Phage lambda Nin221:Gene Product(s)
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Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
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Standard name |
Nin221 |
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Synonyms |
Nin221, lambdap70 |
Product description |
serine/threonine-protein phosphatase Nin protein |
EC number (for enzymes) | |
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Notes
Function
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Gene Ontology
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Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0016791 |
phosphatase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
GO:0016791 |
phosphatase activity |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
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Interactions <protect> See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
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Notes
Localization
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Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
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Notes
Structure and Physical Properties
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Physical Properties
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Name | |
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Sequence |
MRYYEKIDGS KYRNIWVVGD LHGCYTNLMN KLDTIGFDNK KDLLISVGDL VDRGAENVEC LELITFPWFR AVRGNHEQMM IDGLSERGNV NHWLLNGGGW FFNLDYDKEI LAKALAHKAD ELPLIIELVS KDKKYVICHA DYPFDEYEFG KPVDHQQVIW NRERISNSQN GIVKEIKGAD TFIFGHTPAV KPLKFANQMY IDTGAVFCGN LTLIQVQGEG A |
Length |
221 |
Mol. Wt |
25.219 kDa |
pI |
5.6 (calculated) |
Extinction coefficient |
40,910 - 41,410 (calc based on 9 Y, 5 W, and 4 C residues) |
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Domains/Motifs/Modification Sites
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Structure
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Structure figures
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Notes
See Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. [3]
Gene Product Resources
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Resource type | Source | Notes/Reference |
---|---|---|
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Notes
Accessions in Other Databases
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Database | Accession | Notes |
---|---|---|
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Notes
Links
Name | URL | Comments |
---|---|---|
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References
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- ↑ Reiter, TA et al. (2002) Mn2+ is a native metal ion activator for bacteriophage lambda protein phosphatase. Biochemistry 41 15404-9 PubMed
- ↑ Zhuo, S et al. (1994) Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis. J. Biol. Chem. 269 26234-8 PubMed
- ↑ Voegtli, WC et al. (2000) Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. Biochemistry 39 15365-74 PubMed
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