ID A0A0E0BZW4_9ORYZ Unreviewed; 1168 AA.
AC A0A0E0BZW4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G09180.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI01G09180.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI01G09180.2};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI01G09180.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0BZW4; -.
DR EnsemblPlants; OMERI01G09180.2; OMERI01G09180.2; OMERI01G09180.
DR Gramene; OMERI01G09180.2; OMERI01G09180.2; OMERI01G09180.
DR HOGENOM; CLU_002956_2_1_1; -.
DR Proteomes; UP000008021; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 1.
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:SF39; HISTONE ACETYLTRANSFERASE HAC-LIKE 3-RELATED; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02135; zf-TAZ; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00551; ZnF_TAZ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57933; TAZ domain; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 1.
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:UP000008021};
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 664..1022
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 905..968
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1017..1079
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1069..1152
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 187..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 132591 MW; 5DB93FC088E8F0A8 CRC64;
MDQDTSVVRN IIHRKIVEYL NERKEFCNFD LSFLMEIGKC IDRHLFEKAD SKIKYMDLET
LRTRLNAIVN SASFRGSMFH WSASAASSKL NSQQLPVMEV PIYHDRVIPG PNNLPSCAYN
VSSTQGYNQY EHCMGAANFA HSLADKPKQM PERLANTIFT SCASTLPKCS PSIDVLHTGH
IKEHFSGDAY QNDSSQPSTS GSSSSLSAVW DQTTCSSAMR TLPMDSFSTV NGQNLSTNNK
SLYPTTGQGP LLQQYGECEM KQETWSQSLE QSDQSNITTG NHDLYHAQIH PYINGEHKRD
RCIQMKEKLG HTSDHEGFSR EKSSNLSNHF MHHQQGFMTN YGACSPVSKT VDRAEQTSNS
TVSKPTSPAS DGSSGKHYPA KRLKVDVPHL VHVNEMEASK EQQPAANETY ASAETVQSEA
TNSPTKSPCC TSLGDNIACT DNVHGMDMVR LLESAVQTEE EFRRENSDIE MKDTKVDLLD
QTLSGDSLRA RKRRGASVLY ALTSEELKDH LCTLNHDTSQ SKVPTEELLS VEGLPDQNTC
NLCGMERLLF EPPPRFCALC FKIINSTGSY YVEVENGNDK SSICGRCHHL SSAKAKYQKR
FSYAETDAEA EWWVQCDKCK AWQHQICALF NPKIVDPEAE YTCAKCFLKE KDNEDVDSLE
PSTILGAREL PRTRLSDHIE QRLSERLVQE RQQRAIASGK SVDEVPGVEG LTVRVVSSAD
RTLQVQPRFK DFFKKEQYPG EFPYKSKAIL LFQKNEGVDV CLFAMYVQEY GSACPSPNQR
HVYLAYIDSV KYFRPEIKSA SGEALRTFVY HEILNLVKKA VKEGVVVERN TLYDFFLQPT
NECKTNISAA WLPYCDNDFW PGEAERLLEK KDDDTSQKKE TQLGRLLRVA KRDDRKGNLE
DILLVHKQFC KHCHHPIVSG SSWVCTSCKN FFLCERCYAE ELNTPLKDRH PATTKQKHAF
ERIEEEPLPE TDDVDPTMES KYFDSRIDFL KHCQDNQYQF DTLRRAKHST MMILYHLHDS
TCSSCHRAMD QCLAWRCLVC LGCNFCDSCY KQNGESLHIH KLRQTKDHHV LQKYTLQDYL
ESLVHASRCF DRSCTSKLCL TLKKLFFHGV RCHTRARGGG GCHMCVFMWK LLFTHSLLCD
NADCSAPRCR DIKAYIADRS MTDLSISG
//
