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Conserved domains on  [gi|516459781|ref|WP_017848619|]
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hypothetical protein [Pseudomonas veronii]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
47-185 7.14e-04

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 cd06650:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 319  Bit Score: 39.27  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516459781  47 PSRWQRWLHACQRPRWQMafatvaGLALMIGVVMRSPVPQPDIS-----PATFSALHPESARPAPAPMARMAVAPRAESA 121
Cdd:cd06650  171 PERLQGTHYSVQSDIWSM------GLSLVEMAVGRYPIPPPDAKelelmFGCQVEGDAAETPPRPRTPGRPLSSYGMDSR 244
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516459781 122 PVQA--EIAGALSDKSPARLskraPVALPSLEegLQEIVN-LRAAGDSQAADEKLLALHARFPQEDL 185
Cdd:cd06650  245 PPMAifELLDYIVNEPPPKL----PSGVFSLE--FQDFVNkCLIKNPAERADLKQLMVHAFIKRSDA 305
 
Name Accession Description Interval E-value
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
47-185 7.14e-04

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK 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: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 39.27  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516459781  47 PSRWQRWLHACQRPRWQMafatvaGLALMIGVVMRSPVPQPDIS-----PATFSALHPESARPAPAPMARMAVAPRAESA 121
Cdd:cd06650  171 PERLQGTHYSVQSDIWSM------GLSLVEMAVGRYPIPPPDAKelelmFGCQVEGDAAETPPRPRTPGRPLSSYGMDSR 244
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516459781 122 PVQA--EIAGALSDKSPARLskraPVALPSLEegLQEIVN-LRAAGDSQAADEKLLALHARFPQEDL 185
Cdd:cd06650  245 PPMAifELLDYIVNEPPPKL----PSGVFSLE--FQDFVNkCLIKNPAERADLKQLMVHAFIKRSDA 305
 
Name Accession Description Interval E-value
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
47-185 7.14e-04

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK 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: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 39.27  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516459781  47 PSRWQRWLHACQRPRWQMafatvaGLALMIGVVMRSPVPQPDIS-----PATFSALHPESARPAPAPMARMAVAPRAESA 121
Cdd:cd06650  171 PERLQGTHYSVQSDIWSM------GLSLVEMAVGRYPIPPPDAKelelmFGCQVEGDAAETPPRPRTPGRPLSSYGMDSR 244
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516459781 122 PVQA--EIAGALSDKSPARLskraPVALPSLEegLQEIVN-LRAAGDSQAADEKLLALHARFPQEDL 185
Cdd:cd06650  245 PPMAifELLDYIVNEPPPKL----PSGVFSLE--FQDFVNkCLIKNPAERADLKQLMVHAFIKRSDA 305
 
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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