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Conserved domains on  [gi|32967314|ref|NP_872585|]
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ephrin type-A receptor 3 isoform b precursor [Homo sapiens]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
 29-201 1.89e-134

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: 387.49  E-value: 1.89e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10481   1 EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10481  81 IPLVLGTCKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAFQDVGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10481 161 CVALVSVRVYFKK 173
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-528 2.04e-18

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: 80.23  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 437 PSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQE-TSYTILRARGTNVTISSLKPDTIYVFQIRARTAA 515
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                        90
                ....*....|...
gi 32967314 516 GYGTNSRKFEFET 528
Cdd:cd00063  81 GESPPSESVTVTT 93
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
323-516 2.83e-14

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.42  E-value: 2.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 323 TRPPSSPRNV-ISNINETSVILDWswplDTGGRKDVTfniickkcGWNIKQCEPCSPNVRFLPRqfgLTNTTVTVTDLLA 401
Cdd:COG3401 230 TTPPSAPTGLtATADTPGSVTLSW----DPVTESDAT--------GYRVYRSNSGDGPFTKVAT---VTTTSYTDTGLTN 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 402 HTNYTFEIDAVNGVSELSSPPrqfAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPehPNGIILDYEVkyYEKQEQE 481
Cdd:COG3401 295 GTTYYYRVTAVDAAGNESAPS---NVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS--SDADVTGYNV--YRSTSGG 367

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 32967314 482 TSYTIL--RARGTNVTISSLKPDTIYVFQIRARTAAG 516
Cdd:COG3401 368 GTYTKIaeTVTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 269-303 9.02e-05

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 40.02  E-value: 9.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 32967314   269 MCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMN 303
Cdd:pfam07699  10 PCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATS 44
 
Name Accession Description Interval E-value
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
 29-201 1.89e-134

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: 387.49  E-value: 1.89e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10481   1 EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10481  81 IPLVLGTCKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAFQDVGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10481 161 CVALVSVRVYFKK 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
29-201 2.08e-110

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 326.16  E-value: 2.08e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314     29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    109 IPLVLGTCKETFNLYYMESDDDHGVKF----REHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQ 184
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*..
gi 32967314    185 DVGACVALVSVRVYFKK 201
Cdd:smart00615 161 DQGACVALVSVRVFYKK 177
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 30-202 3.15e-94

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: 284.56  E-value: 3.15e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    30 VNLLDSKTIQGELGWISYP-SHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPyDGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314   109 IPLVLGTCKETFNLYYMESDDDHGVK----FREHQFTKIDTIAADESFTQMDlGDRILKLNTEIREVGPVNKKGFYLAFQ 184
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAATAtppaWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 32967314   185 DVGACVALVSVRVYFKKC 202
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-528 2.04e-18

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: 80.23  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 437 PSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQE-TSYTILRARGTNVTISSLKPDTIYVFQIRARTAA 515
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                        90
                ....*....|...
gi 32967314 516 GYGTNSRKFEFET 528
Cdd:cd00063  81 GESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
438-521 1.25e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.06  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314   438 SPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTN-VTISSLKPDTIYVFQIRARTAAG 516
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQAVNGGG 80


                  ....*
gi 32967314   517 YGTNS 521
Cdd:pfam00041  81 EGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 437-518 3.55e-15

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: 70.72  E-value: 3.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    437 PSPVLTIKKDRTSRNSISLSWQEPEHPNGI--ILDYEVKYYEKQEQETSYTIlRARGTNVTISSLKPDTIYVFQIRARTA 514
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 32967314    515 AGYG 518
Cdd:smart00060  80 AGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
323-516 2.83e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.42  E-value: 2.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 323 TRPPSSPRNV-ISNINETSVILDWswplDTGGRKDVTfniickkcGWNIKQCEPCSPNVRFLPRqfgLTNTTVTVTDLLA 401
Cdd:COG3401 230 TTPPSAPTGLtATADTPGSVTLSW----DPVTESDAT--------GYRVYRSNSGDGPFTKVAT---VTTTSYTDTGLTN 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 402 HTNYTFEIDAVNGVSELSSPPrqfAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPehPNGIILDYEVkyYEKQEQE 481
Cdd:COG3401 295 GTTYYYRVTAVDAAGNESAPS---NVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS--SDADVTGYNV--YRSTSGG 367

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 32967314 482 TSYTIL--RARGTNVTISSLKPDTIYVFQIRARTAAG 516
Cdd:COG3401 368 GTYTKIaeTVTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
fn3 pfam00041
Fibronectin type III domain;
327-417 2.79e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314   327 SSPRNV-ISNINETSVILDWSWPlDTGGRKDVTFNIICKKCGwnikqcEPCSPNVRFLPRqfglTNTTVTVTDLLAHTNY 405
Cdd:pfam00041   1 SAPSNLtVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKN------SGEPWNEITVPG----TTTSVTLTGLKPGTEY 69

                          90
                  ....*....|..
gi 32967314   406 TFEIDAVNGVSE 417
Cdd:pfam00041  70 EVRVQAVNGGGE 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 326-432 4.47e-09

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: 53.65  E-value: 4.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 326 PSSPRNV-ISNINETSVILDWSWPLDTGGRkDVTFNIICKKCGW-NIKQCEPCSPNvrflprqfgltNTTVTVTDLLAHT 403
Cdd:cd00063   1 PSPPTNLrVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSgDWKEVEVTPGS-----------ETSYTLTGLKPGT 68

                        90       100       110
                ....*....|....*....|....*....|.
gi 32967314 404 NYTFEIDAVN--GVSELSSPprqfaaVSITT 432
Cdd:cd00063  69 EYEFRVRAVNggGESPPSES------VTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 326-417 1.32e-08

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: 52.23  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    326 PSSPRNV-ISNINETSVILDWSWPLDTGGRKDVTfniickkcGWNIKQCEPCSPNVRFLPRQfglTNTTVTVTDLLAHTN 404
Cdd:smart00060   1 PSPPSNLrVTDVTSTSVTLSWEPPPDDGITGYIV--------GYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTE 69

                           90
                   ....*....|...
gi 32967314    405 YTFEIDAVNGVSE 417
Cdd:smart00060  70 YEFRVRAVNGAGE 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
390-516 2.69e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.55  E-value: 2.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 390 TNTTVTVTDLLAHTNYTFEIDAVNGVSElSSPPRQFAAVSITTNQAAPSPVLTIkkdRTSRNSISLSWQEPEHPNgiILD 469
Cdd:COG3401 190 TTLVDGGGDIEPGTTYYYRVAATDTGGE-SAPSNEVSVTTPTTPPSAPTGLTAT---ADTPGSVTLSWDPVTESD--ATG 263

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32967314 470 YEVkyYEKQEQETSYTIL-RARGTNVTISSLKPDTIYVFQIRARTAAG 516
Cdd:COG3401 264 YRV--YRSNSGDGPFTKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAAG 309
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 269-303 9.02e-05

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 40.02  E-value: 9.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 32967314   269 MCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMN 303
Cdd:pfam07699  10 PCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATS 44
 
Name Accession Description Interval E-value
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
 29-201 1.89e-134

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: 387.49  E-value: 1.89e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10481   1 EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10481  81 IPLVLGTCKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAFQDVGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10481 161 CVALVSVRVYFKK 173
EphR_LBD_A cd10473
Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the ...
 29-201 9.68e-127

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: 367.53  E-value: 9.68e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10473   1 EVVLLDSKTAQGELGWITYPPNGWEEISEMDEDYTPIRTYQVCNVMEPNQNNWLRTNWIYRGEAQRIYIELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10473  81 FPGVLGTCKETFNLYYMESDLDLGRNIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEVREVGPLTKKGFYLAFQDVGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10473 161 CVALVSVRVYYKK 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
29-201 2.08e-110

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 326.16  E-value: 2.08e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314     29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    109 IPLVLGTCKETFNLYYMESDDDHGVKF----REHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQ 184
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*..
gi 32967314    185 DVGACVALVSVRVYFKK 201
Cdd:smart00615 161 DQGACVALVSVRVFYKK 177
EphR_LBD_A6 cd10484
Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the ...
 29-201 6.36e-105

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: 311.95  E-value: 6.36e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10484   1 QVVLLDTTMVLGELNWKTYPCNGWDAITEMDEYNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10484  81 IPWVVGTCKETFNLHYMESDEAHAVKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEVREVGPITRKGFYLAFQDIGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10484 161 CIALVSVRVYYKK 173
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
 29-201 2.66e-103

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: 307.72  E-value: 2.66e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10487   1 EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIELQFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10487  81 IPGVAGTCKETFNLYYAESDADLGRRLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAFQDVGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10487 161 CVALVSVRVYYKQ 173
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
 29-201 3.14e-103

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: 307.73  E-value: 3.14e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10486   1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10486  81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10486 161 CIAIVSVRVYYKK 173
EphR_LBD_A5 cd10483
Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the ...
 29-201 1.27e-100

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: 300.79  E-value: 1.27e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10483   1 EVNLLDSRSVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10483  81 LPGGLGTCKETFNVYYFESNDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAFQDLGA 160

                       170
                ....*....|...
gi 32967314 189 CVALVSVRVYFKK 201
Cdd:cd10483 161 CIALVSVRVYYKK 173
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
 29-202 3.04e-97

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: 292.32  E-value: 3.04e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10485   3 EVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGA 188
Cdd:cd10485  83 LPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 162

                       170
                ....*....|....
gi 32967314 189 CVALVSVRVYFKKC 202
Cdd:cd10485 163 CIALVSVKVYYKKC 176
EphR_LBD_A4 cd10482
Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the ...
 29-201 7.51e-95

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: 286.17  E-value: 7.51e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHG-WEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCN 107
Cdd:cd10482   1 EVTLLDSRSVQGELGWIASPLEGgWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWIPREGAQRVYIEIKFTLRDCN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 108 SIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVG 187
Cdd:cd10482  81 SLPGVMGTCKETFNLYYYESNNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAFQDVG 160

                       170
                ....*....|....
gi 32967314 188 ACVALVSVRVYFKK 201
Cdd:cd10482 161 ACIALVSVRVFYKK 174
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 30-202 3.15e-94

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: 284.56  E-value: 3.15e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    30 VNLLDSKTIQGELGWISYP-SHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPyDGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314   109 IPLVLGTCKETFNLYYMESDDDHGVK----FREHQFTKIDTIAADESFTQMDlGDRILKLNTEIREVGPVNKKGFYLAFQ 184
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAATAtppaWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 32967314   185 DVGACVALVSVRVYFKKC 202
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
EphR_LBD_B cd10472
Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the ...
 32-201 6.79e-87

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: 265.97  E-value: 6.79e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  32 LLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPL 111
Cdd:cd10472   3 LMDTRTATAELGWTAHPPSGWEEVSGYDENMNTIRTYQVCNVFESNQNNWLRTKFIRRRGAHRVYVEMKFTVRDCSSIPN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 112 VLGTCKETFNLYYMESDDDHGVK----FREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVG 187
Cdd:cd10472  83 VPGSCKETFNLYYYESDSDIATKtspfWMENPYVKVDTIAADESFSQVDLGGRVMKVNTEVRSFGPLSRNGFYLAFQDYG 162

                       170
                ....*....|....
gi 32967314 188 ACVALVSVRVYFKK 201
Cdd:cd10472 163 ACMSLISVRVFYKK 176
EphR_LBD_B3 cd10478
Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the ...
 29-201 5.42e-81

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: 250.70  E-value: 5.42e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10478   1 EETLMDTKWVTSELAWTTHPESGWEEVSGYDEAMNPIRTYQVCNVRESNQNNWLRTGFIPRRDVQRVYVELKFTVRDCNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVK----FREHQFTKIDTIAADESFTQMDLGdrilKLNTEIREVGPVNKKGFYLAFQ 184
Cdd:cd10478  81 IPNIPGSCKETFNLFYYESDSDSASAsspfWMENPYVKVDTIAPDESFSRLDSG----RVNTKVRSFGPLSKAGFYLAFQ 156

                       170
                ....*....|....*..
gi 32967314 185 DVGACVALVSVRVYFKK 201
Cdd:cd10478 157 DLGACMSLISVRAFFKK 173
EphR_LBD_B2 cd10477
Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the ...
 29-201 1.19e-77

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: 242.27  E-value: 1.19e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNS 108
Cdd:cd10477   2 EETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKYIRRRGAHRIHVEMKFSVRDCSS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 109 IPLVLGTCKETFNLYYMESDDDHGVK----FREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQ 184
Cdd:cd10477  82 IPSVPGSCKETFNLYYYESDFDSATKtfpnWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGFYLAFQ 161

                       170
                ....*....|....*..
gi 32967314 185 DVGACVALVSVRVYFKK 201
Cdd:cd10477 162 DYGGCMSLIAVRVFYRK 178
EphR_LBD_B1 cd10476
Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the ...
 32-201 1.60e-77

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: 241.50  E-value: 1.60e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  32 LLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPL 111
Cdd:cd10476   3 LMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 112 VLGTCKETFNLYYMESDDDHGVK----FREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVG 187
Cdd:cd10476  83 VPGSCKETFNLYYYETDSVIATKksafWTEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYG 162

                       170
                ....*....|....
gi 32967314 188 ACVALVSVRVYFKK 201
Cdd:cd10476 163 ACMSLLSVRVFFKK 176
EphR_LBD cd10319
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
 30-201 2.49e-75

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: 236.15  E-value: 2.49e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  30 VNLLDSKTIQGELGWISYP--SHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCN 107
Cdd:cd10319   1 VVLLDTTLATSDLGWLTYPygHGGWDEESGLDPDGANIRTYVVCNVAMPNQDNWLRTPFIERRGAQRIYVELKFTVRDCE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 108 SIPLVLGTCKETFNLYYMESDDDHGVK----FREHQFTKIDTIAADESFTQMDlGDRILKLNTEIREVGPVNKKGFYLAF 183
Cdd:cd10319  81 SFPGNARSCKETFNLYYYESDHDTATKefppWNEDPYTKIDTIAADESFKSSN-EDTTEKLNTETRSIGPLTKRGFYLAF 159

                       170
                ....*....|....*...
gi 32967314 184 QDVGACVALVSVRVYFKK 201
Cdd:cd10319 160 QDQGACMSLLSVKVYYKK 177
EphR_LBD_A2 cd10480
Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of ...
 29-202 5.80e-74

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: 232.43  E-value: 5.80e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYP-SHGWEEISGVDEHyTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCN 107
Cdd:cd10480   1 EVVLLDFAAAGGELGWLTHPyGKGWDLMQNVMND-SPIYMYSVCNVMSGEQDNWLRTNWIYRSEAERIFIELKFTVRDCN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 108 SIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVG 187
Cdd:cd10480  80 SFPGGAGSCKETFNLYYAESDVDYGTNFQKRQFRKIDTIAPDEITVSSDFETRNVKLNVEERSVGPLTRKGFYLAFQDIG 159

                       170
                ....*....|....*
gi 32967314 188 ACVALVSVRVYFKKC 202
Cdd:cd10480 160 ACVALLSVRVYYKKC 174
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
 29-201 1.26e-61

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: 200.26  E-value: 1.26e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWI-SYPSHGWEEISGVdEHYTPIRTYQVCNVMDHSQ-NNWLRTNWVPR-NSAQKIYVELKFTLRD 105
Cdd:cd10479   1 EVTLMDTSTAQGELGWLlDPPEVGWSEVQQM-LNGTPLYMYQDCPVQSEGDtDHWLRSNWIYRgEEASRIYVELQFTVRD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 106 CNSIPLVLG--TCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAF 183
Cdd:cd10479  80 CKSFPGGAGplGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAF 159

                       170
                ....*....|....*...
gi 32967314 184 QDVGACVALVSVRVYFKK 201
Cdd:cd10479 160 HNPGACVALVSVRVFYQR 177
EphR_LBD_B6 cd10475
Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the ...
 32-201 4.87e-59

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: 193.61  E-value: 4.87e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  32 LLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNV--MDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSI 109
Cdd:cd10475   4 LLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEVCNVaaQGPGQDNWLRTHFIERRGAHRVHVRLHFSVRDCASL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 110 PLVLGTCKETFNLYYMESDDD----HGVKFREHQFTKIDTIAADESFTQMDL-GDRILKLNTEIREVGPVNKKGFYLAFQ 184
Cdd:cd10475  84 GVPGGTCRETFTLYYRQADEPdepaDKSEWHEGPWTKVDTIAADESFPASLGkGGQGLQMNVKERSFGPLTQRGFYLAFQ 163

                       170
                ....*....|....*..
gi 32967314 185 DVGACVALVSVRVYFKK 201
Cdd:cd10475 164 DSGACLSLVAVKVFFYK 180
EphR_LBD_B4 cd10474
Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the ...
 29-201 1.24e-57

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: 190.17  E-value: 1.24e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314  29 EVNLLDSKTIQGELGWISYP-SHG-WEEISGVDEHYTPIRTYQVCNV-MDHSQNNWLRTNWVPRNSAQKIYVELKFTLRD 105
Cdd:cd10474   1 EETLLNTKLETADLKWVTYPqVDGqWEELSGLDEEQHSVRTYEVCDAqRAGGQAHWLRTGWVPRRGAVHVYATLRFTMLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 106 CNSIPLVLGTCKETFNLYYMESDDD----HGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYL 181
Cdd:cd10474  81 CLSLPRAGRSCKETFTVFYYESDADtataHTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYL 160

                       170       180
                ....*....|....*....|
gi 32967314 182 AFQDVGACVALVSVRVYFKK 201
Cdd:cd10474 161 AFQDQGACMALLSLHLFYKK 180
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 437-528 2.04e-18

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: 80.23  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 437 PSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQE-TSYTILRARGTNVTISSLKPDTIYVFQIRARTAA 515
Cdd:cd00063   1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                        90
                ....*....|...
gi 32967314 516 GYGTNSRKFEFET 528
Cdd:cd00063  81 GESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
438-521 1.25e-15

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 72.06  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314   438 SPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTN-VTISSLKPDTIYVFQIRARTAAG 516
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQAVNGGG 80


                  ....*
gi 32967314   517 YGTNS 521
Cdd:pfam00041  81 EGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 437-518 3.55e-15

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: 70.72  E-value: 3.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    437 PSPVLTIKKDRTSRNSISLSWQEPEHPNGI--ILDYEVKYYEKQEQETSYTIlRARGTNVTISSLKPDTIYVFQIRARTA 514
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNV-TPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 32967314    515 AGYG 518
Cdd:smart00060  80 AGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
323-516 2.83e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 75.42  E-value: 2.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 323 TRPPSSPRNV-ISNINETSVILDWswplDTGGRKDVTfniickkcGWNIKQCEPCSPNVRFLPRqfgLTNTTVTVTDLLA 401
Cdd:COG3401 230 TTPPSAPTGLtATADTPGSVTLSW----DPVTESDAT--------GYRVYRSNSGDGPFTKVAT---VTTTSYTDTGLTN 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 402 HTNYTFEIDAVNGVSELSSPPrqfAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPehPNGIILDYEVkyYEKQEQE 481
Cdd:COG3401 295 GTTYYYRVTAVDAAGNESAPS---NVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS--SDADVTGYNV--YRSTSGG 367

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 32967314 482 TSYTIL--RARGTNVTISSLKPDTIYVFQIRARTAAG 516
Cdd:COG3401 368 GTYTKIaeTVTTTSYTDTGLTPGTTYYYKVTAVDAAG 404
fn3 pfam00041
Fibronectin type III domain;
327-417 2.79e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314   327 SSPRNV-ISNINETSVILDWSWPlDTGGRKDVTFNIICKKCGwnikqcEPCSPNVRFLPRqfglTNTTVTVTDLLAHTNY 405
Cdd:pfam00041   1 SAPSNLtVTDVTSTSLTVSWTPP-PDGNGPITGYEVEYRPKN------SGEPWNEITVPG----TTTSVTLTGLKPGTEY 69

                          90
                  ....*....|..
gi 32967314   406 TFEIDAVNGVSE 417
Cdd:pfam00041  70 EVRVQAVNGGGE 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 326-432 4.47e-09

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: 53.65  E-value: 4.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 326 PSSPRNV-ISNINETSVILDWSWPLDTGGRkDVTFNIICKKCGW-NIKQCEPCSPNvrflprqfgltNTTVTVTDLLAHT 403
Cdd:cd00063   1 PSPPTNLrVTDVTSTSVTLSWTPPEDDGGP-ITGYVVEYREKGSgDWKEVEVTPGS-----------ETSYTLTGLKPGT 68

                        90       100       110
                ....*....|....*....|....*....|.
gi 32967314 404 NYTFEIDAVN--GVSELSSPprqfaaVSITT 432
Cdd:cd00063  69 EYEFRVRAVNggGESPPSES------VTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 326-417 1.32e-08

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: 52.23  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314    326 PSSPRNV-ISNINETSVILDWSWPLDTGGRKDVTfniickkcGWNIKQCEPCSPNVRFLPRQfglTNTTVTVTDLLAHTN 404
Cdd:smart00060   1 PSPPSNLrVTDVTSTSVTLSWEPPPDDGITGYIV--------GYRVEYREEGSEWKEVNVTP---SSTSYTLTGLKPGTE 69

                           90
                   ....*....|...
gi 32967314    405 YTFEIDAVNGVSE 417
Cdd:smart00060  70 YEFRVRAVNGAGE 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
390-516 2.69e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.55  E-value: 2.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 390 TNTTVTVTDLLAHTNYTFEIDAVNGVSElSSPPRQFAAVSITTNQAAPSPVLTIkkdRTSRNSISLSWQEPEHPNgiILD 469
Cdd:COG3401 190 TTLVDGGGDIEPGTTYYYRVAATDTGGE-SAPSNEVSVTTPTTPPSAPTGLTAT---ADTPGSVTLSWDPVTESD--ATG 263

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 32967314 470 YEVkyYEKQEQETSYTIL-RARGTNVTISSLKPDTIYVFQIRARTAAG 516
Cdd:COG3401 264 YRV--YRSNSGDGPFTKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAAG 309
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 437-528 4.35e-07

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 48.17  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314   437 PSPV-LTIKKDRTSrnsISLSWQEPEHPNGIILDYEVKYYE-----KQEQETSYTILRARGTN--VTISSLKPDTIYVFQ 508
Cdd:pfam16656   1 PEQVhLSLTGDSTS---MTVSWVTPSAVTSPVVQYGTSSSAltstaTATSSTYTTGDGGTGYIhrATLTGLEPGTTYYYR 77

                          90       100
                  ....*....|....*....|
gi 32967314   509 IRARTaagyGTNSRKFEFET 528
Cdd:pfam16656  78 VGDDN----GGWSEVYSFTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
325-521 1.82e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 47.30  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 325 PPSSPRNV-ISNINETSVILDWSWPLDTggrkDVTfniickkcGWNIKQCEpcSPNVRFLPRQFGLTNTTVTVTDLLAHT 403
Cdd:COG3401 326 PPAAPSGLtATAVGSSSITLSWTASSDA----DVT--------GYNVYRST--SGGGTYTKIAETVTTTSYTDTGLTPGT 391

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 404 NYTFEIDAVNGVSELSSPPRQFAAVSITTNQAAPS--PVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQE 481
Cdd:COG3401 392 TYYYKVTAVDAAGNESAPSEEVSATTASAASGESLtaSVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFT 471

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 32967314 482 TSyTILRARGTNVTISSLKPDTIYVFQIRARTAAGYGTNS 521
Cdd:COG3401 472 TT-SSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVS 510
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 269-303 9.02e-05

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 40.02  E-value: 9.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 32967314   269 MCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMN 303
Cdd:pfam07699  10 PCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATS 44
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
377-516 1.88e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.55  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32967314 377 SPNVRFLPRQfglTNTTVTVTDLLAHtNYTFEIDAVNgVSELSSPPRQFAAVSITTNQAAPSPVLTIkkdRTSRN--SIS 454
Cdd:COG4733 575 DGNWVSVPRT---SGTSFEVPGIYAG-DYEVRVRAIN-ALGVSSAWAASSETTVTGKTAPPPAPTGL---TATGGlgGIT 646

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32967314 455 LSWQEPEHPNgiILDYEVKYYEKQEQETS-YTILRARGTNVTISSLKPDTIYVFQIRARTAAG 516
Cdd:COG4733 647 LSWSFPVDAD--TLRTEIRYSTTGDWASAtVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSG 707
 
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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