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Conserved domains on  [gi|568971523|ref|XP_006532223|]
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ephrin-B3 isoform X1 [Mus musculus]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 139548)

cupredoxin domain-containing protein that may contain type I Cu center(s) and be involved in inter-molecular electron transfer reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 51-179 9.92e-81

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


The actual alignment was detected with superfamily member cd10426:

Pssm-ID: 473140  Cd Length: 137  Bit Score: 242.35  E-value: 9.92e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971523  51 ARFQAEGGYVLYPQIGDRLDLLCPRARPPGPhssPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQE 130
Cdd:cd10426   12 PKFLPGQGLVLYPQIGDKLDIICPKVDSKTV---GQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDVRFTIKFQE 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568971523 131 YSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVG 179
Cdd:cd10426   89 FSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
 
Name Accession Description Interval E-value
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
 51-179 9.92e-81

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: 242.35  E-value: 9.92e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971523  51 ARFQAEGGYVLYPQIGDRLDLLCPRARPPGPhssPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQE 130
Cdd:cd10426   12 PKFLPGQGLVLYPQIGDKLDIICPKVDSKTV---GQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDVRFTIKFQE 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568971523 131 YSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVG 179
Cdd:cd10426   89 FSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
Ephrin pfam00812
Ephrin;
52-178 2.06e-60

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 190.58  E-value: 2.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971523   52 RFQaEGGYVLYPQIGDRLDLLCPRARPPGPHSSPsYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEY 131
Cdd:pfam00812  15 RFR-NGDYVIYVQIGDYLDIICPHYEPSGVGEAN-GEYYKLYLVSKEQYDTCTPTSKDNKRWECDRPDAPHKFTEKFQEF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568971523  132 SPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRV 178
Cdd:pfam00812  93 SPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLKVKV 139
 
Name Accession Description Interval E-value
Ephrin-B_Ectodomain cd10426
Ectodomain of Ephrin B; Ephrin Bs have several conserved tyrosine phosphorylation sites in ...
 51-179 9.92e-81

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: 242.35  E-value: 9.92e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971523  51 ARFQAEGGYVLYPQIGDRLDLLCPRARPPGPhssPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQE 130
Cdd:cd10426   12 PKFLPGQGLVLYPQIGDKLDIICPKVDSKTV---GQYEYYKLYMVDKDQADRCSIKKDPNPLLTCAKPDQDVRFTIKFQE 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568971523 131 YSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVG 179
Cdd:cd10426   89 FSPNLWGLEFQKNKDYYIISTSNGTLEGLENQEGGVCQTRSMKILMKVG 137
Ephrin pfam00812
Ephrin;
52-178 2.06e-60

Ephrin;


Pssm-ID: 459947  Cd Length: 139  Bit Score: 190.58  E-value: 2.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971523   52 RFQaEGGYVLYPQIGDRLDLLCPRARPPGPHSSPsYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEY 131
Cdd:pfam00812  15 RFR-NGDYVIYVQIGDYLDIICPHYEPSGVGEAN-GEYYKLYLVSKEQYDTCTPTSKDNKRWECDRPDAPHKFTEKFQEF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568971523  132 SPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRV 178
Cdd:pfam00812  93 SPFPLGFEFQPGHDYYYISTSDGTLEGIDSQHGGVCETQNMKLKVKV 139
Ephrin_ectodomain cd02675
Ectodomain of Ephrins; Ephrins and their receptors EphR play an important role in cell ...
 52-179 2.44e-52

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: 169.77  E-value: 2.44e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971523  52 RFQAeGGYVLYPQIGDRLDLLCPRARPPGPhsSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEY 131
Cdd:cd02675   12 IFDN-GDYVIEVNIGDKLDIICPRYESGTE--SEEYEYYKIYMVSKDGYDSCRLNTRSRLLLRCDRPYKEKKFTILFQEF 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568971523 132 SPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVG 179
Cdd:cd02675   89 SPIPGGLEFQPGKDYYFISTSTGTEEGLDNTSGGLCSSHNMKLAIKVC 136
Ephrin-A_Ectodomain cd10425
Ectodomain of Ephrin A; Ephrins and their receptors EphR play an important role in cell ...
 52-152 2.42e-18

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: 80.05  E-value: 2.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971523  52 RFQAeGGYVLYPQIGDRLDLLCPRARPPGPHSSpSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRP---DLDLRFTIKF 128
Cdd:cd10425   13 RFLR-GDYTVQVQINDYLDILCPHYESSDPAGE-EMERYILYMVSEEGYETCSHTDKGFKRWECNRPfapHGPIKFSEKF 90

                         90       100
                 ....*....|....*....|....
gi 568971523 129 QEYSPNLWGHEFRSHHDYYIIATS 152
Cdd:cd10425   91 QRFTPFSLGFEFRPGHEYYYISKP 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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