ID   HAC5_ARATH              Reviewed;        1670 AA.
AC   Q9LE42; Q8LRK5; Q8LRK6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Histone acetyltransferase HAC5;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN   Name=HAC5; Synonyms=PCAT4; OrderedLocusNames=At3g12980;
GN   ORFNames=MGH6.20, MGH6_9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 32-484 AND 529-1540, AND NOMENCLATURE.
RX   PubMed=12466527; DOI=10.1093/nar/gkf660;
RA   Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA   Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT   "Analysis of histone acetyltransferase and histone deacetylase families of
RT   Arabidopsis thaliana suggests functional diversification of chromatin
RT   modification among multicellular eukaryotes.";
RL   Nucleic Acids Res. 30:5036-5055(2002).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=11160878; DOI=10.1093/nar/29.3.589;
RA   Bordoli L., Netsch M., Luethi U., Lutz W., Eckner R.;
RT   "Plant orthologs of p300/CBP: conservation of a core domain in metazoan
RT   p300/CBP acetyltransferase-related proteins.";
RL   Nucleic Acids Res. 29:589-597(2001).
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   -!- TISSUE SPECIFICITY: Rosette leaves, stems and flowers.
CC       {ECO:0000269|PubMed:11160878}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in young seedlings.
CC       {ECO:0000269|PubMed:11160878}.
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DR   EMBL; AB026645; BAB02507.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75270.1; -; Genomic_DNA.
DR   EMBL; AH011642; AAM34787.1; -; mRNA.
DR   EMBL; AH011642; AAM34788.1; -; mRNA.
DR   RefSeq; NP_187904.1; NM_112135.4.
DR   AlphaFoldDB; Q9LE42; -.
DR   SMR; Q9LE42; -.
DR   BioGRID; 5818; 1.
DR   STRING; 3702.Q9LE42; -.
DR   iPTMnet; Q9LE42; -.
DR   PaxDb; 3702-AT3G12980-1; -.
DR   ProteomicsDB; 247158; -.
DR   EnsemblPlants; AT3G12980.1; AT3G12980.1; AT3G12980.
DR   GeneID; 820484; -.
DR   Gramene; AT3G12980.1; AT3G12980.1; AT3G12980.
DR   KEGG; ath:AT3G12980; -.
DR   Araport; AT3G12980; -.
DR   TAIR; AT3G12980; HAC5.
DR   eggNOG; KOG1778; Eukaryota.
DR   HOGENOM; CLU_002956_2_0_1; -.
DR   InParanoid; Q9LE42; -.
DR   OMA; IPQNAGV; -.
DR   OrthoDB; 651475at2759; -.
DR   PhylomeDB; Q9LE42; -.
DR   PRO; PR:Q9LE42; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LE42; baseline and differential.
DR   GO; GO:0016592; C:mediator complex; IPI:TAIR.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006473; P:protein acetylation; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15614; PHD_HAC_like; 1.
DR   Gene3D; 3.30.60.90; -; 2.
DR   Gene3D; 1.20.1020.10; TAZ domain; 2.
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; 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:SF41; HISTONE ACETYLTRANSFERASE HAC4-RELATED; 1.
DR   Pfam; PF08214; HAT_KAT11; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM01250; KAT11; 1.
DR   SMART; SM00551; ZnF_TAZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF57933; TAZ domain; 2.
DR   PROSITE; PS51727; CBP_P300_HAT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50134; ZF_TAZ; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 2.
DR   PROSITE; PS50135; ZF_ZZ_2; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   Genevisible; Q9LE42; AT.
PE   2: Evidence at transcript level;
KW   Activator; Acyltransferase; Chromatin regulator; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1670
FT                   /note="Histone acetyltransferase HAC5"
FT                   /id="PRO_0000269743"
FT   DOMAIN          1061..1497
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT   ZN_FING         611..690
FT                   /note="TAZ-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT   ZN_FING         970..1046
FT                   /note="PHD-type"
FT   ZN_FING         1379..1442
FT                   /note="ZZ-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   ZN_FING         1499..1550
FT                   /note="ZZ-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   ZN_FING         1554..1634
FT                   /note="TAZ-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT   REGION          490..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..737
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..861
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1184..1186
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1203..1204
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1259
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q09472"
FT   BINDING         1384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1387
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1424
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1504
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1507
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1519
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1522
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1528
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1531
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1538
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         1540
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ   SEQUENCE   1670 AA;  188188 MW;  2120E9184B4B98BD CRC64;
     MAQGQNRTVL QSGQMHNSVV ASASSVSSQP NMVNGISQDT LLLRQEMLNR TYAWLQQRQP
     SKTDDASKAK LSEVAKRLES AMWRTATSKE DYLDFRSFDV RVESTLKQLL SQRRANPSSS
     VSTMVQTPGV SHGWGQSYTA TPMVDTSKFN SSNNLSDATT ETGRLLPTNR MYRGTINNGR
     QELSAVGQMI PTPGFDNSAN ADVYQSHRNE EYSGDGGKLL ATGSDFGNPS QLQKQRPTGS
     NDLMGYNLDH QLGGGFRSNI HQNTSGMTSI PLNAGVGMSG NNVHLANVPR SSEGVLSSTH
     FSTFSQPSQQ PVEQLQVSHV NRYSMSNSGT FVSGNLYGVQ TSSGSIETAV DMNSMSLNSM
     RRVDTSFGSQ SGLQNNPLLK PHLRHQFENG NFQSSSNSKE NLAQVSHRPL ERQFNQQAHY
     GQYHQQELLM NNDAYRQSQP ASNLVSQVKN EPRVEYYNEA FQMQAINKVE PSKPQNQYKQ
     NTVKDEYVGA QSAPVSSSQL KMSPSFPPQT HQTQQVSQWK DSSSLSAGVQ PVSGLGQWHS
     SSQNLTPISK NSNEEREHFG VRFHKQHEGT NNSSSVREST NCLTVAPSGT LDVPHLPVGI
     NVLSKQLNGD CGLSYKNQRR WLLFLLHVRK CNAAEDNCES KYCFTAKTLL KHINCCKAPA
     CAYQYCHQTR QLIHHYKHCG DEACPVCVFV KNFKEKQKEK FTFLQRAEPS SASLNHGPKE
     SFESMRTSSE RDSEAPFVVD DLQPSPKRQK VEKPSQFAYP DTQGNPATIS AGVSQAHFSM
     GLQEKDRLPS DVCKPVRSNV PMNADSSDSS RRLVPVSREL EKPVCKDTHM GRHGVKSALD
     GESLRLSKQE KPKRMNEISA PKEENAEQSL GVVSASNCGK SKIKGVSLIE LFTPEQVEEH
     IRGLRQWVGQ SKTKAEKNKA MGLSMSENSC QLCAVERLAF EPTPIYCTPC GARVKRNAMH
     YTVVAGESRH YVCIPCYNEA RANTVSVDGT PVPKSRFEKK KNDEEVEESW VQCDKCQAWQ
     HQICALFNGR RNHGQAEYTC PNCYIQEVEQ GERKPVSQNV ILGAKSLPAS TLSNHLEQRL
     FKKLKQERQE RARLQGKSYE EVPGADSLVI RVVASVDKIL EVKPRFLDIF REDNYSSEFP
     YKSKAILLFQ KIEGVEVCLF GMYVQEFGTD SASPNQRRVY LSYLDSVKYF RPDVRTVSGE
     ALRTFVYHEI LIGYLDYCKK RGFSSCYIWA CPPLKGEDYI LYCHPEIQKT PKTDKLREWY
     LAMLKKASKE KVVVECTNFY DHFFVQSGEC RAKVTAARLP YFDGDYWPGA AEDLIDQMSQ
     EEDGKKSNRK LMPKKVISKR ALKAVGQLDL SVNASKDLLL MHKLGEIILP MKEDFIMVHL
     QHCCKHCCTL MVSGNRWVCN QCKNFQICDK CHEVEENRVE KEKHPVNQKE KHVLYPVAID
     NIPTEIKDND DILESEFFDT RQAFLSLCQG NHYQYDTLRR AKHSSMMILY HLHNPTVPAF
     AMACAICQQE LETAQGWRCE VCPDYDVCNA CYSKGINHPH SIISRPSATD SVVQNTQTNQ
     IQNAQLREVL LHVMTCCTAQ CQYPRCRVIK GLIRHGLVCK TRGCIACKKM WSLFRLHSRN
     CRDPQCKVPK CRELRAHFSR KQQQADSRRR AAVMEMVRQR AADTTASTPE
//