ID RAD25_YEAST Reviewed; 843 AA. AC Q00578; D6VVE4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 27-MAR-2024, entry version 209. DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB; DE Short=TFIIH subunit XPB; DE EC=3.6.4.12; DE AltName: Full=DNA repair helicase RAD25; DE AltName: Full=RNA polymerase II transcription factor B subunit SSL2; DE Short=TFB subunit SSL2; DE AltName: Full=Suppressor of stem-loop mutation 2; GN Name=SSL2; Synonyms=LOM3, RAD25, UVS112; OrderedLocusNames=YIL143C; 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 VARIANT SUPPRESSOR MUTANT LEU-427. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1318786; DOI=10.1016/0092-8674(92)90621-i; RA Gulyas K.D., Donahue T.F.; RT "SSL2, a suppressor of a stem-loop mutation in the HIS4 leader encodes the RT yeast homolog of human ERCC-3."; RL Cell 69:1031-1042(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1333609; DOI=10.1073/pnas.89.23.11416; RA Park E.K., Guzder S.N., Weeda G., Hoeijmakers J.H., Prakash S., Prakash L.; RT "RAD25 (SSL2), the yeast homolog of the human Xeroderma pigmentosum group B RT DNA repair gene, is essential for viability."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11416-11420(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(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. RX PubMed=8269516; DOI=10.1016/0092-8674(93)90624-y; RA Feaver W.J., Svejstrup J.Q., Bardwell L., Bardwell A.J., Buratowski S., RA Gulyas K.D., Donahue T.F., Friedberg E.C., Kornberg R.D.; RT "Dual roles of a multiprotein complex from S. cerevisiae in transcription RT and DNA repair."; RL Cell 75:1379-1387(1993). RN [7] RP FUNCTION. RX PubMed=7693549; DOI=10.1101/gad.7.11.2161; RA Qiu H., Park E., Prakash L., Prakash S.; RT "The Saccharomyces cerevisiae DNA repair gene RAD25 is required for RT transcription by RNA polymerase II."; RL Genes Dev. 7:2161-2171(1993). RN [8] RP FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION. 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 [9] RP FUNCTION. RX PubMed=8202161; DOI=10.1038/369578a0; RA Guzder S.N., Sung P., Bailly V., Prakash L., Prakash S.; RT "RAD25 is a DNA helicase required for DNA repair and RNA polymerase II RT transcription."; RL Nature 369:578-581(1994). RN [10] 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 [11] 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 [12] 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [15] RP FUNCTION. RX PubMed=25775526; DOI=10.1073/pnas.1417709112; RA Fishburn J., Tomko E., Galburt E., Hahn S.; RT "Double-stranded DNA translocase activity of transcription factor TFIIH and RT the mechanism of RNA polymerase II open complex formation."; RL Proc. Natl. Acad. Sci. U.S.A. 112:3961-3966(2015). RN [16] RP STRUCTURE BY ELECTRON MICROSCOPY (6.00 ANGSTROMS) OF 294-785. RX PubMed=26483468; DOI=10.1073/pnas.1518255112; RA Murakami K., Tsai K.L., Kalisman N., Bushnell D.A., Asturias F.J., RA Kornberg R.D.; RT "Structure of an RNA polymerase II preinitiation complex."; RL Proc. Natl. Acad. Sci. U.S.A. 112:13543-13548(2015). RN [17] RP STRUCTURE BY ELECTRON MICROSCOPY (15.30 ANGSTROMS). RX PubMed=27610567; DOI=10.1016/j.cell.2016.08.050; RA Robinson P.J., Trnka M.J., Bushnell D.A., Davis R.E., Mattei P.J., RA Burlingame A.L., Kornberg R.D.; RT "Structure of a complete mediator-RNA polymerase II pre-initiation RT complex."; RL Cell 166:1411-1422(2016). CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general CC transcription and DNA repair factor IIH (TFIIH) core complex, which is CC involved in general and transcription-coupled nucleotide excision CC repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA CC transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA CC around the lesion to allow the excision of the damaged oligonucleotide CC and its replacement by a new DNA fragment. The ATPase activity of CC XPB/SSL2, but not its helicase activity, is required for DNA opening. CC In transcription, TFIIH has an essential role in transcription CC initiation. When the pre-initiation complex (PIC) has been established, CC TFIIH is required for promoter opening and promoter escape. The ATP- CC dependent helicase activity of XPB/SSL2 is required for promoter CC opening and promoter escape. Phosphorylation of the C-terminal tail CC (CTD) of the largest subunit of RNA polymerase II by the kinase module CC TFIIK controls the initiation of transcription (PubMed:8269516, CC PubMed:7693549, PubMed:7961739, PubMed:8202161, PubMed:7813015, CC PubMed:8631896). XPB/SSL2 acts as a double-stranded DNA translocase CC promoting DNA opening by tracking along the nontemplate promoter CC strand, rotating and inserting DNA into the Pol II active site cleft, CC leading to DNA unwinding. May also use this translocase mechanism CC during DNA repair rather than physically wedging open damaged DNA CC (PubMed:25775526). {ECO:0000269|PubMed:25775526, CC ECO:0000269|PubMed:7693549, ECO:0000269|PubMed:7813015, CC ECO:0000269|PubMed:7961739, ECO:0000269|PubMed:8202161, CC ECO:0000269|PubMed:8269516, ECO:0000269|PubMed:8631896}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; 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. CC {ECO:0000269|PubMed:14500720, ECO:0000269|PubMed:7813015, CC ECO:0000269|PubMed:7961739}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: A C-terminal deletion renders yeast hypersensitive to UV CC light. CC -!- MISCELLANEOUS: Present with 825 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily. CC {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; Z38059; CAA86135.1; -; Genomic_DNA. DR EMBL; M94176; AAA35102.1; -; Genomic_DNA. DR EMBL; L01414; AAA34942.1; -; Genomic_DNA. DR EMBL; AY692883; AAT92902.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08410.1; -; Genomic_DNA. DR PIR; S31272; S31272. DR RefSeq; NP_012123.1; NM_001179491.1. DR PDB; 5FMF; EM; 6.00 A; 1=294-785. DR PDB; 5OQJ; EM; 4.70 A; 7=1-843. DR PDB; 5OQM; EM; 5.80 A; 7=1-843. DR PDB; 5SVA; EM; 15.30 A; Z=1-843. DR PDB; 6GYM; EM; 6.70 A; 7=1-843. DR PDB; 7K01; EM; 3.90 A; 7=1-843. DR PDB; 7K04; EM; 9.25 A; 7=1-843. DR PDB; 7M2U; EM; 8.20 A; 7=1-843. DR PDB; 7ML0; EM; 3.00 A; 7=1-843. DR PDB; 7ML1; EM; 4.00 A; 7=1-843. DR PDB; 7ML2; EM; 3.40 A; 7=1-843. DR PDB; 7ML3; EM; 7.60 A; 7=1-843. DR PDB; 7ML4; EM; 3.10 A; 7=1-843. DR PDB; 7O4I; EM; 3.20 A; 7=1-843. DR PDB; 7O4J; EM; 2.90 A; 7=1-843. DR PDB; 7O4K; EM; 3.60 A; 7=1-843. DR PDB; 7O4L; EM; 3.40 A; 7=1-843. DR PDB; 7O72; EM; 3.40 A; 7=1-843. DR PDB; 7O73; EM; 3.40 A; 7=1-843. DR PDB; 7O75; EM; 3.20 A; 7=1-843. DR PDB; 7ZS9; EM; 3.10 A; 7=1-843. DR PDB; 7ZSA; EM; 4.00 A; 7=1-843. DR PDB; 7ZSB; EM; 6.60 A; 7=1-843. DR PDB; 8CEN; EM; 3.00 A; 7=1-843. DR PDB; 8CEO; EM; 3.60 A; 7=1-843. DR PDBsum; 5FMF; -. DR PDBsum; 5OQJ; -. DR PDBsum; 5OQM; -. DR PDBsum; 5SVA; -. 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 PDBsum; 8CEN; -. DR PDBsum; 8CEO; -. DR AlphaFoldDB; Q00578; -. 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-23904; -. 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 EMDB; EMD-8305; -. DR SMR; Q00578; -. DR BioGRID; 34849; 140. DR ComplexPortal; CPX-1659; General transcription factor TFIIH complex. DR DIP; DIP-731N; -. DR IntAct; Q00578; 23. DR MINT; Q00578; -. DR STRING; 4932.YIL143C; -. DR iPTMnet; Q00578; -. DR MaxQB; Q00578; -. DR PaxDb; 4932-YIL143C; -. DR PeptideAtlas; Q00578; -. DR TopDownProteomics; Q00578; -. DR EnsemblFungi; YIL143C_mRNA; YIL143C; YIL143C. DR GeneID; 854663; -. DR KEGG; sce:YIL143C; -. DR AGR; SGD:S000001405; -. DR SGD; S000001405; SSL2. DR VEuPathDB; FungiDB:YIL143C; -. DR eggNOG; KOG1123; Eukaryota. DR GeneTree; ENSGT00390000002204; -. DR HOGENOM; CLU_008213_0_0_1; -. DR InParanoid; Q00578; -. DR OMA; RCQEIDY; -. DR OrthoDB; 1360679at2759; -. DR BioCyc; YEAST:G3O-31393-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; 854663; 7 hits in 10 CRISPR screens. DR PRO; PR:Q00578; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; Q00578; 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:0097550; C:transcription preinitiation complex; IDA:SGD. DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IDA:SGD. DR GO; GO:0015616; F:DNA translocase activity; IMP:SGD. DR GO; GO:0032508; P:DNA duplex unwinding; IDA:SGD. DR GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD. DR GO; GO:0000019; P:regulation of mitotic recombination; IMP:SGD. DR GO; GO:0001111; P:RNA polymerase II promoter clearance; 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 GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IMP:SGD. DR CDD; cd18029; DEXHc_XPB; 1. DR CDD; cd18789; SF2_C_XPB; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR032438; ERCC3_RAD25_C. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001161; XPB/Ssl2. DR InterPro; IPR032830; XPB/Ssl2_N. DR NCBIfam; TIGR00603; rad25; 1. DR PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1. DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1. DR Pfam; PF16203; ERCC3_RAD25_C; 1. DR Pfam; PF13625; Helicase_C_3; 1. DR Pfam; PF04851; ResIII; 1. DR PRINTS; PR00851; XRODRMPGMNTB. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..843 FT /note="General transcription and DNA repair factor IIH FT helicase subunit XPB" FT /id="PRO_0000101994" FT DOMAIN 373..535 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 589..743 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..85 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 64..75 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 487..491 FT /note="DEVH box" FT COMPBIAS 44..62 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 386..393 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 752 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950" FT VARIANT 427 FT /note="W -> L (in suppressor mutant)" FT /evidence="ECO:0000269|PubMed:1318786" FT CONFLICT 9 FT /note="P -> S (in Ref. 2; AAA34942)" FT /evidence="ECO:0000305" FT CONFLICT 48 FT /note="S -> L (in Ref. 2; AAA34942)" FT /evidence="ECO:0000305" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:7ML4" FT TURN 125..129 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 140..144 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:7O4L" FT HELIX 150..160 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 177..183 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 184..187 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 190..200 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 207..216 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 218..221 FT /evidence="ECO:0007829|PDB:7ML4" FT STRAND 224..228 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 242..245 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:7ML0" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:7ML4" FT STRAND 262..267 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:7ML0" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:7ML4" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 323..332 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:7O4L" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:7ML4" FT HELIX 364..374 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 375..380 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 382..385 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 392..403 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 407..410 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 414..427 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:7ML4" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 435..441 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 448..450 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 452..455 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 457..460 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 468..479 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 482..489 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 490..492 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 496..498 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 499..504 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 510..515 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 523..526 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 527..530 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 534..537 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 540..545 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 546..549 FT /evidence="ECO:0007829|PDB:7ML4" FT STRAND 552..560 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 563..571 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 574..582 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 585..600 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 605..608 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 612..622 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 633..645 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 647..649 FT /evidence="ECO:0007829|PDB:7ML0" FT STRAND 651..653 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 656..659 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 669..673 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 677..679 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 680..688 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 689..692 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 694..697 FT /evidence="ECO:0007829|PDB:7ZS9" FT STRAND 698..700 FT /evidence="ECO:0007829|PDB:7ML4" FT STRAND 703..711 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 714..719 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 720..723 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 724..729 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 734..737 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 740..743 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 753..764 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 832..836 FT /evidence="ECO:0007829|PDB:7O4J" SQ SEQUENCE 843 AA; 95341 MW; FA4013E8156FE1C5 CRC64; MTDVEGYQPK SKGKIFPDMG ESFFSSDEDS PATDAEIDEN YDDNRETSEG RGERDTGAMV TGLKKPRKKT KSSRHTAADS SMNQMDAKDK ALLQDTNSDI PADFVPDSVS GMFRSHDFSY LRLRPDHASR PLWISPSDGR IILESFSPLA EQAQDFLVTI AEPISRPSHI HEYKITAYSL YAAVSVGLET DDIISVLDRL SKVPVAESII NFIKGATISY GKVKLVIKHN RYFVETTQAD ILQMLLNDSV IGPLRIDSDH QVQPPEDVLQ QQLQQTAGKP ATNVNPNDVE AVFSAVIGGD NEREEEDDDI DAVHSFEIAN ESVEVVKKRC QEIDYPVLEE YDFRNDHRNP DLDIDLKPST QIRPYQEKSL SKMFGNGRAR SGIIVLPCGA GKTLVGITAA CTIKKSVIVL CTSSVSVMQW RQQFLQWCTL QPENCAVFTS DNKEMFQTES GLVVSTYSMV ANTRNRSHDS QKVMDFLTGR EWGFIILDEV HVVPAAMFRR VVSTIAAHAK LGLTATLVRE DDKIGDLNFL IGPKLYEANW MELSQKGHIA NVQCAEVWCP MTAEFYQEYL RETARKRMLL YIMNPTKFQA CQFLIQYHER RGDKIIVFSD NVYALQEYAL KMGKPFIYGS TPQQERMNIL QNFQYNDQIN TIFLSKVGDT SIDLPEATCL IQISSHYGSR RQEAQRLGRI LRAKRRNDEG FNAFFYSLVS KDTQEMYYST KRQAFLVDQG YAFKVITHLH GMENIPNLAY ASPRERRELL QEVLLKNEEA AGIEVGDDAD NSVGRGSNGH KRFKSKAVRG EGSLSGLAGG EDMAYMEYST NKNKELKEHH PLIRKMYYKN LKK //