NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|151568135|pdb|2V3S|A]
View 

Chain A, SERINE/THREONINE-PROTEIN KINASE OSR1

Protein Classification

OSR1_C domain-containing protein( domain architecture ID 10573556)

OSR1_C domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
OSR1_C pfam12202
Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in ...
3-60 1.81e-26

Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00069. There is a single completely conserved residue F that may be functionally important. OSR1 is involved in the signalling cascade which activates Na/K/2Cl cotransporter during osmotic stress. This domain is the C terminal domain of OSR1 which recognizes a motif (Arg-Phe-Xaa-Val) on the OSR1-activating protein WNK1.


:

Pssm-ID: 463491  Cd Length: 62  Bit Score: 92.33  E-value: 1.81e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
2V3S_A         3 ISLVLRLRNSK----KELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVE 60
Cdd:pfam12202  1 INLVLRVRDPKkkkhKELNAIRFEFTLGKDTAEGVAQEMVKAGLVDEEDVKVVAANLRKRVD 62
 
Name Accession Description Interval E-value
OSR1_C pfam12202
Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in ...
3-60 1.81e-26

Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00069. There is a single completely conserved residue F that may be functionally important. OSR1 is involved in the signalling cascade which activates Na/K/2Cl cotransporter during osmotic stress. This domain is the C terminal domain of OSR1 which recognizes a motif (Arg-Phe-Xaa-Val) on the OSR1-activating protein WNK1.


Pssm-ID: 463491  Cd Length: 62  Bit Score: 92.33  E-value: 1.81e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
2V3S_A         3 ISLVLRLRNSK----KELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVE 60
Cdd:pfam12202  1 INLVLRVRDPKkkkhKELNAIRFEFTLGKDTAEGVAQEMVKAGLVDEEDVKVVAANLRKRVD 62
 
Name Accession Description Interval E-value
OSR1_C pfam12202
Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in ...
3-60 1.81e-26

Oxidative-stress-responsive kinase 1 C-terminal domain; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00069. There is a single completely conserved residue F that may be functionally important. OSR1 is involved in the signalling cascade which activates Na/K/2Cl cotransporter during osmotic stress. This domain is the C terminal domain of OSR1 which recognizes a motif (Arg-Phe-Xaa-Val) on the OSR1-activating protein WNK1.


Pssm-ID: 463491  Cd Length: 62  Bit Score: 92.33  E-value: 1.81e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
2V3S_A         3 ISLVLRLRNSK----KELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVE 60
Cdd:pfam12202  1 INLVLRVRDPKkkkhKELNAIRFEFTLGKDTAEGVAQEMVKAGLVDEEDVKVVAANLRKRVD 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH