ID A0A024UP16_9STRA Unreviewed; 2088 AA.
AC A0A024UP16;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-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=H310_02415 {ECO:0000313|EMBL:ETW08044.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW08044.1};
RN [1] {ECO:0000313|EMBL:ETW08044.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW08044.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC specific tag for transcriptional activation.
CC {ECO:0000256|ARBA:ARBA00002581}.
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};
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DR EMBL; KI913954; ETW08044.1; -; Genomic_DNA.
DR RefSeq; XP_008864137.1; XM_008865915.1.
DR STRING; 157072.A0A024UP16; -.
DR EnsemblFungi; H310_02415-t26_2; H310_02415-t26_2-p1; H310_02415.
DR EnsemblProtists; ETW08044; ETW08044; H310_02415.
DR GeneID; 20079465; -.
DR VEuPathDB; FungiDB:H310_02415; -.
DR eggNOG; KOG1474; Eukaryota.
DR eggNOG; KOG1778; Eukaryota.
DR OrthoDB; 54341at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd15614; PHD_HAC_like; 1.
DR CDD; cd02249; ZZ; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 3.
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; IPR036529; KIX_dom_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
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 Pfam; PF02135; zf-TAZ; 3.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00551; ZnF_TAZ; 3.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 3.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 3.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 484..561
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 565..646
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 932..1004
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1183..1760
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1762..1815
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1970..2055
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 28..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1813..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1895..1925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2088 AA; 226673 MW; 036F6657F6DC8252 CRC64;
MFTLLMLHQQ LINTGLQPPP NLIVNPTPTS EATVSTSTPN AATAIPPAAT TTVPPTTSAN
PTAIATATTT IASATPTATP VPTTAIAPPA DLGNAKESSE GAAKTNGSND EWRNKENDRS
ARQHIARIIL SLIMKSANRP ASNSYNPREI ARRLEHTLYM NSSSKEEYSN LTTLKVRLQH
ALDTSRRRQQ EAQLKQAQGT SSSDTTATAV AATTTTTTTA GPMKAPPGVS ASAAAPAALP
SAGLKAPPAS ATAAQAAQLK AAHTQAMQTQ MQLQQAQFQA QMQMLNKVQP PQPGAVSTPA
SGTGSNPAAP APSSNILEEL EREADEMAGS ISDQPLEMPA SELENTTVAT TANANMINMP
INMLNMGMMQ NRGVPYGMNL LNGNAPYVHP QLQLQQLQQM QMQQLQLQKL QQMQQLHHMQ
LNAAAKINQV NNTASTTAAT THLAQPPATT TAGPTSAASA VPSTVPGGGV ALSMPPGLAG
EVTPKQRREE FRKRLIQLKH ARTCQSNPCE EPFCAKVKVL LTHVSNCSDA ECNTIGCKST
RQLLSHYRKC RDMQCYVCSA IRTQNPTGQA FVLRRQQDRL CMLRHASTCA APLCPMAYCV
DMKVLWKHIC ECRQSQCTVD HCISSRYVLS HFKQCQKPDC GVCVPVRHAI KIIDSTKTNP
QELQQLASSC PNDVKVLIRQ MTTVPISLPM QQGGTGALGM MAPQPQSIGD MKPPQSIHLM
GQPLTQAATA PSGVKQEQPL GPPSNLMAAG GATVPPTKVP AKPKAKTKAA AVGTTGVLAG
TPVQATGKTI KTEGKAKKND ANPQPNVAGA PNAIKKPPAS DKEKKEIRKL KAEKAKERQQ
SKLGNNGVKP VQSQIPNNGS TIKMEPEFKI PTVMPASSPT NVLNNEQDFS YLDSMTEAQL
DEHIKSLRFN FCGHISMVEL KNRLMPLLTA VMETEHGWAF NTPVDPIQWN IPDYLEVIKC
PMDLGTIKKR LESEHYVSVE SFASDVRLTF ENCIAYNSST NKFNQAAKQL LVQFETALLA
LKEQLESELK SRCEQRREEM CQLCGGDSFK FAPCMLFCSG PCTGRIRRHT HYYSDPRGEY
HWCSSCYKQM KDGPLDMSLL PVSSSPATND PPLTKAMLLK KKNSEVAEEP WVACDTCKLW
YHQICGLFNE RNHAISGEQE LFVCPFCTIK TRQSGQIPQT KFPLQAKRLP VTRMAARIEK
RVVDALAKAQ GEELARLNSL GNLESDGSSA LHPKTATPPP SFAVTIREVL SVDKQVQIKP
RMSKLFVAKE FIKPGDGTSQ GVKRTKNNGD ASVKKVKVEG ADAKATVSTA VVKREKKDKF
DLTYRSRCIC VFQELDGVDV LIFTLYVQEY GDTCAEPNRG RVYVSYLDSV AYFQPKKFRV
LMHQQVILGF LEDAKIRGYH TAHIWSCPPL KGDDYIFFCK PENQKIPKAA RLRSWYSKLL
QGAKKEGLVY NISNLYAEYY MKRKTALELP YFEGDYWPRL AEDLIKQVEE KAKPSTSSKS
SHRKSSSDGD PNAAIGAAAV PTQADTVDPL AVVSVSGKHS SKNKGEVNLD PIMQKLKAIL
EPQKEDFFVV DLHPRCHKCN ASVINRPYWT LKTLVPTPDP VNDVIEALKK AKTAAVKTSM
LPRHYQHYYC ASCYDSSKNN IQSRVEASVV GAKKAQDIYA AIQAANSDPS TFNYAGHDVL
DVKYELSLTS SVSSLLLEGE SSRADLALEP DTDELMPCEI FDTREAFLMY CQNNHCQFDQ
IRRSKHSSMM VLYHLFNQGT TGFTFSCHKC NMTLTSGKRW NCSICINFNL CEGCRAKTKH
EHPLHPFQIV SIPQPKHKTS AEIDQHNNMD GSNLLLDSAS SSRKKNAKKR PGPKKGKGKG
AGGGGGATKK AKPDMSSAVD EGAATTAAIA QVPMPSPRAT TTITPVAKSP AGPATIASSQ
TNGANDAATA SGAVAAPSSA AVVAAPSATS LSGSSNSSAA AAGAASAQHQ QQRIHNVDPQ
LLVQLEHASL CKLSDACTYT NCNRMRAMLK HGATCEARKV GPCQLCKRIV GLLSAHAKQC
TKPINECQVP RCTEIRRLVE QQQQKQAAAA AAATASSGCQ VQPPPVQQ
//
