RAD25_YEAST
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 03-AUG-2022, entry version 200.
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}.
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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 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 AlphaFoldDB; Q00578; -.
DR SMR; Q00578; -.
DR BioGRID; 34849; 135.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR DIP; DIP-731N; -.
DR IntAct; Q00578; 23.
DR MINT; Q00578; -.
DR STRING; 4932.YIL143C; -.
DR iPTMnet; Q00578; -.
DR MaxQB; Q00578; -.
DR PaxDb; Q00578; -.
DR PRIDE; Q00578; -.
DR TopDownProteomics; Q00578; -.
DR EnsemblFungi; YIL143C_mRNA; YIL143C; YIL143C.
DR GeneID; 854663; -.
DR KEGG; sce:YIL143C; -.
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; PTHIHEY; -.
DR BioCyc; YEAST:G3O-31393-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 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:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0000019; P:regulation of mitotic recombination; IMP:SGD.
DR GO; GO:0010525; P:regulation of transposition, RNA-mediated; 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 GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00603; rad25; 1.
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 HELIX 110..112
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:7O4J"
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 STRAND 218..222
FT /evidence="ECO:0007829|PDB:7O75"
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 248..250
FT /evidence="ECO:0007829|PDB:7O4I"
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 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 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 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 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 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 HELIX 680..688
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:7O4I"
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 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
