1SM2,1K2P,3PIX


Conserved Protein Domain Family
PTKc_Tec_like

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cd05059: PTKc_Tec_like 
Click on image for an interactive view with Cn3D
Catalytic domain of Tec-like Protein Tyrosine Kinases
PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Statistics
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PSSM-Id: 173637
View PSSM: cd05059
Aligned: 7 rows
Threshold Bit Score: 501.978
Threshold Setting Gi: 32450904
Created: 17-Jul-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 18 residues -Click on image for an interactive view with Cn3D
Feature 1:ATP binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                ##      #           # #                  #                      # ###
1SM2_A      2 IDPSELTFVQEIGSGQFGLVHLGYWlnkDKVAIKTIREGAmsEEDFIEEAEVMMKLSHPKLVQLYGVCLeqaPICLVFEF 81  human
1K2P_B      1 IDPKDLTFLKELGTGQFGVVKYGKWrgqYDVAIKMIKEGSmsEDEFIEEAKVMMNLSHEKLVQLYGVCTkqrPIFIITEY 80  human
P08630    521 IHPMELMLMEELGSGQFGVVRRGKWrgsIDTAVKMMKEGTmsEDDFIEEAKVMTKLQHPNLVQLYGVCSkhrPIYIVTEY 600 fruit fly
BAD52302  373 LDALELTSLRELGRGALGVVQLGMWrgvRHIAIRMLHEGVlaEDDFFHEVKLMMQLSHPNLVQLYGVVTryrPLRIVMEY 452 inshore hagfish
AAP82507  428 IDKVSLSLGKELGSGQFGRVVSGKWkgkIDVAIKMMREGAmnEDDFIEEAKVMKQFQHENLVKLYGVCTkngPIFIVQEL 507 Suberites domuncula
P42681    266 IDPSELAFIKEIGSGQFGVVHLGEWrshIQVAIKAINEGSmsEEDFIEEAKVMMKLSHSKLVQLYGVCIqrkPLYIVTEF 345 human
3PIX_A     12 IDPKDLTFLKELGTGQFGVVKYGKWrgqYDVAIKMIKEGSmsEDEFIEEAKVMMNLSHEKLVQLYGVCTkqrPIFIITEY 91  human
Feature 1     ## #                                              #  #         ##  #            
1SM2_A     82 MEHGCLSDYLRTQrg--lFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGEnQVIKVSDFGMTRFVLDDQYTSS 159 human
1K2P_B     81 MANGCLLNYLREMrh--rFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDqGVVKVSDFGLSRYVLDDEYTSS 158 human
P08630    601 MKHGSLLNYLRRHektliGNMGLLLDMCIQVSKGMTYLERHNYIHRDLAARNCLVGSeNVVKVADFGLARYVLDDQYTSS 680 fruit fly
BAD52302  453 LALGCLRTFLQARpg--kLGSAWLLEACSDVCKAMVYLESNSFLHRDLAARHCLVGEdFSIKVSDFGMARYVLDDQYTCS 530 inshore hagfish
AAP82507  508 MVNGCLLQFLRQRke-lvEKTEIILDMATQICSAMKYLEESGFIHRDLAARNCLVGErNVVKVADFGLARFVVDDEYTAS 586 Suberites domuncula
P42681    346 MENGCLLNYLRENkg--kLRKEMLLSVCQDICEGMEYLERNGYIHRDLAARNCLVSStCIVKISDFGMTRYVLDDEYVSS 423 human
3PIX_A     92 MANGCLLNYLREMrh--rFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDqGVVKVSDFGLSRYVLDDEYTSS 169 human
Feature 1                                                                                     
1SM2_A    160 TGTKFPVKWASPEVFSFsRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCW 239 human
1K2P_B    159 VGSKFPVRWSPPEVLMYsKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCW 238 human
P08630    681 GGTKFPIKWAPPEVLNYtRFSSKSDVWAYGVLMWEIFTCGKMPYGRLKNTEVVERVQRGIILEKPKSCAKEIYDVMKLCW 760 fruit fly
BAD52302  531 QGARFPVKWSPPEVFDRgRFSSKSDVWSFGVVMWEVFSEGTLPYDGWSNGEVVESVHAGYQLPQPTLAPTPVYTIMCDCW 610 inshore hagfish
AAP82507  587 EGTKFPIKWAAPEVITHaKFSSKSDVWSFGILLWELWTGGKTPYPTFTNSQVLDEVLMGYRLDRPKQCPPEVYALMGKCW 666 Suberites domuncula
P42681    424 FGAKFPIKWSPPEVFLFnKYSSKSDVWSFGVLMWEVFTEGKMPFENKSNLQVVEAISEGFRLYRPHLAPMSIYEVMYSCW 503 human
3PIX_A    170 VGSKFPVRWSPPEVLMYsKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCW 249 human
Feature 1                       
1SM2_A    240 KErPEDRPAFSRLLRQLA 257 human
1K2P_B    239 HEkADERPTFKILLSNIL 256 human
P08630    761 SHgPEERPAFRVLMDQLA 778 fruit fly
BAD52302  611 QPdPEKRPYFMKLLELIT 628 inshore hagfish
AAP82507  667 LTnSDDRPQFKTLSSSLG 684 Suberites domuncula
P42681    504 HEkPEGRPTFAELLRAVT 521 human
3PIX_A    250 HEkADERPTFKILLSNIL 267 human

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