UniProt: A0A1S3ZD75

Database: UniProt
Entry: A0A1S3ZD75_TOBAC

LinkDB:  A0A1S3ZD75_TOBAC 
Original site:  A0A1S3ZD75_TOBAC

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (21)   
   InterPro (11)   
   Pfam (2)   
   PROSITE (4)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (34)   

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ID   A0A1S3ZD75_TOBAC        Unreviewed;      1292 AA.
AC   A0A1S3ZD75;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   Name=LOC107785401 {ECO:0000313|RefSeq:XP_016462187.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016462187.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016462187.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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   RefSeq; XP_016462187.1; XM_016606701.1.
DR   SMR; A0A1S3ZD75; -.
DR   STRING; 4097.A0A1S3ZD75; -.
DR   PaxDb; 4097-A0A1S3ZD75; -.
DR   GeneID; 107785401; -.
DR   KEGG; nta:107785401; -.
DR   OrthoDB; 5490807at2759; -.
DR   Proteomes; UP000084051; Unplaced.
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:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd15614; PHD_HAC_like; 1.
DR   Gene3D; 2.10.110.40; -; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.20.1020.10; TAZ domain; 1.
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; IPR038547; RING_CBP-p300_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:SF50; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF08214; HAT_KAT11; 1.
DR   Pfam; PF02135; zf-TAZ; 1.
DR   SMART; SM01250; KAT11; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00551; ZnF_TAZ; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF57933; TAZ domain; 1.
DR   PROSITE; PS51727; CBP_P300_HAT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50134; ZF_TAZ; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
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:UP000084051};
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          746..1179
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51727"
FT   DOMAIN          1191..1276
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   REGION          503..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..537
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1292 AA;  146059 MW;  03AB4D3B91C03E14 CRC64;
     MNLNGFNVWI PSNSGGTYLF QEASDILRLS NTGSRQHSCE KQDFNQIEWT SDQRRAPVSG
     LIGNRIKSFV STKNSDVGKQ MVNNLADLRS HPSVDAVCKQ DHVLKEILSR EYQNLIQQEA
     YYPQPWQDEA RDFLSSNLTP ISHTIDLGDS PLLCSSKLQS AQRDLSTASC MNYSMLQTGS
     SANKPSELGD VLSPVSVSHV PQEIVDSPEP FSSVTVCSDG EWNANKEPYE DGLMYSDSSL
     LSISESISKS SIKPQYSDEV EFNLRNYGGY SESNQNIYHE NVPASHGQSV ALSHLNRWTS
     QPDVKSSEDN TLSAAISYQL PNPRSHGCLV EQDASMINLS RQRSILPNVF QLFPEQLPSI
     QQRDFHQLHS GSSNGSGCDE ECNGYSSYIN EAVLPPSKRK REKNIPVLHF GAFNADAGSG
     NQQSPVAKHL SLGQCSEGPT CSKRNKTEIS NKIASCVEDR NIAGGSCNLA RVDMLGVDNG
     YYFSSTELNN DCELQKIEHT CSSGTENSEI DNSPEKSLDR SSFRHVEPAD DQREEIQQTS
     KYNQITSATR SDLIEPKVKC QMGMRSSTED SERLSVSLTD FFTDEQLKNH VYSLSQTNQG
     STGNMILHSV CENICQLCGT DRLAFVPVPI YCSSCCARIK RNLVYYWTVD KASARHCFCT
     RCFRESRGDN VSSQGLLISK QKFQKAKNSE QNEESWVQCD KCECWQHQIC ALYNAKKDLE
     GQAKYICPFC CLEEIEAGER VPLPATLGAQ DLPRTMLSDH IEHRLFRCLK LEREERAKLS
     GQDADEVLGA TDLIVRVVLS TNKKLKVKQQ FLDLFHNENY PMEFQYKSKV ILLFQNIEGA
     DVCLFGMYVQ EFGSECAPPN KRCVYISYLD SIKYFIPEIE TVKGEALRTS VYHEILIGYL
     DYCKKRGFTT CYIWACPPVK SEDYILYCHP ESQKTPKPDQ LRRWYRSMLR KASEEDIVVN
     YTNLYDHFFV PSARNNARIS AAHLPYFDGD YWSGAAEDLI RNIEKESRGD SPNKVKKLMT
     KRALKAIGHN HLSADATKDI LVMQKLGQTI LPVKEDFIIV NLHVVCTNCH EAILSGSRWF
     CYQCRNFHIC ARCLALKENF GEQKTHTSIN GEKHLLSEVV VDDIPANTED QDTIIDNDLF
     ENRHSFLSFC QKNHYQFDTL RRAKHSSMMI LYHLHKKIHS SETDSGGGSE QFEGQRPLQV
     KLMGVLVHAS QCRATPSNPC SYSGCLKIRK LFQHASRCNV RVPGGCELCF KTWSLLHWHS
     QTCQDFSCLV PRCMDIKKHV ARNSSLQRGE RD
//

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