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Probable ATP-dependent RNA helicase DDX47 (EC 3.6.4.13) (DEAD box protein 47)

 DDX47_HUMAN             Reviewed;         455 AA.
Q9H0S4; B3KXP4; G5E955; Q96GM0; Q96NV8; Q9UI98;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-JUN-2018, entry version 159.
RecName: Full=Probable ATP-dependent RNA helicase DDX47;
EC=3.6.4.13;
AltName: Full=DEAD box protein 47;
Name=DDX47;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-24; 75-102; 142-161; 170-190; 238-248; 285-301;
315-325; 378-384 AND 424-441, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-455 (ISOFORM 2).
TISSUE=Liver;
Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S.,
Liu M., He F.;
"Functional prediction of the coding sequences of 50 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[9]
FUNCTION, INTERACTION WITH GABARAP, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15977068; DOI=10.1007/s10529-005-3628-2;
Lee J.H., Rho S.B., Chun T.;
"GABAA receptor-associated protein (GABARAP) induces apoptosis by
interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX
47).";
Biotechnol. Lett. 27:623-628(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION, INTERACTION WITH NOL8, AND SUBCELLULAR LOCATION.
PubMed=16963496; DOI=10.1093/nar/gkl603;
Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.;
"NOP132 is required for proper nucleolus localization of DEAD-box RNA
helicase DDX47.";
Nucleic Acids Res. 34:4593-4608(2006).
[12]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-149, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-230 IN COMPLEX WITH AMP.
PubMed=20941364; DOI=10.1371/journal.pone.0012791;
Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L.,
Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W.,
Hammarstrom M., Moche M., Thorsell A.G., Schuler H.;
"Comparative structural analysis of human DEAD-box RNA helicases.";
PLoS ONE 5:E12791-E12791(2010).
-!- FUNCTION: Involved in apoptosis. May have a role in rRNA
processing and mRNA splicing. Associates with pre-rRNA precursors.
{ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Interacts with AGO1 and AGO2. Interacts with GABARAP.
Interacts with NOL8; the interaction is RNA-dependent.
{ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:16963496,
ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:20941364}.
-!- INTERACTION:
O95166:GABARAP; NbExp=3; IntAct=EBI-2515241, EBI-712001;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16963496}.
Note=Localizes in the nucleolar-organizing region during ribosome
biogenesis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H0S4-1; Sequence=Displayed;
Name=2;
IsoId=Q9H0S4-2; Sequence=VSP_045239;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF23354.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AL136666; CAB66601.1; -; mRNA.
EMBL; AK054574; BAB70762.1; -; mRNA.
EMBL; AK127712; BAG54556.1; -; mRNA.
EMBL; AC007215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96277.1; -; Genomic_DNA.
EMBL; CH471094; EAW96283.1; -; Genomic_DNA.
EMBL; BC009379; AAH09379.2; -; mRNA.
EMBL; BC068009; AAH68009.1; -; mRNA.
EMBL; AF078843; AAF23354.1; ALT_INIT; mRNA.
CCDS; CCDS8655.1; -. [Q9H0S4-1]
CCDS; CCDS8656.1; -. [Q9H0S4-2]
RefSeq; NP_057439.2; NM_016355.3. [Q9H0S4-1]
RefSeq; NP_957518.1; NM_201224.1. [Q9H0S4-2]
UniGene; Hs.719938; -.
PDB; 3BER; X-ray; 1.40 A; A=5-230.
PDBsum; 3BER; -.
ProteinModelPortal; Q9H0S4; -.
SMR; Q9H0S4; -.
BioGrid; 119375; 65.
IntAct; Q9H0S4; 36.
MINT; Q9H0S4; -.
STRING; 9606.ENSP00000350698; -.
iPTMnet; Q9H0S4; -.
PhosphoSitePlus; Q9H0S4; -.
SwissPalm; Q9H0S4; -.
BioMuta; DDX47; -.
DMDM; 52782792; -.
SWISS-2DPAGE; Q9H0S4; -.
EPD; Q9H0S4; -.
MaxQB; Q9H0S4; -.
PaxDb; Q9H0S4; -.
PeptideAtlas; Q9H0S4; -.
PRIDE; Q9H0S4; -.
ProteomicsDB; 80322; -.
DNASU; 51202; -.
Ensembl; ENST00000352940; ENSP00000319578; ENSG00000213782. [Q9H0S4-2]
Ensembl; ENST00000358007; ENSP00000350698; ENSG00000213782. [Q9H0S4-1]
GeneID; 51202; -.
KEGG; hsa:51202; -.
UCSC; uc001rax.4; human. [Q9H0S4-1]
CTD; 51202; -.
EuPathDB; HostDB:ENSG00000213782.7; -.
GeneCards; DDX47; -.
HGNC; HGNC:18682; DDX47.
HPA; HPA014855; -.
MIM; 615428; gene.
neXtProt; NX_Q9H0S4; -.
OpenTargets; ENSG00000213782; -.
PharmGKB; PA134918403; -.
eggNOG; KOG0330; Eukaryota.
eggNOG; ENOG410XQU7; LUCA.
GeneTree; ENSGT00730000110914; -.
HOGENOM; HOG000268802; -.
HOVERGEN; HBG100512; -.
InParanoid; Q9H0S4; -.
KO; K14777; -.
OMA; LNMDFEV; -.
OrthoDB; EOG091G07QH; -.
PhylomeDB; Q9H0S4; -.
TreeFam; TF105714; -.
Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; DDX47; human.
EvolutionaryTrace; Q9H0S4; -.
GeneWiki; DDX47; -.
GenomeRNAi; 51202; -.
PRO; PR:Q9H0S4; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000213782; -.
CleanEx; HS_DDX47; -.
ExpressionAtlas; Q9H0S4; baseline and differential.
Genevisible; Q9H0S4; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; HDA:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
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; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Complete proteome; Direct protein sequencing; Helicase;
Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
rRNA processing.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|Ref.6}.
CHAIN 2 455 Probable ATP-dependent RNA helicase
DDX47.
/FTId=PRO_0000055050.
DOMAIN 55 226 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 237 397 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 68 75 ATP.
MOTIF 24 52 Q motif.
MOTIF 174 177 DEAD box.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|Ref.6}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 149 149 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 251 299 Missing (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_045239.
CONFLICT 55 55 I -> V (in Ref. 3; BAB70762).
{ECO:0000305}.
HELIX 18 23 {ECO:0000244|PDB:3BER}.
HELIX 27 29 {ECO:0000244|PDB:3BER}.
HELIX 33 41 {ECO:0000244|PDB:3BER}.
HELIX 49 59 {ECO:0000244|PDB:3BER}.
STRAND 64 67 {ECO:0000244|PDB:3BER}.
HELIX 74 88 {ECO:0000244|PDB:3BER}.
STRAND 95 98 {ECO:0000244|PDB:3BER}.
HELIX 102 116 {ECO:0000244|PDB:3BER}.
HELIX 117 119 {ECO:0000244|PDB:3BER}.
STRAND 123 126 {ECO:0000244|PDB:3BER}.
HELIX 132 140 {ECO:0000244|PDB:3BER}.
STRAND 144 148 {ECO:0000244|PDB:3BER}.
HELIX 150 159 {ECO:0000244|PDB:3BER}.
STRAND 170 173 {ECO:0000244|PDB:3BER}.
HELIX 176 181 {ECO:0000244|PDB:3BER}.
HELIX 185 193 {ECO:0000244|PDB:3BER}.
STRAND 197 207 {ECO:0000244|PDB:3BER}.
HELIX 210 219 {ECO:0000244|PDB:3BER}.
STRAND 224 227 {ECO:0000244|PDB:3BER}.
SEQUENCE 455 AA; 50647 MW; 5F64F26AD2C11286 CRC64;
MAAPEEHDSP TEASQPIVEE EETKTFKDLG VTDVLCEACD QLGWTKPTKI QIEAIPLALQ
GRDIIGLAET GSGKTGAFAL PILNALLETP QRLFALVLTP TRELAFQISE QFEALGSSIG
VQSAVIVGGI DSMSQSLALA KKPHIIIATP GRLIDHLENT KGFNLRALKY LVMDEADRIL
NMDFETEVDK ILKVIPRDRK TFLFSATMTK KVQKLQRAAL KNPVKCAVSS KYQTVEKLQQ
YYIFIPSKFK DTYLVYILNE LAGNSFMIFC STCNNTQRTA LLLRNLGFTA IPLHGQMSQS
KRLGSLNKFK AKARSILLAT DVASRGLDIP HVDVVVNFDI PTHSKDYIHR VGRTARAGRS
GKAITFVTQY DVELFQRIEH LIGKKLPGFP TQDDEVMMLT ERVAEAQRFA RMELREHGEK
KKRSREDAGD NDDTEGAIGV RNKVAGGKMK KRKGR


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