ID A0A0B0P8R6_GOSAR Unreviewed; 1535 AA.
AC A0A0B0P8R6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=F383_03976 {ECO:0000313|EMBL:KHG19766.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG19766.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC specific tag for transcriptional activation.
CC {ECO:0000256|ARBA:ARBA00002581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000780};
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DR EMBL; KN413919; KHG19766.1; -; Genomic_DNA.
DR Proteomes; UP000032142; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15614; PHD_HAC_like; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR035898; TAZ_dom_sf.
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 InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KHG19766.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 470..550
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 919..1355
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1237..1300
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1357..1416
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1417..1500
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1535 AA; 171358 MW; 61D7B5ACF4A1A204 CRC64;
MNVQAHMSGQ ISGQAANQGG LPQQNGNLLQ PAQMQSLGVG GASAAGGPPH TMSNMDPDLH
RTREYMRGKI IDVLKLRNQL PITEASMIKF RDFARRLEEG LFKIAHTKED YTNLSTLEHR
LQILLRGSRN VHNQRHPQLV NSASASAPVG TMIPTPGISH SGNPSIVATS SIDKSTSAAS
ASIAPTNINT GSLLPSSGMT SASFTRSEGN ISNGYQQLPA NFPLASGGIS SIGVQRMASQ
MIPTPGFNSN NNNGSINDQS SNNVGLSTVE STMVSQPQQQ KPHGGQNSRI LRTLGSQMGS
GIRSGLQQKA FGLPHGSLNG ALGMMGNNMH IVSEHGTPVG YQTTTAFASS PKPLQQNFDQ
HQLPVMQADG YGMNNADSFG SGNLYGAVTS VGSVTNSQNL NSVNLQAQIP GNISHEQPVQ
EEFRQRTSGP DKAQCNNISA DGSTISPMVD ARSSSEPFNS RGAISKSENG SHDRQYRNQV
KWLLFLRHAR SCKASEGKCD SYCFTVRKLL SHMNKCESSQ CSYPRCRPSK ILIRHYKTCT
NPTCPVCVPV KNFIQAQKAH ACRNSASVLP SSDGGSTKIN DAGDISTRMT SRTASNDASV
GVQPSQKRMK IEQSSQSVIA ESEGPLGSVV AEPHISQDIQ HQDYQHVDRC MLVKPEPMEV
KTDVPVSCSS GNPVFIEMKD DVDDISKQKI DREAVTLDEF GGLPMQESAK FEKEPDSVKQ
ENVTESSESA AGTKSGKPKI KGVSLTELFT PEQVREHITG LRRWVGQSKA KAEKNQAMEH
SMSENSCQLC AVERLTFEPP PIYCSPCGAR IKRNAMYYTM GAGDTRHYFC IPCHNEARGD
SIVVDGTAIP KARLEKKKND EEIEEWWVQC DKCEAWQHQI CALFNGRRND GGQAEYTCPN
CYITEVERGE RKPLPQSAVL GAKDLPRTIL SDHIEQRLFK RLKQERQERA RVQGKSYDEV
PGAESLVIRV VSSVDKKLEV KQRFLEIFQE QNYPLEFPYK SKVVLLFQKI EGVEVCLFGM
YVQEFGSECA FPNQRRVYLS YLDSVKYFRP EVKAVTGEAL RTFVYHEILI GYLEYCKKRG
FTSCYIWACP PLKGEDYILY CHPEIQKTPK SDKLREWYLA MLRKASKENI VVDLTNLYDH
FFVTTGECKA KVTAARLPYF DGDYWPGAAE DLINQFRLEE DGRKLNKKGT IKKTITKRAL
KASGQSDLSA NASKDLLLMH KLGETICPMR EDFIMVHLQH CCTHCCILMV SGNRWVCNQC
KKFQICDKCH EAELKRDERE RHPFNQREKH VLYPIEITDV PTDTTDQDDI LESEFFDTRQ
AFLSLCQGNH YQYDTLRRAK HSSMMVLYHL HNPTAPAFVT PCCICHLDIE TGQGWRCEVC
PDYDVCNACY KKDGGIDHPH KLTNHPSMAE RDAQNKEARQ LRVLQLRKML DLLVHASQCR
SAHCQYPNCR KVKGLFRHGI QCKTRASGGC LLCKKMWYLL QLHARACKES QCHVPRCRDL
KEHLRRLQQQ SDSRRRAAVM EMMRQRAAEV AGSSG
//
