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ATP-dependent RNA helicase DBP5 (EC 3.6.4.13) (DEAD box protein 5) (Helicase CA5/6) (Ribonucleic acid-trafficking protein 8)

 DBP5_YEAST              Reviewed;         482 AA.
P20449; D6W2B2;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
23-MAY-2018, entry version 185.
RecName: Full=ATP-dependent RNA helicase DBP5;
EC=3.6.4.13;
AltName: Full=DEAD box protein 5;
AltName: Full=Helicase CA5/6;
AltName: Full=Ribonucleic acid-trafficking protein 8;
Name=DBP5; Synonyms=RAT8; OrderedLocusNames=YOR046C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chang T.-H.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-425.
PubMed=2406722; DOI=10.1073/pnas.87.4.1571;
Chang T.-H., Arenas J., Abelson J.;
"Identification of five putative yeast RNA helicase genes.";
Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-171; LEU-220;
PHE-236; VAL-345 AND THR-466.
PubMed=9564047; DOI=10.1093/emboj/17.9.2651;
Tseng S.S.-I., Weaver P.L., Liu Y., Hitomi M., Tartakoff A.M.,
Chang T.-H.;
"Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA
export.";
EMBO J. 17:2651-2662(1998).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-170; LEU-267
AND ILE-385.
PubMed=9564048; DOI=10.1093/emboj/17.9.2663;
Snay-Hodge C.A., Colot H.V., Goldstein A.L., Cole C.N.;
"Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein
essential for RNA export.";
EMBO J. 17:2663-2676(1998).
[7]
FUNCTION, INTERACTION WITH NUP159, ASSOCIATION WITH THE NUCLEAR PORE
COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=10428971; DOI=10.1093/emboj/18.15.4332;
Schmitt C., von Kobbe C., Bachi A., Pante N., Rodrigues J.P.,
Boscheron C., Rigaut G., Wilm M., Seraphin B., Carmo-Fonseca M.,
Izaurralde E.;
"Dbp5, a DEAD-box protein required for mRNA export, is recruited to
the cytoplasmic fibrils of nuclear pore complex via a conserved
interaction with CAN/Nup159p.";
EMBO J. 18:4332-4347(1999).
[8]
FUNCTION, INTERACTION WITH GLE1, SUBCELLULAR LOCATION, AND ASSOCIATION
WITH THE NUCLEAR PORE COMPLEX.
PubMed=10610322; DOI=10.1093/emboj/18.20.5761;
Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J.,
Rosbach M., Stutz F.;
"The RNA export factor Gle1p is located on the cytoplasmic fibrils of
the NPC and physically interacts with the FG-nucleoporin Rip1p, the
DEAD-box protein Rat8p/Dbp5p and a new protein Ymr255p.";
EMBO J. 18:5761-5777(1999).
[9]
FUNCTION, INTERACTION WITH NUP159 AND GLE1, ASSOCIATION WITH THE
NUCLEAR PORE COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=10523319; DOI=10.1093/emboj/18.20.5778;
Hodge C.A., Colot H.V., Stafford P., Cole C.N.;
"Rat8p/Dbp5p is a shuttling transport factor that interacts with
Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-
1 cells.";
EMBO J. 18:5778-5788(1999).
[10]
FUNCTION.
PubMed=11350039; DOI=10.1017/S1355838201010147;
Hilleren P., Parker R.;
"Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p
cause hyperadenylation during 3'-end formation of nascent
transcripts.";
RNA 7:753-764(2001).
[11]
FUNCTION.
PubMed=12192043; DOI=10.1128/MCB.22.18.6441-6457.2002;
Hammell C.M., Gross S., Zenklusen D., Heath C.V., Stutz F., Moore C.,
Cole C.N.;
"Coupling of termination, 3' processing, and mRNA export.";
Mol. Cell. Biol. 22:6441-6457(2002).
[12]
FUNCTION, AND INTERACTION WITH TFB1; TFB2 AND RAD3.
PubMed=12686617; DOI=10.1091/mbc.E02-09-0602;
Estruch F., Cole C.N.;
"An early function during transcription for the yeast mRNA export
factor Dbp5p/Rat8p suggested by its genetic and physical interactions
with transcription factor IIH components.";
Mol. Biol. Cell 14:1664-1676(2003).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[14]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15280434; DOI=10.1242/jcs.01296;
Takemura R., Inoue Y., Izawa S.;
"Stress response in yeast mRNA export factor: reversible changes in
Rat8p localization are caused by ethanol stress but not heat shock.";
J. Cell Sci. 117:4189-4197(2004).
[16]
FUNCTION, INTERACTION WITH NUP159, AND SUBCELLULAR LOCATION.
PubMed=15574330; DOI=10.1016/j.molcel.2004.10.032;
Weirich C.S., Erzberger J.P., Berger J.M., Weis K.;
"The N-terminal domain of Nup159 forms a beta-propeller that functions
in mRNA export by tethering the helicase Dbp5 to the nuclear pore.";
Mol. Cell 16:749-760(2004).
[17]
FUNCTION, AND INTERACTION WITH GFD1 AND ZDS1.
PubMed=15619606; DOI=10.1074/jbc.M413025200;
Estruch F., Hodge C.A., Rodriguez-Navarro S., Cole C.N.;
"Physical and genetic interactions link the yeast protein Zds1p with
mRNA nuclear export.";
J. Biol. Chem. 280:9691-9697(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-162, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: ATP-dependent RNA helicase associated with the nuclear
pore complex and essential for mRNA export from the nucleus. May
participate in a terminal step of mRNA export through the removal
of proteins that accompany mRNA through the nucleopore complex.
Contributes to the blocking of bulk poly(A)+ mRNA export in
ethanol-stressed cells. May also be involved in early
transcription. {ECO:0000269|PubMed:10428971,
ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322,
ECO:0000269|PubMed:11350039, ECO:0000269|PubMed:12192043,
ECO:0000269|PubMed:12686617, ECO:0000269|PubMed:15280434,
ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606,
ECO:0000269|PubMed:9564047, ECO:0000269|PubMed:9564048}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Associates with the nuclear pore complex. Interacts with
NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is
necessary for the association to the nuclear pore complex.
Interacts also with the TFIIH complex subunits TFB1, TFB2 and
RAD3. {ECO:0000269|PubMed:10428971, ECO:0000269|PubMed:10523319,
ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:12686617,
ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606}.
-!- INTERACTION:
Q04839:GFD1; NbExp=2; IntAct=EBI-5617, EBI-27549;
Q12315:GLE1; NbExp=8; IntAct=EBI-5617, EBI-7635;
P50111:ZDS1; NbExp=3; IntAct=EBI-5617, EBI-29626;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
Note=Nuclear pore complex cytoplasmic fibrils. Accumulates in the
nucleus rapidly and reversibly in response to ethanol stress.
-!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
box family of RNA helicases and controls ATP binding and
hydrolysis.
-!- MISCELLANEOUS: Present with 14900 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
subfamily. {ECO:0000305}.
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EMBL; U28135; AAB01679.1; -; Genomic_DNA.
EMBL; Z74954; CAA99237.1; -; Genomic_DNA.
EMBL; Z74955; CAA99239.1; -; Genomic_DNA.
EMBL; BK006948; DAA10828.1; -; Genomic_DNA.
PIR; S66920; S66920.
RefSeq; NP_014689.1; NM_001183465.1.
PDB; 2KBE; NMR; -; A=71-296.
PDB; 2KBF; NMR; -; A=296-482.
PDB; 3GFP; X-ray; 1.80 A; A=296-482.
PDB; 3PEU; X-ray; 2.60 A; A=297-482.
PDB; 3PEV; X-ray; 2.50 A; A=297-482.
PDB; 3PEW; X-ray; 1.50 A; A=91-482.
PDB; 3PEY; X-ray; 1.40 A; A=91-482.
PDB; 3RRM; X-ray; 2.88 A; A=91-482.
PDB; 3RRN; X-ray; 4.00 A; A=91-482.
PDB; 5ELX; X-ray; 1.81 A; A=91-481.
PDBsum; 2KBE; -.
PDBsum; 2KBF; -.
PDBsum; 3GFP; -.
PDBsum; 3PEU; -.
PDBsum; 3PEV; -.
PDBsum; 3PEW; -.
PDBsum; 3PEY; -.
PDBsum; 3RRM; -.
PDBsum; 3RRN; -.
PDBsum; 5ELX; -.
ProteinModelPortal; P20449; -.
SMR; P20449; -.
BioGrid; 34447; 332.
DIP; DIP-2352N; -.
IntAct; P20449; 9.
MINT; P20449; -.
STRING; 4932.YOR046C; -.
iPTMnet; P20449; -.
MaxQB; P20449; -.
PaxDb; P20449; -.
PRIDE; P20449; -.
EnsemblFungi; YOR046C; YOR046C; YOR046C.
GeneID; 854211; -.
KEGG; sce:YOR046C; -.
EuPathDB; FungiDB:YOR046C; -.
SGD; S000005572; DBP5.
GeneTree; ENSGT00530000063236; -.
HOGENOM; HOG000268797; -.
InParanoid; P20449; -.
KO; K18655; -.
OMA; PPRNMIA; -.
OrthoDB; EOG092C2B1L; -.
BioCyc; YEAST:G3O-33590-MONOMER; -.
EvolutionaryTrace; P20449; -.
PRO; PR:P20449; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IPI:SGD.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005844; C:polysome; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
GO; GO:0008186; F:RNA-dependent ATPase activity; IDA:SGD.
GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
GO; GO:0006415; P:translational termination; IGI:SGD.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm; Helicase;
Hydrolase; Membrane; mRNA transport; Nuclear pore complex;
Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; RNA-binding; Translocation; Transport.
CHAIN 1 482 ATP-dependent RNA helicase DBP5.
/FTId=PRO_0000055019.
DOMAIN 125 292 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 303 480 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 138 145 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 92 120 Q motif.
MOTIF 239 242 DEAD box.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 170 170 P->H: In RAT8-7; accumulates poly(A)+ RNA
in the nucleus at 16 degrees Celsius.
{ECO:0000269|PubMed:9564048}.
MUTAGEN 171 171 S->P: In DBP5-2; accumulates poly(A)+ RNA
in the nucleus at 37 degrees Celsius;
when associated with L-236 and F-245.
{ECO:0000269|PubMed:9564047}.
MUTAGEN 220 220 L->P: In DBP5-1; accumulates poly(A)+ RNA
in the nucleus at 37 degrees Celsius;
when associated with S-466.
{ECO:0000269|PubMed:9564047}.
MUTAGEN 236 236 F->L: In DBP5-2; accumulates poly(A)+ RNA
in the nucleus at 37 degrees Celsius;
when associated with P-171 and F-245.
{ECO:0000269|PubMed:9564047}.
MUTAGEN 267 267 L->P: In RAT8-2; accumulates poly(A)+ RNA
in the nucleus at 16 and 37 degrees
Celsius. {ECO:0000269|PubMed:9564048}.
MUTAGEN 345 345 V->F: In DBP5-2; accumulates poly(A)+ RNA
in the nucleus at 37 degrees Celsius;
when associated with P-171 and L-236.
{ECO:0000269|PubMed:9564047}.
MUTAGEN 385 385 I->D: In RAT8-3; accumulates poly(A)+ RNA
in the nucleus at 16 and 37 degrees
Celsius. {ECO:0000269|PubMed:9564048}.
MUTAGEN 466 466 T->S: In DBP5-1; accumulates poly(A)+ RNA
in the nucleus at 37 degrees Celsius;
when associated with P-220.
{ECO:0000269|PubMed:9564047}.
STRAND 78 80 {ECO:0000244|PDB:2KBE}.
HELIX 83 85 {ECO:0000244|PDB:2KBE}.
HELIX 87 90 {ECO:0000244|PDB:2KBE}.
HELIX 94 97 {ECO:0000244|PDB:2KBE}.
HELIX 101 109 {ECO:0000244|PDB:3PEY}.
STRAND 110 113 {ECO:0000244|PDB:2KBE}.
HELIX 117 127 {ECO:0000244|PDB:3PEY}.
STRAND 128 130 {ECO:0000244|PDB:3RRM}.
STRAND 134 137 {ECO:0000244|PDB:3PEY}.
HELIX 144 155 {ECO:0000244|PDB:3PEY}.
STRAND 165 168 {ECO:0000244|PDB:3PEY}.
HELIX 172 185 {ECO:0000244|PDB:3PEY}.
TURN 186 188 {ECO:0000244|PDB:3PEY}.
STRAND 193 197 {ECO:0000244|PDB:3PEY}.
STRAND 210 214 {ECO:0000244|PDB:3PEY}.
HELIX 216 224 {ECO:0000244|PDB:3PEY}.
STRAND 235 239 {ECO:0000244|PDB:3PEY}.
HELIX 241 246 {ECO:0000244|PDB:3PEY}.
HELIX 250 259 {ECO:0000244|PDB:3PEY}.
TURN 261 264 {ECO:0000244|PDB:2KBE}.
STRAND 266 272 {ECO:0000244|PDB:3PEY}.
HELIX 276 285 {ECO:0000244|PDB:3PEY}.
STRAND 290 292 {ECO:0000244|PDB:3PEY}.
HELIX 296 298 {ECO:0000244|PDB:3PEY}.
TURN 301 303 {ECO:0000244|PDB:3GFP}.
STRAND 304 310 {ECO:0000244|PDB:3PEY}.
HELIX 314 325 {ECO:0000244|PDB:3PEY}.
TURN 326 329 {ECO:0000244|PDB:3PEY}.
STRAND 330 336 {ECO:0000244|PDB:3PEY}.
HELIX 340 352 {ECO:0000244|PDB:3PEY}.
STRAND 358 360 {ECO:0000244|PDB:3PEY}.
STRAND 362 364 {ECO:0000244|PDB:3RRM}.
HELIX 366 377 {ECO:0000244|PDB:3PEY}.
TURN 378 380 {ECO:0000244|PDB:2KBF}.
STRAND 383 386 {ECO:0000244|PDB:3PEY}.
HELIX 388 390 {ECO:0000244|PDB:3PEY}.
STRAND 391 393 {ECO:0000244|PDB:3PEY}.
STRAND 399 406 {ECO:0000244|PDB:3PEY}.
STRAND 413 415 {ECO:0000244|PDB:3PEY}.
HELIX 417 424 {ECO:0000244|PDB:3PEY}.
HELIX 425 427 {ECO:0000244|PDB:3PEV}.
STRAND 434 440 {ECO:0000244|PDB:3PEY}.
HELIX 443 455 {ECO:0000244|PDB:3PEY}.
TURN 456 458 {ECO:0000244|PDB:3PEU}.
STRAND 462 465 {ECO:0000244|PDB:3GFP}.
HELIX 469 480 {ECO:0000244|PDB:3PEY}.
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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EIAAB10794 ATP-dependent RNA helicase DDX42,DDX42,DEAD box protein 42,Homo sapiens,Human,RHELP,RNA helicase-like protein,RNA helicase-related protein,RNAHP,SF3b DEAD box protein,SF3b125,Splicing factor 3B-associ
EIAAB10817 ATP-dependent RNA helicase DDX54,ATP-dependent RNA helicase DP97,DDX54,DEAD box protein 54,DEAD box RNA helicase 97 kDa,Homo sapiens,Human
EIAAB10806 Ddx5,DEAD box protein 5,DEAD box RNA helicase DEAD1,mDEAD1,Mouse,Mus musculus,Probable ATP-dependent RNA helicase DDX5,RNA helicase p68,Tnz2
EIAAB10824 ATP-dependent 61 kDa nucleolar RNA helicase,DDX21,DDX56,DEAD box protein 21,DEAD box protein 56,Homo sapiens,Human,NOH61,Probable ATP-dependent RNA helicase DDX56
EIAAB10759 DDX17,DEAD box protein 17,DEAD box protein p72,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX17,RNA-dependent helicase p72
EIAAB10783 ATP-dependent RNA helicase DDX3X,D1Pas1-related sequence 2,D1Pas1-rs2,Ddx3,Ddx3x,DEAD box protein 3, X-chromosomal,DEAD box RNA helicase DEAD3,Dead3,Embryonic RNA helicase,Erh,mDEAD3,Mouse,Mus musculu
EIAAB10782 ATP-dependent RNA helicase DDX3X,DBX,DDX3,DDX3X,DEAD box protein 3, X-chromosomal,DEAD box, X isoform,Helicase-like protein 2,HLP2,Homo sapiens,Human
18-003-42773 Probable ATP-dependent RNA helicase DDX6 - EC 3.6.1.-; DEAD box protein 6; ATP-dependent RNA helicase p54; Oncogene RCK Polyclonal 0.1 mg Protein A
18-003-42774 Spliceosome RNA helicase BAT1 - EC 3.6.1.-; DEAD box protein UAP56; 56 kDa U2AF65-associated protein; ATP-dependent RNA helicase p47; HLA-B-associated transcript-1 Polyclonal 0.05 mg Aff Pur
EIAAB12133 ATP-dependent RNA helicase DDX39A,Ddx39,Ddx39a,Ddxl,DEAD box protein 39,Nuclear RNA helicase, DECD variant of DEAD box family,Rat,Rattus norvegicus
18-003-42772 Probable ATP-dependent RNA helicase DDX5 - EC 3.6.1.-; DEAD box protein 5; RNA helicase p68 Polyclonal 0.1 mg Protein A
18-003-42771 Probable ATP-dependent RNA helicase DDX5 - EC 3.6.1.-; DEAD box protein 5; RNA helicase p68 Polyclonal 0.1 mg Protein A
18-003-42777 ATP-dependent RNA helicase DDX39 - EC 3.6.1.-; DEAD box protein 39; Nuclear RNA helicase URH49 Polyclonal 0.1 mg Protein A
EIAAB10696 ATP-dependent RNA helicase DDX19A,Ddx19,Ddx19a,DEAD box protein 19A,DEAD box RNA helicase DEAD5,Eif4a-rs1,Eukaryotic translation initiation factor 4A-related sequence 1,mDEAD5,Mouse,Mus musculus
EIAAB10823 ATP-dependent 61 kDa nucleolar RNA helicase,D11Ertd619e,Ddx56,DEAD box protein 56,Mouse,Mus musculus,Noh61,Probable ATP-dependent RNA helicase DDX56
EIAAB10832 ATP-dependent RNA helicase p54,Ddx6,DEAD box protein 6,Hlr2,Mouse,Mus musculus,Oncogene RCK homolog,Probable ATP-dependent RNA helicase DDX6,Rck
EIAAB10831 ATP-dependent RNA helicase p54,DDX6,DEAD box protein 6,HLR2,Homo sapiens,Human,Oncogene RCK,Probable ATP-dependent RNA helicase DDX6,RCK
EIAAB10825 DDX58,DEAD box protein 58,Pig,Probable ATP-dependent RNA helicase DDX58,Retinoic acid-inducible gene 1 protein,Retinoic acid-inducible gene I protein,RHIV-1,RIG-1,RIG-I,RNA helicase induced by virus,S
EIAAB10774 ATP-dependent RNA helicase DDX25,Ddx25,DEAD box protein 25,Gonadotropin-regulated testicular RNA helicase,Grth,Mouse,Mus musculus
EIAAB10772 ATP-dependent RNA helicase DDX25,Ddx25,DEAD box protein 25,Gonadotropin-regulated testicular RNA helicase,Grth,Rat,Rattus norvegicus
EIAAB12132 ATP-dependent RNA helicase DDX39A,DDX39,DDX39A,DEAD box protein 39,Homo sapiens,Human,Nuclear RNA helicase URH49
EIAAB10797 Ddx46,DEAD box protein 46,Hel117,Helicase of 117.4 kDa,Probable ATP-dependent RNA helicase DDX46,Rat,Rattus norvegicus
EIAAB10805 DDX5,DEAD box protein 5,G17P1,HELR,HLR1,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX5,RNA helicase p68
EIAAB10771 ATP-dependent RNA helicase DDX25,DDX25,DEAD box protein 25,Gonadotropin-regulated testicular RNA helicase,GRTH,Homo sapiens,Human


 

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