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Conserved domains on  [gi|71984507|ref|NP_501955|]
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Ephrin RBD domain-containing protein [Caenorhabditis elegans]

Protein Classification

ephrin domain-containing protein( domain architecture ID 10119358)

ephrin domain-containing protein that contains an Eph receptor (EphR) binding ectodomain, and which together with its EphR, may play a role in cell communication in normal physiology and in disease pathogenesis; similar to Caenorhabditis elegans ephrin-4 that regulates the formation or stabilization of cell-cell contacts at several stages of epithelial morphogenesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 21-154 9.43e-63

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: 191.73  E-value: 9.43e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984507  21 IPDINWISSNPIFDvsNTDHVISVHIGDRVSIRCPKSDETG---KYEYSYIYMVSDEEYDHCFL-SKPRLVGACDNQTIN 96
Cdd:cd02675   1 LPPIYWNSTNPIFD--NGDYVIEVNIGDKLDIICPRYESGTeseEYEYYKIYMVSKDGYDSCRLnTRSRLLLRCDRPYKE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71984507  97 ASINIVFRSFTPTPGGFEFQPGKNYFLISTSDGTLEGIDRKKDGLCTAKQMKIKFEVG 154
Cdd:cd02675  79 KKFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
 
Name Accession Description Interval E-value
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 21-154 9.43e-63

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: 191.73  E-value: 9.43e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984507  21 IPDINWISSNPIFDvsNTDHVISVHIGDRVSIRCPKSDETG---KYEYSYIYMVSDEEYDHCFL-SKPRLVGACDNQTIN 96
Cdd:cd02675   1 LPPIYWNSTNPIFD--NGDYVIEVNIGDKLDIICPRYESGTeseEYEYYKIYMVSKDGYDSCRLnTRSRLLLRCDRPYKE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71984507  97 ASINIVFRSFTPTPGGFEFQPGKNYFLISTSDGTLEGIDRKKDGLCTAKQMKIKFEVG 154
Cdd:cd02675  79 KKFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
Ephrin pfam00812
Ephrin;
23-153 1.69e-40

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 135.11  E-value: 1.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984507    23 DINWISSNPIFDvsNTDHVISVHIGDRVSIRCPKSDETG----KYEYSYIYMVSDEEYDHCFL-SKPRLVGACDNQTINA 97
Cdd:pfam00812   6 TVYWNSSNPRFR--NGDYVIYVQIGDYLDIICPHYEPSGvgeaNGEYYKLYLVSKEQYDTCTPtSKDNKRWECDRPDAPH 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 71984507    98 SINIVFRSFTPTPGGFEFQPGKNYFLISTSDGTLEGIDRKKDGLCTAKQMKIKFEV 153
Cdd:pfam00812  84 KFTEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLKVKV 139
 
Name Accession Description Interval E-value
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 21-154 9.43e-63

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: 191.73  E-value: 9.43e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984507  21 IPDINWISSNPIFDvsNTDHVISVHIGDRVSIRCPKSDETG---KYEYSYIYMVSDEEYDHCFL-SKPRLVGACDNQTIN 96
Cdd:cd02675   1 LPPIYWNSTNPIFD--NGDYVIEVNIGDKLDIICPRYESGTeseEYEYYKIYMVSKDGYDSCRLnTRSRLLLRCDRPYKE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71984507  97 ASINIVFRSFTPTPGGFEFQPGKNYFLISTSDGTLEGIDRKKDGLCTAKQMKIKFEVG 154
Cdd:cd02675  79 KKFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
Ephrin pfam00812
Ephrin;
23-153 1.69e-40

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 135.11  E-value: 1.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984507    23 DINWISSNPIFDvsNTDHVISVHIGDRVSIRCPKSDETG----KYEYSYIYMVSDEEYDHCFL-SKPRLVGACDNQTINA 97
Cdd:pfam00812   6 TVYWNSSNPRFR--NGDYVIYVQIGDYLDIICPHYEPSGvgeaNGEYYKLYLVSKEQYDTCTPtSKDNKRWECDRPDAPH 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 71984507    98 SINIVFRSFTPTPGGFEFQPGKNYFLISTSDGTLEGIDRKKDGLCTAKQMKIKFEV 153
Cdd:pfam00812  84 KFTEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLKVKV 139
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
 24-154 2.11e-30

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: 109.07  E-value: 2.11e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984507  24 INWISSNPIFdVSNTDHVISVHIGDRVSIRCPKSD--ETGKYEYSYIYMVSDEEYDHCFLSK-PRLVGACDNQTINASIN 100
Cdd:cd10426   5 IYWNSSNPKF-LPGQGLVLYPQIGDKLDIICPKVDskTVGQYEYYKLYMVDKDQADRCSIKKdPNPLLTCAKPDQDVRFT 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71984507 101 IVFRSFTPTPGGFEFQPGKNYFLISTSDGTLEGIDRKKDGLCTAKQMKIKFEVG 154
Cdd:cd10426  84 IKFQEFSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
 26-127 1.14e-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: 67.72  E-value: 1.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984507  26 WISSNPIFdvSNTDHVISVHIGDRVSIRCPK---SDETGKYEYSYI-YMVSDEEYDHCFL-SKPRLVGACDN-QTINASI 99
Cdd:cd10425   7 WNSSNNRF--LRGDYTVQVQINDYLDILCPHyesSDPAGEEMERYIlYMVSEEGYETCSHtDKGFKRWECNRpFAPHGPI 84

                        90       100       110
                ....*....|....*....|....*....|
gi 71984507 100 --NIVFRSFTPTPGGFEFQPGKNYFLISTS 127
Cdd:cd10425  85 kfSEKFQRFTPFSLGFEFRPGHEYYYISKP 114
 
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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