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Conserved domains on  [gi|18858593|ref|NP_571098|]
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ephrin-B2a precursor [Danio rerio]

Protein Classification

Ephrin-B_Ectodomain domain-containing protein (domain architecture ID 10179620)

Ephrin-B_Ectodomain domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
26-162 2.90e-91

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: 272.40  E-value: 2.90e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858593  26 ILDSIYWNTTNTKFVPGQGLVLYPQIGDKMDIVCPRVEGGSMEGVEYYKLYMVPLEQLKSCQVTKADTPLLNCVKPDQDV 105
Cdd:cd10426   1 VLEPIYWNSSNPKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18858593 106 KFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKVG 162
Cdd:cd10426  81 RFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
 
Name Accession Description Interval E-value
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
26-162 2.90e-91

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: 272.40  E-value: 2.90e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858593  26 ILDSIYWNTTNTKFVPGQGLVLYPQIGDKMDIVCPRVEGGSMEGVEYYKLYMVPLEQLKSCQVTKADTPLLNCVKPDQDV 105
Cdd:cd10426   1 VLEPIYWNSSNPKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18858593 106 KFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKVG 162
Cdd:cd10426  81 RFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
Ephrin pfam00812
Ephrin;
27-161 3.57e-65

Ephrin;


Pssm-ID: 307107  Cd Length: 136  Bit Score: 205.18  E-value: 3.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858593    27 LDSIYWNTTNTKFVpGQGLVLYPQIGDKMDIVCPRVEGGSM-EGVEYYKLYMVPLEQLKSC-QVTKADTPLLNCVKPDQD 104
Cdd:pfam00812   1 RHPVYWNSSNPRFR-NEDYVIYVRIGDYLDIICPHYEPGGPtDEYEYYKLYLVSKDGYDSCsLPGSNPRKLWECDRPHGP 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18858593   105 VKFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKV 161
Cdd:pfam00812  80 KKFTIKFQEFSPFPLGLEFQPGHDYYYISTSNGTLEGLDNRSGGLCESHNMKLKVKV 136
 
Name Accession Description Interval E-value
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
26-162 2.90e-91

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: 272.40  E-value: 2.90e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858593  26 ILDSIYWNTTNTKFVPGQGLVLYPQIGDKMDIVCPRVEGGSMEGVEYYKLYMVPLEQLKSCQVTKADTPLLNCVKPDQDV 105
Cdd:cd10426   1 VLEPIYWNSSNPKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDV 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18858593 106 KFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKVG 162
Cdd:cd10426  81 RFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
Ephrin pfam00812
Ephrin;
27-161 3.57e-65

Ephrin;


Pssm-ID: 307107  Cd Length: 136  Bit Score: 205.18  E-value: 3.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858593    27 LDSIYWNTTNTKFVpGQGLVLYPQIGDKMDIVCPRVEGGSM-EGVEYYKLYMVPLEQLKSC-QVTKADTPLLNCVKPDQD 104
Cdd:pfam00812   1 RHPVYWNSSNPRFR-NEDYVIYVRIGDYLDIICPHYEPGGPtDEYEYYKLYLVSKDGYDSCsLPGSNPRKLWECDRPHGP 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18858593   105 VKFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKV 161
Cdd:pfam00812  80 KKFTIKFQEFSPFPLGLEFQPGHDYYYISTSNGTLEGLDNRSGGLCESHNMKLKVKV 136
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
27-162 1.35e-56

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: 183.25  E-value: 1.35e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858593  27 LDSIYWNTTNTKFVPGqGLVLYPQIGDKMDIVCPRVE-GGSMEGVEYYKLYMVPLEQLKSCQVTKADTPLLNCVKPDQDV 105
Cdd:cd02675   1 LPPIYWNSTNPIFDNG-DYVIEVNIGDKLDIICPRYEsGTESEEYEYYKIYMVSKDGYDSCRLNTRSRLLLRCDRPYKEK 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18858593 106 KFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKVG 162
Cdd:cd02675  80 KFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
29-135 1.04e-24

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: 98.15  E-value: 1.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858593  29 SIYWNTTNTKFVPGqGLVLYPQIGDKMDIVCPRVEGGSM--EGVEYYKLYMVPLEQLKSCQVTKADTPLLNC---VKPDQ 103
Cdd:cd10425   4 AVYWNSSNNRFLRG-DYTVQVQINDYLDILCPHYESSDPagEEMERYILYMVSEEGYETCSHTDKGFKRWECnrpFAPHG 82
                        90       100       110
                ....*....|....*....|....*....|..
gi 18858593 104 DVKFTLKFQEFSPNLWGLEFFRGKDYYIISTS 135
Cdd:cd10425  83 PIKFSEKFQRFTPFSLGFEFRPGHEYYYISKP 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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