HACL3_ORYSJ
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 03-AUG-2022, entry version 131.
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; 4530.OS01T0246100-01; -.
DR PaxDb; Q9XHY7; -.
DR PRIDE; 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; 27931at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q9XHY7; OS.
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; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_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; 1.
DR Pfam; PF08214; HAT_KAT11; 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; SSF57903; 1.
DR SUPFAM; SSF57933; SSF57933; 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 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
