MLE_DROME
ID MLE_DROME Reviewed; 1293 AA.
AC P24785; Q86NQ4; Q9V9J1;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Dosage compensation regulator;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase mle;
DE AltName: Full=Protein male-less;
DE AltName: Full=Protein maleless;
DE AltName: Full=Protein no action potential;
GN Name=mle {ECO:0000312|FlyBase:FBgn0002774};
GN Synonyms=nap {ECO:0000312|FlyBase:FBgn0002774};
GN ORFNames=CG11680 {ECO:0000312|FlyBase:FBgn0002774};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND A), FUNCTION, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Imaginal disk;
RX PubMed=1653648; DOI=10.1016/0092-8674(91)90439-6;
RA Kuroda M.I., Kernan M.J., Kreber R., Ganetzky B., Baker B.S.;
RT "The maleless protein associates with the X chromosome to regulate dosage
RT compensation in Drosophila.";
RL Cell 66:935-947(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH TOP2.
RX PubMed=23989663; DOI=10.4161/trns.26185;
RA Cugusi S., Ramos E., Ling H., Yokoyama R., Luk K.M., Lucchesi J.C.;
RT "Topoisomerase II plays a role in dosage compensation in Drosophila.";
RL Transcription 4:238-250(2013).
CC -!- FUNCTION: Required in males for dosage compensation of X chromosome
CC linked genes. Mle, msl-1 and msl-3 are colocalized on X chromosome.
CC Each of the msl proteins requires all the other msls for wild-type X-
CC chromosome binding. Probably unwinds double-stranded DNA and RNA in a
CC 3' to 5' direction. {ECO:0000269|PubMed:1653648}.
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=3.6.4.13;
CC -!- SUBUNIT: Interacts with Top2. {ECO:0000269|PubMed:23989663}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1653648}. Chromosome
CC {ECO:0000269|PubMed:1653648}. Note=Mle is associated with hundreds of
CC discrete sites along the length of the X chromosome in males and not in
CC females, and is associated with 30-40 autosomal sites in both sexes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=A; Synonyms=25;
CC IsoId=P24785-1; Sequence=Displayed;
CC Name=12;
CC IsoId=P24785-2; Sequence=VSP_005775, VSP_005776;
CC Name=B;
CC IsoId=P24785-3; Sequence=VSP_015690;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development; highest in
CC embryos and at equal levels in males and females.
CC {ECO:0000269|PubMed:1653648}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH 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; M74121; AAC41573.1; -; mRNA.
DR EMBL; AE013599; AAF57297.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68335.1; -; Genomic_DNA.
DR EMBL; BT003785; AAO41468.1; -; mRNA.
DR EMBL; BT010267; AAQ23585.1; -; mRNA.
DR PIR; B40025; B40025.
DR RefSeq; NP_476641.1; NM_057293.4. [P24785-1]
DR RefSeq; NP_724440.1; NM_165451.3. [P24785-3]
DR PDB; 5AOR; X-ray; 2.08 A; A/B=1-1293.
DR PDB; 5ZTM; X-ray; 2.90 A; A/B=1-264.
DR PDB; 6I3R; NMR; -; A=1-257.
DR PDBsum; 5AOR; -.
DR PDBsum; 5ZTM; -.
DR PDBsum; 6I3R; -.
DR AlphaFoldDB; P24785; -.
DR SASBDB; P24785; -.
DR SMR; P24785; -.
DR BioGRID; 61429; 41.
DR IntAct; P24785; 6.
DR STRING; 7227.FBpp0085367; -.
DR PaxDb; P24785; -.
DR PRIDE; P24785; -.
DR EnsemblMetazoa; FBtr0086031; FBpp0085367; FBgn0002774. [P24785-1]
DR EnsemblMetazoa; FBtr0100576; FBpp0100031; FBgn0002774. [P24785-3]
DR GeneID; 35523; -.
DR KEGG; dme:Dmel_CG11680; -.
DR CTD; 35523; -.
DR FlyBase; FBgn0002774; mle.
DR VEuPathDB; VectorBase:FBgn0002774; -.
DR eggNOG; KOG0921; Eukaryota.
DR GeneTree; ENSGT00940000155924; -.
DR InParanoid; P24785; -.
DR OMA; YGPETRM; -.
DR PhylomeDB; P24785; -.
DR Reactome; R-DME-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-DME-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P24785; -.
DR BioGRID-ORCS; 35523; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35523; -.
DR PRO; PR:P24785; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0002774; Expressed in embryonic/larval hemocyte (Drosophila) and 22 other tissues.
DR ExpressionAtlas; P24785; baseline and differential.
DR Genevisible; P24785; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0072487; C:MSL complex; IDA:FlyBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0000805; C:X chromosome; IDA:FlyBase.
DR GO; GO:0016456; C:X chromosome located dosage compensation complex, transcription activating; NAS:FlyBase.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; IEA:InterPro.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IMP:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0004386; F:helicase activity; ISS:FlyBase.
DR GO; GO:0106222; F:lncRNA binding; IDA:FlyBase.
DR GO; GO:0001069; F:regulatory region RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IPI:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0007549; P:dosage compensation; IDA:FlyBase.
DR GO; GO:0009047; P:dosage compensation by hyperactivation of X chromosome; NAS:FlyBase.
DR GO; GO:0045433; P:male courtship behavior, veined wing generated song production; IGI:FlyBase.
DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IGI:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
DR CDD; cd17972; DEXHc_DHX9; 1.
DR CDD; cd19854; DSRM_DHX9_rpt1; 1.
DR CDD; cd19855; DSRM_DHX9_rpt2; 1.
DR DisProt; DP02836; -.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044447; DHX9_DEXHc.
DR InterPro; IPR044445; DHX9_DSRM_1.
DR InterPro; IPR044446; DHX9_DSRM_2.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1293
FT /note="Dosage compensation regulator"
FT /id="PRO_0000055181"
FT DOMAIN 2..70
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 169..241
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 394..560
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 639..813
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 1202..1208
FT /note="1"
FT REPEAT 1209..1215
FT /note="2"
FT REPEAT 1216..1222
FT /note="3"
FT REPEAT 1223..1229
FT /note="4"
FT REPEAT 1230..1236
FT /note="5"
FT REPEAT 1237..1243
FT /note="6"
FT REPEAT 1244..1250
FT /note="7"
FT REPEAT 1251..1257
FT /note="8"
FT REPEAT 1258..1263
FT /note="9"
FT REGION 80..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1263
FT /note="9 X 7 AA tandem repeats of G-G-G-Y-G-N-N"
FT REGION 1268..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 507..510
FT /note="DEAH box"
FT BINDING 407..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..357
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015690"
FT VAR_SEQ 199..226
FT /note="SFLAELSIYVPALNRTVTARESGSNKKS -> YVLPFQLSSACISDLTRYGL
FT RPNLKCSP (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:1653648"
FT /id="VSP_005775"
FT VAR_SEQ 227..1293
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:1653648"
FT /id="VSP_005776"
FT VARIANT 1276
FT /note="G -> V"
FT CONFLICT 590
FT /note="R -> P (in Ref. 1; AAC41573)"
FT /evidence="ECO:0000305"
FT CONFLICT 1263
FT /note="K -> N (in Ref. 1; AAC41573)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:5ZTM"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:5ZTM"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:5ZTM"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6I3R"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:5ZTM"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:5ZTM"
FT HELIX 53..70
FT /evidence="ECO:0007829|PDB:5ZTM"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5ZTM"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 213..223
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 224..241
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 413..427
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 435..442
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 443..456
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 478..486
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 487..493
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 514..529
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 534..541
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 544..550
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 571..578
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 584..600
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 621..629
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 637..649
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 655..659
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 663..674
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 677..680
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 682..684
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 696..700
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 711..716
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 718..720
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 729..734
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 737..744
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 745..748
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 749..756
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 759..766
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 775..779
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 783..788
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 796..799
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 803..811
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 817..822
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 830..842
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 854..860
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 866..877
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 881..890
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 909..912
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 913..915
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 921..937
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 940..950
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 954..973
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 978..981
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 995..1007
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 1008..1010
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 1012..1017
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 1020..1023
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 1024..1026
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 1027..1031
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 1049..1069
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 1071..1077
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 1082..1084
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 1090..1092
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 1093..1095
FT /evidence="ECO:0007829|PDB:5AOR"
FT STRAND 1096..1100
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 1102..1124
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 1126..1128
FT /evidence="ECO:0007829|PDB:5AOR"
FT HELIX 1134..1147
FT /evidence="ECO:0007829|PDB:5AOR"
FT TURN 1149..1152
FT /evidence="ECO:0007829|PDB:5AOR"
SQ SEQUENCE 1293 AA; 143661 MW; 7667679F069BCAF5 CRC64;
MDIKSFLYQF CAKSQIEPKF DIRQTGPKNR QRFLCEVRVE PNTYIGVGNS TNKKDAEKNA
CRDFVNYLVR VGKLNTNDVP ADAGASGGGP RTGLEGAGMA GGSGQQKRVF DGQSGPQDLG
EAYRPLNHDG GDGGNRYSVI DRIQEQRDMN EAEAFDVNAA IHGNWTIENA KERLNIYKQT
NNIRDDYKYT PVGPEHARSF LAELSIYVPA LNRTVTARES GSNKKSASKS CALSLVRQLF
HLNVIEPFSG TLKKKKDEQL KPYPVKLSPN LINKIDEVIK GLDLPVVNPR NIKIELDGPP
IPLIVNLSRI DSSQQDGEKR QESSVIPWAP PQANWNTWHA CNIDEGELAT TSIDDLSMDY
ERSLRDRRQN DNEYRQFLEF REKLPIAAMR SEILTAINDN PVVIIRGNTG CGKTTQIAQY
ILDDYICSGQ GGYANIYVTQ PRRISAISVA ERVARERCEQ LGDTVGYSVR FESVFPRPYG
AILFCTVGVL LRKLEAGLRG VSHIIVDEIH ERDVNSDFLL VILRDMVDTY PDLHVILMSA
TIDTTKFSKY FGICPVLEVP GRAFPVQQFF LEDIIQMTDF VPSAESRRKR KEVEDEEQLL
SEDKDEAEIN YNKVCEDKYS QKTRNAMAML SESDVSFELL EALLMHIKSK NIPGAILVFL
PGWNLIFALM KFLQNTNIFG DTSQYQILPC HSQIPRDEQR KVFEPVPEGV TKIILSTNIA
ETSITIDDIV FVIDICKARM KLFTSHNNLT SYATVWASKT NLEQRKGRAG RVRPGFCFTL
CSRARFQALE DNLTPEMFRT PLHEMALTIK LLRLGSIHHF LSKALEPPPV DAVIEAEVLL
REMRCLDAND ELTPLGRLLA RLPIEPRLGK MMVLGAVFGC ADLMAIMASY SSTFSEVFSL
DIGQRRLANH QKALSGTKCS DHVAMIVASQ MWRREKQRGE HMEARFCDWK GLQMSTMNVI
WDAKQQLLDL LQQAGFPEEC MISHEVDERI DGDDPVLDVS LALLCLGLYP NICVHKEKRK
VLTTESKAAL LHKTSVNCSN LAVTFPYPFF VFGEKIRTRA VSCKQLSMVS PLQVILFGSR
KIDLAANNIV RVDNWLNFDI EPELAAKIGA LKPALEDLIT VACDNPSDIL RLEEPYAQLV
KVVKDLCVKS AGDFGLQRES GILPHQSRQF SDGGGPPKRG RFETGRFTNS SFGRRGNGRT
FGGGYGNNGG GYGNNGGGYG NIGGGYGNNA GGYGNNGGYG NNGGGYRNNG GGYGNNGGGY
GNKRGGFGDS FESNRGSGGG FRNGDQGGRW GNF