ID:DDX21_MOUSE DESCRIPTION: RecName: Full=Nucleolar RNA helicase 2; EC=220.127.116.11; AltName: Full=DEAD box protein 21; AltName: Full=Gu-alpha; AltName: Full=Nucleolar RNA helicase Gu; AltName: Full=Nucleolar RNA helicase II; AltName: Full=RH II/Gu; FUNCTION: Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Functions as cofactor for JUN-activated transcription (By similarity). CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. SUBUNIT: Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. TISSUE SPECIFICITY: Highly expressed in liver and testis. Expressed at lower level in brain, lungs, and skeletal muscle. DOMAIN: The two enzymatic activities reside in two separate domains, the helicase in the N-terminus and the foldase in the C- terminus. DOMAIN: The 3 X 5 AA repeats seem to be critical for the RNA folding activity. DOMAIN: The 3 X 37 AA tandem repeats may be important for nuclear localization and/or interaction with nucleic acids or other proteins. SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily. SIMILARITY: Contains 1 helicase ATP-binding domain. SIMILARITY: Contains 1 helicase C-terminal domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9JIK5
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.