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   16-JUN-2009, entry version 29.
DE   RecName: Full=Probable histone acetyltransferase HAC-like 1;
DE            EC=2.3.1.48;
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
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=17210932; DOI=10.1101/gr.5509507;
RG   The rice annotation project (RAP);
RT   "Curated genome annotation of Oryza sativa ssp. japonica and
RT   comparative genome analysis with Arabidopsis thaliana.";
RL   Genome Res. 17:175-183(2007).
CC   -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC       specific tag for transcriptional activation (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SIMILARITY: Contains 2 TAZ-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD10378.1; Type=Erroneous gene model prediction;
CC       Sequence=BAD10522.1; Type=Erroneous gene model prediction;
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DR   EMBL; AP005647; BAD10522.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP005474; BAD10378.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008208; BAF07744.1; -; Genomic_DNA.
DR   RefSeq; NP_001045830.1; -.
DR   UniGene; Os.59276; -.
DR   GeneID; 4328238; -.
DR   KEGG; osa:4328238; -.
DR   Gramene; Q6YXY2; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR009255; Trans_coact.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR000197; Znf_TAZ.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.20.1020.10; Znf_TAZ; 2.
DR   Pfam; PF06010; DUF906; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   SMART; SM00551; ZnF_TAZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
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; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1668       Probable histone acetyltransferase HAC-
FT                                like 1.
FT                                /FTId=PRO_0000269745.
FT   ZN_FING     651    732       TAZ-type 1.
FT   ZN_FING    1002   1079       PHD-type.
FT   ZN_FING    1411   1458       ZZ-type.
FT   ZN_FING    1553   1634       TAZ-type 2.
FT   COILED     1342   1365       Potential.
FT   COILED     1630   1650       Potential.
FT   COMPBIAS    111    135       Gln-rich.
FT   COMPBIAS    397    620       Gln-rich.
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
//