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Conserved domains on  [gi|768037829|ref|XP_011529273|]
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serine/threonine-protein kinase PAK 3 isoform X6 [Homo sapiens]

Protein Classification

CRIB_PAK_like domain-containing protein( domain architecture ID 10466519)

CRIB_PAK_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 69-141 8.09e-21

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


:

Pssm-ID: 395634  Cd Length: 59  Bit Score: 84.29  E-value: 8.09e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768037829   69 EISLPSDFEHTIHVGFDAVTGEFTpdlygsqmcpgklpeGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFY 141
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFT---------------GLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFY 58
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 262-292 1.00e-11

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd06654:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 296  Bit Score: 64.75  E-value: 1.00e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 768037829 262 TDEEILEKLRSIVSVGDPKKKYTRFEKIGQG 292
Cdd:cd06654    1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQG 31
 
Name Accession Description Interval E-value
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 69-141 8.09e-21

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 84.29  E-value: 8.09e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768037829   69 EISLPSDFEHTIHVGFDAVTGEFTpdlygsqmcpgklpeGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFY 141
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFT---------------GLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFY 58
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 68-128 1.75e-18

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 77.70  E-value: 1.75e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768037829  68 PEISLPSDFEHTIHVGFDAVTGEFTpdlygsqmcpgklpeGIPEQWARLLQTSNITKLEQK 128
Cdd:cd01093    1 PEISSPTNFKHRVHVGFDPQTGEFT---------------GLPEEWQRLLKSSGITKEEQK 46
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 262-292 1.00e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which 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). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. 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.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 64.75  E-value: 1.00e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 768037829 262 TDEEILEKLRSIVSVGDPKKKYTRFEKIGQG 292
Cdd:cd06654    1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQG 31
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 70-120 1.22e-09

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 52.98  E-value: 1.22e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768037829    70 ISLPSDFEHTIHVGFDAVTGEFTpdlygsqmcpgklpeGIPEQWARLLQTS 120
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFT---------------GLPTEWKSLLKTS 36
 
Name Accession Description Interval E-value
PBD pfam00786
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 69-141 8.09e-21

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 395634  Cd Length: 59  Bit Score: 84.29  E-value: 8.09e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768037829   69 EISLPSDFEHTIHVGFDAVTGEFTpdlygsqmcpgklpeGIPEQWARLLQTSNITKLEQKKNPQAVLDVLKFY 141
Cdd:pfam00786   1 MISAPTNFKHTVHVGFDPDTGFFT---------------GLPPEWAKLLDSSGITEDEQKENPKAVLDVLKFY 58
CRIB_PAK_like cd01093
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 68-128 1.75e-18

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. This subgroup of CRIB/PBD-domains is found N-terminal of Serine/Threonine kinase domains in PAK and PAK-like proteins.


Pssm-ID: 238526  Cd Length: 46  Bit Score: 77.70  E-value: 1.75e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768037829  68 PEISLPSDFEHTIHVGFDAVTGEFTpdlygsqmcpgklpeGIPEQWARLLQTSNITKLEQK 128
Cdd:cd01093    1 PEISSPTNFKHRVHVGFDPQTGEFT---------------GLPEEWQRLLKSSGITKEEQK 46
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 262-292 1.00e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which 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). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. 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.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 64.75  E-value: 1.00e-11
                         10        20        30
                 ....*....|....*....|....*....|.
gi 768037829 262 TDEEILEKLRSIVSVGDPKKKYTRFEKIGQG 292
Cdd:cd06654    1 SDEEILEKLRSIVSVGDPKKKYTRFEKIGQG 31
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
 263-292 1.65e-11

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.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 63.97  E-value: 1.65e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 768037829 263 DEEILEKLRSIVSVGDPKKKYTRFEKIGQG 292
Cdd:cd06656    1 DEEILEKLRSIVSVGDPKKKYTRFEKIGQG 30
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
 263-292 3.48e-10

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which 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). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. 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.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 60.12  E-value: 3.48e-10
                         10        20        30
                 ....*....|....*....|....*....|
gi 768037829 263 DEEILEKLRSIVSVGDPKKKYTRFEKIGQG 292
Cdd:cd06655    1 DEEIMEKLRTIVSIGDPKKKYTRYEKIGQG 30
PBD smart00285
P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also ...
 70-120 1.22e-09

P21-Rho-binding domain; Small domains that bind Cdc42p- and/or Rho-like small GTPases. Also known as the Cdc42/Rac interactive binding (CRIB).


Pssm-ID: 197628  Cd Length: 36  Bit Score: 52.98  E-value: 1.22e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768037829    70 ISLPSDFEHTIHVGFDAVTGEFTpdlygsqmcpgklpeGIPEQWARLLQTS 120
Cdd:smart00285   1 ISTPTNFKHIAHVGFDGQTGGFT---------------GLPTEWKSLLKTS 36
CRIB cd00132
PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; ...
 69-124 1.54e-06

PAK (p21 activated kinase) Binding Domain (PBD), binds Cdc42p- and/or Rho-like small GTPases; also known as the Cdc42/Rac interactive binding (CRIB) motif; has been shown to inhibit transcriptional activation and cell transformation mediated by the Ras-Rac pathway. CRIB-containing effector proteins are functionally diverse and include serine/threonine kinases, tyrosine kinases, actin-binding proteins, and adapter molecules.


Pssm-ID: 238077  Cd Length: 42  Bit Score: 44.35  E-value: 1.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768037829  69 EISLPSDFEHTIHVGFDAVtGEFTpdlygsqmcpgklpEGIPEQWARLLQTSNITK 124
Cdd:cd00132    2 EISTPTDFKHISHVGWDGV-GFDG--------------ANLPPDLQSLFQTAGISA 42
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
 275-292 6.77e-05

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. 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). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 43.76  E-value: 6.77e-05
                         10
                 ....*....|....*...
gi 768037829 275 SVGDPKKKYTRFEKIGQG 292
Cdd:cd06647    1 SVGDPKKKYTRFEKIGQG 18
 
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.
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