ID A0A0C3PKH9_PISTI Unreviewed; 1185 AA.
AC A0A0C3PKH9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 37.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=M404DRAFT_991503 {ECO:0000313|EMBL:KIO14745.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO14745.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO14745.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO14745.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN831944; KIO14745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3PKH9; -.
DR STRING; 870435.A0A0C3PKH9; -.
DR HOGENOM; CLU_272503_0_0_1; -.
DR InParanoid; A0A0C3PKH9; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000054217; 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; 2.
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; 2.
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:UP000054217};
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 124..182
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 179..229
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 478..801
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..331
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 656
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1185 AA; 131591 MW; C5DAFECFB4488A84 CRC64;
MRGLPFPTNA LFDRETTSEV GTPASHVDDI PIDPALAGTA LTDTAFERHS NGPLCDPAQL
RSVIPHHDPR PVCRRHYSQE PSQYDQGPRG DPFAPQPPAT YVPIQEVIAQ TPKPQKRRRK
PRREEECGFC QGNDSKNKLG EPELMVSCDE CGRSGHPSCM ELARVADVMR SYPWRCIECK
ICEVCHEKGD DERILFCDFC DRGWHMDCLD TPLDKAPPGQ WHCPECPPIE FLQPPDAPLT
QSDTVPTEPP QYFHVSNPND PICGLEPEPE VDVEAGAEDS AEATEEDESE SESESSSSDS
GSDESTVGAP TPRRPSAVKK KRPKRKSEPA RPPKRMRLTV RPSAPPLVVR LRIPPKGKGK
DREEDPEKNI FEDLLAPAER DVSKTAIEST DRTRFDRSRL AADEKLAPPP PPTSATDVTD
SPVAGPSSRP LRSHTLHQIS IPSTIPTPSP VPSTPSLHPN TPGYSFQSPN TPAGHEQTPV
LRIRIIRFGR YDIHPWYDAP FPEEYANIPD GRLWICEFCL KYMRSGFAFG RHKMKCKARH
PPGDEIYRDG QVSIFEVDGR KNKIYCQNLC LLSKMFLDHK SLFYDVEPFL FYVMTEFDDI
GARFVGYFSK EKCSPKDYNV SCIMTLPVRQ RQGWGGFLID FSYLLSKKER RTGSPEKPLS
ALGALGYKNY WTLAIMRYLK TAPPRPSLED ISRATSMTLE DIYNTLVQQD MITQAATPPP
VRPSPGQSIK FPRGRKNGIA RRHLQRTNTQ KEEEGSKQGS PLVLPTRYEI SWDPDVVDRW
LESWEQKGYL KVKLEKLKWT PFFLTRTKAT GEILQSEMGI GIETLSGGGA PKTPVLPSEN
GTPAAAVDES NNREKLPAPD PVEVAKENRA AVGDALTDVS EASAARLFDD LLIDSVATPK
KQLRSRVKDD NSNTRLPDLR TRSSIKRHED HHLPPLRHTR SSRRLVVDED DDDGDVPNIV
NGNLADDLAA VPAKRRGGRL SRKPSSSPPE PCDRVIAATP RSRSPPPSAT SCKRRRIDTP
SRNGSLSPSE PASDERRADP FIHPMKPVIN LTNGQSNQSN GVSWPPSSPE QRSATDAKKG
QEEPVRDCSH ADGANGFCDD QDVKTEDVGT PLTGLTCQQS ASSDYTVVVT NQVNGGGLVD
KSPNDIRQST MLPEPFHSVL IDGPVNFGEV HDSDLDAEGD TDDEM
//
