Q0ILZ4 · RH9_ORYSJ
- ProteinDEAD-box ATP-dependent RNA helicase 9
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids628 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Biological Process | Group II intron splicing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDEAD-box ATP-dependent RNA helicase 9
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ0ILZ4
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000282475 | 1-628 | UniProt | DEAD-box ATP-dependent RNA helicase 9 | |||
Sequence: MYSILRRAAPLRRRAVSALAAAVLRREEAAAEVVVSRRATIPAAWFHSSPAWLGFRETGAAGAAARPQYAADEGLFYEEDKRGAKAGGVAAGGAEEGLEVAKLGISPKIVSQLASRGITKLFPIQRAVLEPAMQGKDMVGRAKTGTGKTLAFGIPILDAIIRHNEKNSPGKFPLAIVLAPTRELAKQVEREFSDSSNVETICVYGGTPISQQIRQLNYGVDVVIGTPGRVIDLLKRGALNLSEVRFVVLDEADQMLSVGFDEDVETILDRVPPKRQTLMFSATMPTWIQRLTQKYLKNPVTIDLVGEDDQKLAEGISLYSIASEGHAKPAVLGELIKEHAKGGKCIVFTQTKRDADRLSYTMGRSFQCQALHGDITQAQRERTLKGFREGHFNILIATDVAARGLDIPNVDLVIHFELPNSSELFVHRSGRTGRAGKKGKAIVMHSYQQSRAIRMVENDVGCKFTELPKINVEGSDLMSGGFDSFGGGGFGREGGGSYGRRGSFGSSSSRGGGFGDSGFGRSGGGFGRSGGGGFGRSSGGGFGDSGFGRSGGGGFGDSGFGRSGGGGYGDSGFGSSGGGSGRSGFGRSGGFGDSGSGRFGGGFGNSGSGSFGNFGGNNSGQSGGFGSS | |||||||
Modified residue (large scale data) | 168 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 503 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 98-126 | Q motif | ||||
Sequence: LEVAKLGISPKIVSQLASRGITKLFPIQR | ||||||
Domain | 129-302 | Helicase ATP-binding | ||||
Sequence: LEPAMQGKDMVGRAKTGTGKTLAFGIPILDAIIRHNEKNSPGKFPLAIVLAPTRELAKQVEREFSDSSNVETICVYGGTPISQQIRQLNYGVDVVIGTPGRVIDLLKRGALNLSEVRFVVLDEADQMLSVGFDEDVETILDRVPPKRQTLMFSATMPTWIQRLTQKYLKNPVTI | ||||||
Motif | 250-253 | DEAD box | ||||
Sequence: DEAD | ||||||
Domain | 331-478 | Helicase C-terminal | ||||
Sequence: VLGELIKEHAKGGKCIVFTQTKRDADRLSYTMGRSFQCQALHGDITQAQRERTLKGFREGHFNILIATDVAARGLDIPNVDLVIHFELPNSSELFVHRSGRTGRAGKKGKAIVMHSYQQSRAIRMVENDVGCKFTELPKINVEGSDLM | ||||||
Region | 496-548 | Disordered | ||||
Sequence: GSYGRRGSFGSSSSRGGGFGDSGFGRSGGGFGRSGGGGFGRSSGGGFGDSGFG | ||||||
Region | 571-628 | Disordered | ||||
Sequence: SGFGSSGGGSGRSGFGRSGGFGDSGSGRFGGGFGNSGSGSFGNFGGNNSGQSGGFGSS | ||||||
Compositional bias | 601-628 | Polar residues | ||||
Sequence: GGFGNSGSGSFGNFGGNNSGQSGGFGSS |
Domain
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence similarities
Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length628
- Mass (Da)65,595
- Last updated2006-10-03 v1
- ChecksumEFBFE0AC2784EF9A
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 601-628 | Polar residues | ||||
Sequence: GGFGNSGSGSFGNFGGNNSGQSGGFGSS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP008218 EMBL· GenBank· DDBJ | BAF30271.2 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AP014968 EMBL· GenBank· DDBJ | BAT18038.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK287833 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |