ID TAF5_YEAST Reviewed; 798 AA. AC P38129; D6VQJ4; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 217. DE RecName: Full=Transcription initiation factor TFIID subunit 5; DE AltName: Full=TAFII-90; DE AltName: Full=TBP-associated factor 5; DE AltName: Full=TBP-associated factor 90 kDa; GN Name=TAF5; Synonyms=TAF90; OrderedLocusNames=YBR198C; GN ORFNames=YBR1410; 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]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7975899; DOI=10.1002/yea.320100612; RA Mallet L., Bussereau F., Jacquet M.; RT "Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II RT including BEM1, a new gene of the WD-40 repeat family and a new member of RT the KRE2/MNT1 family."; RL Yeast 10:819-831(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [3] 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 [4] 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 [5] RP PROTEIN SEQUENCE OF 726-747, AND CHARACTERIZATION. RC STRAIN=Y57; RX PubMed=7935765; DOI=10.1038/371523a0; RA Reese J.C., Apone L., Walker S.S., Griffin L.A., Green M.R.; RT "Yeast TAFIIS in a multisubunit complex required for activated RT transcription."; RL Nature 371:523-527(1994). RN [6] RP PROTEIN SEQUENCE OF 22-63 AND 726-752, AND CHARACTERIZATION. 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 [7] RP FUNCTION, IDENTIFICATION IN THE IN 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 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 IDENTIFICATION IN THE IN 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-411 AND SER-787, AND 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [20] 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 transcription regulatory CC histone acetylation (HAT) complexes SAGA, SALSA and SLIK. 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. SAGA is involved in RNA polymerase II- CC dependent transcriptional regulation of approximately 10% of yeast CC genes. At the promoters, SAGA is required for recruitment of the basal CC transcription machinery. It influences RNA polymerase II CC transcriptional activity through different activities such as TBP CC interaction (SPT3, SPT8 and SPT20) and promoter selectivity, CC interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), CC and chromatin modification through histone acetylation (GCN5) and CC deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some CC extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts CC with DNA via upstream activating sequences (UASs). SALSA, an altered CC form of SAGA, may be involved in positive transcriptional regulation. CC SLIK is proposed to have partly overlapping functions with SAGA. It CC preferentially acetylates methylated histone H3, at least after CC activation at the GAL1-10 locus. {ECO:0000269|PubMed:10026213, CC ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12052880, CC ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863, CC ECO:0000269|PubMed:9674426}. CC -!- SUBUNIT: 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 P38129; Q12060: HFI1; NbExp=15; IntAct=EBI-18868, EBI-8287; CC P38129; P23255: TAF2; NbExp=9; IntAct=EBI-18868, EBI-18862; CC P38129; P50105: TAF4; NbExp=12; IntAct=EBI-18868, EBI-11231; CC P38129; P38129: TAF5; NbExp=8; IntAct=EBI-18868, EBI-18868; CC P38129; P53040: TAF6; NbExp=12; IntAct=EBI-18868, EBI-18876; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- MISCELLANEOUS: Present with 14834 (+/-203) molecules/cell in log phase CC SD medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat TAF5 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z21487; CAA79685.1; -; Genomic_DNA. DR EMBL; Z36067; CAA85160.1; -; Genomic_DNA. DR EMBL; AY692890; AAT92909.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07314.1; -; Genomic_DNA. DR PIR; S34023; S34023. DR RefSeq; NP_009757.1; NM_001178546.1. DR PDB; 2J49; X-ray; 2.30 A; A=147-290. DR PDB; 6T9I; EM; 3.90 A; D=1-798. DR PDB; 6T9K; EM; 3.30 A; D=1-798. DR PDBsum; 2J49; -. DR PDBsum; 6T9I; -. DR PDBsum; 6T9K; -. DR AlphaFoldDB; P38129; -. DR EMDB; EMD-10412; -. DR EMDB; EMD-10414; -. DR SMR; P38129; -. DR BioGRID; 32895; 870. 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-740N; -. DR IntAct; P38129; 212. DR MINT; P38129; -. DR STRING; 4932.YBR198C; -. DR GlyGen; P38129; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P38129; -. DR MaxQB; P38129; -. DR PaxDb; 4932-YBR198C; -. DR PeptideAtlas; P38129; -. DR EnsemblFungi; YBR198C_mRNA; YBR198C; YBR198C. DR GeneID; 852497; -. DR KEGG; sce:YBR198C; -. DR AGR; SGD:S000000402; -. DR SGD; S000000402; TAF5. DR VEuPathDB; FungiDB:YBR198C; -. DR eggNOG; KOG0263; Eukaryota. DR GeneTree; ENSGT00940000153342; -. DR HOGENOM; CLU_005884_2_1_1; -. DR InParanoid; P38129; -. DR OMA; RCAFAPE; -. DR OrthoDB; 3138699at2759; -. DR BioCyc; YEAST:G3O-29139-MONOMER; -. 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 BioGRID-ORCS; 852497; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P38129; -. DR PRO; PR:P38129; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P38129; Protein. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. 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:0043130; F:ubiquitin binding; IDA:SGD. DR GO; GO:0006325; P:chromatin organization; IDA: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:0006366; P:transcription by RNA polymerase II; IDA:SGD. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central. DR CDD; cd08044; TAF5_NTD2; 1. DR CDD; cd00200; WD40; 1. DR Gene3D; 1.25.40.500; TFIID subunit TAF5, NTD2 domain; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR006594; LisH. DR InterPro; IPR007582; TFIID_NTD2. DR InterPro; IPR037264; TFIID_NTD2_sf. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19879:SF1; CANNONBALL-RELATED; 1. DR PANTHER; PTHR19879; TRANSCRIPTION INITIATION FACTOR TFIID; 1. DR Pfam; PF08513; LisH; 1. DR Pfam; PF04494; TFIID_NTD2; 1. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00667; LisH; 1. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF160897; Taf5 N-terminal domain-like; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50896; LISH; 1. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Direct protein sequencing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; WD repeat. FT CHAIN 1..798 FT /note="Transcription initiation factor TFIID subunit 5" FT /id="PRO_0000051260" FT DOMAIN 56..88 FT /note="LisH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126" FT REPEAT 464..503 FT /note="WD 1" FT REPEAT 523..562 FT /note="WD 2" FT REPEAT 565..604 FT /note="WD 3" FT REPEAT 607..646 FT /note="WD 4" FT REPEAT 649..688 FT /note="WD 5" FT REPEAT 692..731 FT /note="WD 6" FT REGION 1..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 82..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 371..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 329..349 FT /evidence="ECO:0000255" FT COMPBIAS 85..133 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 371..414 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 411 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 415 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 787 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT HELIX 57..70 FT /evidence="ECO:0007829|PDB:6T9K" FT HELIX 75..86 FT /evidence="ECO:0007829|PDB:6T9K" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:6T9K" FT HELIX 152..164 FT /evidence="ECO:0007829|PDB:2J49" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 171..192 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 194..204 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 209..217 FT /evidence="ECO:0007829|PDB:2J49" FT TURN 218..221 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 225..230 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 232..238 FT /evidence="ECO:0007829|PDB:2J49" FT STRAND 242..246 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 248..260 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 266..276 FT /evidence="ECO:0007829|PDB:2J49" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:2J49" FT HELIX 432..443 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 456..462 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 469..474 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 476..478 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 480..485 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 490..494 FT /evidence="ECO:0007829|PDB:6T9K" FT TURN 504..506 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 517..521 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 528..533 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 537..547 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 549..553 FT /evidence="ECO:0007829|PDB:6T9K" FT TURN 554..556 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 558..563 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 570..574 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 577..580 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 583..586 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 589..595 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 598..606 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 612..617 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 621..628 FT /evidence="ECO:0007829|PDB:6T9K" FT TURN 629..631 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 632..637 FT /evidence="ECO:0007829|PDB:6T9K" FT TURN 638..640 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 643..648 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 654..659 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 661..670 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 675..679 FT /evidence="ECO:0007829|PDB:6T9K" FT TURN 680..682 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 684..689 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 704..706 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 708..712 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 714..728 FT /evidence="ECO:0007829|PDB:6T9K" FT TURN 747..749 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 768..773 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 781..784 FT /evidence="ECO:0007829|PDB:6T9K" FT STRAND 788..795 FT /evidence="ECO:0007829|PDB:6T9K" SQ SEQUENCE 798 AA; 88968 MW; B42315B8C752D0B6 CRC64; MSQKQSTNQN QNGTHQPQPV KNQRTNNAAG ANSGQQPQQQ SQGQSQQQGR SNGPFSASDL NRIVLEYLNK KGYHRTEAML RAESGRTLTP QNKQSPANTK TGKFPEQSSI PPNPGKTAKP ISNPTNLSSK RDAEGGIVSS GRLEGLNAPE NYIRAYSMLK NWVDSSLEIY KPELSYIMYP IFIYLFLNLV AKNPVYARRF FDRFSPDFKD FHGSEINRLF SVNSIDHIKE NEVASAFQSH KYRITMSKTT LNLLLYFLNE NESIGGSLII SVINQHLDPN IVESVTAREK LADGIKVLSD SENGNGKQNL EMNSVPVKLG PFPKDEEFVK EIETELKIKD DQEKQLNQQT AGDNYSGANN RTLLQEYKAM NNEKFKDNTG DDDKDKIKDK IAKDEEKKES ELKVDGEKKD SNLSSPARDI LPLPPKTALD LKLEIQKVKE SRDAIKLDNL QLALPSVCMY TFQNTNKDMS CLDFSDDCRI AAAGFQDSYI KIWSLDGSSL NNPNIALNNN DKDEDPTCKT LVGHSGTVYS TSFSPDNKYL LSGSEDKTVR LWSMDTHTAL VSYKGHNHPV WDVSFSPLGH YFATASHDQT ARLWSCDHIY PLRIFAGHLN DVDCVSFHPN GCYVFTGSSD KTCRMWDVST GDSVRLFLGH TAPVISIAVC PDGRWLSTGS EDGIINVWDI GTGKRLKQMR GHGKNAIYSL SYSKEGNVLI SGGADHTVRV WDLKKATTEP SAEPDEPFIG YLGDVTASIN QDIKEYGRRR TVIPTSDLVA SFYTKKTPVF KVKFSRSNLA LAGGAFRP //