ID A0A1D6QUF5_MAIZE Unreviewed; 1658 AA.
AC A0A1D6QUF5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE Flags: Fragment;
GN ORFNames=ZEAMMB73_Zm00001d054003 {ECO:0000313|EMBL:AQK61011.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK61011.1};
RN [1] {ECO:0000313|EMBL:AQK61011.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK61011.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000780; AQK61011.1; -; Genomic_DNA.
DR ExpressionAtlas; A0A1D6QUF5; baseline and differential.
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; 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.
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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AQK61011.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 631..712
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 1080..1516
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1398..1461
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1518..1570
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1576..1658
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT NON_TER 1658
FT /evidence="ECO:0000313|EMBL:AQK61011.1"
SQ SEQUENCE 1658 AA; 186929 MW; DC8AD8B5B63954B4 CRC64;
MNVGHAAHLS GQTAHMNQVP GSGVGIGVGG SDGLPQHQPM QEMAALSGMD QQFVMLRTAM
RDKISDYIGR KQSPGDWRKR LPELAKRLEE ILYRKFPNKH EYYNMMKGPV EPQLQFAIKT
LSAQNQHNQQ NPQMTRQISS SSSYGAMIPT PGMVPQNANM GTSMQGPMSN GYQHLNTNIS
QNSTTNNVES TMGSVGVQRQ LSHMIPTPGF SNQQNVPSNP DYSNGTGYFN GESAVAPHMQ
HQKQFPSNHN SNQIQHIGGH NNSGIHSSLL DNSSAYGLSD GHMNGGIGVH GSNMQLTNRT
TAPEAYMNIS SYGNSPKPMQ QQFNQHPQQR IPTSVDMAGS GSFYAIGSTP LTTANSQSMN
VANLQSRSSM NQMLVSNQLN IQSVQQQSQI KNGPLDQTEK VNFQSTQLTH DQLLHQHPMS
QHQVQPNSQF IQNQYHINQQ QPNSQHQQAM LRNNSLKQSQ MASNHSMQLP EQGTLPHTEL
VSSQASDPAD LPNFQGQYQQ RNALDNVKGG QMLGHLSSSQ NFLPSASHGS QQLLPSNPQL
DNGSNAVSYV LKGSQTEQML LSQWQPQTME KAPVATNSSL EKQVQEDCCQ RIMSQDGVQQ
PFSSDWCLSN GTLASVDPAV PKPTAGGFGQ VKRNIHYLRQ IKWLLLLFHA KTCTYPVGSC
KFNGCVQVQE LLNHFQNCQR KDCSYRSCTK SKAMSHHYKT CVDEQCPVCS VVRKFLRQST
EQASKQKTLE SRKLAQQNVP QRIMNGIEGD RMDVDPMSAE AFEDQPSVPK RLKMHLPSLS
GPENDISVVS NHHVNPGFLL QEAQPEQLEH NNRTTYLKRE VDAKADIRAP QKPIKISYDI
DENVTTSRHN VIPGVPSEMD SHIKQENLSV NKETSETALE VKNETNDLTD ATVTKSGKPK
IKGVSMIELF YPDEVDVHID SLKLWVGQSK AKAEKNQAIG HSENENSCQL CRVEKLTFEP
PPMYCSPCGA RIKRNAPYYA VGTGDTRHYL CIPCYNESRG ETIEVEGQTF PKAKLEKKRN
EEETEEWWVQ CDKCQCWQHQ ICALFNGRRN GGGQAEYTCP HCYVEEVKCG LRKPLPQSAV
LGAKDLPRTV LSDHIEDRLF KRLKQEKQDR AAAAGKSIDE IPGAEGLVVR VVSSVDKKLE
VKPRFLEIFQ EDNYPTEFPY KSKAVLLFQR IEGVEVCLFG MYVQEFGAEC SSPNQRRVYL
SYLDSVKYFR PEIKTVSGEA LRTYVYHEIL IGYLEYCKLR GFTSCYIWAC PPLKGEDYIL
YCHPEIQKTP KSDKLREWYL SMLRKASKEE IVVELTNLYD HFFITMGGCK AKVTASRLPY
FDGDYWPGAA EDMINQLRQE EDDRKLQKKS KTKKIITKRA LKAAGHTDLS GNASKDAMLM
QKLGETIYPM KEDFIMVHLQ YSCSHCCTLM VSGRRWVCHQ CRSFYICDKC YDAEQQLEDR
ERHPCNSRDT HMLHPVDIVG VPKDTKDRDD ILESEFFDTR QAFLSLCQGN HYQYDTLRRA
KHSSIMVLYH LHNPTAPAFV TTCNACCHDI ETGQSWRCEI CPDFDVCNAC FQKGAVTHPH
KLTNHPSAAD RDAQNAEARQ MRVQQLRKML DLLVHASMCR SGSCQYPHCR KVKGLFRHGM
QCKTRASGGC VLCKKMWYML QLHARACKDS ECKVPRCR
//
