TAF5_YEAST
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 03-AUG-2022, entry version 209.
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; 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}.
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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 SMR; P38129; -.
DR BioGRID; 32895; 864.
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 iPTMnet; P38129; -.
DR MaxQB; P38129; -.
DR PaxDb; P38129; -.
DR PRIDE; P38129; -.
DR EnsemblFungi; YBR198C_mRNA; YBR198C; YBR198C.
DR GeneID; 852497; -.
DR KEGG; sce:YBR198C; -.
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 BioCyc; YEAST:G3O-29139-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 EvolutionaryTrace; P38129; -.
DR PRO; PR:P38129; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38129; protein.
DR GO; GO:0005634; C:nucleus; IC: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:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
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; IC:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd08044; TAF5_NTD2; 1.
DR Gene3D; 1.25.40.500; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037783; Taf5.
DR InterPro; IPR007582; TFIID_NTD2.
DR InterPro; IPR037264; TFIID_NTD2_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19879; PTHR19879; 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; SSF160897; 1.
DR SUPFAM; SSF50978; SSF50978; 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
