7JTK


Conserved Protein Domain Family
DD_CrRSP11-like

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cd22985: DD_CrRSP11-like 
Click on image for an interactive view with Cn3D
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 11 (RSP11) and similar proteins
Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP11 is a non-PKA (cAMP-dependent protein kinase) RIIa protein that contains a RII domain but lack any features required for cAMP signaling or phosphorylation. It is involved in the control of ciliary and flagellar beating. RSP11 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of PKA. The D/D domain of RSP11 heterodimerizes with the D/D domain of RSP7 to form an X-type four-helix bundle within the radial spoke RS1 complex.
Statistics
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PSSM-Id: 438554
Aligned: 29 rows
Threshold Bit Score: 77.6003
Created: 27-Apr-2021
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interfaceRSP3 interface
Conserved site includes 17 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Structure:7JTK: Chlamydomonas reinhardtii flagellar radial spoke protein 7 (RSP7) and RSP11 form a heterodimer within the radial spoke RS1 complex; contacts at 4A
  • Comment:similar to the dimer of R subunits, the Dimerization/Docking (D/D) domains of RSP7 and RSP11 dimerize to form an X-type four-helix bundle

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                 #    #  ##  ##  ##  #              ### ##  ## #    
7JTK_U         4 EPIFCAEQIVIPHNLADILKAYTKEVIRRQPt-----------DLIAFSAKYFTNLANVA 52  Chlamydomonas reinhardtii
XP_001435880   7 QRIYCAEQIVVPPELPVILKHYAKEVIRNKPg-----------DIVDFSAKYFRSLLEKR 55  Paramecium tetraurelia strain d4-2
OQS01655       4 NRIFSAEQIAVPLDLPLILKEWTKDVIRAAPa-----------DVIAFSLTWFQEKAAEA 52  Achlya hypogyna
OLQ09137      41 WRIFCAEQINVPPELPDILKDFTKAVIREDPsaga----sakmKLYQWSRDYFKKKLGEV 96  Symbiodinium microadriaticum
CEM09773       7 ERIFCAEQINVPQELPLVLKEFTKEIIRRNPvesekdvelakqKIYEWAAEYFRKKANDQ 66  Vitrella brassicaformis CCMP3155
OMJ71108      22 MRIFAAEQISVPEELPGILKNYAKEVIKNNPk-----------DIITFSANYFEKLYEET 70  Stentor coeruleus
CDW76891       7 MRIFSAEQIIVQDDFPKILKDFTKEIIRKNPd-----------DITKFGREYFEQVLKER 55  Stylonychia lemnae
EFJ37893       6 DPIYCVEQIQIPPALPDILKGFAKEAIRSQPp-----------CLHEFACTYFQRLLATA 54  Selaginella moellendorffii
OAE26430       8 NPIYCVEQILIPEGLPAMLKVFAKEAIRANPk-----------ELENFAWRYFEKLAATV 56  Marchantia polymorpha subsp. ruderalis
RYG95977       4 ERIFSADQIKIHPELAKILREYTKAAIRANPs-----------DLYDFSWTYFKKKVDEA 52  archaeon

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