ID A0A1B6PDV0_SORBI Unreviewed; 1263 AA.
AC A0A1B6PDV0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=SORBI_3008G149800 {ECO:0000313|EMBL:KXG23863.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG23863.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG23863.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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; CM000767; KXG23863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6PDV0; -.
DR EnsemblPlants; KXG23863; KXG23863; SORBI_3008G149800.
DR Gramene; KXG23863; KXG23863; SORBI_3008G149800.
DR eggNOG; KOG1778; Eukaryota.
DR OMA; CERCYAE; -.
DR Proteomes; UP000000768; Chromosome 8.
DR ExpressionAtlas; A0A1B6PDV0; baseline and differential.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000000768};
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 691..1117
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1000..1063
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1164..1248
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 366..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 143429 MW; 4B24F0D1F941D6F3 CRC64;
MMTQTLQGKV MAYTPSSFPV QQQILPEDIE MLQLDNMNQN TSPIRAIIIE KIEACLRNME
EFCDLCPDSC LKASRIIDNM LYKNAPQLHF YLDLETVEGR VNDLLRSFPY RKQRDPCISS
AVPSTKDLRQ LPGIQMTDSS VYHNRVAPAF TNLPAHSGDV PPHTVFTSQR YVPQNHNMAA
ANLALVERPE SFMSTVVAPS VSGLPNCISG LGGIDSAGLQ NGYLKDHFPG DAYHVDSPQP
SMSGSSSPLS AVCDPTTSSG AMIRSSVDSV SKASGQKLFT REEQLFQQYR EYEKELDGAW
SHPAEKAVHS NRTTQSNEIY FKEECRPDTF MEMKENYWHT SDSRDSCREI YSNLSTPNAQ
YQCFMSDCDP RDPEREIVER SEQTSNSTVS KPTSPISDES SGKRPAKRLK ADAPTLVNVN
QVESSKDQKP VTNENHVSGG ETVQSEITEL PAKSPCSSLG DINTDSNNML EQGSEDAPNT
ELVKEEELYC AKGDIEMNEA NTVAFDQTPR GVSLSTRRKR GASILYALTA EELRDHMSSL
INQHTCLGKV ISQEFPSIDG LPDQNTCSLC GMERLLFEPP PRFCGLCFKI INSAGCYYVE
VENGIEKTSI CSKCHHLSSS RAKYQKKFNY AETDAEAEWW VQCDKCKAWQ HEICALFNRK
CEGAKAEYTC AKCFLNEKDS GDIQALESST VLGAQELPRT KLSDHIEQRL SERLEQDRQQ
RASASGKVAE EVPGVKGLTV RVVSSAERIL QVQPRFRDFF KQEKYPGEFP YKSKAILLFQ
KIEGVDVCLF AMYVQEYGSD CPSPNQRHVY LAYIDSVKYF RPEIKSASGE ALRTFVYHEI
LIGYLDYCKK RGFVSCSIWA CPSTKRDDYV LYCHPTVQKM PKSDKLRSWY QNLVKKAVKE
GVVVERNTLS DFFLQPTNEC KANISAACLP YCENDFWPGE AERLLEKKDD NTSQKKETQV
GRLLRVAKRD DRKGNLEDIL LVHKLGERMR TMKEDFIMLC LQQFCKHCHQ PIISGKSWVC
TSCKNFHLCD KCHAEEQNTA QKDRHPATTK QKHAFQRMEV EPLPETDDGD PTMESKYFDS
RIDFLKHCQD NQFQFDTLRR AKHSTMMILY YLHNSTCSAC HRAVDQCLVW RCLECLGCTF
CDQCYKQNGQ SLHSHELRQI HTSETLQKHT LQDYIDGLLH ASRCYDPRNC THPVCLTLKK
LFFHGVRCDI RARNWSGCNK CVFMWKLLLC HSKDCNDVNC SVPRCRDIKA YIAEKLKVVG
PVL
//
