ID DBP5_YEAST Reviewed; 482 AA. AC P20449; D6W2B2; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 02-SEP-2026, entry version 227. DE RecName: Full=ATP-dependent RNA helicase DBP5; DE EC=3.6.4.13; DE AltName: Full=DEAD box protein 5; DE AltName: Full=Helicase CA5/6; DE AltName: Full=Ribonucleic acid-trafficking protein 8; GN Name=DBP5; Synonyms=RAT8; OrderedLocusNames=YOR046C; 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]. RA Chang T.-H.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; DOI=10.1038/387s098; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(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] OF 237-425. RX PubMed=2406722; DOI=10.1073/pnas.87.4.1571; RA Chang T.-H., Arenas J., Abelson J.; RT "Identification of five putative yeast RNA helicase genes."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-171; LEU-220; RP PHE-236; VAL-345 AND THR-466. RX PubMed=9564047; DOI=10.1093/emboj/17.9.2651; RA Tseng S.S.-I., Weaver P.L., Liu Y., Hitomi M., Tartakoff A.M., Chang T.-H.; RT "Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export."; RL EMBO J. 17:2651-2662(1998). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-170; LEU-267 AND RP ILE-385. RX PubMed=9564048; DOI=10.1093/emboj/17.9.2663; RA Snay-Hodge C.A., Colot H.V., Goldstein A.L., Cole C.N.; RT "Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential RT for RNA export."; RL EMBO J. 17:2663-2676(1998). RN [7] RP FUNCTION, INTERACTION WITH NUP159, ASSOCIATION WITH THE NUCLEAR PORE RP COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=10428971; DOI=10.1093/emboj/18.15.4332; RA Schmitt C., von Kobbe C., Bachi A., Pante N., Rodrigues J.P., Boscheron C., RA Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M., Izaurralde E.; RT "Dbp5, a DEAD-box protein required for mRNA export, is recruited to the RT cytoplasmic fibrils of nuclear pore complex via a conserved interaction RT with CAN/Nup159p."; RL EMBO J. 18:4332-4347(1999). RN [8] RP FUNCTION, INTERACTION WITH GLE1, SUBCELLULAR LOCATION, AND ASSOCIATION WITH RP THE NUCLEAR PORE COMPLEX. RX PubMed=10610322; DOI=10.1093/emboj/18.20.5761; RA Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., RA Stutz F.; RT "The RNA export factor Gle1p is located on the cytoplasmic fibrils of the RT NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box RT protein Rat8p/Dbp5p and a new protein Ymr255p."; RL EMBO J. 18:5761-5777(1999). RN [9] RP FUNCTION, INTERACTION WITH NUP159 AND GLE1, ASSOCIATION WITH THE NUCLEAR RP PORE COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=10523319; DOI=10.1093/emboj/18.20.5778; RA Hodge C.A., Colot H.V., Stafford P., Cole C.N.; RT "Rat8p/Dbp5p is a shuttling transport factor that interacts with RT Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 RT cells."; RL EMBO J. 18:5778-5788(1999). RN [10] RP FUNCTION. RX PubMed=11350039; DOI=10.1017/s1355838201010147; RA Hilleren P., Parker R.; RT "Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p cause RT hyperadenylation during 3'-end formation of nascent transcripts."; RL RNA 7:753-764(2001). RN [11] RP FUNCTION. RX PubMed=12192043; DOI=10.1128/mcb.22.18.6441-6457.2002; RA Hammell C.M., Gross S., Zenklusen D., Heath C.V., Stutz F., Moore C., RA Cole C.N.; RT "Coupling of termination, 3' processing, and mRNA export."; RL Mol. Cell. Biol. 22:6441-6457(2002). RN [12] RP FUNCTION, AND INTERACTION WITH TFB1; TFB2 AND RAD3. RX PubMed=12686617; DOI=10.1091/mbc.e02-09-0602; RA Estruch F., Cole C.N.; RT "An early function during transcription for the yeast mRNA export factor RT Dbp5p/Rat8p suggested by its genetic and physical interactions with RT transcription factor IIH components."; RL Mol. Biol. Cell 14:1664-1676(2003). RN [13] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [14] 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 [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15280434; DOI=10.1242/jcs.01296; RA Takemura R., Inoue Y., Izawa S.; RT "Stress response in yeast mRNA export factor: reversible changes in Rat8p RT localization are caused by ethanol stress but not heat shock."; RL J. Cell Sci. 117:4189-4197(2004). RN [16] RP FUNCTION, INTERACTION WITH NUP159, AND SUBCELLULAR LOCATION. RX PubMed=15574330; DOI=10.1016/j.molcel.2004.10.032; RA Weirich C.S., Erzberger J.P., Berger J.M., Weis K.; RT "The N-terminal domain of Nup159 forms a beta-propeller that functions in RT mRNA export by tethering the helicase Dbp5 to the nuclear pore."; RL Mol. Cell 16:749-760(2004). RN [17] RP FUNCTION, AND INTERACTION WITH GFD1 AND ZDS1. RX PubMed=15619606; DOI=10.1074/jbc.m413025200; RA Estruch F., Hodge C.A., Rodriguez-Navarro S., Cole C.N.; RT "Physical and genetic interactions link the yeast protein Zds1p with mRNA RT nuclear export."; RL J. Biol. Chem. 280:9691-9697(2005). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-162, AND RP IDENTIFICATION BY 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: ATP-dependent RNA helicase associated with the nuclear pore CC complex and essential for mRNA export from the nucleus. May participate CC in a terminal step of mRNA export through the removal of proteins that CC accompany mRNA through the nucleopore complex. Contributes to the CC blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May CC also be involved in early transcription. {ECO:0000269|PubMed:10428971, CC ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, CC ECO:0000269|PubMed:11350039, ECO:0000269|PubMed:12192043, CC ECO:0000269|PubMed:12686617, ECO:0000269|PubMed:15280434, CC ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606, CC ECO:0000269|PubMed:9564047, ECO:0000269|PubMed:9564048}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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: Associates with the nuclear pore complex. Interacts with CC NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary CC for the association to the nuclear pore complex. Also interacts with CC the TFIIH complex subunits TFB1, TFB2 and RAD3. CC {ECO:0000269|PubMed:10428971, ECO:0000269|PubMed:10523319, CC ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:12686617, CC ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606}. CC -!- INTERACTION: CC P20449; Q04839: GFD1; NbExp=2; IntAct=EBI-5617, EBI-27549; CC P20449; Q12315: GLE1; NbExp=8; IntAct=EBI-5617, EBI-7635; CC P20449; P50111: ZDS1; NbExp=3; IntAct=EBI-5617, EBI-29626; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex. Nucleus CC membrane; Peripheral membrane protein; Cytoplasmic side. Note=Nuclear CC pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly CC and reversibly in response to ethanol stress. CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box CC family of RNA helicases and controls ATP binding and hydrolysis. CC -!- MISCELLANEOUS: Present with 14900 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5 CC subfamily. {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; U28135; AAB01679.1; -; Genomic_DNA. DR EMBL; Z74954; CAA99237.1; -; Genomic_DNA. DR EMBL; Z74955; CAA99239.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10828.1; -; Genomic_DNA. DR PIR; S66920; S66920. DR RefSeq; NP_014689.1; NM_001183465.1. DR PDB; 2KBE; NMR; -; A=71-296. DR PDB; 2KBF; NMR; -; A=296-482. DR PDB; 3GFP; X-ray; 1.80 A; A=296-482. DR PDB; 3PEU; X-ray; 2.60 A; A=297-482. DR PDB; 3PEV; X-ray; 2.50 A; A=297-482. DR PDB; 3PEW; X-ray; 1.50 A; A=91-482. DR PDB; 3PEY; X-ray; 1.40 A; A=91-482. DR PDB; 3RRM; X-ray; 2.88 A; A=91-482. DR PDB; 3RRN; X-ray; 4.00 A; A=91-482. DR PDB; 5ELX; X-ray; 1.81 A; A=91-481. DR AlphaFoldDB; P20449; -. DR SMR; P20449; -. DR BioGRID; 34447; 510. DR DIP; DIP-2352N; -. DR FunCoup; P20449; 924. DR IntAct; P20449; 25. DR MINT; P20449; -. DR STRING; 4932.YOR046C; -. DR iPTMnet; P20449; -. DR PaxDb; 4932-YOR046C; -. DR PeptideAtlas; P20449; -. DR EnsemblFungi; YOR046C_mRNA; YOR046C; YOR046C. DR GeneID; 854211; -. DR KEGG; sce:YOR046C; -. DR AGR; SGD:S000005572; -. DR SGD; S000005572; DBP5. DR VEuPathDB; FungiDB:YOR046C; -. DR eggNOG; KOG0332; Eukaryota. DR HOGENOM; CLU_003041_1_0_1; -. DR InParanoid; P20449; -. DR OMA; IAAETRW; -. DR OrthoDB; 10265785at2759; -. DR BioCyc; YEAST:G3O-33590-MONOMER; -. DR BioGRID-ORCS; 854211; 1 hit in 10 CRISPR screens. DR EvolutionaryTrace; P20449; -. DR PRO; PR:P20449; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P20449; protein. DR GO; GO:0005934; C:cellular bud tip; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD. DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD. DR GO; GO:0006415; P:translational termination; IGI:SGD. DR GO; GO:0006409; P:tRNA export from nucleus; IDA:SGD. DR CDD; cd17963; DEADc_DDX19_DDX25; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR FunFam; 3.40.50.300:FF:000849; ATP-dependent RNA helicase DBP5; 1. DR FunFam; 3.40.50.300:FF:000318; ATP-dependent RNA helicase DDX19B; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. DR PDBsum; 2KBE; -. DR PDBsum; 2KBF; -. DR PDBsum; 3GFP; -. DR PDBsum; 3PEU; -. DR PDBsum; 3PEV; -. DR PDBsum; 3PEW; -. DR PDBsum; 3PEY; -. DR PDBsum; 3RRM; -. DR PDBsum; 3RRN; -. DR PDBsum; 5ELX; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Helicase; Hydrolase; Membrane; KW mRNA transport; Nuclear pore complex; Nucleotide-binding; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; RNA-binding; KW Translocation; Transport. FT CHAIN 1..482 FT /note="ATP-dependent RNA helicase DBP5" FT /id="PRO_0000055019" FT DOMAIN 125..292 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 303..480 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 1..62 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 92..120 FT /note="Q motif" FT MOTIF 239..242 FT /note="DEAD box" FT COMPBIAS 17..62 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 138..145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956" FT MOD_RES 93 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MUTAGEN 170 FT /note="P->H: In RAT8-7; accumulates poly(A)+ RNA in the FT nucleus at 16 degrees Celsius." FT /evidence="ECO:0000269|PubMed:9564048" FT MUTAGEN 171 FT /note="S->P: In DBP5-2; accumulates poly(A)+ RNA in the FT nucleus at 37 degrees Celsius; when associated with L-236 FT and F-245." FT /evidence="ECO:0000269|PubMed:9564047" FT MUTAGEN 220 FT /note="L->P: In DBP5-1; accumulates poly(A)+ RNA in the FT nucleus at 37 degrees Celsius; when associated with S-466." FT /evidence="ECO:0000269|PubMed:9564047" FT MUTAGEN 236 FT /note="F->L: In DBP5-2; accumulates poly(A)+ RNA in the FT nucleus at 37 degrees Celsius; when associated with P-171 FT and F-245." FT /evidence="ECO:0000269|PubMed:9564047" FT MUTAGEN 267 FT /note="L->P: In RAT8-2; accumulates poly(A)+ RNA in the FT nucleus at 16 and 37 degrees Celsius." FT /evidence="ECO:0000269|PubMed:9564048" FT MUTAGEN 345 FT /note="V->F: In DBP5-2; accumulates poly(A)+ RNA in the FT nucleus at 37 degrees Celsius; when associated with P-171 FT and L-236." FT /evidence="ECO:0000269|PubMed:9564047" FT MUTAGEN 385 FT /note="I->D: In RAT8-3; accumulates poly(A)+ RNA in the FT nucleus at 16 and 37 degrees Celsius." FT /evidence="ECO:0000269|PubMed:9564048" FT MUTAGEN 466 FT /note="T->S: In DBP5-1; accumulates poly(A)+ RNA in the FT nucleus at 37 degrees Celsius; when associated with P-220." FT /evidence="ECO:0000269|PubMed:9564047" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:2KBE" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:2KBE" FT HELIX 87..90 FT /evidence="ECO:0007829|PDB:2KBE" FT HELIX 94..97 FT /evidence="ECO:0007829|PDB:2KBE" FT HELIX 101..109 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:2KBE" FT HELIX 117..127 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:3RRM" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 144..155 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 172..185 FT /evidence="ECO:0007829|PDB:3PEY" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:5ELX" FT STRAND 210..214 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 216..224 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 241..246 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:3PEY" FT TURN 261..264 FT /evidence="ECO:0007829|PDB:2KBE" FT STRAND 266..272 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:3PEY" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:3GFP" FT STRAND 304..310 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 314..325 FT /evidence="ECO:0007829|PDB:3PEY" FT TURN 326..329 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 330..336 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 340..352 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:3RRM" FT HELIX 366..377 FT /evidence="ECO:0007829|PDB:3PEY" FT TURN 378..380 FT /evidence="ECO:0007829|PDB:2KBF" FT STRAND 383..386 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:3GFP" FT STRAND 399..406 FT /evidence="ECO:0007829|PDB:3PEY" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 417..424 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 425..427 FT /evidence="ECO:0007829|PDB:3PEV" FT STRAND 434..440 FT /evidence="ECO:0007829|PDB:3PEY" FT HELIX 443..455 FT /evidence="ECO:0007829|PDB:3PEY" FT TURN 456..458 FT /evidence="ECO:0007829|PDB:3PEU" FT STRAND 462..465 FT /evidence="ECO:0007829|PDB:3GFP" FT HELIX 469..480 FT /evidence="ECO:0007829|PDB:3PEY" SQ SEQUENCE 482 AA; 53874 MW; C50CAFE8C060D46B CRC64; MSDTKRDPAD LLASLKIDNE KEDTSEVSTK ETVKSQPEKT ADSIKPAEKL VPKVEEKKTK QEDSNLISSE YEVKVKLADI QADPNSPLYS AKSFDELGLA PELLKGIYAM KFQKPSKIQE RALPLLLHNP PRNMIAQSQS GTGKTAAFSL TMLTRVNPED ASPQAICLAP SRELARQTLE VVQEMGKFTK ITSQLIVPDS FEKNKQINAQ VIVGTPGTVL DLMRRKLMQL QKIKIFVLDE ADNMLDQQGL GDQCIRVKRF LPKDTQLVLF SATFADAVRQ YAKKIVPNAN TLELQTNEVN VDAIKQLYMD CKNEADKFDV LTELYGLMTI GSSIIFVATK KTANVLYGKL KSEGHEVSIL HGDLQTQERD RLIDDFREGR SKVLITTNVL ARGIDIPTVS MVVNYDLPTL ANGQADPATY IHRIGRTGRF GRKGVAISFV HDKNSFNILS AIQKYFGDIE MTRVPTDDWD EVEKIVKKVL KD //