ID A0A1B0AR68_9MUSC Unreviewed; 799 AA.
AC A0A1B0AR68;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Glossina palpalis gambiensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI005539-PA, ECO:0000313|Proteomes:UP000092460};
RN [1] {ECO:0000313|Proteomes:UP000092460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPPI005539-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI005539-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000256|ARBA:ARBA00008607}.
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DR EMBL; JXJN01002267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0AR68; -.
DR STRING; 67801.A0A1B0AR68; -.
DR EnsemblMetazoa; GPPI005539-RA; GPPI005539-PA; GPPI005539.
DR VEuPathDB; VectorBase:GPPI005539; -.
DR Proteomes; UP000092460; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05509; Bromo_gcn5_like; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR016376; GCN5/PCAF.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR009464; PCAF_N.
DR PANTHER; PTHR45750; GH11602P; 1.
DR PANTHER; PTHR45750:SF3; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF06466; PCAF_N; 1.
DR PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 467..613
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 707..777
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 532
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
SQ SEQUENCE 799 AA; 91456 MW; B063DC6E1EAF7747 CRC64;
MSGGSLIALK EDAIDGNAGS NGNVNQQTHQ QQQQQPQQNG PSSGSASSAP AEGTRQNSLQ
RIQQRKQKVF NLPISQKLAK LSMYSACQAE GCRCTGWKTP QENRHRDVES SYCPEFNEEC
RNTNCRHTLQ SHIAHLDGIS GVEMNNLLGA IIDMENLFMS MQRVDDEDTK KVYLYLFRLL
RQCVITRQQA VIRGPLGDPP FESPCIAKAV YSFVFYKYHH LSPNELQTMT EVAKTFLNFL
NHYNFEPPSL RKADLKNEDA STYKINYTRW LVFCHVPAFC NSLRHFETSL VFGRTLLRTV
FQYMAQQLKK KCISERDRFP ADKRSIITQM PKFLEALKGE LLKDESPIWD QTYRPPSAFL
MQQRKRQQDT ATNVSGTVNN ANGKRANIGE PIHKRPKKDV DRNSGDSNYE DLPDETVIRA
MKAVSESKAI NKTEILFPVN VSRDENVKAE EQQRAIEFHV VGNSLTKPVD KETILWLLGL
QSVFAHQLPE MPREYISQLV FDTKHKTLAL IKENMPIGGI CFRPFPSQGF TEIVFCAVTM
SEQVKGYGTH LMNHLKDYSI QKGVLHLLTY ADCDAIGYFK KQGFSKDIKL ARPVYAGFIK
EYDGATLMHC ELHPSIVNTQ FISVIRRQSE ILKELIAERH NEVQKVRPGL TCFKEGLPSI
PVESIPGLRD IGWKPQTRAP RTSRPLEEST DPEKLAASFA AVLQAVRHHA SAWPFLKPVT
AAEVPDYYDH IKYPMDLKTM ADRLKRGYYV TRRLFMADMA HIFSNCRFYN SPETEYYRCA
NNLERYFQTK MRELGLWDK
//
