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Conserved domains on  [gi|17539606|ref|NP_499947|]
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Ephrin-4 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ephrin pfam00812
Ephrin;
19-178 1.28e-57

Ephrin;


:

Pssm-ID: 459947  Cd Length: 139  Bit Score: 183.26  E-value: 1.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606    19 AADEHIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCPDNEE---GRNDGEYLIVYEVTEFAMDDCALESHSREVIRCAPEG 95
Cdd:pfam00812   1 SADRHTVYWNSSNPRFRNGDYVIYVQIGDYLDIICPHYEPsgvGEANGEYYKLYLVSKEQYDTCTPTSKDNKRWECDRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606    96 TAEKVlrtqqlsggrredwkkqkvppknvAQLIRQLNPIPNGKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLS 175
Cdd:pfam00812  81 APHKF------------------------TEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLK 136


                  ...
gi 17539606   176 MKV 178
Cdd:pfam00812 137 VKV 139
 
Name Accession Description Interval E-value
Ephrin pfam00812
Ephrin;
19-178 1.28e-57

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 183.26  E-value: 1.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606    19 AADEHIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCPDNEE---GRNDGEYLIVYEVTEFAMDDCALESHSREVIRCAPEG 95
Cdd:pfam00812   1 SADRHTVYWNSSNPRFRNGDYVIYVQIGDYLDIICPHYEPsgvGEANGEYYKLYLVSKEQYDTCTPTSKDNKRWECDRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606    96 TAEKVlrtqqlsggrredwkkqkvppknvAQLIRQLNPIPNGKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLS 175
Cdd:pfam00812  81 APHKF------------------------TEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLK 136


                  ...
gi 17539606   176 MKV 178
Cdd:pfam00812 137 VKV 139
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 23-179 1.92e-55

Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrins contain a highly conserved ectodomain for receptor binding, which is characterized by this domain hierarchy.


Pssm-ID: 259861  Cd Length: 136  Bit Score: 177.48  E-value: 1.92e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606  23 HIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCPDNEEG--RNDGEYLIVYEVTEFAMDDCALESHSREVIRCAPEGTaekv 100
Cdd:cd02675   2 PPIYWNSTNPIFDNGDYVIEVNIGDKLDIICPRYESGteSEEYEYYKIYMVSKDGYDSCRLNTRSRLLLRCDRPYK---- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539606 101 lrtqqlsggrredwkkqkvpPKNVAQLIRQLNPIPNGKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLSMKVS 179
Cdd:cd02675  78 --------------------EKKFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
 
Name Accession Description Interval E-value
Ephrin pfam00812
Ephrin;
19-178 1.28e-57

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 183.26  E-value: 1.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606    19 AADEHIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCPDNEE---GRNDGEYLIVYEVTEFAMDDCALESHSREVIRCAPEG 95
Cdd:pfam00812   1 SADRHTVYWNSSNPRFRNGDYVIYVQIGDYLDIICPHYEPsgvGEANGEYYKLYLVSKEQYDTCTPTSKDNKRWECDRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606    96 TAEKVlrtqqlsggrredwkkqkvppknvAQLIRQLNPIPNGKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLS 175
Cdd:pfam00812  81 APHKF------------------------TEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLK 136


                  ...
gi 17539606   176 MKV 178
Cdd:pfam00812 137 VKV 139
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 23-179 1.92e-55

Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrins contain a highly conserved ectodomain for receptor binding, which is characterized by this domain hierarchy.


Pssm-ID: 259861  Cd Length: 136  Bit Score: 177.48  E-value: 1.92e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606  23 HIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCPDNEEG--RNDGEYLIVYEVTEFAMDDCALESHSREVIRCAPEGTaekv 100
Cdd:cd02675   2 PPIYWNSTNPIFDNGDYVIEVNIGDKLDIICPRYESGteSEEYEYYKIYMVSKDGYDSCRLNTRSRLLLRCDRPYK---- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17539606 101 lrtqqlsggrredwkkqkvpPKNVAQLIRQLNPIPNGKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLSMKVS 179
Cdd:cd02675  78 --------------------EKKFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
 21-153 3.78e-14

Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin As contain a highly conserved receptor binding ectodomain described by this model. Although ephrin As do not have a cytoplasmic tail (in contrast to ephrin Bs), they are still capable of downstream activation of Src family kinases and phosphoinositide-3-kinases, most likely involving coreceptors such as neurotrophin receptors.


Pssm-ID: 259896  Cd Length: 130  Bit Score: 68.49  E-value: 3.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606  21 DEHIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCP---DNEEGRNDGEYLIVYEVTEFAMDDCALESHSREVIRCApegta 97
Cdd:cd10425   1 DRHAVYWNSSNNRFLRGDYTVQVQINDYLDILCPhyeSSDPAGEEMERYILYMVSEEGYETCSHTDKGFKRWECN----- 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17539606  98 ekvlRTQQLSGGRREDWKKQKvppknvaqlirqLNPIPNGKEYQPGQTYYYMTTST 153
Cdd:cd10425  76 ----RPFAPHGPIKFSEKFQR------------FTPFSLGFEFRPGHEYYYISKPI 115
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
 25-178 4.85e-09

Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in their cytoplasmic PDZ-like domain, which are important for signal transduction. Ephrins and their receptors EphR play an important role in cell communication in normal physiology, as well as in disease pathogenesis. Binding of the ephrin (Eph) ligand to EphR requires cell-cell contact, since both molecules are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling, depending on Eph kinase activity) and ephrin-expressing cells (reverse signaling). Eph signaling controls cell morphology, adhesion, migration and invasion. Ephrins can be subdivided into 2 groups, A and B, depending on their respective receptors EphA or EphB. The nine human EphA receptors bind to five GPI-linked ephrin-A ligands and the five EphB receptors bind to three transmembrane ephrin-B ligands. Interactions are promiscuous within each class, and some Eph receptors can also bind to ephrins of the other class. All ephrin Bs contain a highly conserved receptor binding ectodomain described in this model.


Pssm-ID: 259897  Cd Length: 137  Bit Score: 53.99  E-value: 4.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606  25 VYWNSTNSLFRNRQ-----PTIevrmGDVVRFVCPDNEEGRNDG-EYLIVYEVTEFAMDDCALESHSREVIRCA-PEGTA 97
Cdd:cd10426   5 IYWNSSNPKFLPGQglvlyPQI----GDKLDIICPKVDSKTVGQyEYYKLYMVDKDQADRCSIKKDPNPLLTCAkPDQDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539606  98 EKVLRTQQLSggrredwkkqkvppknvaqlirqlnpiPN--GKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLS 175
Cdd:cd10426  81 RFTIKFQEFS---------------------------PNlwGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKIL 133


                ...
gi 17539606 176 MKV 178
Cdd:cd10426 134 MKV 136
 
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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