ID   HACL3_ORYSJ             Reviewed;        1276 AA.
AC   Q9XHY7; A0A0P0V0J4; Q0JP42; Q1EHS1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Probable histone acetyltransferase HAC-like 3;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN   OrderedLocusNames=Os01g0246100, LOC_Os01g14370;
GN   ORFNames=OSJNBa0004G10.16, OSJNBa0049B20.5;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC       specific tag for transcriptional activation.
CC       {ECO:0000250|UniProtKB:Q9C5X9}.
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:0000250|UniProtKB:Q9C5X9};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD38279.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAE95818.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC007789; AAD38279.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP003074; BAE95818.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008207; BAF04486.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS71309.1; -; Genomic_DNA.
DR   EMBL; AK120732; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015621172.1; XM_015765686.1.
DR   AlphaFoldDB; Q9XHY7; -.
DR   SMR; Q9XHY7; -.
DR   STRING; 39947.Q9XHY7; -.
DR   PaxDb; 39947-Q9XHY7; -.
DR   EnsemblPlants; Os01t0246100-01; Os01t0246100-01; Os01g0246100.
DR   GeneID; 4326755; -.
DR   Gramene; Os01t0246100-01; Os01t0246100-01; Os01g0246100.
DR   KEGG; osa:4326755; -.
DR   eggNOG; KOG1778; Eukaryota.
DR   HOGENOM; CLU_002956_2_1_1; -.
DR   InParanoid; Q9XHY7; -.
DR   OMA; CERCYAE; -.
DR   OrthoDB; 465345at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
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   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.
DR   Genevisible; Q9XHY7; OS.
PE   2: Evidence at transcript level;
KW   Activator; Acyltransferase; Chromatin regulator; Coiled coil;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1276
FT                   /note="Probable histone acetyltransferase HAC-like 3"
FT                   /id="PRO_0000269747"
FT   DOMAIN          704..1130
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT   ZN_FING         621..689
FT                   /note="PHD-type"
FT   ZN_FING         1013..1076
FT                   /note="ZZ-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   ZN_FING         1125..1187
FT                   /note="ZZ-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   ZN_FING         1177..1260
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT   REGION          391..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          953..973
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        391..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         827..829
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         846..847
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         902
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1018
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1021
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1033
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1036
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1042
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1045
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1058
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1066
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   CONFLICT        468
FT                   /note="P -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1276 AA;  145098 MW;  902E2A329079778E CRC64;
     MMAKTLQGTQ QQYAASGFPT QQYPTSGWTQ SAAEILQLDN MDQDTSVVRN IIHRKIVEYL
     NERKEFCNFD LSFLMEIGKC IDRHLFEKAD SKIKYMDLET LRTRLNAIVN SASFRGSMFH
     WSASAASSKL NSQQLPVMEV PIYHDRVTPG PNNLPSCAYN VSSTQGYNQY ENCMGAANFA
     HSLADKPKQM PERLANTIFT SCASTLPKCS PSIDVLHIGH IKEHFSGDAY QNDSSQPSTS
     GSSSSLSAVW DQTTCSSAMR TLPMDSFSTV NGQNLSTNNK SLYPTTGQGP LLQQYIECEM
     KQETWSRSLE QSDQSNITTG NRDLYHAQIH PYINGEHKRD RCIQMKEKLG HTSDHEGFSR
     EKSSNLSNHF MHHQQGFMTN YGACSPVSKT VDRAEQTSNS TVSKPTSPAS DGSSGKHYPA
     KRLKVDVPHL VHVNEMEASK EQQPAANETY ASAETVQSEV TNSPTKSPCC TSLGDNIACT
     DNVHGMDMVR LSGSAVQTEE EFRRENSDIE MKDAKVDLLD 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 HEILIGYLDF CKKRGFVSCS IWTCPSTKRD DYVLYCHPTI QKMPKSDKLR
     SWYQNLVKKA VKEGVVVERN TLYDFFLQPT NECKTNISAA WLPYCDNDFW PGEAERLLEK
     KDDDTSQKKE TQLGRLLRVA KRDDRKGNLE DILLVHKLGE RLRTMKEDFL MLCLQQFCKH
     CHHPIVSGSS WVCTSCKNFF LCERCYAEEL NTPLKDRHPA TTKQKHAFER IEEEPLPETD
     DVDPTMESKY FDSRIDFLKH CQDNQYQFDT LRRAKHSTMM ILYHLHDSTC SSCHRAMDQC
     LAWRCLVCLG CNFCDSCYKQ DGESLHIHKL RQKKDHHVLQ KYTLQDYLEG LVHASRCFDR
     SCTSKLCLTL KKLFFHGVRC HTRARGGGGC HMCVFMWKLL FTHSLLCDNA DCSAPRCRDI
     KAYIADRSMT DLSISG
//