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Database: UniProt
Entry: C6HIU9_AJECH
LinkDB: C6HIU9_AJECH
Original site: C6HIU9_AJECH 
ID   C6HIU9_AJECH            Unreviewed;      1092 AA.
AC   C6HIU9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=HCDG_05983 {ECO:0000313|EMBL:EER39761.1};
OS   Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=544712 {ECO:0000313|EMBL:EER39761.1, ECO:0000313|Proteomes:UP000002624};
RN   [1] {ECO:0000313|Proteomes:UP000002624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA   Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA   Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain H143.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC       {ECO:0000256|ARBA:ARBA00010107}.
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DR   EMBL; GG692428; EER39761.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6HIU9; -.
DR   STRING; 544712.C6HIU9; -.
DR   VEuPathDB; FungiDB:HCDG_05983; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_005327_1_2_1; -.
DR   OMA; DNAHRQC; -.
DR   Proteomes; UP000002624; 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:UP000002624};
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          183..242
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          506..780
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          1..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1019..1092
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..109
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..142
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..176
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..966
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        971..995
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1041
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1076
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        682
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   1092 AA;  121166 MW;  CD40CF76C8374E31 CRC64;
     MAATVPATYG NTSIDRQPEL VDSDQDAEGD EDDELYPTLT QSATVIPQEN IDPPLTLGNG
     DETIEASERE ENDGVGVGEV HEPETNHTDD VADMDEDEDA DADADADEDT EAIGAVKFPD
     GNAKSDSDDE DDDIDDPDVE FENESSDVKA GSDGESSEES EVDEEWEAES NDGEDADADA
     LNPNNCIVCG QDEEHDPSEE FEEYLSCAVC GDHCHRQCAR ERGTLNSEEA AENWRCPSCV
     KNKLEPDKHE RTPSQRRSGT SNIAIDLLPA HSEALGPESH SIFSSLIVDD DPLDGSRSLR
     KRRASDEGPE GNMVTQKRQK KIPARFEGMI PTPLPRNMKT VQALIEHSTE NNVTSRQSRP
     RRTRKTEKAL CNIVQRQAGK IILSFHLNST KLNRILNSRQ KQISRRRPPK PPPVVESPQI
     PFQPIAPSAY SAPFYAFHDR ENDELKSKPY GGILSEADAD TSRTLPLAAD REKFEAARQK
     AEEEWRQKMA AADQPGESAP RAKISGPPSK IKYISFGGYE IETWYAAPYP EEYSRNRVLY
     ICEFCLKYMN SDFVAWRHKL KCPAKHPPGD EIYRDGSVSV FEVDGRKNPV YCQNLCLLAK
     LFLGSKTLYY DVEPFLFYVM TEYDELGCHF VGYFSKEKRP SSSNNVSCIL TLPIHQRKGY
     GNLLIDFSYL LTRVERKTGS PEKPLSDLGL VSYRNYWRLV LSYQLRNQKS PVSIAELSER
     TGMTADDIVS GLEGLRALVR DPQTKTYALR LNYAYFEEYI RNWEKKNYIR LNPNALVWTP
     YVMGRSNQSH YDRAPLHTVA PRDEPDVDDD IEGNSDSNVY TNRAENMNGD TSSMQDGFVN
     GHSHARSVSP PFDPPGPPSM SVMPFDGASL RQANGVRTPS VSSMMQNPAA GIPPTRFEIF
     PPIPGTITKR RPGRPFGSTR ANKFRGRTTT TTAPTTARTS GRSTPKRTAS QVTGTPTPSS
     RTIGLRRGRS SRFLDPNDAD EVMGDGIESR EGGELEQLES PTLQSTEVEA ANMEIRANAT
     PESHAAASNN GRATGALENG NTNVDKAACA VPPSGDNKVN KHQATDLDHE RSQEAIQGPE
     NHQSIDGIDE HT
//
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