Conserved Protein Domain Family
STKc_PAK3

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cd06656: STKc_PAK3 
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3
Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.
Statistics
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PSSM-Id: 132987
View PSSM: cd06656
Aligned: 3 rows
Threshold Bit Score: 604.022
Threshold Setting Gi: 118089619
Created: 26-Aug-2008
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Feature 1:active site [active site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                               #####   #            # #                            # 
O75914    263 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTALDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 342 human
XP_420314 247 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 326 chicken
AAN52281  268 DEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVN 347 African clawed frog
Feature 1                   ##### ##  #                                  # #### #         ##  
O75914    343 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 422 human
XP_420314 327 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 406 chicken
AAN52281  348 YLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 427 African clawed frog
Feature 1     #            ##### #                          #        ###                      
O75914    423 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 502 human
XP_420314 407 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 486 chicken
AAN52281  428 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPER 507 African clawed frog
Feature 1                                                              
O75914    503 LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKlAKPLSSLTPLIIAAKEAIKNSSR 559 human
XP_420314 487 LSAVFRDFLNCCLEMDVDRRGSAKELLQHPFLKlAKPLSSLTPLIIAAKEAIKNSSR 543 chicken
AAN52281  508 LSAIFRDFLNRCLEMDVDRRGSAKELLQHPFLKiAKPLSSLTPLIIAAKEAIKNSSR 564 African clawed frog

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