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Database: UniProt
Entry: H3H0Z0_PHYRM
LinkDB: H3H0Z0_PHYRM
Original site: H3H0Z0_PHYRM 
ID   H3H0Z0_PHYRM            Unreviewed;      1304 AA.
AC   H3H0Z0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra83858, ECO:0000313|Proteomes:UP000005238};
RN   [1] {ECO:0000313|Proteomes:UP000005238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
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).
RN   [2] {ECO:0000313|EnsemblProtists:Phyra83858}
RP   IDENTIFICATION.
RC   STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra83858};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
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DR   EMBL; DS566095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 164328.H3H0Z0; -.
DR   EnsemblProtists; Phyra83858; Phyra83858; Phyra83858.
DR   VEuPathDB; FungiDB:PSURA_83858; -.
DR   eggNOG; KOG1474; Eukaryota.
DR   eggNOG; KOG1778; Eukaryota.
DR   HOGENOM; CLU_003823_0_0_1; -.
DR   InParanoid; H3H0Z0; -.
DR   OMA; HAQNSSC; -.
DR   Proteomes; UP000005238; Unassembled WGS sequence.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR001965; Znf_PHD.
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   SMART; SM00249; PHD; 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:UP000005238};
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          455..527
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          726..1186
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51727"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          42..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1243..1288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1243..1267
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1268..1288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1304 AA;  146734 MW;  0FBAF8535D93077A CRC64;
     MEVHEAASRL LACPRLSRER EAERQRAIHR PLAVNWREKV EVNGQEEEEE QDAAKSQVKR
     PLNVKKELPA PGPEVVTIDS DSDDADEAPY EVEESVRTKR KLEELSVPVE RKQHRHQVAT
     KDKVVWEQLH VAGVRRRRLG EEDAAFLLFY GDRETPSAGI LRLIVGSTDE FLTRFVKYLL
     WRKLSAAVDA GLVSERLVQS EWTKIVFSCP VPPHRRRSGP MPRPELLPRP VTITVRPLQF
     ARRQPQRRSL CVVNSSAELA TKQEPLSPRT TPEEAAIALA NRLAGKGARK SSAKSPKKSS
     KAPQTKSPRG EVRKRPLGGS TYSEGVAGVN GYSQAAGFSP RKQRRRNGEV SVPPVTPRQV
     VRAKGSGGKS ISQKLMEPLP YDCRTLGENR SLPLGWRPPG RCGGEASHAL DPVEVNPMLQ
     MTADEIVQHI ASVRREGRFT SFEKVTDILL KLMSDPRNRH GVFNMPVDPV ALDLPTYTMI
     VQHPMDLGTI KRNLTAGEYL ELEDFVSDVR LVFENAMLFN PESHYIHVDA ETLLKRFNES
     VKAEQNRQAK SKRVQHVCLV CRGNTCIVCN QQCLPITQPH LQCSAGCSTD IRKGSVYFIS
     EDGTRVWCQK CKTRLARDRS STDRMTDDTN SFLDSLIKMK SEPSVEPWVK CGECDRWLHQ
     VCGLYNPVIG AYETQKAQTP EPGGLVMETN PYLCPLCRCR RKRAIPPPES PMRTILNADL
     GEHARSSSCL NIPSCELSIF IQNFLRRGLR DIGEHEAAQT LHVRALSFPG ERMTVPEGVV
     QAFDENAELL AQLRPGTDTS AQRLPAHVSY LSRGLYLFQK HEGMEVCLFT IFAQEFGDDC
     ELAANRRAVY IAYLDSVRYL KPASARTAAY HLIMLAYFDY VRRHGFSRVH IWSCPPQKRI
     SYVFWCRPIF QKTPSAEHLR RWYNKLLTKA KEHGIVKGWS TMHDRYFSES VCSSTAADDS
     KPPASFVSMK EESGVGVSTR GTTVLSVNPD ELVWPVNQLP PIFDGDIIPS ELERILGRII
     SRNEKQKRAS ENKKLAVRGK SSSVARAGGK LSVGNVVTRI KDEVSTAQTA APPSLQLDVK
     VREVFAKCQF AVQRLKQDLL VVDLEVPSEE ETKEDQVGTG FAGERHTKGC HPETLVPSWY
     GQVPRFFGSR FMFHQLCSYS SYQFDSLRRA KHSTMMMLHH YFNERVVQLN VFCRECSLLI
     TRADFWSCRS CERYALCDAC FRRAGNEHPH QLVFGPAPPF PPRIQQMPEH PAAPVPLSPP
     PPQQQQHLAP QRPNLQSEQV QSVASATSVQ PSALSPTVNV CELC
//
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