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Conserved domains on  [gi|24416458|gb|AAH38796|]
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EPH receptor A8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EphR_LBD super family cl02704
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
 31-203 1.52e-136

Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). They are subdivided into 2 groups, A and B type receptors, depending on their ligand ephrin-A or ephrin-B, respectively. In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.


The actual alignment was detected with superfamily member cd10486:

Pssm-ID: 470656  Cd Length: 173  Bit Score: 390.93  E-value: 1.52e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10486   1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10486  81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10486 161 CIAIVSVRVYYKK 173
fn3 pfam00041
Fibronectin type III domain;
330-418 7.46e-10

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458   330 SAPVNL-ISSVNGTSVTLEWAPPLDPGGrsDITYNAVcrrcpwalsRCEACGSGTRFVPQQTSLVQASLLVANLLAHMNY 408
Cdd:pfam00041   1 SAPSNLtVTDVTSTSLTVSWTPPPDGNG--PITGYEV---------EYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEY 69

                          90
                  ....*....|
gi 24416458   409 SFWIEAVNGV 418
Cdd:pfam00041  70 EVRVQAVNGG 79
 
Name Accession Description Interval E-value
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
 31-203 1.52e-136

Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198454  Cd Length: 173  Bit Score: 390.93  E-value: 1.52e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10486   1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10486  81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10486 161 CIAIVSVRVYYKK 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
31-203 9.78e-104

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 307.67  E-value: 9.78e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458     31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458    111 MPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQ 186
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*..
gi 24416458    187 DIGACLAILSLRIYYKK 203
Cdd:smart00615 161 DQGACVALVSVRVFYKK 177
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 32-204 2.70e-92

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 278.40  E-value: 2.70e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458    32 VNLLDTSTIHGDWGWLTYPA-HGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYdGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458   111 MPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADlGVRRLKLNTEVRSVGPLSKRGFYLAFQ 186
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAATATppawRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 24416458   187 DIGACLAILSLRIYYKKC 204
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
fn3 pfam00041
Fibronectin type III domain;
330-418 7.46e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458   330 SAPVNL-ISSVNGTSVTLEWAPPLDPGGrsDITYNAVcrrcpwalsRCEACGSGTRFVPQQTSLVQASLLVANLLAHMNY 408
Cdd:pfam00041   1 SAPSNLtVTDVTSTSLTVSWTPPPDGNG--PITGYEV---------EYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEY 69

                          90
                  ....*....|
gi 24416458   409 SFWIEAVNGV 418
Cdd:pfam00041  70 EVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 329-418 8.53e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.62  E-value: 8.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458    329 PSAPVNL-ISSVNGTSVTLEWAPPLDPGGRSDITYnavcrrcpWALSRCEacgSGTRFVPQQTSLVQASLLVANLLAHMN 407
Cdd:smart00060   1 PSPPSNLrVTDVTSTSVTLSWEPPPDDGITGYIVG--------YRVEYRE---EGSEWKEVNVTPSSTSYTLTGLKPGTE 69

                           90
                   ....*....|.
gi 24416458    408 YSFWIEAVNGV 418
Cdd:smart00060  70 YEFRVRAVNGA 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 329-435 9.07e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.80  E-value: 9.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 329 PSAPVNL-ISSVNGTSVTLEWAPPLDPGGRsDITYNavcrrcpwaLSRCEACGSGTRFVPQQTSLVQaSLLVANLLAHMN 407
Cdd:cd00063   1 PSPPTNLrVTDVTSTSVTLSWTPPEDDGGP-ITGYV---------VEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGTE 69

                        90       100       110
                ....*....|....*....|....*....|
gi 24416458 408 YSFWIEAVN--GVSDLSPEprraavVNITT 435
Cdd:cd00063  70 YEFRVRAVNggGESPPSES------VTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
313-472 2.51e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 46.92  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 313 YYR-AALD------PPSSA-----CTRPPSAPVNL-ISSVNGTSVTLEWAPPLDPggrsDITYNAVCRrcpwalsrceAC 379
Cdd:COG3401 299 YYRvTAVDaagnesAPSNVvsvttDLTPPAAPSGLtATAVGSSSITLSWTASSDA----DVTGYNVYR----------ST 364

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 380 GSGTRFVPQQTSLVQASLLVANLLAHMNYSFWIEAVNGVSDLSPEPRRAAVVNITTNQAGRRRNSVPQRPGPPASPASDP 459
Cdd:COG3401 365 SGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444

                       170
                ....*....|...
gi 24416458 460 SRDQSSAGDVLWA 472
Cdd:COG3401 445 ASAASNPGVSAAV 457
 
Name Accession Description Interval E-value
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
 31-203 1.52e-136

Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA8 has been implicated in various cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198454  Cd Length: 173  Bit Score: 390.93  E-value: 1.52e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10486   1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10486  81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10486 161 CIAIVSVRVYYKK 173
EphR_LBD_A cd10473
Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the ...
 31-203 2.60e-118

Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.


Pssm-ID: 198441  Cd Length: 173  Bit Score: 344.42  E-value: 2.60e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10473   1 EVVLLDSKTAQGELGWITYPPNGWEEISEMDEDYTPIRTYQVCNVMEPNQNNWLRTNWIYRGEAQRIYIELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10473  81 FPGVLGTCKETFNLYYMESDLDLGRNIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEVREVGPLTKKGFYLAFQDVGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10473 161 CVALVSVRVYYKK 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
31-203 9.78e-104

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 307.67  E-value: 9.78e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458     31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458    111 MPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQ 186
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*..
gi 24416458    187 DIGACLAILSLRIYYKK 203
Cdd:smart00615 161 DQGACVALVSVRVFYKK 177
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
 31-203 1.02e-96

Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA3 has been implicated in leukemia, lung and other cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


Pssm-ID: 198449  Cd Length: 173  Bit Score: 289.65  E-value: 1.02e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10481   1 EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10481  81 IPLVLGTCKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAFQDVGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10481 161 CVALVSVRVYFKK 173
EphR_LBD_A6 cd10484
Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the ...
 31-203 3.76e-95

Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA6, like other Eph receptors and their ephrin ligands, seems to play a role in neural development, underlying learning and memory. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198452  Cd Length: 173  Bit Score: 285.37  E-value: 3.76e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10484   1 QVVLLDTTMVLGELNWKTYPCNGWDAITEMDEYNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10484  81 IPWVVGTCKETFNLHYMESDEAHAVKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEVREVGPITRKGFYLAFQDIGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10484 161 CIALVSVRVYYKK 173
EphR_LBD_A5 cd10483
Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the ...
 31-203 9.22e-94

Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA5 is almost exclusively expressed in the nervous system. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198451  Cd Length: 173  Bit Score: 281.92  E-value: 9.22e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10483   1 EVNLLDSRSVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10483  81 LPGGLGTCKETFNVYYFESNDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAFQDLGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10483 161 CIALVSVRVYYKK 173
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
 31-203 3.94e-93

Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction results in cell-cell repulsion or adhesion.


Pssm-ID: 198455  Cd Length: 173  Bit Score: 280.37  E-value: 3.94e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10487   1 EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIELQFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10487  81 IPGVAGTCKETFNLYYAESDADLGRRLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAFQDVGA 160

                       170
                ....*....|...
gi 24416458 191 CLAILSLRIYYKK 203
Cdd:cd10487 161 CVALVSVRVYYKQ 173
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 32-204 2.70e-92

Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are a large family of receptor tyrosine kinases. This family represents the amino terminal domain which binds the ephrin ligand.


Pssm-ID: 460198  Cd Length: 177  Bit Score: 278.40  E-value: 2.70e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458    32 VNLLDTSTIHGDWGWLTYPA-HGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYdGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458   111 MPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADlGVRRLKLNTEVRSVGPLSKRGFYLAFQ 186
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAATATppawRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 24416458   187 DIGACLAILSLRIYYKKC 204
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
 31-204 1.20e-89

Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA7 has been implicated in various cancers, including prostate, gastic and colorectal cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198453  Cd Length: 177  Bit Score: 271.52  E-value: 1.20e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10485   3 EVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGA 190
Cdd:cd10485  83 LPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 162

                       170
                ....*....|....
gi 24416458 191 CLAILSLRIYYKKC 204
Cdd:cd10485 163 CIALVSVKVYYKKC 176
EphR_LBD_A4 cd10482
Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the ...
 31-203 6.40e-88

Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. A loss of EphA4, as well as EphB2, precedes memory decline in a murine model of Alzheimers disease. EphA4 has been shown to have a negative effect on axon regeneration and functional restoration in corticospinal lesions and is downregulated in some cervical cancers. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198450  Cd Length: 174  Bit Score: 266.91  E-value: 6.40e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHG-WDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCN 109
Cdd:cd10482   1 EVTLLDSRSVQGELGWIASPLEGgWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWIPREGAQRVYIEIKFTLRDCN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 110 SMPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIG 189
Cdd:cd10482  81 SLPGVMGTCKETFNLYYYESNNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAFQDVG 160

                       170
                ....*....|....
gi 24416458 190 ACLAILSLRIYYKK 203
Cdd:cd10482 161 ACIALVSVRVFYKK 174
EphR_LBD_B cd10472
Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the ...
 34-203 2.67e-81

Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. They play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphB receptors are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.


Pssm-ID: 198440  Cd Length: 176  Bit Score: 250.18  E-value: 2.67e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  34 LLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNSMPG 113
Cdd:cd10472   3 LMDTRTATAELGWTAHPPSGWEEVSGYDENMNTIRTYQVCNVFESNQNNWLRTKFIRRRGAHRVYVEMKFTVRDCSSIPN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 114 VLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIG 189
Cdd:cd10472  83 VPGSCKETFNLYYYESDSDIATKTspfwMENPYVKVDTIAADESFSQVDLGGRVMKVNTEVRSFGPLSRNGFYLAFQDYG 162

                       170
                ....*....|....
gi 24416458 190 ACLAILSLRIYYKK 203
Cdd:cd10472 163 ACMSLISVRVFYKK 176
EphR_LBD cd10319
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
 32-203 1.19e-78

Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). They are subdivided into 2 groups, A and B type receptors, depending on their ligand ephrin-A or ephrin-B, respectively. In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.


Pssm-ID: 198439  Cd Length: 177  Bit Score: 243.08  E-value: 1.19e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  32 VNLLDTSTIHGDWGWLTYP--AHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCN 109
Cdd:cd10319   1 VVLLDTTLATSDLGWLTYPygHGGWDEESGLDPDGANIRTYVVCNVAMPNQDNWLRTPFIERRGAQRIYVELKFTVRDCE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 110 SMPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTgADLGVRRLKLNTEVRSVGPLSKRGFYLAF 185
Cdd:cd10319  81 SFPGNARSCKETFNLYYYESDHDTATKEfppwNEDPYTKIDTIAADESFK-SSNEDTTEKLNTETRSIGPLTKRGFYLAF 159

                       170
                ....*....|....*...
gi 24416458 186 QDIGACLAILSLRIYYKK 203
Cdd:cd10319 160 QDQGACMSLLSVKVYYKK 177
EphR_LBD_B1 cd10476
Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the ...
 34-203 4.04e-76

Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. Using EphB1 knockout-mice, EphB1 has been shown to be essential to the development of long-term potentiation (LTP), a cellular model of synaptic plasticity, learning and memory formation. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198444  Cd Length: 176  Bit Score: 236.88  E-value: 4.04e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  34 LLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNSMPG 113
Cdd:cd10476   3 LMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 114 VLGTCKETFNLYYLESDRDLGASTQ----ESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIG 189
Cdd:cd10476  83 VPGSCKETFNLYYYETDSVIATKKSafwtEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYG 162

                       170
                ....*....|....
gi 24416458 190 ACLAILSLRIYYKK 203
Cdd:cd10476 163 ACMSLLSVRVFFKK 176
EphR_LBD_A2 cd10480
Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of ...
 31-204 7.65e-76

Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA2 negatively regulates cell differentiation and has been shown to be overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


Pssm-ID: 198448  Cd Length: 174  Bit Score: 235.89  E-value: 7.65e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYP-AHGWDSINEVDESfQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCN 109
Cdd:cd10480   1 EVVLLDFAAAGGELGWLTHPyGKGWDLMQNVMND-SPIYMYSVCNVMSGEQDNWLRTNWIYRSEAERIFIELKFTVRDCN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 110 SMPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIG 189
Cdd:cd10480  80 SFPGGAGSCKETFNLYYAESDVDYGTNFQKRQFRKIDTIAPDEITVSSDFETRNVKLNVEERSVGPLTRKGFYLAFQDIG 159

                       170
                ....*....|....*
gi 24416458 190 ACLAILSLRIYYKKC 204
Cdd:cd10480 160 ACVALLSVRVYYKKC 174
EphR_LBD_B3 cd10478
Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the ...
 31-203 1.40e-74

Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB3 plays a role in cell positioning in the gastrointestinal tract by being preferentially expressed in Paneth cells. It also has been implicated in early colorectal cancer and early stage squamous cell lung cancer. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198446  Cd Length: 173  Bit Score: 232.59  E-value: 1.40e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10478   1 EETLMDTKWVTSELAWTTHPESGWEEVSGYDEAMNPIRTYQVCNVRESNQNNWLRTGFIPRRDVQRVYVELKFTVRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGvrrlKLNTEVRSVGPLSKRGFYLAFQ 186
Cdd:cd10478  81 IPNIPGSCKETFNLFYYESDSDSASASspfwMENPYVKVDTIAPDESFSRLDSG----RVNTKVRSFGPLSKAGFYLAFQ 156

                       170
                ....*....|....*..
gi 24416458 187 DIGACLAILSLRIYYKK 203
Cdd:cd10478 157 DLGACMSLISVRAFFKK 173
EphR_LBD_B2 cd10477
Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the ...
 31-203 2.20e-71

Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB2 plays a role in cell positioning in the gastrointestinal tract by being expressed in proliferating progenitor cells. It also has been implicated in colorectal cancer. A loss of EphB2, as well as EphA4, also precedes memory decline in a murine model of Alzheimers disease. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198445  Cd Length: 178  Bit Score: 224.55  E-value: 2.20e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNS 110
Cdd:cd10477   2 EETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKYIRRRGAHRIHVEMKFSVRDCSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 111 MPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQ 186
Cdd:cd10477  82 IPSVPGSCKETFNLYYYESDFDSATKTfpnwMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGFYLAFQ 161

                       170
                ....*....|....*..
gi 24416458 187 DIGACLAILSLRIYYKK 203
Cdd:cd10477 162 DYGGCMSLIAVRVFYRK 178
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
 31-203 3.58e-59

Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphA1 is downregulated in some advanced colorectal and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion.


Pssm-ID: 198447  Cd Length: 177  Bit Score: 192.94  E-value: 3.58e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYPAH-GWDSINEVDESfQPIHTYQVCNVMSP-NQNNWLRTSWVPR-DGARRVYAEIKFTLRD 107
Cdd:cd10479   1 EVTLMDTSTAQGELGWLLDPPEvGWSEVQQMLNG-TPLYMYQDCPVQSEgDTDHWLRSNWIYRgEEASRIYVELQFTVRD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 108 CNSMPGVLG--TCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAF 185
Cdd:cd10479  80 CKSFPGGAGplGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAF 159

                       170
                ....*....|....*...
gi 24416458 186 QDIGACLAILSLRIYYKK 203
Cdd:cd10479 160 HNPGACVALVSVRVFYQR 177
EphR_LBD_B6 cd10475
Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the ...
 34-203 4.18e-55

Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB6, a kinase-defective member of this family, is downregulated in MDA-MB-231-breast cancer cells and myeloid cancers and upregulated in neuroblasoma and glioblastoma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198443  Cd Length: 180  Bit Score: 182.44  E-value: 4.18e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  34 LLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNV--MSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNSM 111
Cdd:cd10475   4 LLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEVCNVaaQGPGQDNWLRTHFIERRGAHRVHVRLHFSVRDCASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 112 PGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADL-GVRRLKLNTEVRSVGPLSKRGFYLAFQ 186
Cdd:cd10475  84 GVPGGTCRETFTLYYRQADEPDEPADksewHEGPWTKVDTIAADESFPASLGkGGQGLQMNVKERSFGPLTQRGFYLAFQ 163

                       170
                ....*....|....*..
gi 24416458 187 DIGACLAILSLRIYYKK 203
Cdd:cd10475 164 DSGACLSLVAVKVFFYK 180
EphR_LBD_B4 cd10474
Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the ...
 31-203 7.96e-55

Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EhpB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. EphB4 plays a role in osteoblast differentiation and has been linked to multiple myeloma. EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling).


Pssm-ID: 198442  Cd Length: 180  Bit Score: 181.70  E-value: 7.96e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458  31 EVNLLDTSTIHGDWGWLTYP-AHG-WDSINEVDESFQPIHTYQVCNVMSP-NQNNWLRTSWVPRDGARRVYAEIKFTLRD 107
Cdd:cd10474   1 EETLLNTKLETADLKWVTYPqVDGqWEELSGLDEEQHSVRTYEVCDAQRAgGQAHWLRTGWVPRRGAVHVYATLRFTMLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 108 CNSMPGVLGTCKETFNLYYLESDRDLGAST----QESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYL 183
Cdd:cd10474  81 CLSLPRAGRSCKETFTVFYYESDADTATAHtpawMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYL 160

                       170       180
                ....*....|....*....|
gi 24416458 184 AFQDIGACLAILSLRIYYKK 203
Cdd:cd10474 161 AFQDQGACMALLSLHLFYKK 180
fn3 pfam00041
Fibronectin type III domain;
330-418 7.46e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.50  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458   330 SAPVNL-ISSVNGTSVTLEWAPPLDPGGrsDITYNAVcrrcpwalsRCEACGSGTRFVPQQTSLVQASLLVANLLAHMNY 408
Cdd:pfam00041   1 SAPSNLtVTDVTSTSLTVSWTPPPDGNG--PITGYEV---------EYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEY 69

                          90
                  ....*....|
gi 24416458   409 SFWIEAVNGV 418
Cdd:pfam00041  70 EVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 329-418 8.53e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 52.62  E-value: 8.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458    329 PSAPVNL-ISSVNGTSVTLEWAPPLDPGGRSDITYnavcrrcpWALSRCEacgSGTRFVPQQTSLVQASLLVANLLAHMN 407
Cdd:smart00060   1 PSPPSNLrVTDVTSTSVTLSWEPPPDDGITGYIVG--------YRVEYRE---EGSEWKEVNVTPSSTSYTLTGLKPGTE 69

                           90
                   ....*....|.
gi 24416458    408 YSFWIEAVNGV 418
Cdd:smart00060  70 YEFRVRAVNGA 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 329-435 9.07e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.80  E-value: 9.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 329 PSAPVNL-ISSVNGTSVTLEWAPPLDPGGRsDITYNavcrrcpwaLSRCEACGSGTRFVPQQTSLVQaSLLVANLLAHMN 407
Cdd:cd00063   1 PSPPTNLrVTDVTSTSVTLSWTPPEDDGGP-ITGYV---------VEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGTE 69

                        90       100       110
                ....*....|....*....|....*....|
gi 24416458 408 YSFWIEAVN--GVSDLSPEprraavVNITT 435
Cdd:cd00063  70 YEFRVRAVNggGESPPSES------VTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
313-472 2.51e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 46.92  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 313 YYR-AALD------PPSSA-----CTRPPSAPVNL-ISSVNGTSVTLEWAPPLDPggrsDITYNAVCRrcpwalsrceAC 379
Cdd:COG3401 299 YYRvTAVDaagnesAPSNVvsvttDLTPPAAPSGLtATAVGSSSITLSWTASSDA----DVTGYNVYR----------ST 364

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24416458 380 GSGTRFVPQQTSLVQASLLVANLLAHMNYSFWIEAVNGVSDLSPEPRRAAVVNITTNQAGRRRNSVPQRPGPPASPASDP 459
Cdd:COG3401 365 SGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444

                       170
                ....*....|...
gi 24416458 460 SRDQSSAGDVLWA 472
Cdd:COG3401 445 ASAASNPGVSAAV 457
 
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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