCLSPAIT QPPPGDFACP VCRGVSYQQR VEEEEDKRRE EEKEKDKEKE TLIAQSTSPT
NTNHTTKHTT TNPSLPHHTS QSPLALQLQM QLQNPTLAPT FQPPPPMHDN QPTPRQSATI
LNASKAMLMG RQTLPHSLLP QTPDLSTVVP TETPLKRGRG RPPKKVQDGP LGTPHLFKDK
PDKPKNPVGR PPGPRASLSA PKRINTFVVI DNDEDKLVEK EKKERDEREE KEKEEKIDMG
KKKHAENMQV DGQPHKQEHR QSPYPETRDD SGQQPMEGVD TAESAAPSAP VEQSYREMQQ
LQQISQKTLQ QPPHPHHINS EDKENEHDTE DNDPFGGVLK PDEAQVLHTT PHAEEKNKFE
ITRRRAEIEL QQKAKRPAQV LQTVPSTSHT DEHKSKSQPI KSLLFGDYEI QTWYAAPYPE
EYTNLPNGRM YLCEWCLSYR KSEFQMKRHH RKCKYHSPPG DEIYRSGNVK IFEVDGRKNR
IYCQNLCLLA KMFLDHKTLY YDVEPFLFYV ITQHTPLGEE FVGYFSKEKR SGMGYNLSCI
MTLPIRQRKG WGMFAIDFSY LLSRKEDKIG TPERPLSKLG LLSYKRYWTT AIYKALLNTP
EPHTLGQLSD VTGMTIPDVT YTLRLNHLIH GVNTGDGENH YVNESNTYRT RTNKPVLEEH
PERVKNDDPT SVPVPPPNSY RISFNRNTLE AYLAKDAIKG YVRLDKDQLR WQPFITHHTQ
LFKSDDKEKK VDEEGKKESS DNVEQRIAQQ TDQQIEEHND EPSSQQTQPP QDTPMTC
//
