RAD3_YEAST
ID RAD3_YEAST Reviewed; 778 AA.
AC P06839; D3DM79;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPD;
DE Short=TFIIH subunit XPD;
DE EC=3.6.4.12;
DE AltName: Full=DNA repair helicase RAD3;
DE AltName: Full=RNA polymerase II transcription factor B subunit RAD3;
DE Short=TFB subunit RAD3;
GN Name=RAD3; Synonyms=REM1; OrderedLocusNames=YER171W;
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].
RX PubMed=2987851; DOI=10.1093/nar/13.7.2357;
RA Reynolds P., Higgins D.R., Prakash L., Prakash S.;
RT "The nucleotide sequence of the RAD3 gene of Saccharomyces cerevisiae: a
RT potential adenine nucleotide binding amino acid sequence and a nonessential
RT acidic carboxyl terminal region.";
RL Nucleic Acids Res. 13:2357-2372(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3885009; DOI=10.1128/mcb.5.1.17-26.1985;
RA Naumovski L., Chu G., Berg P., Friedberg E.C.;
RT "RAD3 gene of Saccharomyces cerevisiae: nucleotide sequence of wild-type
RT and mutant alleles, transcript mapping, and aspects of gene regulation.";
RL Mol. Cell. Biol. 5:17-26(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 PROTEIN SEQUENCE OF 1-10, AND 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 [6]
RP MUTAGENESIS OF LYS-48.
RX PubMed=2846277; DOI=10.1002/j.1460-2075.1988.tb03193.x;
RA Sung P., Higgins D., Prakash L., Prakash S.;
RT "Mutation of lysine-48 to arginine in the yeast RAD3 protein abolishes its
RT ATPase and DNA helicase activities but not the ability to bind ATP.";
RL EMBO J. 7:3263-3269(1988).
RN [7]
RP MUTAGENESIS OF LYS-48.
RX PubMed=1719538; DOI=10.1073/pnas.88.21.9712;
RA Bailly V., Sung P., Prakash L., Prakash S.;
RT "DNA.RNA helicase activity of RAD3 protein of Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9712-9716(1991).
RN [8]
RP MUTANTS.
RX PubMed=2174856; DOI=10.1128/jb.172.12.6620-6630.1990;
RA Song J.M., Montelone B.A., Siede W., Friedberg E.C.;
RT "Effects of multiple yeast rad3 mutant alleles on UV sensitivity,
RT mutability, and mitotic recombination.";
RL J. Bacteriol. 172:6620-6630(1990).
RN [9]
RP PRESENCE OF A DEAH MOTIF.
RX PubMed=1956796; DOI=10.1093/nar/19.22.6331;
RA Harosh I., Deschavanne P.J.;
RT "The RAD3 gene is a member of the DEAH family RNA helicase-like protein.";
RL Nucleic Acids Res. 19:6331-6331(1991).
RN [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP REVIEW.
RX PubMed=8387143; DOI=10.1111/j.1365-2958.1993.tb01173.x;
RA Deschavanne P.J., Harosh I.;
RT "The Rad3 protein from Saccharomyces cerevisiae: a DNA and DNA:RNA helicase
RT with putative RNA helicase activity.";
RL Mol. Microbiol. 7:831-835(1993).
RN [15]
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 [16]
RP COFACTOR, IRON-SULFUR-BINDING, AND MUTAGENESIS OF LYS-48; ARG-111 AND
RP CYS-115.
RX PubMed=16973432; DOI=10.1016/j.molcel.2006.07.019;
RA Rudolf J., Makrantoni V., Ingledew W.J., Stark M.J., White M.F.;
RT "The DNA repair helicases XPD and FancJ have essential iron-sulfur
RT domains.";
RL Mol. Cell 23:801-808(2006).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.00 ANGSTROMS).
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 [18]
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 5'-3' 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 ATP-dependent helicase
CC activity of XPD/RAD3 is required for DNA opening. In transcription,
CC TFIIH has an essential role in transcription initiation. When the pre-
CC initiation complex (PIC) has been established, TFIIH is required for
CC promoter opening and promoter escape. Phosphorylation of the C-terminal
CC tail (CTD) of the largest subunit of RNA polymerase II by the kinase
CC module TFIIK controls the initiation of transcription. XPD/RAD3 acts by
CC forming a bridge between TFIIK and the core-TFIIH complex. Involved in
CC the maintenance of the fidelity of DNA replication.
CC {ECO:0000269|PubMed:7813015, ECO:0000269|PubMed:7961739,
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:16973432};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305|PubMed:16973432};
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: Present with 14400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000305}.
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DR EMBL; X02368; CAA26215.1; -; Genomic_DNA.
DR EMBL; K03293; AAA34943.1; -; Genomic_DNA.
DR EMBL; U18922; AAB64698.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07833.1; -; Genomic_DNA.
DR PIR; A23308; A23308.
DR RefSeq; NP_011098.3; NM_001179061.3.
DR PDB; 5FMF; EM; 6.00 A; Y=1-778.
DR PDB; 5OQJ; EM; 4.70 A; 0=1-778.
DR PDB; 5OQM; EM; 5.80 A; 0=1-778.
DR PDB; 5SVA; EM; 15.30 A; Y=1-778.
DR PDB; 6GYM; EM; 6.70 A; 0=1-778.
DR PDB; 7K01; EM; 3.90 A; 0=1-778.
DR PDB; 7K04; EM; 9.25 A; 0=1-778.
DR PDB; 7M2U; EM; 8.20 A; 0=1-778.
DR PDB; 7O4I; EM; 3.20 A; 0=1-778.
DR PDB; 7O4J; EM; 2.90 A; 0=1-778.
DR PDB; 7O4K; EM; 3.60 A; 0=1-778.
DR PDB; 7O4L; EM; 3.40 A; 0=1-778.
DR PDB; 7O72; EM; 3.40 A; 0=1-778.
DR PDB; 7O73; EM; 3.40 A; 0=1-778.
DR PDB; 7O75; EM; 3.20 A; 0=1-778.
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; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; P06839; -.
DR SMR; P06839; -.
DR BioGRID; 36924; 195.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR DIP; DIP-2425N; -.
DR IntAct; P06839; 71.
DR MINT; P06839; -.
DR STRING; 4932.YER171W; -.
DR MaxQB; P06839; -.
DR PaxDb; P06839; -.
DR PRIDE; P06839; -.
DR EnsemblFungi; YER171W_mRNA; YER171W; YER171W.
DR GeneID; 856918; -.
DR KEGG; sce:YER171W; -.
DR SGD; S000000973; RAD3.
DR VEuPathDB; FungiDB:YER171W; -.
DR eggNOG; KOG1131; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_011312_1_0_1; -.
DR InParanoid; P06839; -.
DR OMA; IREQFFR; -.
DR BioCyc; YEAST:G3O-30331-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:P06839; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P06839; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0051539; F:4 iron, 4 sulfur cluster binding; IMP:UniProtKB.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IDA:SGD.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; IBA:GO_Central.
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:0045951; P:positive regulation of mitotic recombination; 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 Gene3D; 1.10.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR010643; HBB.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR001945; RAD3/XPD.
DR InterPro; IPR042493; XPD_DNA_FeS.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR PANTHER; PTHR11472:SF1; PTHR11472:SF1; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF06777; HBB; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR PRINTS; PR00852; XRODRMPGMNTD.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; Direct protein sequencing; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..778
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPD"
FT /id="PRO_0000101983"
FT DOMAIN 7..285
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 750..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 235..238
FT /note="DEAH box"
FT COMPBIAS 763..778
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MUTAGEN 48
FT /note="K->R,A: Abolishes ATPase and DNA helicase activities
FT but not ATP-binding capacity."
FT /evidence="ECO:0000269|PubMed:16973432,
FT ECO:0000269|PubMed:1719538, ECO:0000269|PubMed:2846277"
FT MUTAGEN 111
FT /note="R->H: Confers an UV-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:16973432"
FT MUTAGEN 115
FT /note="C->S: Confers an UV-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:16973432"
FT CONFLICT 2
FT /note="K -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7O4L"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 76..96
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:7O4I"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 254..277
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:7O4I"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7O4L"
FT HELIX 328..344
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:7O73"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 414..422
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 447..452
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 468..472
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 492..499
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 516..532
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 534..542
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 544..557
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 559..566
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 576..591
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 596..601
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 618..624
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 633..645
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 650..666
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:7O4L"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 684..688
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 695..698
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 710..723
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 730..733
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 734..737
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 741..751
FT /evidence="ECO:0007829|PDB:7O4J"
SQ SEQUENCE 778 AA; 89786 MW; 978BCA01751949B4 CRC64;
MKFYIDDLPV LFPYPKIYPE QYNYMCDIKK TLDVGGNSIL EMPSGTGKTV SLLSLTIAYQ
MHYPEHRKII YCSRTMSEIE KALVELENLM DYRTKELGYQ EDFRGLGLTS RKNLCLHPEV
SKERKGTVVD EKCRRMTNGQ AKRKLEEDPE ANVELCEYHE NLYNIEVEDY LPKGVFSFEK
LLKYCEEKTL CPYFIVRRMI SLCNIIIYSY HYLLDPKIAE RVSNEVSKDS IVIFDEAHNI
DNVCIESLSL DLTTDALRRA TRGANALDER ISEVRKVDSQ KLQDEYEKLV QGLHSADILT
DQEEPFVETP VLPQDLLTEA IPGNIRRAEH FVSFLKRLIE YLKTRMKVLH VISETPKSFL
QHLKQLTFIE RKPLRFCSER LSLLVRTLEV TEVEDFTALK DIATFATLIS TYEEGFLLII
EPYEIENAAV PNPIMRFTCL DASIAIKPVF ERFSSVIITS GTISPLDMYP RMLNFKTVLQ
KSYAMTLAKK SFLPMIITKG SDQVAISSRF EIRNDPSIVR NYGSMLVEFA KITPDGMVVF
FPSYLYMESI VSMWQTMGIL DEVWKHKLIL VETPDAQETS LALETYRKAC SNGRGAILLS
VARGKVSEGI DFDHQYGRTV LMIGIPFQYT ESRILKARLE FMRENYRIRE NDFLSFDAMR
HAAQCLGRVL RGKDDYGVMV LADRRFSRKR SQLPKWIAQG LSDADLNLST DMAISNTKQF
LRTMAQPTDP KDQEGVSVWS YEDLIKHQNS RKDQGGFIEN ENKEGEQDED EDEDIEMQ
