ID F0X1N5_9STRA Unreviewed; 2004 AA.
AC F0X1N5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=AlNc14C657G12347 {ECO:0000313|EMBL:CCA27731.1};
GN ORFNames=ALNC14_138750 {ECO:0000313|EMBL:CCA27731.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA27731.1};
RN [1] {ECO:0000313|EMBL:CCA27731.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA27731.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) 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};
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DR EMBL; FR824653; CCA27731.1; -; Genomic_DNA.
DR EnsemblProtists; CCA27731; CCA27731; ALNC14_138750.
DR HOGENOM; CLU_235572_0_0_1; -.
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: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 Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
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; PF00628; PHD; 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; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50134; ZF_TAZ; 3.
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 344..421
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 427..507
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 737..809
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 885..994
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1007..1698
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1700..1753
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1879..1967
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 56..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1972..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1390
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2004 AA; 225247 MW; F3FCAA2C4A22816D CRC64;
MNYNPREIAR RLEHNLYMTA QSKEEYGNVH TLKARLQQAL DQSRRRQLLY QQQSTAFSNP
QHINQQTIQA QARSSSFEGQ GRMQSHTPQG LPVSQYSQSH NQSVPRYHQS VPFSSPVISQ
SGPRSIPVDP VPIQSERLAG YGNSILDELD READEMANGT SDEPIAMPES ERQAINGLNG
NHMTRSNANS PSLTMVPEFA AAQSMNPMTY TSVPLSAPQE ISGPTNSTGN TTAPISTNVS
TSGSNMYHGM NLTDAQMQQI QQLQQFQQLR RMQQLQQMQR QQHVAGSVMP QQPRNPKPLT
PSENGPTISA TPSPILTKEE NPNANTLTAT ASAPPTLSLN QAAIAQKREE LKRRLVQLKH
ARTCTNVECS VDYCGRVKVL LAHVSRCTEA ACSTIGCKST RQLLSHFRKC RNMQCEVCSA
IRPPMNEQEQ RLVLRRQQER LCMLRHVSTC TEAACILPYC ASMKVLWKHI CQCHQRQCRT
DHCISSRYVL SHFKQCNKVV CEVCGPVRRA IKIVDLCKRS AAQLQLAIAQ SPETIRGLIR
IMNTISLSGN ERLNDLDEDD ATTGAVASSD LTVAPAGQTG IDVKEEKAVN LSETLESSSE
LILKRKPLRL QTEKEKKKRR KEQAKIAKAR TLARAQANAP DTIGNRGTSS DVEVFDLSTR
LARARTGTSS LSGLVVRGMP SALRSDQLVT QQDISFLDSM TTEQLDEHIR SLRFNFCGYI
SLTELKNRLM PLLTKLMESE HGWAFNSPVD PVQWNIPDYF DIIKCPMDLG AIKKRLENEH
YNSVDAFAAD VRLVFENCIA YNSSTNKFNI AAKQLLTQFE KNLTSIKSQL ERQLCRRCEQ
RREEMCQLCG GDSFKFAPCM LFCSGPCRGR IRRHTHYYSD PRGEHHWCST CYKQMKDGPI
DLTALPQLAS VTSSTKNLQE FANCFGSDKY NSSDQALTKA VLVKRKNSEV AEEPWVECDS
CKLWYHQTCA LFNERNHAIS GEQEPFVCPI CVKEQRTTGV KPSIDNGLKA SRLPITRMAK
LIEDRVNQAI DKANEEEATR MGNLGNGESI GCGSGTHGTE LNSTTRLAIT VREVLSVDKL
VQVKTRMGAL LSAHYCKSKS PKNQLNGQQS SGQKATKRKR AASQKSATKQ PCDSTDTSPL
HLTYRSRCIC VFQELDGVDV LIFTLYVQEY GPESLPPNAG RVYVSYLDSV NYFQPKKWRT
LMHQQVMVGF LQDSKQRGFH TAHIWSCPPL KGDDYIFFCK PENQKIPKSA RLRQWYHKLL
QEAKKEKIVV NISNLYAEYY LKKKEAHQLP YFEGDYWPRL AEDLLKQLQD KSGRGEINIR
DDLTHPGESG LKADPSSLSV DDTQSRRASP TASEAQSGRN VEGNTSCTGK TNFMTKSKKK
RGRKSKRSAH SPRIASPETQ VSEGGSQPAQ GTRSNTKKKF KKPKQSQLNR LSSFTKGKAI
VNPDPLMQKL KLILEPQKDD FFVVDLYPKC HKCGTANVNV PYWELHTIPP TPTVIELIDA
VKKARTSSTS ARNSPPRHYH HYYCLQCYVC NKNQLQHRIT QAESAAAWGE ELSVTVMESQ
DKVANRIADV DLQEIKYRLV LRRVDPVTEE ATITDAACPT ADPKQLPHNE PQKIKCEQHE
MDPQEEKSTA AESEKPPSES LVMKMQRDLD DVLMPCEIFD TRESFLMYCQ NNHCQFDQIR
RAKHSSMMVL YHLFNQGTTG FTFTCSGCRT LLARGNRWNC SVCPLFNLCD ECNAKVRHEH
LLHVFKVVAI PRLTTNEREV ELGTKEQAHM EGMRFNANVN GGSNLRTPHN KVLQNSSSLE
EADASIYDQV KVESFTSPRT LQQEQSNKTD TACKMRKVPQ QSPLTSPADP EGSGTFGSRK
STTIPKAEAT SRGRSPNTDP SKKLKRIHNV DPQLLVQLEH ASSCAVAECT FVNCHRIKAM
LKHGSVCELR ATGSCVLCKR IVGLLSAHAR QCQKEYDICQ VPRCSDIRRH LHKQIKQRQS
QSQEAIDTRS QTHKASETEQ ENSA
//
