TFB1_YEAST
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 03-AUG-2022, entry version 192.
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; 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 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; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; P32776; -.
DR BMRB; P32776; -.
DR SMR; P32776; -.
DR BioGRID; 32364; 711.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR DIP; DIP-1702N; -.
DR IntAct; P32776; 45.
DR MINT; P32776; -.
DR STRING; 4932.YDR311W; -.
DR iPTMnet; P32776; -.
DR MaxQB; P32776; -.
DR PaxDb; P32776; -.
DR PRIDE; P32776; -.
DR EnsemblFungi; YDR311W_mRNA; YDR311W; YDR311W.
DR GeneID; 851906; -.
DR KEGG; sce:YDR311W; -.
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; IYNENVP; -.
DR BioCyc; YEAST:G3O-29870-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
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-75955; RNA Polymerase II Transcription Elongation.
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 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:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
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 from RNA polymerase II promoter; IDA:ComplexPortal.
DR DisProt; DP01638; -.
DR Gene3D; 1.10.3970.10; -; 1.
DR Gene3D; 2.30.29.30; -; 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; PTHR12856; 1.
DR Pfam; PF03909; BSD; 2.
DR Pfam; PF08567; PH_TFIIH; 1.
DR SMART; SM00751; BSD; 2.
DR SUPFAM; SSF140383; SSF140383; 2.
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 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 HELIX 414..419
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:7O4J"
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
