ID A0A0J8QVN5_COCIT Unreviewed; 1104 AA.
AC A0A0J8QVN5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=CISG_01264 {ECO:0000313|EMBL:KMU76531.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU76531.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; DS268120; KMU76531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8QVN5; -.
DR STRING; 454286.A0A0J8QVN5; -.
DR Proteomes; UP000054559; 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 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 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:UP000054559};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMU76531.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 168..227
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 489..763
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..31
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 665
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1104 AA; 122457 MW; 2D0742F398B9CE5B CRC64;
MAATMPAEYE NATVEEDENM ADSEQDAEGE DDVDMYHPLT APGNFGGSEY VGTQHGLAAL
SAEPNHVNTV EETAQKVERT GALDSADINE NNGDNERVRP VKYLPVDYKS ESDADDAGDV
DPSFTNEESE SARDVVSNQS SDDDSEVDED WEAESDDRDS ADAEDLTLNN CIVCGQDEEH
DPSEEFEEPL VCAVCGDHCH RQCAREQECL NDADDTDKWR CPSCVQNKLE ADPGDRVEAH
RRSIVSNIAK ELLPAHSDAL GPDSHSIFDN PILDDDPLDG SRSLRKRKAS IDEVDNSRPL
TRKRLRRTID DQTDVAQSNE DAGDRAADNS NPSSRPSRPR RARRSQNGLC SVVLRQHGRL
VLSFHLDREK LSNVLKSRPR SRTQRRRPPK PPVIPEEPPP PQFPPIISTP YTAPFYSFHE
KEDHELNSKP YGGILADADA DTSKTVPQQS DRDKFEVARQ KAEEEWRQKI LAAEQSGEGS
PQASQKLSGP PSKMKCINFG GFEIETWYAA PYPEEYSRNR VLYICEFCLK YMNSDFVAWR
HKLKCPVKHP PGDEIYRDGT ISVFEVDGRK NPVYCQNLCL LAKLFLGSKT LYYDVEPFLF
YVMTEYDELG FHFVGYFSKE KRPSSSNNVS CILTLPIHQR KGYGNLLIDF SYLLTRIERK
VGSPEKPLSD MGLVSYRNYW HLVLSYQLRD QRTPTSIGEL SERTGMTPDD VVSGLEGLRA
LVRDPVTKTY ALRLNYTYFE EVIQNWEKKG YVQLNPDALV WTPYVMGRSN QSHYDRAPLH
AVAPRDDHEE AIDDGDINPF ENGNGLSGLN EQSTNHDCGA TSGQNHVDSV PQFEAPGPPS
MEVMSYGGQS MKHSNGYSTP SVTSTIPSAN IPPTRFEIFP PIQSAAVKRR PGRPFGSTKK
TRPNATNASP VRTSGRNTPR KNYNLTLATP TPAVRASPGL RRGRSKLLDN TLQTDGPADE
PGYECVEHGN EDQDGSRSGA AGVGDEDIQL KVNGEIHFDG DNVQNGARDT NESKSTNGSV
EACQGPETNL VTRVKDQRDN VSELESGGAA QQLTADILAA SKIPTGKDGH TQNHPSHDER
DTSQNSIGGE RNFEAAPVSA SAES
//
