ID   HACL2_ORYSJ             Reviewed;        1439 AA.
AC   Q5Z8V7; A0A0P0X0L7; Q0D9P7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 119.
DE   RecName: Full=Probable histone acetyltransferase HAC-like 2;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN   OrderedLocusNames=Os06g0704800, LOC_Os06g49130; ORFNames=P0018H04.4;
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=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   [2]
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   [3]
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).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAD53797.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF20426.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP003761; BAD53797.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008212; BAF20426.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014962; BAS99388.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5Z8V7; -.
DR   SMR; Q5Z8V7; -.
DR   STRING; 39947.Q5Z8V7; -.
DR   PaxDb; 39947-Q5Z8V7; -.
DR   EnsemblPlants; Os06t0704800-00; Os06t0704800-00; Os06g0704800.
DR   Gramene; Os06t0704800-00; Os06t0704800-00; Os06g0704800.
DR   eggNOG; KOG1778; Eukaryota.
DR   HOGENOM; CLU_002956_2_0_1; -.
DR   InParanoid; Q5Z8V7; -.
DR   OMA; TAQMNPG; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
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; IPR011011; Znf_FYVE_PHD.
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; PF02135; zf-TAZ; 1.
DR   SMART; SM01250; KAT11; 1.
DR   SMART; SM00551; ZnF_TAZ; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF57933; TAZ domain; 1.
DR   PROSITE; PS51727; CBP_P300_HAT; 1.
DR   PROSITE; PS50134; ZF_TAZ; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   3: Inferred from homology;
KW   Activator; Acyltransferase; Chromatin regulator; Coiled coil;
KW   Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1439
FT                   /note="Probable histone acetyltransferase HAC-like 2"
FT                   /id="PRO_0000269746"
FT   DOMAIN          948..1383
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT   ZN_FING         607..687
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT   ZN_FING         827..933
FT                   /note="PHD-type; degenerate"
FT   ZN_FING         1265..1328
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          964..989
FT                   /evidence="ECO:0000255"
FT   BINDING         1071..1073
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1090..1091
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1146
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ   SEQUENCE   1439 AA;  163087 MW;  35E3EA99C1F6AFF7 CRC64;
     MKQGQGAHLS GQRIGHHPTA QMNPGDGDGN GRHQVASGHA SADPELMNLR IRMTNRLIWE
     LLSREPKLQT RPRKLVSDLA KRFEAVIYKK NPNKAAYYSI LNGEIFPHLQ HALSTHMAQH
     QQGQQMLQQL TSSSSYGTTI PIPDVVQNAS GNTRALYEMD NTSGPMSNGH HHFSANFPLH
     STTKGASLEM SAVSMQEGKI THMIPTPGSS NQQSLPGNFH YSTGTGYLNG KSNVMAQMQE
     QQAPFASKIN CCPVQRDLGG YAGSGVHSDI LNNSSPYGVS EAHMIDGMGL HRSNVQVINR
     TVVPETFINP SPYGISPNKP LQRHVNPSTR STPTPADIAA STSFNGTGSS ALSTTSYLDM
     TTVNSLPKSR MDSGLIMSQP TIQSFQTEYY IQTEGLDLQE KISLEQLHQQ VNQLHLIQPH
     SQYAQNQCSL KLQQQNSLHH LVMSRGNVLT QCHLGSDHAE KLLDKRNQLH SELVSSQINE
     HVGLTNLQGH YEQTQYHDNY KKGQMSASSQ NLGIPAPHDL LPPQQQFDDG SYRLSCFLKE
     TYTKPLQPHC KSKPMKEVIM TSLLSGKIQD GFCQKKMARD REHHPIISGW HSAGCAATSF
     GSEEVMENTK QYHAQARWLL FLFHAKSCTS PPGSCKSSYC DRVRELVVHL TDCQIKDCSY
     RHCRESKMVS DHYKNCINEH CHVCCKAKEM LRRSSELAHK QNPAEPILIT QHNMNQRSAD
     RVHGDRMDID QAVETFDDQP PAAKRPKLQL VSPDASENVP VCQKNPGFML QEAHPRQLDQ
     NKKMVPDQEV DVGLDIRHPQ VTLVSCHGSD EKIGAAQNTV IPGALNKIHC HVQQETVVAD
     KESVTVVDVK KKTGSVDVTI SKTGKPKVKG VSLMELFTPE QIHEHINSLR QWIGQWVQCD
     KCECWQHQIC ALFNARRNDV EEAEYTCFKC YIEEFKRGLR MPLPESVVRG AKDLPRTLLS
     DHIEERLFKR LREERQERAN KLKTSLDEVP GADGLVVRVV SSVDKKLEVK PHFFKILQED
     NYPAEFPYKS KAILLFQKIE GVEVCLFGMY VQEYGAECKF PNQRRVYLSY LDSVKYFRPD
     IETVSGQALR TYVYHEILIG YLEYYKQRGF TSCYIWACPP VKGEDYILYC HPEIQKTPKS
     DKLRQWYLSM LQKAIKENIV VELTNLYDQF FVTAKECKIK VSAARLPYFD GDYWPGAAED
     IINQLQLEGD GKLLKKGRVN KIITKRALKA AGHTDLSGNA SKEAMLMQKL GEIICPIKDD
     LIMVHLQYSC SHCCTFMVSG RRWVCNECKS FYICDRCYNA EQRLEEKERH PSNSKCLHIL
     HPVEIVGVSE DTKDRDIILE NEIFDTRQAF LSFCQGYHYQ YDTLRRAKHS TMMMLYHLHN
     PTGPAFVATC NVCNCDIENG QGWDFKSFER KQNQLSESRR MASVNERVRQ RVAEVTRHE
//