Conserved Protein Domain Family
PTKc_EphR_A10

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cd05064: PTKc_EphR_A10 
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10
PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Statistics
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PSSM-Id: 133195
View PSSM: cd05064
Aligned: 3 rows
Threshold Bit Score: 556.845
Threshold Setting Gi: 74762207
Created: 17-May-2007
Updated: 2-Mar-2014
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:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                     # ###   #               # #                                         
gi 74762207   639 ELDAKSVTLERSLGGGRFGELCCGCLQLPgrQELLVAVHMLRDSASDsQRLGFLAEALTLGQFDHSHIVRLEGVVTrgsT 718
gi 47222199   302 ELDNSSIKIERIVHTGDFGEVCRGCLKLPskRELPVAIKTLRAGCSDkQRRSFLSEVAILGQFDHANIVRLEGVITtgnT 381
gi 118101622  621 ELDNASIKIERIIGTGEFGEICRGWLKLPskRELPVAIQTLRAGCSAkQQRCFLAKACTMGQFDHTNVIRLEGVITrgnT 700
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1             ## #                                           #   ## #          #          
gi 74762207   719 LMIVTEYMSHGALDGFLRRHegqLVAGQLMGLLPGLASAMKYLSEMGYVHRGLAARHVLVSSdLVCKISGFGRGPRDRSE 798
gi 47222199   382 MMIVVESMSNGALDSFLRKHegqLSVMQLMDMLTGVASGMKYLTEMGFVHKRLAAHKVLVNSnLGCKVSGFRPLQEDKIE 461
gi 118101622  701 MMIVMEYMGNGVLDSFLRKHegqLTASQLLSMLQGIAAGMKYLAEMGYIHKSLAAHKVLVNSsLACKITGFRRLQEDKME 780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                #####        #                                 #                         
gi 74762207   799 AVYTTM-SGRSPALWAAPETLQFgHFSSASDVWSFGIIMWEVMAFGERPYWDMSGQDVIKAVEDGFRLPPPRNCPNLLHR 877
gi 47222199   462 AIYTTLhGGKSVVLWTAPEAIQYhRFSSASDVWSFGIVMWEVMSYGERPYWDMGNQDVIKAIEDGFRLPAPVNCPQHLHQ 541
gi 118101622  781 TIFSTM-RGKSLVLWSAPEAIQYhHFSPASDVWSFGIVMWEVMSYGERPYWDMSHQDVMKAVEDGFRLPAPAHCQPPLHQ 859
                         250       260
                  ....*....|....*....|....*..
Feature 1                                    
gi 74762207   878 LMLDCWQKdPGERPRFSQIHSILSKMV 904
gi 47222199   542 LMLDCWQKeRTERPSFSQIHSALSKSI 568
gi 118101622  860 LMLDCWQKeRSQRPKFSHIHDVLSKML 886

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