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Database: UniProt
Entry: P20449
LinkDB: P20449
Original site: P20449 
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   13-NOV-2019, entry version 197.
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;
OC   Saccharomycetes; 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.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   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.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Chang T.-H.;
RT   "Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA
RT   export.";
RL   EMBO J. 17:2651-2662(1998).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-170; LEU-267
RP   AND 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
RT   essential 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.,
RA   Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M.,
RA   Izaurralde E.;
RT   "Dbp5, a DEAD-box protein required for mRNA export, is recruited to
RT   the cytoplasmic fibrils of nuclear pore complex via a conserved
RT   interaction with CAN/Nup159p.";
RL   EMBO J. 18:4332-4347(1999).
RN   [8]
RP   FUNCTION, INTERACTION WITH GLE1, SUBCELLULAR LOCATION, AND ASSOCIATION
RP   WITH 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.,
RA   Rosbach M., Stutz F.;
RT   "The RNA export factor Gle1p is located on the cytoplasmic fibrils of
RT   the NPC and physically interacts with the FG-nucleoporin Rip1p, the
RT   DEAD-box 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
RP   NUCLEAR 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-
RT   1 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
RT   cause hyperadenylation during 3'-end formation of nascent
RT   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
RT   factor Dbp5p/Rat8p suggested by its genetic and physical interactions
RT   with 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.,
RA   Dephoure N., 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
RT   Rat8p 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
RT   in 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
RT   mRNA nuclear export.";
RL   J. Biol. Chem. 280:9691-9697(2005).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION
RP   BY 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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION
RP   BY 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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: ATP-dependent RNA helicase associated with the nuclear
CC       pore complex and essential for mRNA export from the nucleus. May
CC       participate in a terminal step of mRNA export through the removal
CC       of proteins that accompany mRNA through the nucleopore complex.
CC       Contributes to the blocking of bulk poly(A)+ mRNA export in
CC       ethanol-stressed cells. May also be involved in early
CC       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
CC       necessary for the association to the nuclear pore complex.
CC       Interacts also with the TFIIH complex subunits TFB1, TFB2 and
CC       RAD3. {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       Q04839:GFD1; NbExp=2; IntAct=EBI-5617, EBI-27549;
CC       Q12315:GLE1; NbExp=8; IntAct=EBI-5617, EBI-7635;
CC       P50111:ZDS1; NbExp=3; IntAct=EBI-5617, EBI-29626;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
CC       Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Note=Nuclear pore complex cytoplasmic fibrils. Accumulates in the
CC       nucleus rapidly and reversibly in response to ethanol stress.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       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}.
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   SMR; P20449; -.
DR   BioGrid; 34447; 338.
DR   DIP; DIP-2352N; -.
DR   IntAct; P20449; 9.
DR   MINT; P20449; -.
DR   STRING; 4932.YOR046C; -.
DR   iPTMnet; P20449; -.
DR   MaxQB; P20449; -.
DR   PaxDb; P20449; -.
DR   PRIDE; P20449; -.
DR   EnsemblFungi; YOR046C_mRNA; YOR046C; YOR046C.
DR   GeneID; 854211; -.
DR   KEGG; sce:YOR046C; -.
DR   EuPathDB; FungiDB:YOR046C; -.
DR   SGD; S000005572; DBP5.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; P20449; -.
DR   KO; K18655; -.
DR   OMA; CKLYGLM; -.
DR   BioCyc; YEAST:G3O-33590-MONOMER; -.
DR   EvolutionaryTrace; P20449; -.
DR   PRO; PR:P20449; -.
DR   Proteomes; UP000002311; Chromosome XV.
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:0005844; C:polysome; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR   GO; GO:0008186; F:RNA-dependent ATPase 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   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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; Membrane; mRNA transport; Nuclear pore complex;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; RNA-binding; Translocation; Transport.
FT   CHAIN         1    482       ATP-dependent RNA helicase DBP5.
FT                                /FTId=PRO_0000055019.
FT   DOMAIN      125    292       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      303    480       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     138    145       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        92    120       Q motif.
FT   MOTIF       239    242       DEAD box.
FT   MOD_RES      86     86       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956}.
FT   MOD_RES      93     93       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     162    162       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MUTAGEN     170    170       P->H: In RAT8-7; accumulates poly(A)+ RNA
FT                                in the nucleus at 16 degrees Celsius.
FT                                {ECO:0000269|PubMed:9564048}.
FT   MUTAGEN     171    171       S->P: In DBP5-2; accumulates poly(A)+ RNA
FT                                in the nucleus at 37 degrees Celsius;
FT                                when associated with L-236 and F-245.
FT                                {ECO:0000269|PubMed:9564047}.
FT   MUTAGEN     220    220       L->P: In DBP5-1; accumulates poly(A)+ RNA
FT                                in the nucleus at 37 degrees Celsius;
FT                                when associated with S-466.
FT                                {ECO:0000269|PubMed:9564047}.
FT   MUTAGEN     236    236       F->L: In DBP5-2; accumulates poly(A)+ RNA
FT                                in the nucleus at 37 degrees Celsius;
FT                                when associated with P-171 and F-245.
FT                                {ECO:0000269|PubMed:9564047}.
FT   MUTAGEN     267    267       L->P: In RAT8-2; accumulates poly(A)+ RNA
FT                                in the nucleus at 16 and 37 degrees
FT                                Celsius. {ECO:0000269|PubMed:9564048}.
FT   MUTAGEN     345    345       V->F: In DBP5-2; accumulates poly(A)+ RNA
FT                                in the nucleus at 37 degrees Celsius;
FT                                when associated with P-171 and L-236.
FT                                {ECO:0000269|PubMed:9564047}.
FT   MUTAGEN     385    385       I->D: In RAT8-3; accumulates poly(A)+ RNA
FT                                in the nucleus at 16 and 37 degrees
FT                                Celsius. {ECO:0000269|PubMed:9564048}.
FT   MUTAGEN     466    466       T->S: In DBP5-1; accumulates poly(A)+ RNA
FT                                in the nucleus at 37 degrees Celsius;
FT                                when associated with P-220.
FT                                {ECO:0000269|PubMed:9564047}.
FT   STRAND       78     80       {ECO:0000244|PDB:2KBE}.
FT   HELIX        83     85       {ECO:0000244|PDB:2KBE}.
FT   HELIX        87     90       {ECO:0000244|PDB:2KBE}.
FT   HELIX        94     97       {ECO:0000244|PDB:2KBE}.
FT   HELIX       101    109       {ECO:0000244|PDB:3PEY}.
FT   STRAND      110    113       {ECO:0000244|PDB:2KBE}.
FT   HELIX       117    127       {ECO:0000244|PDB:3PEY}.
FT   STRAND      128    130       {ECO:0000244|PDB:3RRM}.
FT   STRAND      134    137       {ECO:0000244|PDB:3PEY}.
FT   HELIX       144    155       {ECO:0000244|PDB:3PEY}.
FT   STRAND      165    168       {ECO:0000244|PDB:3PEY}.
FT   HELIX       172    185       {ECO:0000244|PDB:3PEY}.
FT   TURN        186    188       {ECO:0000244|PDB:3PEY}.
FT   STRAND      193    197       {ECO:0000244|PDB:3PEY}.
FT   STRAND      210    214       {ECO:0000244|PDB:3PEY}.
FT   HELIX       216    224       {ECO:0000244|PDB:3PEY}.
FT   STRAND      235    239       {ECO:0000244|PDB:3PEY}.
FT   HELIX       241    246       {ECO:0000244|PDB:3PEY}.
FT   HELIX       250    259       {ECO:0000244|PDB:3PEY}.
FT   TURN        261    264       {ECO:0000244|PDB:2KBE}.
FT   STRAND      266    272       {ECO:0000244|PDB:3PEY}.
FT   HELIX       276    285       {ECO:0000244|PDB:3PEY}.
FT   STRAND      290    292       {ECO:0000244|PDB:3PEY}.
FT   HELIX       296    298       {ECO:0000244|PDB:3PEY}.
FT   TURN        301    303       {ECO:0000244|PDB:3GFP}.
FT   STRAND      304    310       {ECO:0000244|PDB:3PEY}.
FT   HELIX       314    325       {ECO:0000244|PDB:3PEY}.
FT   TURN        326    329       {ECO:0000244|PDB:3PEY}.
FT   STRAND      330    336       {ECO:0000244|PDB:3PEY}.
FT   HELIX       340    352       {ECO:0000244|PDB:3PEY}.
FT   STRAND      358    360       {ECO:0000244|PDB:3PEY}.
FT   STRAND      362    364       {ECO:0000244|PDB:3RRM}.
FT   HELIX       366    377       {ECO:0000244|PDB:3PEY}.
FT   TURN        378    380       {ECO:0000244|PDB:2KBF}.
FT   STRAND      383    386       {ECO:0000244|PDB:3PEY}.
FT   HELIX       388    390       {ECO:0000244|PDB:3PEY}.
FT   STRAND      391    393       {ECO:0000244|PDB:3PEY}.
FT   STRAND      399    406       {ECO:0000244|PDB:3PEY}.
FT   STRAND      413    415       {ECO:0000244|PDB:3PEY}.
FT   HELIX       417    424       {ECO:0000244|PDB:3PEY}.
FT   HELIX       425    427       {ECO:0000244|PDB:3PEV}.
FT   STRAND      434    440       {ECO:0000244|PDB:3PEY}.
FT   HELIX       443    455       {ECO:0000244|PDB:3PEY}.
FT   TURN        456    458       {ECO:0000244|PDB:3PEU}.
FT   STRAND      462    465       {ECO:0000244|PDB:3GFP}.
FT   HELIX       469    480       {ECO:0000244|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
//
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