HACL2_ORYSJ
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 03-AUG-2022, entry version 112.
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; 4530.OS06T0704800-00; -.
DR PaxDb; Q5Z8V7; -.
DR PRIDE; 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; ASKINCC; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.1020.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 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; PTHR13808; 2.
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; SSF57903; 1.
DR SUPFAM; SSF57933; SSF57933; 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