ID   TFB1_YEAST              Reviewed;         642 AA.
AC   P32776; D6VSU0; E9P948;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=General transcription and DNA repair factor IIH subunit TFB1;
DE            Short=TFIIH subunit TFB1;
DE   AltName: Full=RNA polymerase II transcription factor B 73 kDa subunit;
DE   AltName: Full=RNA polymerase II transcription factor B p73 subunit;
DE   AltName: Full=RNA polymerase II transcription factor B subunit 1;
GN   Name=TFB1; OrderedLocusNames=YDR311W; ORFNames=D9740.3;
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 314-322 AND
RP   630-639.
RX   PubMed=1445600; DOI=10.1126/science.1445600;
RA   Gileadi O., Feaver W.J., Kornberg R.D.;
RT   "Cloning of a subunit of yeast RNA polymerase II transcription factor b and
RT   CTD kinase.";
RL   Science 257:1389-1392(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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   FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION, AND IDENTIFICATION IN
RP   THE TFIIH COMPLEX.
RX   PubMed=7961739; DOI=10.1016/s0021-9258(18)46892-5;
RA   Svejstrup J.Q., Feaver W.J., LaPointe J., Kornberg R.D.;
RT   "RNA polymerase transcription factor IIH holoenzyme from yeast.";
RL   J. Biol. Chem. 269:28044-28048(1994).
RN   [6]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=7813015; DOI=10.1016/0092-8674(95)90447-6;
RA   Svejstrup J.Q., Wang Z., Feaver W.J., Wu X., Bushnell D.A., Donahue T.F.,
RA   Friedberg E.C., Kornberg R.D.;
RT   "Different forms of TFIIH for transcription and DNA repair: holo-TFIIH and
RT   a nucleotide excision repairosome.";
RL   Cell 80:21-28(1995).
RN   [7]
RP   FUNCTION OF THE TFIIH CORE COMPLEX IN DNA REPAIR.
RX   PubMed=8631896; DOI=10.1074/jbc.271.18.10821;
RA   Sung P., Guzder S.N., Prakash L., Prakash S.;
RT   "Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3
RT   and Rad25, in the incision step of nucleotide excision repair.";
RL   J. Biol. Chem. 271:10821-10826(1996).
RN   [8]
RP   IDENTIFICATION IN THE TFIIH CORE COMPLEX.
RX   PubMed=14500720; DOI=10.1074/jbc.c300417200;
RA   Takagi Y., Komori H., Chang W.-H., Hudmon A., Erdjument-Bromage H.,
RA   Tempst P., Kornberg R.D.;
RT   "Revised subunit structure of yeast transcription factor IIH (TFIIH) and
RT   reconciliation with human TFIIH.";
RL   J. Biol. Chem. 278:43897-43900(2003).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150, AND IDENTIFICATION BY
RP   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   [11]
RP   STRUCTURE BY NMR OF 2-115, AND INTERACTION WITH RAD2.
RX   PubMed=22373916; DOI=10.1093/nar/gks194;
RA   Lafrance-Vanasse J., Arseneault G., Cappadocia L., Chen H.T., Legault P.,
RA   Omichinski J.G.;
RT   "Structural and functional characterization of interactions involving the
RT   Tfb1 subunit of TFIIH and the NER factor Rad2.";
RL   Nucleic Acids Res. 40:5739-5750(2012).
RN   [12]
RP   STRUCTURE BY NMR OF 2-115.
RX   PubMed=23295669; DOI=10.1093/nar/gks1321;
RA   Lafrance-Vanasse J., Arseneault G., Cappadocia L., Legault P.,
RA   Omichinski J.G.;
RT   "Structural and functional evidence that Rad4 competes with Rad2 for
RT   binding to the Tfb1 subunit of TFIIH in NER.";
RL   Nucleic Acids Res. 41:2736-2745(2013).
CC   -!- FUNCTION: Component of the general transcription and DNA repair factor
CC       IIH (TFIIH) core complex, which is involved in general and
CC       transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC       and, when complexed to TFIIK, in RNA transcription by RNA polymerase
CC       II. In NER, TFIIH acts by opening DNA around the lesion to allow the
CC       excision of the damaged oligonucleotide and its replacement by a new
CC       DNA fragment. In transcription, TFIIH has an essential role in
CC       transcription initiation. When the pre-initiation complex (PIC) has
CC       been established, TFIIH is required for promoter opening and promoter
CC       escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC       subunit of RNA polymerase II by the kinase module TFIIK controls the
CC       initiation of transcription. {ECO:0000269|PubMed:7813015,
CC       ECO:0000269|PubMed:7961739, ECO:0000269|PubMed:8631896}.
CC   -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC       XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in
CC       NER. The core complex associates with the 3-subunit CTD-kinase module
CC       TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit
CC       holoenzyme (holo-TFIIH) active in transcription (PubMed:7961739,
CC       PubMed:7813015, PubMed:14500720). Interacts with XPC/RAD4. XPC/RAD4
CC       recruits TFIIH to the NER machinery (PubMed:23295669). Interacts with
CC       the NER 3'-endonuclease XPG/RAD2. XPG/RAD2 displaces XPC/RAD4 from the
CC       repair complex (PubMed:22373916, PubMed:23295669).
CC       {ECO:0000269|PubMed:14500720, ECO:0000269|PubMed:22373916,
CC       ECO:0000269|PubMed:23295669, ECO:0000269|PubMed:7813015,
CC       ECO:0000269|PubMed:7961739}.
CC   -!- INTERACTION:
CC       P32776; Q13351: KLF1; Xeno; NbExp=3; IntAct=EBI-19146, EBI-8284732;
CC       P32776; P04637: TP53; Xeno; NbExp=7; IntAct=EBI-19146, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 5150 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TFB1 family. {ECO:0000305}.
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DR   EMBL; M95750; AAA35143.1; -; Genomic_DNA.
DR   EMBL; U28374; AAB64747.1; -; Genomic_DNA.
DR   EMBL; AY723790; AAU09707.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12150.1; -; Genomic_DNA.
DR   PIR; S31285; S31285.
DR   RefSeq; NP_010597.3; NM_001180619.3.
DR   PDB; 1Y5O; NMR; -; A=1-115.
DR   PDB; 2GS0; NMR; -; A=1-115.
DR   PDB; 2K2U; NMR; -; A=1-115.
DR   PDB; 2L2I; NMR; -; A=2-115.
DR   PDB; 2LOX; NMR; -; A=2-115.
DR   PDB; 2M14; NMR; -; A=2-115.
DR   PDB; 2MKR; NMR; -; A=1-115.
DR   PDB; 2N0Y; NMR; -; A=1-115.
DR   PDB; 2N23; NMR; -; A=2-115.
DR   PDB; 5OQJ; EM; 4.70 A; 1=1-642.
DR   PDB; 5OQM; EM; 5.80 A; 1=1-642.
DR   PDB; 5URN; NMR; -; A=2-115.
DR   PDB; 6GYM; EM; 6.70 A; 1=1-642.
DR   PDB; 7K01; EM; 3.90 A; 1=1-642.
DR   PDB; 7K04; EM; 9.25 A; 1=2-642.
DR   PDB; 7M2U; EM; 8.20 A; 1=1-642.
DR   PDB; 7ML0; EM; 3.00 A; 1=1-642.
DR   PDB; 7ML1; EM; 4.00 A; 1=1-642.
DR   PDB; 7ML2; EM; 3.40 A; 1=1-642.
DR   PDB; 7ML3; EM; 7.60 A; 1=1-642.
DR   PDB; 7ML4; EM; 3.10 A; 1=1-642.
DR   PDB; 7O4I; EM; 3.20 A; 1=1-642.
DR   PDB; 7O4J; EM; 2.90 A; 1=1-642.
DR   PDB; 7O4K; EM; 3.60 A; 1=1-642.
DR   PDB; 7O4L; EM; 3.40 A; 1=1-642.
DR   PDB; 7O72; EM; 3.40 A; 1=1-642.
DR   PDB; 7O73; EM; 3.40 A; 1=1-642.
DR   PDB; 7O75; EM; 3.20 A; 1=1-642.
DR   PDB; 7ZS9; EM; 3.10 A; 1=1-642.
DR   PDB; 7ZSA; EM; 4.00 A; 1=1-642.
DR   PDB; 7ZSB; EM; 6.60 A; 1=1-642.
DR   PDBsum; 1Y5O; -.
DR   PDBsum; 2GS0; -.
DR   PDBsum; 2K2U; -.
DR   PDBsum; 2L2I; -.
DR   PDBsum; 2LOX; -.
DR   PDBsum; 2M14; -.
DR   PDBsum; 2MKR; -.
DR   PDBsum; 2N0Y; -.
DR   PDBsum; 2N23; -.
DR   PDBsum; 5OQJ; -.
DR   PDBsum; 5OQM; -.
DR   PDBsum; 5URN; -.
DR   PDBsum; 6GYM; -.
DR   PDBsum; 7K01; -.
DR   PDBsum; 7K04; -.
DR   PDBsum; 7M2U; -.
DR   PDBsum; 7ML0; -.
DR   PDBsum; 7ML1; -.
DR   PDBsum; 7ML2; -.
DR   PDBsum; 7ML3; -.
DR   PDBsum; 7ML4; -.
DR   PDBsum; 7O4I; -.
DR   PDBsum; 7O4J; -.
DR   PDBsum; 7O4K; -.
DR   PDBsum; 7O4L; -.
DR   PDBsum; 7O72; -.
DR   PDBsum; 7O73; -.
DR   PDBsum; 7O75; -.
DR   PDBsum; 7ZS9; -.
DR   PDBsum; 7ZSA; -.
DR   PDBsum; 7ZSB; -.
DR   AlphaFoldDB; P32776; -.
DR   BMRB; P32776; -.
DR   EMDB; EMD-0092; -.
DR   EMDB; EMD-12719; -.
DR   EMDB; EMD-12720; -.
DR   EMDB; EMD-12721; -.
DR   EMDB; EMD-12722; -.
DR   EMDB; EMD-12743; -.
DR   EMDB; EMD-12744; -.
DR   EMDB; EMD-12745; -.
DR   EMDB; EMD-14927; -.
DR   EMDB; EMD-14928; -.
DR   EMDB; EMD-14929; -.
DR   EMDB; EMD-22587; -.
DR   EMDB; EMD-22588; -.
DR   EMDB; EMD-23905; -.
DR   EMDB; EMD-23906; -.
DR   EMDB; EMD-23907; -.
DR   EMDB; EMD-23908; -.
DR   EMDB; EMD-3846; -.
DR   EMDB; EMD-3850; -.
DR   SMR; P32776; -.
DR   BioGRID; 32364; 714.
DR   ComplexPortal; CPX-1659; General transcription factor TFIIH complex.
DR   DIP; DIP-1702N; -.
DR   IntAct; P32776; 45.
DR   MINT; P32776; -.
DR   STRING; 4932.YDR311W; -.
DR   iPTMnet; P32776; -.
DR   MaxQB; P32776; -.
DR   PaxDb; 4932-YDR311W; -.
DR   PeptideAtlas; P32776; -.
DR   EnsemblFungi; YDR311W_mRNA; YDR311W; YDR311W.
DR   GeneID; 851906; -.
DR   KEGG; sce:YDR311W; -.
DR   AGR; SGD:S000002719; -.
DR   SGD; S000002719; TFB1.
DR   VEuPathDB; FungiDB:YDR311W; -.
DR   eggNOG; KOG2074; Eukaryota.
DR   GeneTree; ENSGT00390000015066; -.
DR   HOGENOM; CLU_019188_0_0_1; -.
DR   InParanoid; P32776; -.
DR   OMA; QYVFSFT; -.
DR   OrthoDB; 1447146at2759; -.
DR   BioCyc; YEAST:G3O-29870-MONOMER; -.
DR   Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR   Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-SCE-72086; mRNA Capping.
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-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   BioGRID-ORCS; 851906; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P32776; -.
DR   PRO; PR:P32776; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P32776; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:SGD.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IMP:SGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal.
DR   CDD; cd13229; PH_TFIIH; 1.
DR   DisProt; DP01638; -.
DR   Gene3D; 1.10.3970.10; BSD domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   IDEAL; IID50021; -.
DR   InterPro; IPR005607; BSD_dom.
DR   InterPro; IPR035925; BSD_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR027079; Tfb1/GTF2H1.
DR   InterPro; IPR013876; TFIIH_BTF_p62_N.
DR   PANTHER; PTHR12856:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 1; 1.
DR   PANTHER; PTHR12856; TRANSCRIPTION INITIATION FACTOR IIH-RELATED; 1.
DR   Pfam; PF03909; BSD; 2.
DR   Pfam; PF08567; PH_TFIIH; 1.
DR   SMART; SM00751; BSD; 2.
DR   SUPFAM; SSF140383; BSD domain-like; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50858; BSD; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA damage; DNA repair; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..642
FT                   /note="General transcription and DNA repair factor IIH
FT                   subunit TFB1"
FT                   /id="PRO_0000119261"
FT   DOMAIN          165..221
FT                   /note="BSD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT   DOMAIN          243..295
FT                   /note="BSD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT   REGION          65..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         150
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        209
FT                   /note="F -> L (in Ref. 4; AAU09707)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          12..19
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          26..35
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:7O4L"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:1Y5O"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:2K2U"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           94..120
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           171..176
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           178..187
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           189..199
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:7O75"
FT   HELIX           206..209
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           214..224
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           233..236
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          246..252
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           253..262
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           264..271
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   TURN            272..277
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           280..289
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           291..296
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          302..304
FT                   /evidence="ECO:0007829|PDB:7ML4"
FT   HELIX           309..312
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           315..329
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           335..337
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           339..343
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           356..358
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           371..389
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   TURN            395..397
FT                   /evidence="ECO:0007829|PDB:7ML0"
FT   HELIX           398..411
FT                   /evidence="ECO:0007829|PDB:7ML0"
FT   HELIX           414..419
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           422..424
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           426..430
FT                   /evidence="ECO:0007829|PDB:7ML0"
FT   HELIX           466..482
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           487..489
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   STRAND          493..495
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           496..514
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           544..568
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           573..575
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           576..604
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   TURN            605..608
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           609..615
FT                   /evidence="ECO:0007829|PDB:7O4J"
FT   HELIX           617..638
FT                   /evidence="ECO:0007829|PDB:7O4J"
SQ   SEQUENCE   642 AA;  72894 MW;  DAE369FE90A224F8 CRC64;
     MSHSGAAIFE KVSGIIAINE DVSPAELTWR STDGDKVHTV VLSTIDKLQA TPASSEKMML
     RLIGKVDESK KRKDNEGNEV VPKPQRHMFS FNNRTVMDNI KMTLQQIISR YKDADIYEEK
     RRREESAQHT ETPMSSSSVT AGTPTPHLDT PQLNNGAPLI NTAKLDDSLS KEKLLTNLKL
     QQSLLKGNKV LMKVFQETVI NAGLPPSEFW STRIPLLRAF ALSTSQKVGP YNVLSTIKPV
     ASSENKVNVN LSREKILNIF ENYPIVKKAY TDNVPKNFKE PEFWARFFSS KLFRKLRGEK
     IMQNDRGDVI IDRYLTLDQE FDRKDDDMLL HPVKKIIDLD GNIQDDPVVR GNRPDFTMQP
     GVDINGNSDG TVDILKGMNR LSEKMIMALK NEYSRTNLQN KSNITNDEED EDNDERNELK
     IDDLNESYKT NYAIIHLKRN AHEKTTDNDA KSSADSIKNA DLKVSNQQML QQLSLVMDNL
     INKLDLNQVV PNNEVSNKIN KRVITAIKIN AKQAKHNNVN SALGSFVDNT SQANELEVKS
     TLPIDLLESC RMLHTTCCEF LKHFYIHFQS GEQKQASTVK KLYNHLKDCI EKLNELFQDV
     LNGDGESMSN TCTAYLKPVL NSITLATHKY DEYFNEYNNN SN
//