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Conserved domains on  [gi|17507247|ref|NP_491852|]
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Protein kinase domain-containing protein [Caenorhabditis elegans]

Protein Classification

SH2 and PKc_like domain-containing protein( domain architecture ID 10074615)

SH2 and PKc_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
42-107 6.72e-04

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


:

Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 38.21  E-value: 6.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507247  42 KNPGDF--SMSKSLDGAYYLSIVPGNNKMKketsraiHLRIDHSENEYAIQGMLFARSQTLEQLVYHL 107
Cdd:cd00173  19 KPDGTFlvRESSSEPGDYVLSVRSGDGKVK-------HYLIERNEGGYYLLGGSGRTFPSLPELVEHY 79
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
151-397 8.18e-03

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 cd13992:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 268  Bit Score: 37.75  E-value: 8.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 151 IQSQDFFHLVYTGEMKFADGK---IKKALFEELHNPTISDL-----KVFYENLVEGkalaarnlpirlpIGAILNPPTL- 221
Cdd:cd13992   6 GASSHTGEPKYVKKVGVYGGRtvaIKHITFSRTEKRTILQElnqlkELVHDNLNKF-------------IGICINPPNIa 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 222 -IYEHQENQvgcSLKDFLKNFDTHLDLAQRIKLCSAAVRILSELHR-FDIYHGASK-----VDNFYVLgykneKTMNYel 294
Cdd:cd13992  73 vVTEYCTRG---SLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHSsSIGYHGRLKssnclVDSRWVV-----KLTDF-- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 295 vfnGASGLLYEGKSDNTVTMVDYDS---NAPEV----AFTRKLSKESGVFTLGRLFEQILESE---ILKSYSEPPQEEPR 364
Cdd:cd13992 143 ---GLRNLLEEQTNHQLDEDAQHKKllwTAPELlrgsLLEVRGTQKGDVYSFAIILYEILFRSdpfALEREVAIVEKVIS 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17507247 365 VLNDMRR----------------LIGRATRANPSQRPTMNGIVMLIREL 397
Cdd:cd13992 220 GGNKPFRpelavlldefpprlvlLVKQCWAENPEKRPSFKQIKKTLTEN 268
 
Name Accession Description Interval E-value
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
42-107 6.72e-04

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 38.21  E-value: 6.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507247  42 KNPGDF--SMSKSLDGAYYLSIVPGNNKMKketsraiHLRIDHSENEYAIQGMLFARSQTLEQLVYHL 107
Cdd:cd00173  19 KPDGTFlvRESSSEPGDYVLSVRSGDGKVK-------HYLIERNEGGYYLLGGSGRTFPSLPELVEHY 79
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
151-397 8.18e-03

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 37.75  E-value: 8.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 151 IQSQDFFHLVYTGEMKFADGK---IKKALFEELHNPTISDL-----KVFYENLVEGkalaarnlpirlpIGAILNPPTL- 221
Cdd:cd13992   6 GASSHTGEPKYVKKVGVYGGRtvaIKHITFSRTEKRTILQElnqlkELVHDNLNKF-------------IGICINPPNIa 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 222 -IYEHQENQvgcSLKDFLKNFDTHLDLAQRIKLCSAAVRILSELHR-FDIYHGASK-----VDNFYVLgykneKTMNYel 294
Cdd:cd13992  73 vVTEYCTRG---SLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHSsSIGYHGRLKssnclVDSRWVV-----KLTDF-- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 295 vfnGASGLLYEGKSDNTVTMVDYDS---NAPEV----AFTRKLSKESGVFTLGRLFEQILESE---ILKSYSEPPQEEPR 364
Cdd:cd13992 143 ---GLRNLLEEQTNHQLDEDAQHKKllwTAPELlrgsLLEVRGTQKGDVYSFAIILYEILFRSdpfALEREVAIVEKVIS 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17507247 365 VLNDMRR----------------LIGRATRANPSQRPTMNGIVMLIREL 397
Cdd:cd13992 220 GGNKPFRpelavlldefpprlvlLVKQCWAENPEKRPSFKQIKKTLTEN 268
 
Name Accession Description Interval E-value
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
42-107 6.72e-04

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 38.21  E-value: 6.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507247  42 KNPGDF--SMSKSLDGAYYLSIVPGNNKMKketsraiHLRIDHSENEYAIQGMLFARSQTLEQLVYHL 107
Cdd:cd00173  19 KPDGTFlvRESSSEPGDYVLSVRSGDGKVK-------HYLIERNEGGYYLLGGSGRTFPSLPELVEHY 79
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
151-397 8.18e-03

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 37.75  E-value: 8.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 151 IQSQDFFHLVYTGEMKFADGK---IKKALFEELHNPTISDL-----KVFYENLVEGkalaarnlpirlpIGAILNPPTL- 221
Cdd:cd13992   6 GASSHTGEPKYVKKVGVYGGRtvaIKHITFSRTEKRTILQElnqlkELVHDNLNKF-------------IGICINPPNIa 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 222 -IYEHQENQvgcSLKDFLKNFDTHLDLAQRIKLCSAAVRILSELHR-FDIYHGASK-----VDNFYVLgykneKTMNYel 294
Cdd:cd13992  73 vVTEYCTRG---SLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHSsSIGYHGRLKssnclVDSRWVV-----KLTDF-- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507247 295 vfnGASGLLYEGKSDNTVTMVDYDS---NAPEV----AFTRKLSKESGVFTLGRLFEQILESE---ILKSYSEPPQEEPR 364
Cdd:cd13992 143 ---GLRNLLEEQTNHQLDEDAQHKKllwTAPELlrgsLLEVRGTQKGDVYSFAIILYEILFRSdpfALEREVAIVEKVIS 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 17507247 365 VLNDMRR----------------LIGRATRANPSQRPTMNGIVMLIREL 397
Cdd:cd13992 220 GGNKPFRpelavlldefpprlvlLVKQCWAENPEKRPSFKQIKKTLTEN 268
 
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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