ID A0A251PUB3_PRUPE Unreviewed; 1739 AA.
AC A0A251PUB3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=PRUPE_3G028200 {ECO:0000313|EMBL:ONI15164.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI15164.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI15164.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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};
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; CM007653; ONI15164.1; -; Genomic_DNA.
DR STRING; 3760.A0A251PUB3; -.
DR EnsemblPlants; ONI15164; ONI15164; PRUPE_3G028200.
DR Gramene; ONI15164; ONI15164; PRUPE_3G028200.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000006882; Chromosome g3.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15614; PHD_HAC_like; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 2.
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; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_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 Pfam; PF00569; ZZ; 2.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 2.
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:UP000006882};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 671..753
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 1123..1559
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1441..1504
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1561..1614
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1621..1704
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1739 AA; 195986 MW; DDBC20880CF9BB06 CRC64;
MNVQTHMSGQ ISGQVPNQAG TQMPVLPQHN GNSLPPQMQN LGGPARAMSN MDPEIPTLRS
IMQEKICQII QQRQHPQPMS DTKFREFVKK LEEGLLRNAQ TKDDYMNMET LESRLQNLMK
PPQNQSQQYQ QLVNSSSPIG TMIPTPGMSH NGNSNMMVSS SVDASMNTTR GSTSIAPTTV
NTGNLLPAGP LPGGSFNRSD GSMSNGYQQS PASFSIGTGG NMSSMGVQRI TSQMIPTPGF
NSSSNQSYMN LESSNNGGGF STVDSSMVTQ PQQQKQHIGG QNSRILHNVG SQMGSGIRSG
MQQKPYGLPN GALNGGLGLI GNNLPLVNES GTSEGYMALT PYANSSKPSQ HFDQHQRPIM
QGDSYGMSNA DSFGPGNYYG AATPVGSMLN AQNLNSVSST AISKTNPPLI SNQSNMHGAQ
QSVHVKPQQL DQLEKINFQT PLSSRENILH SHQQQQFQHQ PNQFQQQQQL VHQQRQQKQQ
NPQRQQMLNN DAFGQSQMTS DLSSAKRDMD HHNEAMHQQA TEPFRLSEMH NQFHQHSVED
RLRNAQHIPS GQHDISSSLS QTSQQMQQIL QPHQLVAESQ NDFRSLSVGA QSEPVLQGQW
HPQLQDGSHR QANMSHEQHV HEDFRQRISG QDEAQCNNSS SEGPNVVQNM GSRSISRPPN
SSSAASRSGY VNRDKWFLNQ QRWLLLMLHA RCCTAPEGKC REARCVIVQK LVQHMKSCES
SQCTYSRCRI SKLLVLHSQT CKSKKACPVC GPVLNYLNKE KNRRVSDSGL QNSINGSGKV
YDSGDTSARL VLKTAPVVET SEDRQPSMKR MKIEQSSQSV VPDSVSVSSA VKVSAISEPH
VSEDIQIHDY QHSEISMPVK SEFAEVKMEI PVSSGQGSLD EMKDSVDDNC NSRHDGEAVS
YNEPAVLARQ ENIKLEKETD PAKQENVAQP VENAAATKSG KPKIKGVSMT ELFTPEQVRA
HITGLRQWVG QSKAKAEKNQ AMENSMSENS CQLCAVEKLT FEPPPIYCTP CGARIKRNAM
YYTMGAGDTR HYFCIPCYNE ARGDTIVVDG TAIPKARLEK KKNDEETEEW WVQCDKCEAW
QHQICALFNG RRNDGGQAEY TCPNCYIQEV ERGERKPLPQ SAVLGAKDLP RTILSDHIEQ
RLFKKLKVER QERARQQGKS YDEVPGAESL VIRVVSSVDK KLEVKQRFLE IFQEENYPTE
FPYKSKVVLL FQKIEGVEVC LFGMYVQEFG AECQFPNQRR VYLSYLDSVK YFRPEVKAVT
GEALRTFVYH EILIGYLEYC KKRGFTSCYI WACPPLKGED YILYCHPEIQ KTPKSDKLRE
WYLAMLRKAA KESIVVELTN LYDHFFVTTA ECKAKVTAAR LPYFDGDYWP GAAEDLIYQM
RQEEDGRKQN KKGTTKKTIT KRALKASGQT DLSGNASKDL LLMHKLGETI CPMKEDFIMV
HLQYACSHCC ILMVSGNRWS CTQCKNFQLC DKCYEAEQKR EERDRHPSNQ REKHELRPFD
ITDVPADTKD KDEILESEFF DTRQAFLSLC QGNHYQYDTL RRAKHSSMMV LYHLHNPTAP
AFVTTCNICH LDIETGQGWR CEVCPEYDVC NNCYQKEGGV DHHHKLTNHP SIADRDAQNK
EARQMRVLQL RKMLDLLVHA SQCRSAQCQY PNCRKVKGLF RHGIQCKVRA SGGCVLCKKM
WYLLQLHARA CKESECHVPR CRDLKEHLRR LQQQSDSRRR AAVMEMMRQR AAELHNNTG
//
