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Conserved domains on  [gi|119568905|gb|EAW48520|]
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EPH receptor A7, isoform CRA_c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
 30-206 6.50e-132

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: 383.61  E-value: 6.50e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  30 AKEVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 109
Cdd:cd10485    1 AKEVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 110 NSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDV 189
Cdd:cd10485   81 NSLPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDV 160

                        170
                 ....*....|....*..
gi 119568905 190 GACIALVSVKVYYKKCW 206
Cdd:cd10485  161 GACIALVSVKVYYKKCW 177
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-534 3.29e-19

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: 82.54  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 443 PSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRE-RTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAA 521
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                         90
                 ....*....|...
gi 119568905 522 GYGNYSPRLDVAT 534
Cdd:cd00063   81 GESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
314-539 4.57e-18

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 87.75  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 314 DGYYRAPSDPPYV-ACTRPPSAPQNLIF-NINQTTVSLEWSPPADNGGRNdvtYRILckRCSWEQGECVPCGSnigympq 391
Cdd:COG3401  214 TGGESAPSNEVSVtTPTTPPSAPTGLTAtADTPGSVTLSWDPVTESDATG---YRVY--RSNSGDGPFTKVAT------- 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 392 qtgLEDNYVTVMDLLAHANYTFEVEAVNG---VSDLSrsqrlfAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPeh 468
Cdd:COG3401  282 ---VTTTSYTDTGLTNGTTYYYRVTAVDAagnESAPS------NVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS-- 350

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119568905 469 PNGVITEYEIkyYEKDQRERTYSTVKT--KSTSASINNLKPGTVYVFQIRAFTAAgyGNYSPRLDVATLEEAT 539
Cdd:COG3401  351 SDADVTGYNV--YRSTSGGGTYTKIAEtvTTTSYTDTGLTPGTTYYYKVTAVDAA--GNESAPSEEVSATTAS 419
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 275-312 9.20e-06

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: 43.11  E-value: 9.20e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 119568905  275 TCEPCGRGFYKSSSQDLQCSRCPTHSFSDKEGS-SRCEC 312
Cdd:pfam07699  10 PCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGAtSISDC 48
 
Name Accession Description Interval E-value
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
 30-206 6.50e-132

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: 383.61  E-value: 6.50e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  30 AKEVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 109
Cdd:cd10485    1 AKEVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 110 NSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDV 189
Cdd:cd10485   81 NSLPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDV 160

                        170
                 ....*....|....*..
gi 119568905 190 GACIALVSVKVYYKKCW 206
Cdd:cd10485  161 GACIALVSVKVYYKKCW 177
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
32-204 8.14e-108

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 321.54  E-value: 8.14e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905    32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   112 LPGVLGTCKETFNLYYYETDYDTGRNI----RENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQ 187
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*..
gi 119568905   188 DVGACIALVSVKVYYKK 204
Cdd:smart00615 161 DQGACVALVSVRVFYKK 177
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 33-205 1.74e-95

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: 289.95  E-value: 1.74e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   33 VLLLDSKAQQTELEWISSPP-NGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYdGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  112 LPGVLGTCKETFNLYYYETDYDTG----RNIRENLYVKIDTIAADESFTQGDlGERKMKLNTEVREIGPLSKKGFYLAFQ 187
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAAtatpPAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 119568905  188 DVGACIALVSVKVYYKKC 205
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-534 3.29e-19

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: 82.54  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 443 PSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRE-RTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAA 521
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                         90
                 ....*....|...
gi 119568905 522 GYGNYSPRLDVAT 534
Cdd:cd00063   81 GESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
314-539 4.57e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 87.75  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 314 DGYYRAPSDPPYV-ACTRPPSAPQNLIF-NINQTTVSLEWSPPADNGGRNdvtYRILckRCSWEQGECVPCGSnigympq 391
Cdd:COG3401  214 TGGESAPSNEVSVtTPTTPPSAPTGLTAtADTPGSVTLSWDPVTESDATG---YRVY--RSNSGDGPFTKVAT------- 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 392 qtgLEDNYVTVMDLLAHANYTFEVEAVNG---VSDLSrsqrlfAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPeh 468
Cdd:COG3401  282 ---VTTTSYTDTGLTNGTTYYYRVTAVDAagnESAPS------NVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS-- 350

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119568905 469 PNGVITEYEIkyYEKDQRERTYSTVKT--KSTSASINNLKPGTVYVFQIRAFTAAgyGNYSPRLDVATLEEAT 539
Cdd:COG3401  351 SDADVTGYNV--YRSTSGGGTYTKIAEtvTTTSYTDTGLTPGTTYYYKVTAVDAA--GNESAPSEEVSATTAS 419
fn3 pfam00041
Fibronectin type III domain;
444-527 4.30e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.60  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  444 SQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKD--QRERTYSTVKTKsTSASINNLKPGTVYVFQIRAFTAA 521
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNGG 79


                  ....*.
gi 119568905  522 GYGNYS 527
Cdd:pfam00041  80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 443-524 9.40e-16

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: 72.65  E-value: 9.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   443 PSQVSGVMKERVLQRSVELSWQEPEHPNGV--ITEYEIKYYEKDQRERTYsTVKTKSTSASINNLKPGTVYVFQIRAFTA 520
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 119568905   521 AGYG 524
Cdd:smart00060  80 AGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
411-534 1.67e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.95  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 411 YTFEVEAVNGVSDLSRSQRlfaaVSITTGQAAPSQVSGVMKERVLQRSVELSWQepEHPNGVITEYEIkyYEKDQRERTY 490
Cdd:COG3401  205 YYYRVAATDTGGESAPSNE----VSVTTPTTPPSAPTGLTATADTPGSVTLSWD--PVTESDATGYRV--YRSNSGDGPF 276

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119568905 491 STV-KTKSTSASINNLKPGTVYVFQIRAFTAAgyGNYSPRLDVAT 534
Cdd:COG3401  277 TKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAA--GNESAPSNVVS 319
fn3 pfam00041
Fibronectin type III domain;
333-427 2.31e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  333 SAPQNLIF-NINQTTVSLEWSPPADNGGrNDVTYRIlckrcsweqgECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANY 411
Cdd:pfam00041   1 SAPSNLTVtDVTSTSLTVSWTPPPDGNG-PITGYEV----------EYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEY 69

                          90
                  ....*....|....*.
gi 119568905  412 TFEVEAVNGVSDLSRS 427
Cdd:pfam00041  70 EVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 332-438 2.46e-10

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: 57.51  E-value: 2.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 332 PSAPQNLIF-NINQTTVSLEWSPPADNGGRNDvTYRILCKRCSWEQGECVPcgsnigympqQTGLEDNYVTVMDLLAHAN 410
Cdd:cd00063    1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGPIT-GYVVEYREKGSGDWKEVE----------VTPGSETSYTLTGLKPGTE 69

                         90       100       110
                 ....*....|....*....|....*....|
gi 119568905 411 YTFEVEAVN--GVSDLSRSqrlfaaVSITT 438
Cdd:cd00063   70 YEFRVRAVNggGESPPSES------VTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 332-421 5.01e-10

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: 56.08  E-value: 5.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   332 PSAPQNLIF-NINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNigympqqtgleDNYVTVMDLLAHAN 410
Cdd:smart00060   1 PSPPSNLRVtDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPS-----------STSYTLTGLKPGTE 69

                           90
                   ....*....|.
gi 119568905   411 YTFEVEAVNGV 421
Cdd:smart00060  70 YEFRVRAVNGA 80
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 275-312 9.20e-06

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: 43.11  E-value: 9.20e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 119568905  275 TCEPCGRGFYKSSSQDLQCSRCPTHSFSDKEGS-SRCEC 312
Cdd:pfam07699  10 PCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGAtSISDC 48
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 265-322 3.20e-04

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 39.89  E-value: 3.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119568905 265 CKAGYQQK------GDT-CEPCGRGFYKSSSQDLQ----CSRCPTHSFSDKEGSSR-----CECEDGYYRAPSD 322
Cdd:cd00185    5 CPPGEYLSsdctatTDTvCSPCPPGTYSESWNSLSkclpCTTCGGGNQVEKTPCTAtdnrcCTCKPGFYCDEGT 78
 
Name Accession Description Interval E-value
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
 30-206 6.50e-132

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: 383.61  E-value: 6.50e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  30 AKEVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 109
Cdd:cd10485    1 AKEVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 110 NSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDV 189
Cdd:cd10485   81 NSLPGVLGTCKETFNLYYYETDYDTGRNIRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDV 160

                        170
                 ....*....|....*..
gi 119568905 190 GACIALVSVKVYYKKCW 206
Cdd:cd10485  161 GACIALVSVKVYYKKCW 177
EphR_LBD_A cd10473
Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the ...
 32-204 1.83e-123

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: 361.76  E-value: 1.83e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10473    1 EVVLLDSKTAQGELGWITYPPNGWEEISEMDEDYTPIRTYQVCNVMEPNQNNWLRTNWIYRGEAQRIYIELKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 191
Cdd:cd10473   81 FPGVLGTCKETFNLYYMESDLDLGRNIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEVREVGPLTKKGFYLAFQDVGA 160

                        170
                 ....*....|...
gi 119568905 192 CIALVSVKVYYKK 204
Cdd:cd10473  161 CVALVSVRVYYKK 173
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
 32-204 6.11e-112

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: 332.37  E-value: 6.11e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10487    1 EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIELQFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 191
Cdd:cd10487   81 IPGVAGTCKETFNLYYAESDADLGRRLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAFQDVGA 160

                        170
                 ....*....|...
gi 119568905 192 CIALVSVKVYYKK 204
Cdd:cd10487  161 CVALVSVRVYYKQ 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
32-204 8.14e-108

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 321.54  E-value: 8.14e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905    32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   112 LPGVLGTCKETFNLYYYETDYDTGRNI----RENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQ 187
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNTlpnwMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*..
gi 119568905   188 DVGACIALVSVKVYYKK 204
Cdd:smart00615 161 DQGACVALVSVRVFYKK 177
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
 32-204 1.77e-101

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: 305.44  E-value: 1.77e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10481    1 EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 191
Cdd:cd10481   81 IPLVLGTCKETFNLYYMESDEDQGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFYLAFQDVGA 160

                        170
                 ....*....|...
gi 119568905 192 CIALVSVKVYYKK 204
Cdd:cd10481  161 CVALVSVRVYFKK 173
EphR_LBD_A5 cd10483
Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the ...
 32-204 2.19e-99

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: 300.02  E-value: 2.19e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10483    1 EVNLLDSRSVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 191
Cdd:cd10483   81 LPGGLGTCKETFNVYYFESNDEDGRNIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAFQDLGA 160

                        170
                 ....*....|...
gi 119568905 192 CIALVSVKVYYKK 204
Cdd:cd10483  161 CIALVSVRVYYKK 173
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 33-205 1.74e-95

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: 289.95  E-value: 1.74e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   33 VLLLDSKAQQTELEWISSPP-NGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPYdGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  112 LPGVLGTCKETFNLYYYETDYDTG----RNIRENLYVKIDTIAADESFTQGDlGERKMKLNTEVREIGPLSKKGFYLAFQ 187
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAAtatpPAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 119568905  188 DVGACIALVSVKVYYKKC 205
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
EphR_LBD_A4 cd10482
Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the ...
 32-204 3.94e-94

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: 286.55  E-value: 3.94e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSP-PNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCN 110
Cdd:cd10482    1 EVTLLDSRSVQGELGWIASPlEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWIPREGAQRVYIEIKFTLRDCN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 111 SLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVG 190
Cdd:cd10482   81 SLPGVMGTCKETFNLYYYESNNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAFQDVG 160

                        170
                 ....*....|....
gi 119568905 191 ACIALVSVKVYYKK 204
Cdd:cd10482  161 ACIALVSVRVFYKK 174
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
 32-204 9.57e-94

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: 285.39  E-value: 9.57e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10486    1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 191
Cdd:cd10486   81 MPGVLGTCKETFNLYYYESDRDLGTSTWESQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGA 160

                        170
                 ....*....|...
gi 119568905 192 CIALVSVKVYYKK 204
Cdd:cd10486  161 CIAIVSVRVYYKK 173
EphR_LBD_A6 cd10484
Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the ...
 32-204 3.77e-92

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: 281.52  E-value: 3.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10484    1 QVVLLDTTMVLGELNWKTYPCNGWDAITEMDEYNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGA 191
Cdd:cd10484   81 IPWVVGTCKETFNLHYMESDEAHAVKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEVREVGPITRKGFYLAFQDIGA 160

                        170
                 ....*....|...
gi 119568905 192 CIALVSVKVYYKK 204
Cdd:cd10484  161 CIALVSVRVYYKK 173
EphR_LBD_B cd10472
Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the ...
 35-204 6.15e-88

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: 270.60  E-value: 6.15e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  35 LLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPG 114
Cdd:cd10472    3 LMDTRTATAELGWTAHPPSGWEEVSGYDENMNTIRTYQVCNVFESNQNNWLRTKFIRRRGAHRVYVEMKFTVRDCSSIPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 115 VLGTCKETFNLYYYETDYD----TGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVG 190
Cdd:cd10472   83 VPGSCKETFNLYYYESDSDiatkTSPFWMENPYVKVDTIAADESFSQVDLGGRVMKVNTEVRSFGPLSRNGFYLAFQDYG 162

                        170
                 ....*....|....
gi 119568905 191 ACIALVSVKVYYKK 204
Cdd:cd10472  163 ACMSLISVRVFYKK 176
EphR_LBD cd10319
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
 33-204 7.88e-81

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: 252.32  E-value: 7.88e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  33 VLLLDSKAQQTELEWISSPP--NGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCN 110
Cdd:cd10319    1 VVLLDTTLATSDLGWLTYPYghGGWDEESGLDPDGANIRTYVVCNVAMPNQDNWLRTPFIERRGAQRIYVELKFTVRDCE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 111 SLPGVLGTCKETFNLYYYETDYDTGR----NIRENLYVKIDTIAADESFTQGDlGERKMKLNTEVREIGPLSKKGFYLAF 186
Cdd:cd10319   81 SFPGNARSCKETFNLYYYESDHDTATkefpPWNEDPYTKIDTIAADESFKSSN-EDTTEKLNTETRSIGPLTKRGFYLAF 159

                        170
                 ....*....|....*...
gi 119568905 187 QDVGACIALVSVKVYYKK 204
Cdd:cd10319  160 QDQGACMSLLSVKVYYKK 177
EphR_LBD_B3 cd10478
Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the ...
 32-204 1.46e-80

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: 251.47  E-value: 1.46e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10478    1 EETLMDTKWVTSELAWTTHPESGWEEVSGYDEAMNPIRTYQVCNVRESNQNNWLRTGFIPRRDVQRVYVELKFTVRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGRN----IRENLYVKIDTIAADESFTQGDLGerkmKLNTEVREIGPLSKKGFYLAFQ 187
Cdd:cd10478   81 IPNIPGSCKETFNLFYYESDSDSASAsspfWMENPYVKVDTIAPDESFSRLDSG----RVNTKVRSFGPLSKAGFYLAFQ 156

                        170
                 ....*....|....*..
gi 119568905 188 DVGACIALVSVKVYYKK 204
Cdd:cd10478  157 DLGACMSLISVRAFFKK 173
EphR_LBD_B2 cd10477
Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the ...
 32-204 1.83e-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: 243.43  E-value: 1.83e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNS 111
Cdd:cd10477    2 EETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKYIRRRGAHRIHVEMKFSVRDCSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 112 LPGVLGTCKETFNLYYYETDYDTGR----NIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQ 187
Cdd:cd10477   82 IPSVPGSCKETFNLYYYESDFDSATktfpNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGFYLAFQ 161

                        170
                 ....*....|....*..
gi 119568905 188 DVGACIALVSVKVYYKK 204
Cdd:cd10477  162 DYGGCMSLIAVRVFYRK 178
EphR_LBD_B1 cd10476
Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the ...
 35-204 4.03e-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: 242.65  E-value: 4.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  35 LLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPG 114
Cdd:cd10476    3 LMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 115 VLGTCKETFNLYYYETDYDTGRNIR----ENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVG 190
Cdd:cd10476   83 VPGSCKETFNLYYYETDSVIATKKSafwtEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYG 162

                        170
                 ....*....|....
gi 119568905 191 ACIALVSVKVYYKK 204
Cdd:cd10476  163 ACMSLLSVRVFFKK 176
EphR_LBD_A2 cd10480
Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of ...
 32-205 3.84e-72

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: 229.35  E-value: 3.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSP-PNGWEEISGLdENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCN 110
Cdd:cd10480    1 EVVLLDFAAAGGELGWLTHPyGKGWDLMQNV-MNDSPIYMYSVCNVMSGEQDNWLRTNWIYRSEAERIFIELKFTVRDCN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 111 SLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVG 190
Cdd:cd10480   80 SFPGGAGSCKETFNLYYAESDVDYGTNFQKRQFRKIDTIAPDEITVSSDFETRNVKLNVEERSVGPLTRKGFYLAFQDIG 159

                        170
                 ....*....|....*
gi 119568905 191 ACIALVSVKVYYKKC 205
Cdd:cd10480  160 ACVALLSVRVYYKKC 174
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
 32-204 1.27e-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: 202.19  E-value: 1.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPP-NGWEEISGLdENYTPIRTYQVCQVMEP-NQNNWLRTNWISKGN-AQRIFVELKFTLRD 108
Cdd:cd10479    1 EVTLMDTSTAQGELGWLLDPPeVGWSEVQQM-LNGTPLYMYQDCPVQSEgDTDHWLRSNWIYRGEeASRIYVELQFTVRD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 109 CNSLPGVLG--TCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAF 186
Cdd:cd10479   80 CKSFPGGAGplGCKETFNLYYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRGLYLAF 159

                        170
                 ....*....|....*...
gi 119568905 187 QDVGACIALVSVKVYYKK 204
Cdd:cd10479  160 HNPGACVALVSVRVFYQR 177
EphR_LBD_B4 cd10474
Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the ...
 32-204 1.40e-60

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: 199.42  E-value: 1.40e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSP--PNGWEEISGLDENYTPIRTYQVCQVMEP-NQNNWLRTNWISKGNAQRIFVELKFTLRD 108
Cdd:cd10474    1 EETLLNTKLETADLKWVTYPqvDGQWEELSGLDEEQHSVRTYEVCDAQRAgGQAHWLRTGWVPRRGAVHVYATLRFTMLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 109 CNSLPGVLGTCKETFNLYYYETDYDTGRNIR----ENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYL 184
Cdd:cd10474   81 CLSLPRAGRSCKETFTVFYYESDADTATAHTpawmENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYL 160

                        170       180
                 ....*....|....*....|
gi 119568905 185 AFQDVGACIALVSVKVYYKK 204
Cdd:cd10474  161 AFQDQGACMALLSLHLFYKK 180
EphR_LBD_B6 cd10475
Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the ...
 32-204 4.61e-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: 195.53  E-value: 4.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  32 EVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQV--MEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 109
Cdd:cd10475    1 EEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEVCNVaaQGPGQDNWLRTHFIERRGAHRVHVRLHFSVRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 110 NSLPGVLGTCKETFNLYYYETDYDTGRNIR----ENLYVKIDTIAADESFTQGDLGERK-MKLNTEVREIGPLSKKGFYL 184
Cdd:cd10475   81 ASLGVPGGTCRETFTLYYRQADEPDEPADKsewhEGPWTKVDTIAADESFPASLGKGGQgLQMNVKERSFGPLTQRGFYL 160

                        170       180
                 ....*....|....*....|
gi 119568905 185 AFQDVGACIALVSVKVYYKK 204
Cdd:cd10475  161 AFQDSGACLSLVAVKVFFYK 180
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 443-534 3.29e-19

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: 82.54  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 443 PSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRE-RTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAA 521
Cdd:cd00063    1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                         90
                 ....*....|...
gi 119568905 522 GYGNYSPRLDVAT 534
Cdd:cd00063   81 GESPPSESVTVTT 93
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
314-539 4.57e-18

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 87.75  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 314 DGYYRAPSDPPYV-ACTRPPSAPQNLIF-NINQTTVSLEWSPPADNGGRNdvtYRILckRCSWEQGECVPCGSnigympq 391
Cdd:COG3401  214 TGGESAPSNEVSVtTPTTPPSAPTGLTAtADTPGSVTLSWDPVTESDATG---YRVY--RSNSGDGPFTKVAT------- 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 392 qtgLEDNYVTVMDLLAHANYTFEVEAVNG---VSDLSrsqrlfAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPeh 468
Cdd:COG3401  282 ---VTTTSYTDTGLTNGTTYYYRVTAVDAagnESAPS------NVVSVTTDLTPPAAPSGLTATAVGSSSITLSWTAS-- 350

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119568905 469 PNGVITEYEIkyYEKDQRERTYSTVKT--KSTSASINNLKPGTVYVFQIRAFTAAgyGNYSPRLDVATLEEAT 539
Cdd:COG3401  351 SDADVTGYNV--YRSTSGGGTYTKIAEtvTTTSYTDTGLTPGTTYYYKVTAVDAA--GNESAPSEEVSATTAS 419
fn3 pfam00041
Fibronectin type III domain;
444-527 4.30e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 73.60  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  444 SQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKD--QRERTYSTVKTKsTSASINNLKPGTVYVFQIRAFTAA 521
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNsgEPWNEITVPGTT-TSVTLTGLKPGTEYEVRVQAVNGG 79


                  ....*.
gi 119568905  522 GYGNYS 527
Cdd:pfam00041  80 GEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 443-524 9.40e-16

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: 72.65  E-value: 9.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   443 PSQVSGVMKERVLQRSVELSWQEPEHPNGV--ITEYEIKYYEKDQRERTYsTVKTKSTSASINNLKPGTVYVFQIRAFTA 520
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                   ....
gi 119568905   521 AGYG 524
Cdd:smart00060  80 AGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
411-534 1.67e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 66.95  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 411 YTFEVEAVNGVSDLSRSQRlfaaVSITTGQAAPSQVSGVMKERVLQRSVELSWQepEHPNGVITEYEIkyYEKDQRERTY 490
Cdd:COG3401  205 YYYRVAATDTGGESAPSNE----VSVTTPTTPPSAPTGLTATADTPGSVTLSWD--PVTESDATGYRV--YRSNSGDGPF 276

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119568905 491 STV-KTKSTSASINNLKPGTVYVFQIRAFTAAgyGNYSPRLDVAT 534
Cdd:COG3401  277 TKVaTVTTTSYTDTGLTNGTTYYYRVTAVDAA--GNESAPSNVVS 319
fn3 pfam00041
Fibronectin type III domain;
333-427 2.31e-10

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 57.04  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905  333 SAPQNLIF-NINQTTVSLEWSPPADNGGrNDVTYRIlckrcsweqgECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANY 411
Cdd:pfam00041   1 SAPSNLTVtDVTSTSLTVSWTPPPDGNG-PITGYEV----------EYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEY 69

                          90
                  ....*....|....*.
gi 119568905  412 TFEVEAVNGVSDLSRS 427
Cdd:pfam00041  70 EVRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 332-438 2.46e-10

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: 57.51  E-value: 2.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 332 PSAPQNLIF-NINQTTVSLEWSPPADNGGRNDvTYRILCKRCSWEQGECVPcgsnigympqQTGLEDNYVTVMDLLAHAN 410
Cdd:cd00063    1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGPIT-GYVVEYREKGSGDWKEVE----------VTPGSETSYTLTGLKPGTE 69

                         90       100       110
                 ....*....|....*....|....*....|
gi 119568905 411 YTFEVEAVN--GVSDLSRSqrlfaaVSITT 438
Cdd:cd00063   70 YEFRVRAVNggGESPPSES------VTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 332-421 5.01e-10

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: 56.08  E-value: 5.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905   332 PSAPQNLIF-NINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNigympqqtgleDNYVTVMDLLAHAN 410
Cdd:smart00060   1 PSPPSNLRVtDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPS-----------STSYTLTGLKPGTE 69

                           90
                   ....*....|.
gi 119568905   411 YTFEVEAVNGV 421
Cdd:smart00060  70 YEFRVRAVNGA 80
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 275-312 9.20e-06

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: 43.11  E-value: 9.20e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 119568905  275 TCEPCGRGFYKSSSQDLQCSRCPTHSFSDKEGS-SRCEC 312
Cdd:pfam07699  10 PCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGAtSISDC 48
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
340-528 3.66e-05

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 46.86  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 340 FNINQTTVSLEWSPPAdnggrNDVTYRIlckrcSWEQGecvpcGSNIGYMPQQTGLEdnyVTVMDLLAHaNYTFEVEAVN 419
Cdd:COG4733  547 QGTAVTTLTVSWDAPA-----GAVAYEV-----EWRRD-----DGNWVSVPRTSGTS---FEVPGIYAG-DYEVRVRAIN 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 420 gvsDLSRSQRLFAAVSITTGQ--AAPSQVSGVMKERVLqRSVELSWQEPEHPNgvITEYEIKYYEKDQRE-RTYSTVKTK 496
Cdd:COG4733  608 ---ALGVSSAWAASSETTVTGktAPPPAPTGLTATGGL-GGITLSWSFPVDAD--TLRTEIRYSTTGDWAsATVAQALYP 681

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119568905 497 STSASINNLKPGTVYVFQIRAFTAagYGNYSP 528
Cdd:COG4733  682 GNTYTLAGLKAGQTYYYRARAVDR--SGNVSA 711
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 456-517 3.82e-05

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: 42.78  E-value: 3.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568905  456 QRSVELSWQEPEHPNGVITEYEIKYYEKDQR----ERTYSTVKTKS---TSASINNLKPGTVYVFQIRA 517
Cdd:pfam16656  12 STSMTVSWVTPSAVTSPVVQYGTSSSALTSTatatSSTYTTGDGGTgyiHRATLTGLEPGTTYYYRVGD 80
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
442-522 5.96e-05

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 45.53  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 442 APSQVSGVMKERVLQRSVELSWQEPEHPNGViTEYEIkyYEKDQRERTYSTvktkSTSASINNLKPGTVYVFQIRAFTAA 521
Cdd:COG3979    2 APTAPTGLTASNVTSSSVSLSWDASTDNVGV-TGYDV--YRGGDQVATVTG----LTAWTVTGLTPGTEYTFTVGACDAA 74


                 .
gi 119568905 522 G 522
Cdd:COG3979   75 G 75
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 265-322 3.20e-04

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 39.89  E-value: 3.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119568905 265 CKAGYQQK------GDT-CEPCGRGFYKSSSQDLQ----CSRCPTHSFSDKEGSSR-----CECEDGYYRAPSD 322
Cdd:cd00185    5 CPPGEYLSsdctatTDTvCSPCPPGTYSESWNSLSkclpCTTCGGGNQVEKTPCTAtdnrcCTCKPGFYCDEGT 78
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 396-523 1.28e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 41.88  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 396 EDNYVTVMDLLAHaNYTF-EVEAVNG-VSDLSRSQRLFAAVSITTGQAAPSQVSGVMKerVLQRSVELSWQEPEHPNGV- 472
Cdd:COG4932  202 ADGKYTFTDLPPG-TYTLtETKAPEGyVLDTKDPTGATITVTVNAGGTVTVTLKNTPK--YTKGSVTVTKTDADTGEPLa 278

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119568905 473 ITEYEIKYYEKDQRERTYSTVKTKSTSASINNLKPGTVYVFQIRAftAAGY 523
Cdd:COG4932  279 GATFTLTDADGNTVVTTTVTVTDADGSYTFTDLPPGTYTVTETKA--PAGY 327
TNFRSF5_teleost cd13422
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5) in teleosts; also known as CD40; ...
 263-317 1.62e-03

Tumor necrosis factor receptor superfamily member 5 (TNFRSF5) in teleosts; also known as CD40; TNFRSF5 (commonly known as CD40 and also as CDW40, p50, Bp50) is widely expressed in diverse cell types including B lymphocytes, dendritic cells, platelets, monocytes, endothelial cells, and fibroblasts. It is essential in mediating a wide variety of immune and inflammatory responses, including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. Its natural immunomodulating ligand is CD40L, and a primary defect in the CD40/CD40L system is associated with X-linked hyper-IgM (XHIM) syndrome. It is also involved in tumorigenesis; CD40 expression is significantly higher in gastric carcinomas and it is associated with the lymphatic metastasis of cancer cells and their tumor node metastasis (TNM) classification. Upregulated levels of CD40/CD40L on B cells and T cells may play an important role in the immune pathogenesis of breast cancer. Consequently, the CD40/CD40L system serves as a link between tumorigenesis, atherosclerosis, and the immune system, and offers a potential target for drug therapy for related diseases, such as cancer, atherosclerosis, diabetes mellitus, and immunological rejection. Salmon CD40 and CD40L are widely expressed, particularly in immune tissues, and their importance for the immune response is indicated by their relatively high expression in salmon lymphoid organs and gills.


Pssm-ID: 276927 [Multi-domain]  Cd Length: 161  Bit Score: 39.72  E-value: 1.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 263 CICKAGYQQKGDTCE------PCGRGFYKSS----SQDLQCSRCPTHSFS-DKEGSSRC----ECEDGYY 317
Cdd:cd13422   78 CKCKPGFHCSSEECLtcvphtTCGPGQGVKSkgnhIRDTVCEECPDGTFSnNSSAEGVCkkwtECESGYK 147
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
316-526 2.02e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.14  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 316 YYR-----------APSDPPYV-ACTRPPSAPQNLIF-NINQTTVSLEWSPPADNggrnDVT-YRIlcKRCSWEQGECvp 381
Cdd:COG3401  299 YYRvtavdaagnesAPSNVVSVtTDLTPPAAPSGLTAtAVGSSSITLSWTASSDA----DVTgYNV--YRSTSGGGTY-- 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568905 382 cgSNIGympqqTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVEL 461
Cdd:COG3401  371 --TKIA-----ETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATA 443

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119568905 462 SWQEPEHPNGVITEYEIKYYE---KDQRERTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAAGYGNY 526
Cdd:COG3401  444 AASAASNPGVSAAVLADGGDTgnaVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV 511
 
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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