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Database: UniProt
Entry: A0A022PQ82_ERYGU
LinkDB: A0A022PQ82_ERYGU
Original site: A0A022PQ82_ERYGU 
ID   A0A022PQ82_ERYGU        Unreviewed;       549 AA.
AC   A0A022PQ82;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=MIMGU_mgv1a004007mg {ECO:0000313|EMBL:EYU17891.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU17891.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU17891.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008607}.
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DR   EMBL; KI632344; EYU17891.1; -; Genomic_DNA.
DR   RefSeq; XP_012829023.1; XM_012973569.1.
DR   AlphaFoldDB; A0A022PQ82; -.
DR   STRING; 4155.A0A022PQ82; -.
DR   GeneID; 105950225; -.
DR   KEGG; egt:105950225; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   OMA; FAQPVNR; -.
DR   OrthoDB; 1760108at2759; -.
DR   PhylomeDB; A0A022PQ82; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010484; F:histone H3 acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR000182; GNAT_dom.
DR   PANTHER; PTHR45750; GH11602P; 1.
DR   PANTHER; PTHR45750:SF3; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          197..351
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          452..523
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  61791 MW;  4337861758BBDC67 CRC64;
     MDGHSSHLTA PVRSRSSQSP SPSHSASASA TSSIHKRKLQ PDDHALPFPP SFSDTRDGAL
     TSNDDLESIS VRGADSDSDD ESEEVVDDEE EEYDNSMRNF TSSRLENTNA GGPPTARNTK
     IKAENSVKVE PADVSKDGNT NTNNSGAPVA TGGNGSIPGI VVKEDTVKSI FTDNIQTSGA
     YSAREESLKR EEEAGRLRFV CASNDGIDEH MVWLIGLKNI FARQLPNMPR EYIVRLVMDR
     NHKSVMVVRR NLVVGGITYR PYLSQKFGEI AFCAITADEQ VKGYGTRLMN HLKQHARDVD
     GLTHFLTYAD NNAVGYFVKQ GFTKEIYLER DRWHGYIKDY DGGILMECRI DPKLPFTDIS
     TMIRRQRQAI DEKIRELSNC HIVYPGIDFQ KKEAGIPKKT IKVEDIPGLR EAGWTTEQYG
     HSRFKTVTLS TDATSHQKSL TAFMRSLIKA MHDHPDAWPF KEPVDARDVP DYYEIIKDPM
     DLKTMSKRVE SEQYYVTFEM FVADVRRMFS NARTYNSPDT IYYKCSTRLE GHFSNKVQAG
     LQSGIKIQP
//
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