TAF6_YEAST
ID TAF6_YEAST Reviewed; 516 AA.
AC P53040; D6VU35;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Transcription initiation factor TFIID subunit 6;
DE AltName: Full=TBP-associated factor 6;
DE AltName: Full=TBP-associated factor 60 kDa;
DE Short=TAFII-60;
DE Short=TAFII60;
GN Name=TAF6; Synonyms=TAF60; OrderedLocusNames=YGL112C; ORFNames=G2985;
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], AND PROTEIN SEQUENCE OF 72-92; 99-132
RP AND 222-229.
RC STRAIN=ATCC 76621 / YPH252;
RX PubMed=7667272; DOI=10.1073/pnas.92.18.8224;
RA Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S.,
RA Kornberg R.D., Weil P.A.;
RT "Identification and characterization of a TFIID-like multiprotein complex
RT from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9046090;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<85::aid-yea53>3.0.co;2-e;
RA Paoluzi S., Minenkova O., Castagnoli L.;
RT "The genes encoding the transcription factor yTAFII60, the G4p1 protein and
RT a putative glucose transporter are contained in a 12.3 kb DNA fragment on
RT the left arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:85-91(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
RX PubMed=9695952; DOI=10.1016/s0092-8674(00)81423-3;
RA Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C.,
RA Davidson I., Moras D.;
RT "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by
RT atypical evolutionary conserved motifs also found in the SPT3 family.";
RL Cell 94:239-249(1998).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674426; DOI=10.1016/s0092-8674(00)81220-9;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
RA Yates J.R. III, Workman J.L.;
RT "A subset of TAF(II)s are integral components of the SAGA complex required
RT for nucleosome acetylation and transcriptional stimulation.";
RL Cell 94:45-53(1998).
RN [8]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE TFIID COMPLEX.
RX PubMed=10788514; DOI=10.1074/jbc.275.18.13895;
RA Sanders S.L., Weil P.A.;
RT "Identification of two novel TAF subunits of the yeast Saccharomyces
RT cerevisiae TFIID complex.";
RL J. Biol. Chem. 275:13895-13900(2000).
RN [10]
RP FUNCTION, AND INTERACTION IN TFIID AND SAGA.
RX PubMed=11238921; DOI=10.1128/mcb.21.5.1841-1853.2001;
RA Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A., Tora L.,
RA Davidson I.;
RT "Histone folds mediate selective heterodimerization of yeast TAF(II)25 with
RT TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7.";
RL Mol. Cell. Biol. 21:1841-1853(2001).
RN [11]
RP FUNCTION, AND HISTONE-FOLD DOMAIN CHARACTERIZATION.
RX PubMed=11295558; DOI=10.1016/s0968-0004(00)01741-2;
RA Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.;
RT "The histone fold is a key structural motif of transcription factor
RT TFIID.";
RL Trends Biochem. Sci. 26:250-257(2001).
RN [12]
RP FUNCTION, AND TAF OCTAMER FORMATION.
RX PubMed=11473260; DOI=10.1038/90408;
RA Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S.,
RA Tan S.;
RT "A histone fold TAF octamer within the yeast TFIID transcriptional
RT coactivator.";
RL Nat. Struct. Biol. 8:695-700(2001).
RN [13]
RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=12052880; DOI=10.1128/mcb.22.13.4723-4738.2002;
RA Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.;
RT "Proteomics of the eukaryotic transcription machinery: identification of
RT proteins associated with components of yeast TFIID by multidimensional mass
RT spectrometry.";
RL Mol. Cell. Biol. 22:4723-4738(2002).
RN [14]
RP IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [15]
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 [16]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [17]
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 [18]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [19]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [20]
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 [21]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Functions as a component of the DNA-binding general
CC transcription factor complex TFIID and the regulatory transcription
CC regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK.
CC Binding of TFIID to a promoter (with or without TATA element) is the
CC initial step in preinitiation complex (PIC) formation. TFIID plays a
CC key role in the regulation of gene expression by RNA polymerase II
CC through different activities such as transcription activator
CC interaction, core promoter recognition and selectivity, TFIIA and TFIIB
CC interaction, chromatin modification (histone acetylation by TAF1),
CC facilitation of DNA opening and initiation of transcription. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation of
CC approximately 10% of yeast genes. At the promoters, SAGA is required
CC for recruitment of the basal transcription machinery. It influences RNA
CC polymerase II transcriptional activity through different activities
CC such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC selectivity, interaction with transcription activators (GCN5, ADA2,
CC ADA3 and TRA1), and chromatin modification through histone acetylation
CC (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC interacts with DNA via upstream activating sequences (UASs). SALSA, an
CC altered form of SAGA, may be involved in positive transcriptional
CC regulation. SLIK is proposed to have partly overlapping functions with
CC SAGA. It preferentially acetylates methylated histone H3, at least
CC after activation at the GAL1-10 locus. {ECO:0000269|PubMed:10026213,
CC ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:11238921,
CC ECO:0000269|PubMed:11295558, ECO:0000269|PubMed:11473260,
CC ECO:0000269|PubMed:12052880, ECO:0000269|PubMed:12138208,
CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9674426,
CC ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: In TFIID, TAF6 heterodimerizes with TAF9, forming ultimately
CC an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by
CC TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4
CC octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein
CC (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2,
CC TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6,
CC TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa
CC SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3,
CC SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2,
CC SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19,
CC TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5
CC distinct domains with specialized functions. Domain I (containing TRA1)
CC probably represents the activator interaction surface. Domain II
CC (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III
CC (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3
CC and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably
CC TAF9) are believed to play primarily an architectural role. Domain III
CC also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and
CC probably SPT8) represents the TBP-interacting module, which may be
CC associated transiently with SAGA. Component of the SALSA complex, which
CC consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5,
CC ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the
CC SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3,
CC SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10
CC and TAF9. {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12052880,
CC ECO:0000269|PubMed:12186975, ECO:0000269|PubMed:12446794,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:9674426}.
CC -!- INTERACTION:
CC P53040; P35817: BDF1; NbExp=2; IntAct=EBI-18876, EBI-3493;
CC P53040; Q12060: HFI1; NbExp=9; IntAct=EBI-18876, EBI-8287;
CC P53040; P46677: TAF1; NbExp=6; IntAct=EBI-18876, EBI-18855;
CC P53040; Q12030: TAF10; NbExp=8; IntAct=EBI-18876, EBI-18889;
CC P53040; P38129: TAF5; NbExp=12; IntAct=EBI-18876, EBI-18868;
CC P53040; P53040: TAF6; NbExp=2; IntAct=EBI-18876, EBI-18876;
CC P53040; Q05027: TAF9; NbExp=11; IntAct=EBI-18876, EBI-27500;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 6506 (+/-1290) molecules/cell in log phase
CC SD medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
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DR EMBL; X97644; CAA66240.1; -; Genomic_DNA.
DR EMBL; L40145; AAA83389.1; -; Genomic_DNA.
DR EMBL; Z72634; CAA96819.1; -; Genomic_DNA.
DR EMBL; AY723809; AAU09726.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07996.1; -; Genomic_DNA.
DR PIR; S64120; S64120.
DR RefSeq; NP_011403.1; NM_001180977.1.
DR PDB; 6T9I; EM; 3.90 A; E=1-516.
DR PDB; 6T9K; EM; 3.30 A; E=1-516.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; P53040; -.
DR SMR; P53040; -.
DR BioGRID; 33139; 423.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-981N; -.
DR IntAct; P53040; 122.
DR MINT; P53040; -.
DR STRING; 4932.YGL112C; -.
DR MaxQB; P53040; -.
DR PaxDb; P53040; -.
DR PRIDE; P53040; -.
DR EnsemblFungi; YGL112C_mRNA; YGL112C; YGL112C.
DR GeneID; 852766; -.
DR KEGG; sce:YGL112C; -.
DR SGD; S000003080; TAF6.
DR VEuPathDB; FungiDB:YGL112C; -.
DR eggNOG; KOG2549; Eukaryota.
DR GeneTree; ENSGT00640000091486; -.
DR HOGENOM; CLU_021711_3_1_1; -.
DR InParanoid; P53040; -.
DR OMA; YFVQFIA; -.
DR BioCyc; YEAST:G3O-30610-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-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 PRO; PR:P53040; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53040; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR CDD; cd08050; TAF6C; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.25.40.770; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037796; TAF6.
DR InterPro; IPR011442; TAF6_C.
DR InterPro; IPR046344; TAF6_C_sf.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR PANTHER; PTHR10221; PTHR10221; 1.
DR Pfam; PF02969; TAF; 1.
DR Pfam; PF07571; TAF6_C; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..516
FT /note="Transcription initiation factor TFIID subunit 6"
FT /id="PRO_0000118878"
FT DOMAIN 6..75
FT /note="Histone-fold"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 31..58
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 156..160
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 191..196
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 201..205
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 333..360
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 363..367
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 387..398
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 413..419
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:6T9K"
SQ SEQUENCE 516 AA; 57902 MW; 14B590E02C16F289 CRC64;
MSTQQQSYTI WSPQDTVKDV AESLGLENIN DDVLKALAMD VEYRILEIIE QAVKFKRHSK
RDVLTTDDVS KALRVLNVEP LYGYYDGSEV NKAVSFSKVN TSGGQSVYYL DEEEVDFDRL
INEPLPQVPR LPTFTTHWLA VEGVQPAIIQ NPNLNDIRVS QPPFIRGAIV TALNDNSLQT
PVTSTTASAS VTDTGASQHL SNVKPGQNTE VKPLVKHVLS KELQIYFNKV ISTLTAKSQA
DEAAQHMKQA ALTSLRTDSG LHQLVPYFIQ FIAEQITQNL SDLQLLTTIL EMIYSLLSNT
SIFLDPYIHS LMPSILTLLL AKKLGGSPKD DSPQEIHEFL ERTNALRDFA ASLLDYVLKK
FPQAYKSLKP RVTRTLLKTF LDINRVFGTY YGCLKGVSVL EGESIRFFLG NLNNWARLVF
NESGITLDNI EEHLNDDSNP TRTKFTKEET QILVDTVISA LLVLKKDLPD LYEGKGEKVT
DEDKEKLLER CGVTIGFHIL KRDDAKELIS AIFFGE
