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 27-MAR-2024, entry version 217.
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;
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 + 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: 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. Interacts also 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 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; -.
DR AlphaFoldDB; P20449; -.
DR SMR; P20449; -.
DR BioGRID; 34447; 504.
DR DIP; DIP-2352N; -.
DR IntAct; P20449; 9.
DR MINT; P20449; -.
DR STRING; 4932.YOR046C; -.
DR iPTMnet; P20449; -.
DR MaxQB; 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 GeneTree; ENSGT00940000173368; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; P20449; -.
DR OMA; DPQTYLH; -.
DR OrthoDB; 1087080at2759; -.
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:UniProtKB-KW.
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:0003723; F:RNA binding; IBA:GO_Central.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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 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.
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 PANTHER; PTHR47958:SF31; RNA HELICASE; 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.
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 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 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
//
