ID G4ZB91_PHYSP Unreviewed; 1223 AA.
AC G4ZB91;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=PHYSODRAFT_491564 {ECO:0000313|EMBL:EGZ22057.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ22057.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ22057.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ22057.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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DR EMBL; JH159153; EGZ22057.1; -; Genomic_DNA.
DR RefSeq; XP_009524774.1; XM_009526479.1.
DR AlphaFoldDB; G4ZB91; -.
DR STRING; 1094619.G4ZB91; -.
DR EnsemblProtists; EGZ22057; EGZ22057; PHYSODRAFT_491564.
DR GeneID; 20656721; -.
DR KEGG; psoj:PHYSODRAFT_491564; -.
DR InParanoid; G4ZB91; -.
DR OMA; HAQNSSC; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640};
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}.
FT DOMAIN 391..463
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 664..1111
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT REGION 222..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 137865 MW; C62D6612A0C02BE9 CRC64;
MEVQEAASRL LACPRLSRER EAERQRAIQR PLAVSWREKV EENGQKQQRQ VATRSNVVWE
QHHIPGVRKR RMDEEDAAFL LFYGERESSS ADILRLIVEL ISTGVGSSDT FVSRLVKYML
WRKLSSAVAA GLASERVVQS EWTKIVFSCP VPPHRRRSGP MPRPDLLPRP ITITVRPLQF
ARKQPQRRSL CVPSGGVEIV TKHEPSSPRA TPQEAAVALA NKLAGKGARS KSGAKSPKKS
TKAAQTKSPR GAVRKRPLAA TYDEDTPTSN GYTNGAEFSP RKQRRRNGEV GVPTVTPRQV
VRAKSSNGQS ISQKLMEPLP YDCRTLGDNR SLPIGWKPPG DQPLRVDLVE VNPMLQMTAD
EIAQHIGSVR QEGRFTSFEK VTDILLKLMS DPRNRHGVFN TPVDPVALEL PTYTTIVQHP
MDLGTIKRNL AAGEYLELED FVSDVRLVFE NAMLFNPESH YIHVDAEVLL KRFNDSVKAE
EKRQAKRQRV QHACLVCRGN TCIVCNQQCL EVTQPHLQCS GGCSTDIRKG SVYFVSEDGT
RVWCQKCRTR LARDRNSPDR EPDDDTDALL DSLIKKKCEA GVEPWVKCGE CDRWLHQVCG
LYNPVIGAYE SEKALKKEAE GLSIETGPSY ACPLCRCRRK RATPSPESPM RKILHVDPDE
HAQNSSCLNI PSCELSIFIQ NFLRRGLDKI GEREAAQTLY VRALSFPGER MAVPEAVVRT
FDENVELLAQ VRPGKDTSSQ RIPAHISYLS RGLYLFQKHE GMEVCLFTIY AQEFGDDCEL
EANRRAVYIA YLDSVRYLKP ASARTAAYHL ILLAYFDYVR RHGFSRVHIW SCPPQKRISY
VFWCRPSFQK TPSAEHLRRW YNKLLTKAKD CGIVKDWTTM YDRYFSESVC GAVAKDDSKS
SASFVSVKEE NGVGVSTRGT TVQSVNPNEL EWPAKQLPPI FDGDIIPSEL DRILGRIMSR
NEKQKRASEN KKLAARGKSS SIARAGGKLS VGGVITRIKE EAPTCIAPPS VPASLQVDVK
VREVFSKCQF AVQRLKQDLL VVDLVTLDGE QAEGCRPEAL VPSWCSQVPR FFGSRFMFHQ
LCSYAGYQFD SLRRAKHSTM MMLHHYFNEQ VAQLNVFCRE CNLLITRADF WSCRSCKRYA
LCDSCYRRQG KEHEHELVFG PAPLPTPPRA SAANSEHAAH PAQQQQQQDE PMEPQPAQVQ
TLLSHRSRKP STYLTAVPPR PES
//
