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Database: UniProt
Entry: A0A453N8V8_AEGTS
LinkDB: A0A453N8V8_AEGTS
Original site: A0A453N8V8_AEGTS 
ID   A0A453N8V8_AEGTS        Unreviewed;      1616 AA.
AC   A0A453N8V8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET6Gv20278000.7, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET6Gv20278000.7}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
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   EnsemblPlants; AET6Gv20278000.7; AET6Gv20278000.7; AET6Gv20278000.
DR   Gramene; AET6Gv20278000.7; AET6Gv20278000.7; AET6Gv20278000.
DR   Proteomes; UP000015105; Chromosome 6D.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd15614; PHD_HAC_like; 1.
DR   Gene3D; 3.30.60.90; -; 2.
DR   Gene3D; 1.20.1020.10; TAZ domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031162; CBP_P300_HAT.
DR   InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR   InterPro; IPR035898; TAZ_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_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; PF08214; HAT_KAT11; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM01250; KAT11; 1.
DR   SMART; SM00551; ZnF_TAZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   SUPFAM; SSF57933; TAZ domain; 2.
DR   PROSITE; PS51727; CBP_P300_HAT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50134; ZF_TAZ; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 2.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
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          553..635
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   DOMAIN          1003..1439
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51727"
FT   DOMAIN          1321..1384
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          1441..1493
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          1499..1583
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   REGION          166..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1591..1616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1591..1605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1616 AA;  181832 MW;  123C974B4DBF9DCE CRC64;
     MMRQPVEPQL QFAIKTLSAQ NQLNQQNQQM SRQMASSSGY STMIPTPGIT QGASGNSRMS
     YGTDNMGLSS SGAGMVPQNA NMGTSMPGTM SNGYQHLTTS APLNSTTNSV PSTMGPVGIQ
     RQVTHMIPTP GFSNQQNVPT NSDYSNGTGY FNGESAMTPH MQQQKQFQSN QSSHQIQHIG
     GHSNSGIHSS MLENSSAFGL SDGHVNGGMG LHGSNTQITN RNAAPEGYMN MSSFGSSPRP
     LQQQFNQHPT QRISTSVDMG GSGSFYGTGS SALATANNQN MGAANLQSRS RMNSMLLSNQ
     LNMQSIQGQP QIKTEVLDQS EKLNFQPSQL SHEQLLRQQL SMQQHQVQPS SQFVQNQYHL
     NQQIPNSQHQ QAMLRSNSFK QSQLNSSHSM QVSEQGTLPH TELTSSQATE PPALPNFQGQ
     YQQRSAHDNV KGAQVFGHLS GSQNFSASGS HDSQPLLHPN QQLDVSSSDV SYVLKGTQTE
     QMQQHQWRPQ TMEKVPISSN LSLEKQMQDD FCQRAMAQDG AQQPFSSDWR VSGCTVTSVD
     PALPKLPAGG LEQPTGNINY LRQMRWLLLL FHAKGCSSPL GSCKLPRCVQ LQDFVKHLDN
     CQRKDCPQKK CSKSRMLIEH YKTCVDEQCP VCSNVKKFLR LSAEHASKQK VPEPRKVAQQ
     NMTQRIMNGV DSDIMDIDPV SVESFDGQPS VPKRLKMQPA SPNVPEHEIL RASNPQVNPG
     FVLQESHPEL LEQNKKTAYM KRELDVKADM RPLQKPVKMG YGADGNVPTA RHNVIPGVSN
     EMKSHVKQEI LPVDKGASEN VHEVKNETND STEATALKSG KPKIKGVSLT ELFTPEQINA
     HIESLRLWVG QSKAKAEKNQ LLVSSENENS CQLCKVEKLT FEPPPIYCSP CGARIKRNAP
     YYTVGSGDTR HFFCIPCYNE SRGDTIEVEG QNFLKARFEK KRNDEETEEW WVQCDKCECW
     QHQICALFNG RRNDGGQAEY TCPNCYSNEV KCGLRMPLPQ SAVLGASDLP RTVLSDHIEE
     RLFKRLKWER QSRANNSNCS VDEVAGAEGL VVRVVSSVDK KVEVKPRFLE IFQEDNYPTE
     FPYKSKAVLL FQKIEGVEVC LFGMYVQEFG ADCAYPNQRR VYLSYLDSVK YFRPEIKAAT
     GEALRTFVYH EILIGYLEYC KQRGFTSCYI WACPPLKGED YILYCHPEIQ KTPKSDKLRE
     WYLAMLRKAT KEEIVVELTN LYDHFFITMG ECKAKVTASR LPYFDGDYWP GAAEDMINQL
     RQEEDDRKLQ KKSKTKKIIT KRALKAAGHT DLSGNASKDA MLMQKLGETI YPMKEDFIMV
     HLQYSCSHCC ILMSSGKRWV CHQCRSFYIC DKCYSAEQQL DDRERHPSNS RDTHKLHPVD
     IVGVPEETKD RDDILESEFF DTRQAFLSLC QGNHYQYDTL RRAKHSSMMV LYHLHNPTAP
     AFVTTCNVCS HDIETGQGWR CEICPDFDVC NGCYQKGAVN HPHKLTNHPS VADRDAQNKE
     ARQMRVQQLR KMLDLLVHAS TCRSGSCQYP NCRKVKGLFR HGMQCKTRAS GGCALCKKMW
     YMLQLHARAC RDSGCSVPRC RDLKEHLRRL QQQSDSRRRA AVNEMMRQRA AEVATT
//
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