ID A0A2A9N6R7_9AGAR Unreviewed; 1333 AA.
AC A0A2A9N6R7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Histone acetyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMATHDRAFT_159553 {ECO:0000313|EMBL:PFH45479.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH45479.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH45479.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH45479.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ302370; PFH45479.1; -; Genomic_DNA.
DR STRING; 703135.A0A2A9N6R7; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000242287; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04369; Bromodomain; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000242287};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 134..184
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 188..302
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 476..546
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1093..1163
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 573..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..336
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 582..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 148638 MW; 9AF955A2CFCF4368 CRC64;
MARGARASPA GISTSVLPKV SYSKTEEEYT LKLFGVHNLQ ARSYGFNDFS QFKRPKYYIQ
HIEPIESDLA RQVEYDMDEQ DQEWLDAVNA ERKKEQIDTV SYETFEIIMD RLEKEWFDLT
KNIPKADFAM PSEDSTCAIC DDSEGENSNA IVFCDGCNLA VHQDCYGVPY IPEGQWLCRK
CTVSPEFPVS CILCPNEGGA FKQTVTGDWV HLLCAIWVPE TRVANEVFME PITGVDKISK
QRWKLKCNIC EIKEGACIQC AKASCFTAFH ATCARKEKLL MPMKSTQGTE PLVLTCYCER
HLPKEHQDTR LAALAAEQAA EEMENDENDM KSSKSARAYA KSYKPGPPLV PALIINRILS
YIAKVQLRKR QEFVQMMARY WSLKREARRG APLLKRLHLE PWTANGSSAQ SDDQRLKKLE
YLTQLREDLE KVWEITELTR KREIRKRAQA RIIRDTLLSF LTPFEDLLRD SFHRIIAVDR
SEHFRYPVSK AEVPDYFDIV KKPMCWSTIE EKINSHAYFE SQEFKNDITL VLDNAMLYNA
PNTAYFKTAK RVQVAAQTIF DDIDRVLAER KAEMEGRQRA DNTDANGVNG GSGFPTQLQS
QIGDLEPPVG FLELLASADA IKDDIDLLLE KEPLESLFSF ELPKVKPRPP PPPPPPPKQT
KSTKPKRDRK ADLERKKRER EAEAAARALE AQYYGEPTGR TRRAVASVVV ETGALKISPP
PIVEIQEAKP LTPPVPSSAV EEQAVPEVEL PPAAPPPVVE VKRALPRKRA STSGMVEVPP
MVKGVDNRGS FKMFDQGWIF PPEQRRGGRP PLERLPLPPP RKRIKTSKDA MSRLSVVSTS
ASDNQTLQQM SPVEVMSPVS VVQRSQIEAP VMEMMEVDTS ALRTTISEEI LVAPPVVSET
LPTAVASASE FVALAPPSFV VNATPPPSIP VSPVVPSISG PELPFSNDLK RIVHGPDGTI
IVEELDTPLI RRHKALRRRE ERRRMLEEQR RQQEGQYRAA TSAVMANKEG DTGLIRLAPG
RGNADGESDL SSLSDVGSEV VEAQGQGVAP STPSAPLSQG PKNGELSRRA SMVMTTGIPD
DLGVIREDQL LEGGTLVWAK ASTYPWWPAV IFEEDDISIP LKVKGKCLAQ AKKATKHYMV
RFFDKGKTWA YLPSDRLKML GEFPELDEEL LSAHSTKQRW KNNSSRLDCN NAFKLKAMAE
METTSDAALY EALREQALQE ESGVLTAEGV TVEGDLSVAT AAGDNQGLGT VLVLDAEAEP
ETQQETETGR NREYVTNVSD HDGLHNSHID GSLVYPLEIA DSADSDVYKN ELAQGQRALE
GVKLDVETNP SDS
//
