HACL1_ORYSJ
ID HACL1_ORYSJ Reviewed; 1668 AA.
AC Q6YXY2; Q0E444;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable histone acetyltransferase HAC-like 1;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN OrderedLocusNames=Os02g0137500, LOC_Os02g04490;
GN ORFNames=OSJNBa0026E05.8, OSJNBa0081C13.32;
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=BAD10378.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD10522.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF07744.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005474; BAD10378.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005647; BAD10522.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF07744.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6YXY2; -.
DR SMR; Q6YXY2; -.
DR STRING; 4530.OS02T0137500-01; -.
DR PaxDb; Q6YXY2; -.
DR PRIDE; Q6YXY2; -.
DR eggNOG; KOG1778; Eukaryota.
DR InParanoid; Q6YXY2; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 2.
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; 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; 2.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF57933; SSF57933; 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; 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; Repeat; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1668
FT /note="Probable histone acetyltransferase HAC-like 1"
FT /id="PRO_0000269745"
FT DOMAIN 1094..1530
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 651..732
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 1002..1079
FT /note="PHD-type"
FT ZN_FING 1412..1475
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1553..1634
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1342..1365
FT /evidence="ECO:0000255"
FT COILED 1630..1650
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1217..1219
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1236..1237
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1292
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 1435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 1668 AA; 188439 MW; 3319FB6DD28BB3DC CRC64;
MNVGQAAHLS GQMSGQAPQT NQVGGSGVGG ADGLPQQMQD VVGLGGLDTQ FLLMRNTMRD
RIFEYIGRKQ SSTDWRRRLP ELAKRLEEIL YRKFLNKADY LNMMRGPVEP QLQFAIKTLS
AQNQQNQQNQ QMPRQMASSS GYGTMIPTPG ITQSATGNSR MPYVTDNTGL PSSGATMVPQ
GANTGSMSNG YQHLTTSVPL NSTTSSIPST MGPVGIQRQV THMIPTPGFN NQQNVPVNPD
FSNGAGYFNG EPTVTSQMQQ QKQFPSNQNS HQIQHIGGHS NSGMHSNMLE NSSAYGLSDG
HVNGGMGVHG SNMQLTNRSA ASEAYINIST YGNSPKPVQQ QFNQHPPQRI PTPVDISGSG
NFYNTGSSAL TAANNHSMGA TNLPSRSRMN SMLHTNQLNM QSIQPQPQIK TEVLDQPEKM
NFQSSQLTHE QLIRQQHSMQ QHQMQPSSQF VQNQYHLNQQ QPNSQHQQSI LRSNSLKQPQ
LSSSHSMQLS EQGALPHTEL ISSQATEHAD IPIYQGQYQQ RSAHDNVKGG QVFGHLSSSQ
NFHSNASHDS QQLLPTNQQL DDSSNDVSYV LKGSQPEQMH QAQWRPQTME KAPVTNDSSL
EKQIQADLCQ RTMSQDGAQQ PFSSDWRLPG CTVTPADPAL PKLPSGGLEQ AAGNIYYFRQ
MKWLLLLFHA KSCLTPVGSC KFHRCFQVQE LVKHFENCKR KDCSYRDCRR SRMVTEHYKA
CVDLQCPVCS NAKKLLQRSA ELASKQKPPE PRKIAQQNTA QRIMNGVEGD IMDIDLVSDE
IFDSQPSVPK RLKMQPVSPS TAEREVSMPS NAGLILQETH SELPDQNNKV GQLKMDVKID
PRPLQKPAKI GYGTDGNVPT ARHNVAPGGS NEIKTHVKQE IMPIDKETSE TAPEVKNEAN
DSTDITVSKS GKPKIKGVSM TELFTPEQIQ EHINSLRLWV GQSKAKAEKN QLMGHNENEN
SCQLCKVEKL TFEPPPIYCS PCGARIKRNA PYYTVGTGDT RHFFCIPCYN ESRGDTIEVE
GQNFLKARFE KKRNDEETEE WWVQCDKCEC WQHQICALFN GRRNDGGQAE YTCPNCYVEE
VKRGLRMPLP QSAVLGAKDL PRTVLSDHIE DRLFKRLKQE RQDRAAQERK SIEEVPGAEG
LVVRVVSSVD KKLEVKPRFL EIFQEDNYPT EFPYKSKAVL LFQKIEGVEV CLFGMYVQEF
GAECSYPNQR RVYLSYLDSV KYFRPEIRTV SGEALRTFVY HEILIGYLEY CKQRGFTSCY
IWACPPLKGE DYILYCHPEI QKTPKSDKLR EWYLSMLRKA TKEEIVVELT NLYDHFFITM
GECKAKVTAS RLPYFDGDYW PGAAEDMINQ LRQEEDDRKQ QKKGKTKKII TKRALKAAGH
TDLSGNASKD AMLMHKLGET IYPMKEDFIM VHLQYSCSHC CTLMVSGKRW VCHQCRSFYI
CDKCYDAEQQ LEDRERHPSN SRDTHTLHPV DIVGLPKDTK DRDDILESEF FDTRQAFLSL
CQGNHYQYDT LRRAKHSSMM VLYHLHNPTA PAFVTTCNVC CHDIETGQGW RCEVCPDFDL
RKMLDLLVHA STCRSGSCQY PNCRKVKGLF RHGMQCKTRA SGGCVLCKKM WYMLQLHARA
CRDSGCNVPR CRDLKEHLRR LQQQSDSRRR AAVNEMMRQR AAEVAANE
