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Conserved domains on  [gi|1861540908|ref|XP_034970983|]
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ephrin-B2 isoform X2 [Zootoca vivipara]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10179620)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions| multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

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 ...
 167-303 2.62e-102

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: 300.13  E-value: 2.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 167 VLEPIYWNSSNSKFHPGQGLVLYPKIGDKLDIICPKVDSKTSGQYEYYKVYMVDKDQADSCTIKKDNTPLLNCAKPDQDV 246
Cdd:cd10426     1 VLEPIYWNSSNPKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1861540908 247 KFTIKFQEFSPNLWGLEFQRNKDYYIISTSNGSLEGLDNQEGGVCQTKAMKILMKVG 303
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 ...
 167-303 2.62e-102

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: 300.13  E-value: 2.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 167 VLEPIYWNSSNSKFHPGQGLVLYPKIGDKLDIICPKVDSKTSGQYEYYKVYMVDKDQADSCTIKKDNTPLLNCAKPDQDV 246
Cdd:cd10426     1 VLEPIYWNSSNPKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1861540908 247 KFTIKFQEFSPNLWGLEFQRNKDYYIISTSNGSLEGLDNQEGGVCQTKAMKILMKVG 303
Cdd:cd10426    81 RFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
Ephrin pfam00812
Ephrin;
165-302 8.14e-74

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 227.56  E-value: 8.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 165 SLVLEPIYWNSSNSKFHpGQGLVLYPKIGDKLDIICPKVDSKTSGQ--YEYYKVYMVDKDQADSCTIKKDNTPLLNCAKP 242
Cdd:pfam00812   1 SADRHTVYWNSSNPRFR-NGDYVIYVQIGDYLDIICPHYEPSGVGEanGEYYKLYLVSKEQYDTCTPTSKDNKRWECDRP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 243 DQDVKFTIKFQEFSPNLWGLEFQRNKDYYIISTSNGSLEGLDNQEGGVCQTKAMKILMKV 302
Cdd:pfam00812  80 DAPHKFTEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLKVKV 139
 
Name Accession Description Interval E-value
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
 167-303 2.62e-102

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: 300.13  E-value: 2.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 167 VLEPIYWNSSNSKFHPGQGLVLYPKIGDKLDIICPKVDSKTSGQYEYYKVYMVDKDQADSCTIKKDNTPLLNCAKPDQDV 246
Cdd:cd10426     1 VLEPIYWNSSNPKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1861540908 247 KFTIKFQEFSPNLWGLEFQRNKDYYIISTSNGSLEGLDNQEGGVCQTKAMKILMKVG 303
Cdd:cd10426    81 RFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
Ephrin pfam00812
Ephrin;
165-302 8.14e-74

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 227.56  E-value: 8.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 165 SLVLEPIYWNSSNSKFHpGQGLVLYPKIGDKLDIICPKVDSKTSGQ--YEYYKVYMVDKDQADSCTIKKDNTPLLNCAKP 242
Cdd:pfam00812   1 SADRHTVYWNSSNPRFR-NGDYVIYVQIGDYLDIICPHYEPSGVGEanGEYYKLYLVSKEQYDTCTPTSKDNKRWECDRP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 243 DQDVKFTIKFQEFSPNLWGLEFQRNKDYYIISTSNGSLEGLDNQEGGVCQTKAMKILMKV 302
Cdd:pfam00812  80 DAPHKFTEKFQEFSPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLKVKV 139
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 168-303 5.80e-70

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: 217.54  E-value: 5.80e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 168 LEPIYWNSSNSKFHPGqGLVLYPKIGDKLDIICPKVDSKT-SGQYEYYKVYMVDKDQADSCTIKKDNTPLLNCAKPDQDV 246
Cdd:cd02675     1 LPPIYWNSTNPIFDNG-DYVIEVNIGDKLDIICPRYESGTeSEEYEYYKIYMVSKDGYDSCRLNTRSRLLLRCDRPYKEK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1861540908 247 KFTIKFQEFSPNLWGLEFQRNKDYYIISTSNGSLEGLDNQEGGVCQTKAMKILMKVG 303
Cdd:cd02675    80 KFTILFQEFSPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
 170-276 4.80e-26

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: 102.00  E-value: 4.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861540908 170 PIYWNSSNSKFHPGqGLVLYPKIGDKLDIICPK--VDSKTSGQYEYYKVYMVDKDQADSCTIKKDNTPLLNC---AKPDQ 244
Cdd:cd10425     4 AVYWNSSNNRFLRG-DYTVQVQINDYLDILCPHyeSSDPAGEEMERYILYMVSEEGYETCSHTDKGFKRWECnrpFAPHG 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1861540908 245 DVKFTIKFQEFSPNLWGLEFQRNKDYYIISTS 276
Cdd:cd10425    83 PIKFSEKFQRFTPFSLGFEFRPGHEYYYISKP 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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