1CWS,1C25


Conserved Protein Domain Family
Cdc25

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cd01530: Cdc25 
Click on image for an interactive view with Cn3D
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).
Statistics
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PSSM-Id: 238788
Aligned: 21 rows
Threshold Bit Score: 165.47
Created: 6-Jul-2004
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
oxyanionactive site
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:oxyanion binding site
Evidence:
  • Comment:this is the catalytic pocket
  • Structure:1C25 binds tungstate
  • Comment:both sulfate and tungstate anions are shown to bind in the catalytic site

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                     
1CWS_A     43 LKYISPETMVALLtgkfs-nivdkFVIVDCRYPYEYEGGHIKTAVNLPLerdAESFLlkspiap---------------- 105  human
EAK81262  661 LMRITPQTMTDLLagkyt-naimsYQVVDCRFGYEYQGGHIPGAINLSTvqrVVGHFlqpglgrhangeplpprsqsgkp 739  Ustilago maydis 521
P06652    410 LKRITQETLLGLLdgkfk-difdkCIIIDCRFEYEYLGGHISTAVNLNTkqaIVDAFlskp------------------- 469  fission yeast
AAD16238  362 LKRIDSDIIVRLLdghyh-dqcdeYIIVDCRFEYEYNGGHIMGAININTkdaLDALLldnp------------------- 421  Pneumocystis carinii
P30303    352 LGRIDKATLVDIKegkyd-nmfdnIMIIDCRFEYEYDGGHIVGAVNYNDkenLAAELfadp------------------- 411  Emericella nidulans
P23748    241 FPRISPETLKNILqnnmcesfynsCRIIDCRFEYEYTGGHIINSVNIHSrdeLEYEFihkvlhsd--------------- 305  baker's yeast
NP_983033 176 LPRISVDVLAAILdgkfs-shyseVYIIDCRFEYEFQAGHIKNAINVSSrreLEAEFiqkriqrc--------------- 239  Eremothecium goss...
EAK90950  266 LPRIDAHQLARILrgdhd-dqfdeFIIIDCRFEYEFNGGHITKAINISTqeaLQEKLfqyqetdt--------------- 329  Candida albicans ...
CAA88725  152 FRSISATVFASLLrdrs---rclqLIIFDCRYPFEYFGGHIKGAVNIYSldeLGKYLydeygv----------------- 211  nematode
NP_491862 286 FRSISPTTLLLEFqrlgd-dfdkkYIIVDCRFPFEYKGGHVKGAINLFRhdkIKPIFfpenge----------------- 347  nematode
Feature 1                   #######                                        
1CWS_A    106 --csldkrVILIFHCEFSSERGPRMCRFIRERDRa--vNDYPSLYYPEMYILKGGYKEFFP 162  human
EAK81262  740 dkfgnrrkHVLVFHCEFSCKRAPTMALALRQADRgl-aHDYPNCHFPEIYILQGGYCNFFQ 799  Ustilago maydis 521
P06652    470 ----lthrVALVFHCEHSAHRAPHLALHFRNTDRrmnsHRYPFLYYPEVYILHGGYKSFYE 526  fission yeast
AAD16238  422 ----ktkrCLIIFHCEYSSHRAPRLALYLRNKDRqlnmKRYPLLYYPEIYILHGGYRSFYE 478  Pneumocystis carinii
P30303    412 -----kprTAIVFHCEYSVHRAPLMAKYIRHRDRaynvDHYPQLSYPDMYILEGGYSGFFA 467  Emericella nidulans
P23748    306 tsnnntlpTLLIIHCEFSSHRGPSLASHLRNCDRiinqDHYPKLFYPDILILDGGYKAVFD 366  baker's yeast
NP_983033 240 -sadpgrpPLLVFHCEYSSYRGPIIAAHLRNYDRilnhGQYPRLHYPDIVVLQGGFKSFIE 299  Eremothecium gossypii
EAK90950  330 -kdteskkRLIIFHCEFSMFRGPMMAKHLRKCDRmcnyDNYPLLTYPDIAILEGGYKNFYE 389  Candida albicans SC5314
CAA88725  212 --kstlggLIPIFYCEYSQVRGPAMARRLRKIDThrnnHRAAALDFPEIYLLDKGYVNFWS 270  nematode
NP_491862 348 --assfqnRVPIFYCEYSQKRGPTMAHAVRSIDRvlneLRYPHVEYPEMYLLDYGYKSLWS 406  nematode

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