ID C0NJW4_AJECG Unreviewed; 1079 AA.
AC C0NJW4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=HCBG_03444 {ECO:0000313|EMBL:EEH08155.1}, HCBG_03493
GN {ECO:0000313|EMBL:EEH08204.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH08155.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
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.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEH08155.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G186AR {ECO:0000313|EMBL:EEH08155.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG663366; EEH08155.1; -; Genomic_DNA.
DR EMBL; GG663366; EEH08204.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NJW4; -.
DR STRING; 447093.C0NJW4; -.
DR VEuPathDB; FungiDB:I7I50_07055; -.
DR HOGENOM; CLU_005327_1_2_1; -.
DR InParanoid; C0NJW4; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
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 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 PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 490..764
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1079
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..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..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 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 666
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1079 AA; 119593 MW; 6E806CF70FFC9FFF CRC64;
MAATVPATYG NTSIDRQPEL VDSDQDAEGD EDDELYPTLT QSATVIPQEN IDPPLTLGNG
DETIEASERE ENDGVGVGEV HEPETNHRDD VADMDEDEDA DADADADEDT EAIGAVKFPD
GNAKSDSDDE DDDIDDPDVE FENESSDVKA GSDGESSEES EVDEEWEAES NDGEDADADA
LNPNNCIVCG QDEEHDPSEE FEEYLSCAVC GDHSAENWRC PSCVENKLEP DKHERTPSRR
RSGTSNIAID LLPAHSEALG PESHSIFSSL IVDDDPLDGS RSLRKRRASD EGPEGNMVTQ
KRQKKIPARF EGMIPTPLPR NMKTVQALIE HSTENNVTSR QSRPRRTRKT EKALCNIVQR
QAGKIILSFH LNSTKLNRIL NSRQKQISRR RPPKPPPVVE SPQIPFQPIA PSAYSAPFYA
FHDRENDELK SKPYGGILSE ADADTSRTLP LAADREKFEA ARQKAEEEWR QKMAAADQPG
ESAPRAKISG PPSKIKYISF GGYEIETWYA APYPEEYSRN RVLYICEFCL KYMNSDFVAW
RHKLKCPAKH PPGDEIYRDG SVSVFEVDGR KNPVYCQNLC LLAKLFLGSK TLYYDVEPFL
FYVMTEYDEL GCHFVGYFSK EKRPSSSNNV SCILTLPIHQ RKGYGNLLID FSYLLTRVER
KTGSPEKPLS DLGLVSYRNY WRLVLSYQLR NQKSPVSIAE LSERTGMTAD DIVSGLEGLR
ALVRDPQTKT YALRLNFAYF EEYIRNWEKK NYIRLNPNAL VWTPYVMGRS NQSHYDRAPL
HTVAPRDEPD ADDDIEGNGD SNVYTNRAEN MNGDTSSMQD GFVNGHSHAR SVSPPFDPPG
PPSMSVMPFD GASLRQANGV RTPSVSSMMQ NPAAGIPPTR FEIFPPIPGT ITKRRPGRPF
GSTRANKFRG RTTTTTAPTT ARTSGRSTPK RTASQVTGTP TPSSRTIGLR RGRSSRFLDP
NDADEVMGDG IESREGGELE QLESPTLQST EVEAANMEIG ANATPESHAA ASNNGRATGA
LENGNTNIDK ATCAVPPSGD NKVNKHQATD LDIVDHERSQ EAIQGPENHQ SIDGIDEHT
//
