ID A0A368REX6_SETIT Unreviewed; 1161 AA.
AC A0A368REX6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=SETIT_5G418300v2 {ECO:0000313|EMBL:RCV28624.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV28624.1};
RN [1] {ECO:0000313|EMBL:RCV28624.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV28624.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV28624.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV28624.1};
RA Noorani M.;
RL Submitted (JUL-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};
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DR EMBL; CM003532; RCV28624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368REX6; -.
DR STRING; 4555.A0A368REX6; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 1.
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; IPR001965; Znf_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:SF39; HISTONE ACETYLTRANSFERASE HAC-LIKE 3-RELATED; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02135; zf-TAZ; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00551; ZnF_TAZ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57933; TAZ domain; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 1.
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 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 697..1015
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 898..961
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1062..1146
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 211..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1161 AA; 131123 MW; 00E28367B0CA87AD CRC64;
MTQTLQGKVM ASNAPSSFSI RQQMSPSDFD MLQPDNMDQS TSPIRSIVIQ KIASCLGKRE
LFAKFSPDYL LKISRNIDEL LYRSAPKVRY MDLDTLEARV DALLSSVSYR NHRDSWVSSA
AASTKNLHQL PGIQMTDSSV YHDVVAPGFT NLPARARDVP THTMFTSQRY LPHNYNVVAA
NFPLTVRPES FRTTIVSPCV SVPPKCSSGL GGTASDGLPN GHVKDHFPGD AHPVDSPISS
MSGSSSPLSA VCDPTTSPSA MIRSSMDSVS KASGQKLSAG SDVYSTGEGQ SFQQHREYER
ELDGAWSQPV ELSIQSNRTT ERHELYLKGE CHLDRCMEVE GKYCRVSDCE DLCREKYSSL
STPRAQYQCC FMTDCDPCDP ERERVGRSEQ TSNSTVSKPS STVSDESYGK RPAKRLKADV
PSLVNVNQAE SPKEQKPVVN ENHAYGETVQ SEITELPTKS PCSSSGDINA DTNNTLEQGS
EDVHNMDVVA EEELHCVKGD IEMKDSKTVA LDQTANQVNI SSRRKRGASI LYALTAEELR
DHLSSLINQH TCLSKVISQE IQLIEGLPDQ NTCSFCGMER LLFEPPPRFC ALCFKIINST
GCYYAEVENG KDKTSICSKC HHLSSSRAKY VKRFNYAETD AEAEWWVQCD KCKAWQHEIC
ALFNRKCEGA KAEYTCAKCF LKEKDSGDIH ALESSTVLGA RELPRTKLSD HIEQRLSERL
EQDRQQRANA SAKGAEEVPR VEGLAVRVVS SADRVLQVQP RFHDFFKQEK YPGEFPYKSK
AILLFQKIEG VDVCLFAMYV QEYGSDCPSP NQRHVYLAYI DSVKYFRPEI KSASGEALRT
FVYHEILIGY LDYCKKRGFV SCSIWTCPST KRNLEDILLV HKLGERMRTM KEDFIMLCLE
QFCKHCHQPI VSGRSWVCTS CKNFHLCDRC HAEEQNTAQK DRHPATTKQK HAFQRIEVEP
LPETDDGDPT MESKYFDSRI DFLKHCQDNQ FQFDTIRRAK HSTMMILYYL HNSTCSACHC
AVDQCLVWRC LECLGCTFCD PCYKQNGESL HIHELRQIDA SKTMQMNAIQ DYVEGLVHAS
RCFDPCNCTL QVCLTLKKLF FHGVRCDIRA RNWGGCNKCV FMWKLLLWHS KHCNDANCMV
PRCRDIKAYM TEKIKLGGPV L
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