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Database: UniProt
Entry: A0A099P7B8_PICKU
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ID   A0A099P7B8_PICKU        Unreviewed;       558 AA.
AC   A0A099P7B8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   ORFNames=BOH78_2429 {ECO:0000313|EMBL:ONH74327.1}, C5L36_0A11210
GN   {ECO:0000313|EMBL:AWU74538.1}, JL09_g102
GN   {ECO:0000313|EMBL:KGK40825.1};
OS   Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK40825.1, ECO:0000313|Proteomes:UP000029867};
RN   [1] {ECO:0000313|Proteomes:UP000029867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX   PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA   Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT   "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL   Microb. Cell Fact. 13:121-121(2014).
RN   [2] {ECO:0000313|EMBL:KGK40825.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD108 {ECO:0000313|EMBL:KGK40825.1};
RA   Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT   "Exploiting Issatchenkia orientalis SD108 for Succinic Acid Production.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000189274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129 {ECO:0000313|Proteomes:UP000189274};
RX   PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA   van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT   "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT   and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT   Zimbabwe.";
RL   Genome Announc. 5:E00064-E00064(2017).
RN   [4] {ECO:0000313|EMBL:ONH74327.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129 {ECO:0000313|EMBL:ONH74327.1};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:AWU74538.1, ECO:0000313|Proteomes:UP000249293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS573 {ECO:0000313|EMBL:AWU74538.1,
RC   ECO:0000313|Proteomes:UP000249293};
RA   Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA   Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT   "Population genomics shows no distinction between pathogenic Candida krusei
RT   and environmental Pichia kudriavzevii: One species, four names.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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};
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; CP028773; AWU74538.1; -; Genomic_DNA.
DR   EMBL; JQFK01000001; KGK40825.1; -; Genomic_DNA.
DR   EMBL; MQVM01000010; ONH74327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099P7B8; -.
DR   STRING; 4909.A0A099P7B8; -.
DR   VEuPathDB; FungiDB:C5L36_0A11210; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   HOGENOM; CLU_015741_2_0_1; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000029867; Unassembled WGS sequence.
DR   Proteomes; UP000189274; Unassembled WGS sequence.
DR   Proteomes; UP000249293; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
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:UP000249293};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000313|EMBL:ONH74327.1}.
FT   DOMAIN          215..370
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          458..528
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  63725 MW;  49DEB7417EDB2B9C CRC64;
     MPPVKRRSDR THVGKNDVKR PKIKGADTQL SDGKDKTAIV NVDGDQTKGT EETEKMAEQN
     LGSSNEEEVC GGFKSENNED AENENENENE NEIENEIEID NKNEIEQESL GTDDNHNNGH
     DEHDEKQADG HKESDLKNEP KEQAKEEGTG DQNNGNQADN GSVQDTVDPI IAGEGADEEE
     VNDEDSKRVH TFTFDGCQYT YKDRPSVIEE KTGDIEFRVV NNDDSRDSMI ILTGLKNIFQ
     KQLPEMPKAY IARLVYDRSH VSIAVVRKPL TVVGGITIRP FESHEFAEIV FCAISSTEQV
     RGYGAHLMNH LKDYVRNTSK IKYFLTYADN YAIGYFKKQG FTKDITLPKH VWMGYIKDYE
     GGTLMQCSML PKIRYLDSNK ILALQKASIL SKIRTIGKSH VVYKGLDYFK KKNFEPLNPF
     NIPGLKEAGW TREMDDLAQK PKRGAHYIAM LTILTEMQNH PSNWPFVQPV SRTDVPDYYE
     VIKEPMDLST MEVKLENDAY QTMEDFIYDC KLIFNNCRQY NGENTTFYKN ANKLEKAVIA
     KLKDFPEYSH CLDTLTHR
//
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