ID   EMBP1_WHEAT             Reviewed;         354 AA.
AC   P25032; Q41555;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=DNA-binding protein EMBP-1;
DE   AltName: Full=Histone promoter-binding protein 1a(1);
DE            Short=HBP-1a(1);
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2145628; DOI=10.1126/science.2145628;
RA   Guiltinan M.J., Marcotte W.R. Jr., Quatrano R.S.;
RT   "A plant leucine zipper protein that recognizes an abscisic acid response
RT   element.";
RL   Science 250:267-271(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 98-354, AND DNA-BINDING.
RX   PubMed=8144592; DOI=10.1016/s0021-9258(17)36978-8;
RA   Mikami K., Sakamoto A., Iwabuchi M.;
RT   "The HBP-1 family of wheat basic/leucine zipper proteins interacts with
RT   overlapping cis-acting hexamer motifs of plant histone genes.";
RL   J. Biol. Chem. 269:9974-9985(1994).
RN   [3]
RP   DNA-BINDING.
RX   PubMed=7800488; DOI=10.1093/nar/22.23.4969;
RA   Niu X., Guiltinan M.J.;
RT   "DNA binding specificity of the wheat bZIP protein EmBP-1.";
RL   Nucleic Acids Res. 22:4969-4978(1994).
CC   -!- FUNCTION: Interacts specifically with the 8-bp sequence 5'-CACGTGGC-
CC       3'in the abscisic acid response element (ABARE). Also binds to the
CC       hexamer motif 5'-ACGTCA-3' of histone gene promoters.
CC   -!- SUBUNIT: Heterodimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; M62893; AAA68428.1; -; mRNA.
DR   EMBL; D12919; BAA02303.2; -; mRNA.
DR   PIR; A38486; A38486.
DR   PIR; T06487; T06487.
DR   AlphaFoldDB; P25032; -.
DR   SMR; P25032; -.
DR   STRING; 4565.Traes_5BL_F3018E8CA.1; -.
DR   PRIDE; P25032; -.
DR   eggNOG; ENOG502QVYY; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P25032; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd14702; bZIP_plant_GBF1; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR045314; bZIP_plant_GBF1.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR044827; GBF-like.
DR   PANTHER; PTHR45967; PTHR45967; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..354
FT                   /note="DNA-binding protein EMBP-1"
FT                   /id="PRO_0000076563"
FT   DOMAIN          250..313
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..271
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          278..299
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        120..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  36193 MW;  8950666897E98590 CRC64;
     MASSSSATSG DDRPPAAGGG TPAQAHAEWA ASMHAYYAAA ASAAGHPYAA WPLPPQAQQH
     GLVAAGAGAA YGAGAVPHVP PPPAGTRHAH ASMAAGVPYM AGESASAAGK GKRVGKTQRV
     PSGEINSSSG SGDAGSQGSS EKGDAGANQK GSSSSAKRRK SGAAKTEGEP SQAATVQNAV
     TEPPLEDKER SASKLLVLAP GRAALTSAAP NLNIGMDPLS ASPSSLVQGE VNAAASSQSN
     ASLSQMDERE LKRERRKQSN RESARRSRLR KQQECEELAQ KVSELTAANG TLRSELDQLK
     KDCKTMETEN KKLMGKILSH DDKMQQSEGP SVVTTLSIQV EAPEPHQGGH GKAS