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Database: UniProt
Entry: A0A0E0JVA9_ORYPU
LinkDB: A0A0E0JVA9_ORYPU
Original site: A0A0E0JVA9_ORYPU 
ID   A0A0E0JVA9_ORYPU        Unreviewed;      1684 AA.
AC   A0A0E0JVA9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G02380.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC02G02380.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC02G02380.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC       specific tag for transcriptional activation.
CC       {ECO:0000256|ARBA:ARBA00002581}.
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:0000256|ARBA:ARBA00000780};
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DR   STRING; 4537.A0A0E0JVA9; -.
DR   EnsemblPlants; OPUNC02G02380.1; OPUNC02G02380.1; OPUNC02G02380.
DR   Gramene; OPUNC02G02380.1; OPUNC02G02380.1; OPUNC02G02380.
DR   eggNOG; KOG1778; Eukaryota.
DR   HOGENOM; CLU_002956_2_0_1; -.
DR   OMA; MVPNGGM; -.
DR   Proteomes; UP000026962; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; -; 1.
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; 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:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF08214; HAT_KAT11; 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; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
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; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          651..721
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   DOMAIN          1083..1509
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51727"
FT   DOMAIN          1511..1563
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          1569..1650
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..292
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          875..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1684 AA;  190073 MW;  FC8046F0B7C6CEA0 CRC64;
     MNVGQAAHLS GQMSGQAPQI NQVGGSGVSG ADGLPQQMQD VVGLGGLDAQ FLMMRNTMRD
     RIFEYIGRKQ SSTDWRRRLP ELAKRLEEIL YRKFLNKTDY YNMMRGPVEP QLQFAIKTLS
     AQNQQNQQNQ QMPRQMASSS GYGTMIPTPG ITQSATGNSR MPYVTDNTGL PSSGATMVPQ
     GANTGSMSNG YQHLTTSVPL NSTTSSIPST MGPVGVQRQV THMIPTPGFN NQQNVPANPD
     FSNGAGYFNG ESTVTSQMQQ QKQFPSNQNS HQIQHIGGHS NSGMHSNMLE NSSAYGLSDG
     HVNGGMGVHG SNMQLTNRSA VSEAYINISP YGNSPKPVQQ QFNQHPPQRI PTPVDISGSG
     NFYNTGSSAL TAANNHNMGA TNLPSRSRMN SMLHTNQLNM QSIQPQPQIK TEVLDQPEKM
     NFQSSQLTHE QLIRQQHSMQ QHQMQPSSQF VQNQYHLNQQ QPNSQHQQSI LRSNSLKQPQ
     LSSSHSMQLS EQGALPHTEL ISSQATEHTD LPIYQGQYQQ RSAHDNVKGG QVFGHLSSSQ
     NFHSNASHDS QQLLPTNQQL DDSSNDVSYV LKGSQPEQMH QAQWRPQKME KAPVTNDSSL
     EKQIQADLCQ RTMSQDGAQQ PFSSDWRLSG CTVTPADPAL PKLPSGGLEQ AAGNIYYFRQ
     MKWLLLLFHA KSCLTPVQEL VKHFENCKRK DCSYRDCGRS RMVTEHYKAC VDLQCPVCSN
     AKKLLQRSAE LASKQKPPEP RKIAQQNTAQ RIMNGLEGDI MDIDPVSDEI FDSQPSVPKR
     LKMQPVSPST AEREVSMPSN AGLILQETHS ELPDQNNKVG QLKMDVKIDP RPLQKPAKIG
     YGTDGNVPTA RHNVAPGGSN EIKTHVKQEI MPIDKETSET APEVKNEAND STDITVSKSG
     KPKIKGVSMT ELFTPEQIQE HINSLRLWVG QSKAKAEKNQ LMGHNENENS CQLCKVEKLT
     FEPPPIYCSP CGARIKRNAP YYTVGTGDTR HFFCIPCYNE SRGDTIEVEG QNFLKARFEK
     KRNDEETEEW WVQCDKCECW QHQICALFNG RRNDGGQAEY TCPNCYVEEV KRGLRMPLPQ
     SAVLGAKDLP RTVLSDHIED RLFKRLKQER QDRAAQERKS IEEVPGAEGL VVRVVSSVDK
     KLEVKPRFLE IFQEDNYPTE FPYKSKAVLL FQKIEGVEVC LFGMYVQEFG AECSYPNQRR
     VYLSYLDSVK YFRPEIRTVS GEALRTFVYH EILIGYLEYC KQRGFTSCYI WACPPLKGED
     YILYCHPEIQ KTPKSDKLRE WYLSMLRKAT KEEIVVELTN LYDHFFITMG ECKAKVTASR
     LPYFDGDYWP GAAEDMINQL RQEEDDRKQQ KKGKTKKIIT KRALKAAGHT DLSGNASKDA
     MLMHKLGETI YPMKEDFIMS LLYPYGVWKT LGLPSMQKLL HMCYDAEQQL EDRERHPSNS
     RDTHTLHPVD IVGVPKDTKD RDDILESEFF DTRQAFLSLC QGNHYQYDTL RRAKHSSMMV
     LYHLHNPTAP AFVTTCNVCC HDIETGQGWR CEVCPDFDVC NSCYQKGAVN HAHKLTNHPS
     AADRDAQNKE ARQMRLRKML DLLVHASTCR SGSCQYPNCR KVKGLFRHGM QCKTRASGGC
     VLCKKMWYML QLHARACRDS GCNVPRCRDL KEHLRRLQQQ SDSRRRAAVN EMMRQRAAEV
     AANE
//
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