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Database: UniProt
Entry: A0A0L8HFF6_OCTBM
LinkDB: A0A0L8HFF6_OCTBM
Original site: A0A0L8HFF6_OCTBM 
ID   A0A0L8HFF6_OCTBM        Unreviewed;       852 AA.
AC   A0A0L8HFF6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=OCBIM_22015912mg {ECO:0000313|EMBL:KOF87864.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF87864.1};
RN   [1] {ECO:0000313|EMBL:KOF87864.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF87864.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF87864.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ418303; KOF87864.1; -; Genomic_DNA.
DR   RefSeq; XP_014772776.1; XM_014917290.1.
DR   AlphaFoldDB; A0A0L8HFF6; -.
DR   STRING; 37653.A0A0L8HFF6; -.
DR   EnsemblMetazoa; Ocbimv22015912m; Ocbimv22015912m.p; Ocbimv22015912m.g.
DR   EnsemblMetazoa; XM_014917290.1; XP_014772776.1; LOC106871034.
DR   GeneID; 106871034; -.
DR   KEGG; obi:106871034; -.
DR   OMA; YFQTKMR; -.
DR   OrthoDB; 1760108at2759; -.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
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; 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   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:ARBA00023212};
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          521..669
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          760..830
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  97233 MW;  78A40E306EE879CA CRC64;
     MASTNGDTSS VITSSNLSSS VAMSQVSTTE TTVLTASMSN STASTTESQS TTTITTGRQI
     SQPSTTGEMS RSNTMQRIAH KKAMVKGYPR PKKLEKLAVY SSCKTEGCNC NGWKNPNPPP
     TPPRVDVSQP LASLTDPCRS CSHTLGAHVS HLENVAEEEL NRLLRIVVDV ENLFMCVHKE
     EDTETKRVYF HLFKLLRKCI MNMCKPSIDM AIGTPPFEKP SIAKGVTNFV LYKFGHLAQK
     EWQTMYDLAK MFLHCMNHWK LENPTLHTQH TNMDDRNNYQ SNYTRWLCYC HVPALCDSLP
     RYETTLIFGR TLLRSVFETM RRQVLDKFRA EKEMMPPEKR TLVLTHFPRF LSMLEEEVYG
     NNSPIWDPDF CQSTTGMSLS PSRISGNAFI ASTNASTVGG VNRFTNSTPT TSTASGTEGS
     NTVKSNYSTP TNSHPTKTKD GGTGDKRHLD EIQTSEVIKK RKIEGDVDQE LVAEIVSLIT
     DPEHMVGPDK TLFPTHAARD EIARQEEGKG VIEFKVMANT FTERPSREQL IWLIGLQNVF
     SHQLPRMPRE YITRLVFDPK HKCLALIKEN RVIGGICFRM FPTQGFTEIV FCAVTSNEQV
     KGYGTHMMNH LKDYHIQHGI LHFLTFADEY AIGYFKKQGF SKDIKLQKSA YLGYIKDYEG
     ATLMGCELNP RIHYTCFSQI IRRQKEIVKK ILEKKQELQD KVYPGISCFK EGVRQIPVES
     IPGLLEAGWK TSPNNNIQKE PDPDPERLQS VLKMILLQVK NHQSAWPFQK PVDKTEAPDY
     LEHIRFPMDL KTMSDRLKNR YYCNKRLFTA DMTRIFTNCR AYNQPDTDYY KCANTLDKFF
     QSKLKEYNLW DK
//
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