TBP_YEAST
ID TBP_YEAST Reviewed; 240 AA.
AC P13393; D3DM55;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=TATA-box-binding protein;
DE AltName: Full=TATA sequence-binding protein;
DE Short=TBP;
DE AltName: Full=TATA-binding factor;
DE AltName: Full=TATA-box factor;
DE AltName: Full=Transcription factor D;
DE AltName: Full=Transcription initiation factor TFIID TBP subunit;
GN Name=SPT15; Synonyms=BTF1, TBP1; OrderedLocusNames=YER148W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2550146; DOI=10.1016/0092-8674(89)90515-1;
RA Hahn S., Buratowski S., Sharp P.A., Guarente L.;
RT "Isolation of the gene encoding the yeast TATA binding protein TFIID: a
RT gene identical to the SPT15 suppressor of Ty element insertions.";
RL Cell 58:1173-1181(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2673545; DOI=10.1016/0092-8674(89)90516-3;
RA Eisenmann D.M., Dollard C., Winston F.;
RT "SPT15, the gene encoding the yeast TATA binding factor TFIID, is required
RT for normal transcription initiation in vivo.";
RL Cell 58:1183-1191(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 2-34;
RP 122-162 AND 198-233, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=2677740; DOI=10.1038/341299a0;
RA Horikoshi M., Wang C.K., Fujii H., Cromlish J.A., Weil P.A., Roeder R.G.;
RT "Cloning and structure of a yeast gene encoding a general transcription
RT initiation factor TFIID that binds to the TATA box.";
RL Nature 341:299-303(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2682626; DOI=10.1073/pnas.86.20.7785;
RA Schmidt M.C., Kao C., Pei R., Berk A.J.;
RT "Yeast TATA-box transcription factor gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7785-7789(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2690073; DOI=10.1073/pnas.86.24.9803;
RA Cavallini B., Faus I., Matthes H., Chipoulet J.M., Winsor B., Egly J.-M.,
RA Chambon P.;
RT "Cloning of the gene encoding the yeast protein BTF1Y, which can substitute
RT for the human TATA box-binding factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9803-9807(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [7]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [8]
RP REPEAT IN SEQUENCE.
RX PubMed=2405282; DOI=10.1038/343417b0;
RA Hoeijmakers J.H.J.;
RT "Cryptic initiation sequence revealed.";
RL Nature 343:417-418(1990).
RN [9]
RP REPEAT IN SEQUENCE.
RA Nagai K.;
RT "Cryptic initiation sequence revealed.";
RL Nature 343:418-418(1990).
RN [10]
RP FUNCTION.
RX PubMed=9618449; DOI=10.1128/mmbr.62.2.465-503.1998;
RA Hampsey M.;
RT "Molecular genetics of the RNA polymerase II general transcriptional
RT machinery.";
RL Microbiol. Mol. Biol. Rev. 62:465-503(1998).
RN [11]
RP FUNCTION, AND TFIID STOICHIOMETRY.
RX PubMed=12138208; DOI=10.1128/mcb.22.16.6000-6013.2002;
RA Sanders S.L., Garbett K.A., Weil P.A.;
RT "Molecular characterization of Saccharomyces cerevisiae TFIID.";
RL Mol. Cell. Biol. 22:6000-6013(2002).
RN [12]
RP FUNCTION.
RX PubMed=12516863; DOI=10.1023/a:1021258713850;
RA Martinez E.;
RT "Multi-protein complexes in eukaryotic gene transcription.";
RL Plant Mol. Biol. 50:925-947(2002).
RN [13]
RP INTERACTION WITH TFC8.
RX PubMed=17052456; DOI=10.1016/j.molcel.2006.08.013;
RA Mylona A., Fernandez-Tornero C., Legrand P., Haupt M., Sentenac A.,
RA Acker J., Mueller C.W.;
RT "Structure of the tau60/Delta tau91 subcomplex of yeast transcription
RT factor IIIC: insights into preinitiation complex assembly.";
RL Mol. Cell 24:221-232(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 61-240.
RX PubMed=8413604; DOI=10.1038/365512a0;
RA Kim Y., Geiger J.H., Hahn S., Sigler P.B.;
RT "Crystal structure of a yeast TBP/TATA-box complex.";
RL Nature 365:512-520(1993).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 61-240.
RX PubMed=8367480; DOI=10.1073/pnas.90.17.8174;
RA Chasman D.I., Flaherty K.M., Sharp P.A., Kornberg R.D.;
RT "Crystal structure of yeast TATA-binding protein and model for interaction
RT with DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8174-8178(1993).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 61-240.
RX PubMed=8610010; DOI=10.1038/381127a0;
RA Tan S., Hunziker Y., Sargent D.F., Richmond T.J.;
RT "Crystal structure of a yeast TFIIA/TBP/DNA complex.";
RL Nature 381:127-134(1996).
RN [18]
RP STRUCTURE BY NMR OF 61-240.
RX PubMed=9741622; DOI=10.1016/s0092-8674(00)81599-8;
RA Liu D., Ishima R., Tong K.I., Bagby S., Kokubo T., Muhandiram D.R.,
RA Kay L.E., Nakatani Y., Ikura M.;
RT "Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the
RT minor groove surface of the TATA box unwound by TBP.";
RL Cell 94:573-583(1998).
RN [19]
RP 3D-STRUCTURE, AND ELECTRON MICROSCOPY OF TFIID.
RX PubMed=12093743; DOI=10.1093/emboj/cdf342;
RA Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A.,
RA Kirschner D.B., Tora L., Schultz P.;
RT "Mapping histone fold TAFs within yeast TFIID.";
RL EMBO J. 21:3424-3433(2002).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 61-240 IN COMPLEX WITH BRF1.
RX PubMed=12660736; DOI=10.1038/nature01534;
RA Juo Z.S., Kassavetis G.A., Wang J., Geiduschek E.P., Sigler P.B.;
RT "Crystal structure of a transcription factor IIIB core interface ternary
RT complex.";
RL Nature 422:534-539(2003).
CC -!- FUNCTION: General transcription factor that functions at the core of
CC the DNA-binding general transcription factor complex TFIID. Binding of
CC TFIID to a promoter (with or without TATA element) is the initial step
CC in preinitiation complex (PIC) formation. TFIID plays a key role in the
CC regulation of gene expression by RNA polymerase II through different
CC activities such as transcription activator interaction, core promoter
CC recognition and selectivity, TFIIA and TFIIB interaction, chromatin
CC modification (histone acetylation by TAF1), facilitation of DNA opening
CC and initiation of transcription. {ECO:0000269|PubMed:12138208,
CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9618449}.
CC -!- SUBUNIT: Binds DNA as monomer. The 1.2 MDa TFIID complex is composed of
CC TATA binding protein (TBP) and the 14 TBP-associated factors. One copy
CC of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each
CC TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14.
CC Interacts with TFC8. {ECO:0000269|PubMed:12660736,
CC ECO:0000269|PubMed:17052456}.
CC -!- INTERACTION:
CC P13393; P29056: BRF1; NbExp=2; IntAct=EBI-19129, EBI-19142;
CC P13393; P38304: MED8; NbExp=3; IntAct=EBI-19129, EBI-20932;
CC P13393; P32333: MOT1; NbExp=7; IntAct=EBI-19129, EBI-11152;
CC P13393; Q01939: RPT6; NbExp=2; IntAct=EBI-19129, EBI-13914;
CC P13393; Q04712: RRN11; NbExp=2; IntAct=EBI-19129, EBI-27790;
CC P13393; Q03940: RVB1; NbExp=3; IntAct=EBI-19129, EBI-30712;
CC P13393; Q12464: RVB2; NbExp=3; IntAct=EBI-19129, EBI-31814;
CC P13393; P38915: SPT8; NbExp=3; IntAct=EBI-19129, EBI-17964;
CC P13393; P32774: TOA2; NbExp=2; IntAct=EBI-19129, EBI-19323;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}.
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DR EMBL; M27135; AAA35147.1; -; Genomic_DNA.
DR EMBL; X16860; CAA34751.1; -; Genomic_DNA.
DR EMBL; M26403; AAA35146.1; -; Genomic_DNA.
DR EMBL; M29459; AAA34458.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64675.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07809.1; -; Genomic_DNA.
DR PIR; A30366; A30366.
DR RefSeq; NP_011075.3; NM_001179038.3.
DR PDB; 1NGM; X-ray; 2.95 A; A/E/I/M=61-240.
DR PDB; 1NH2; X-ray; 1.90 A; A=61-240.
DR PDB; 1RM1; X-ray; 2.50 A; A=1-240.
DR PDB; 1TBA; NMR; -; B=61-240.
DR PDB; 1TBP; X-ray; 2.60 A; A/B=62-240.
DR PDB; 1YTB; X-ray; 1.80 A; A/B=61-240.
DR PDB; 1YTF; X-ray; 2.50 A; A=61-240.
DR PDB; 4B0A; X-ray; 1.97 A; A=61-240.
DR PDB; 4V1N; EM; 7.80 A; O=61-240.
DR PDB; 4V1O; EM; 9.70 A; O=61-240.
DR PDB; 5FMF; EM; 6.00 A; Q=61-240.
DR PDB; 5FYW; EM; 4.35 A; O=1-240.
DR PDB; 5FZ5; EM; 8.80 A; O=1-240.
DR PDB; 5OQJ; EM; 4.70 A; O=1-240.
DR PDB; 5OQM; EM; 5.80 A; O=1-240.
DR PDB; 5SVA; EM; 15.30 A; j=1-240.
DR PDB; 6CNB; EM; 4.10 A; R=61-240.
DR PDB; 6CNC; EM; 4.10 A; R=61-240.
DR PDB; 6CND; EM; 4.80 A; R=61-240.
DR PDB; 6CNF; EM; 4.50 A; R=61-240.
DR PDB; 6E16; X-ray; 2.40 A; A=61-240.
DR PDB; 6E24; X-ray; 3.00 A; A=61-240.
DR PDB; 6EU0; EM; 4.00 A; Y=1-240.
DR PDB; 6F40; EM; 3.70 A; U=1-240.
DR PDB; 6F41; EM; 4.30 A; U=1-240.
DR PDB; 6F42; EM; 5.50 A; U=1-240.
DR PDB; 6F44; EM; 4.20 A; U=1-240.
DR PDB; 6GYK; EM; 5.10 A; O=1-240.
DR PDB; 6GYL; EM; 4.80 A; O=1-240.
DR PDB; 6GYM; EM; 6.70 A; O=1-240.
DR PDB; 6TBM; EM; 20.00 A; M=1-240.
DR PDB; 7ML0; EM; 3.00 A; O=1-240.
DR PDB; 7ML1; EM; 4.00 A; O=1-240.
DR PDB; 7ML4; EM; 3.10 A; O=1-240.
DR PDB; 7O4I; EM; 3.20 A; O=1-240.
DR PDB; 7O4J; EM; 2.90 A; O=1-240.
DR PDB; 7O72; EM; 3.40 A; O=1-240.
DR PDB; 7O73; EM; 3.40 A; O=1-240.
DR PDB; 7O75; EM; 3.20 A; O=1-240.
DR PDB; 7Q5B; EM; 3.98 A; Y=1-240.
DR PDBsum; 1NGM; -.
DR PDBsum; 1NH2; -.
DR PDBsum; 1RM1; -.
DR PDBsum; 1TBA; -.
DR PDBsum; 1TBP; -.
DR PDBsum; 1YTB; -.
DR PDBsum; 1YTF; -.
DR PDBsum; 4B0A; -.
DR PDBsum; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6E16; -.
DR PDBsum; 6E24; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 6TBM; -.
DR PDBsum; 7ML0; -.
DR PDBsum; 7ML1; -.
DR PDBsum; 7ML4; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR PDBsum; 7Q5B; -.
DR AlphaFoldDB; P13393; -.
DR BMRB; P13393; -.
DR SMR; P13393; -.
DR BioGRID; 36897; 318.
DR ComplexPortal; CPX-1141; MOT1-TBP transcription regulation complex.
DR ComplexPortal; CPX-1143; Transcription factor TFIIIB complex.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-44N; -.
DR IntAct; P13393; 74.
DR MINT; P13393; -.
DR STRING; 4932.YER148W; -.
DR iPTMnet; P13393; -.
DR MaxQB; P13393; -.
DR PaxDb; P13393; -.
DR PRIDE; P13393; -.
DR EnsemblFungi; YER148W_mRNA; YER148W; YER148W.
DR GeneID; 856891; -.
DR KEGG; sce:YER148W; -.
DR SGD; S000000950; SPT15.
DR VEuPathDB; FungiDB:YER148W; -.
DR eggNOG; KOG3302; Eukaryota.
DR GeneTree; ENSGT00940000159561; -.
DR HOGENOM; CLU_060161_4_2_1; -.
DR InParanoid; P13393; -.
DR OMA; NCEYEPE; -.
DR BioCyc; YEAST:G3O-30309-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; P13393; -.
DR PRO; PR:P13393; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P13393; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005672; C:transcription factor TFIIA complex; IMP:CAFA.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IDA:SGD.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:CAFA.
DR GO; GO:0140223; F:general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IDA:SGD.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IC:SGD.
DR GO; GO:0001016; F:RNA polymerase III transcription regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0001092; F:TFIIA-class transcription factor complex binding; IPI:CAFA.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IMP:SGD.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IMP:SGD.
DR GO; GO:0070898; P:RNA polymerase III preinitiation complex assembly; IDA:SGD.
DR GO; GO:0070893; P:transposon integration; IDA:SGD.
DR CDD; cd04516; TBP_eukaryotes; 1.
DR Gene3D; 3.30.310.10; -; 2.
DR HAMAP; MF_00408; TATA_bind_prot_arch; 1.
DR InterPro; IPR000814; TBP.
DR InterPro; IPR030491; TBP_CS.
DR InterPro; IPR012295; TBP_dom_sf.
DR InterPro; IPR033710; TBP_eukaryotic.
DR PANTHER; PTHR10126; PTHR10126; 1.
DR Pfam; PF00352; TBP; 2.
DR PRINTS; PR00686; TIFACTORIID.
DR PROSITE; PS00351; TFIID; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Nucleus;
KW Reference proteome; Repeat; Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2677740"
FT CHAIN 2..240
FT /note="TATA-box-binding protein"
FT /id="PRO_0000153990"
FT REPEAT 67..143
FT /note="1"
FT REPEAT 157..234
FT /note="2"
FT REGION 21..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 50
FT /note="A -> T (in Ref. 4; AAA35146)"
FT /evidence="ECO:0000305"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1YTB"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1YTB"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1YTB"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:1YTB"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 153..165
FT /evidence="ECO:0007829|PDB:1YTB"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:1YTB"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1RM1"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1YTB"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1YTB"
FT HELIX 220..236
FT /evidence="ECO:0007829|PDB:1YTB"
SQ SEQUENCE 240 AA; 27003 MW; 50365FFF1D3718CE CRC64;
MADEERLKEF KEANKIVFDP NTRQVWENQN RDGTKPATTF QSEEDIKRAA PESEKDTSAT
SGIVPTLQNI VATVTLGCRL DLKTVALHAR NAEYNPKRFA AVIMRIREPK TTALIFASGK
MVVTGAKSED DSKLASRKYA RIIQKIGFAA KFTDFKIQNI VGSCDVKFPI RLEGLAFSHG
TFSSYEPELF PGLIYRMVKP KIVLLIFVSG KIVLTGAKQR EEIYQAFEAI YPVLSEFRKM
