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Conserved domains on  [gi|568928965|ref|XP_006503091|]
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ephrin type-A receptor 10 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EphR_LBD super family cl02704
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
 35-210 2.45e-126

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


The actual alignment was detected with superfamily member cd10487:

Pssm-ID: 470656  Cd Length: 173  Bit Score: 369.35  E-value: 2.45e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10487    1 EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIELQFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGRgrpRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQD 194
Cdd:cd10487   81 IPGVAGTCKETFNLYYAESDADLGR---RLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAFQD 157

                        170
                 ....*....|....*.
gi 568928965 195 VGACVALVSVRVYYKQ 210
Cdd:cd10487  158 VGACVALVSVRVYYKQ 173
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 465-551 1.23e-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: 58.28  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 465 VEPQSVSLSWREPVPAGAPGTNsteYEIRYYEKGQSE-QTYSTVKTGAPAVTVTNLKPATRYVFQIRAASPGplwEAQSF 543
Cdd:cd00063   12 VTSTSVTLSWTPPEDDGGPITG---YVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG---GESPP 85


                 ....*...
gi 568928965 544 SPSIEVQT 551
Cdd:cd00063   86 SESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
339-431 5.97e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.71  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  339 SAPRDLQYSlSRSPLALRLRWLPPADSGGrSDVTYSLLCLRCGRDGPagacqpcgPRVAFVPRQaglrERAATLLHLRPG 418
Cdd:pfam00041   1 SAPSNLTVT-DVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEP--------WNEITVPGT----TTSVTLTGLKPG 66

                          90
                  ....*....|...
gi 568928965  419 ARYTVRVAALNGV 431
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
 
Name Accession Description Interval E-value
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
 35-210 2.45e-126

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: 369.35  E-value: 2.45e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10487    1 EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIELQFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGRgrpRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQD 194
Cdd:cd10487   81 IPGVAGTCKETFNLYYAESDADLGR---RLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAFQD 157

                        170
                 ....*....|....*.
gi 568928965 195 VGACVALVSVRVYYKQ 210
Cdd:cd10487  158 VGACVALVSVRVYYKQ 173
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
35-209 1.58e-94

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 287.64  E-value: 1.58e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965    35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   115 IPGATGTCKETFNAYYLETETDLGRG-RPRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNtLPNWMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*.
gi 568928965   194 DVGACVALVSVRVYYK 209
Cdd:smart00615 161 DQGACVALVSVRVFYK 176
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 36-211 1.07e-87

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: 269.92  E-value: 1.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   36 VILLDSKASQAELGWTALP-STGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPyDGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  115 IPGATGTCKETFNAYYLETETDLG-RGRPRLGGNRPRKIDTIAADESFTQGDlGERKMKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAAtATPPAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 568928965  194 DVGACVALVSVRVYYKQC 211
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 465-551 1.23e-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: 58.28  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 465 VEPQSVSLSWREPVPAGAPGTNsteYEIRYYEKGQSE-QTYSTVKTGAPAVTVTNLKPATRYVFQIRAASPGplwEAQSF 543
Cdd:cd00063   12 VTSTSVTLSWTPPEDDGGPITG---YVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG---GESPP 85


                 ....*...
gi 568928965 544 SPSIEVQT 551
Cdd:cd00063   86 SESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 451-531 1.37e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.93  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   451 PGAPWEedeIRRDRVEPQSVSLSWREPVPAGaPGTNSTEYEIRYYEKGQSEQTYsTVKTGAPAVTVTNLKPATRYVFQIR 530
Cdd:smart00060   1 PSPPSN---LRVTDVTSTSVTLSWEPPPDDG-ITGYIVGYRVEYREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVR 75


                   .
gi 568928965   531 A 531
Cdd:smart00060  76 A 76
fn3 pfam00041
Fibronectin type III domain;
469-533 3.35e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 3.35e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568928965  469 SVSLSWREPVPAGAPGTNsteYEIRYYEKG-QSEQTYSTVKTGAPAVTVTNLKPATRYVFQIRAAS 533
Cdd:pfam00041  15 SLTVSWTPPPDGNGPITG---YEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
415-584 1.76e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 54.24  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 415 LRPGARYTVRVAALNG---VSGPAAAagatyaqVTVSTGPGAPWEEDEIRRDRVEPQSVSLSWrepvpAGAPGTNSTEYE 491
Cdd:COG3401  292 LTNGTTYYYRVTAVDAagnESAPSNV-------VSVTTDLTPPAAPSGLTATAVGSSSITLSW-----TASSDADVTGYN 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 492 IryYEKGQSEQTYSTVKTGAPAV--TVTNLKPATRYVFQIRAASPGPLWEAQSFSPSIEVQTPGEGTPNTcaswcAPPWR 569
Cdd:COG3401  360 V--YRSTSGGGTYTKIAETVTTTsyTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLT-----ASVDA 432

                        170
                 ....*....|....*
gi 568928965 570 MPSLIKIASLWTLLD 584
Cdd:COG3401  433 VPLTDVAGATAAASA 447
fn3 pfam00041
Fibronectin type III domain;
339-431 5.97e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.71  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  339 SAPRDLQYSlSRSPLALRLRWLPPADSGGrSDVTYSLLCLRCGRDGPagacqpcgPRVAFVPRQaglrERAATLLHLRPG 418
Cdd:pfam00041   1 SAPSNLTVT-DVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEP--------WNEITVPGT----TTSVTLTGLKPG 66

                          90
                  ....*....|...
gi 568928965  419 ARYTVRVAALNGV 431
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 338-431 2.10e-05

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: 42.99  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   338 PSAPRDLQYSlSRSPLALRLRWLPPADSGGRSDVTYsllCLRCGRDGpagacqpcGPRVAFVPRQAglRERAATLLHLRP 417
Cdd:smart00060   1 PSPPSNLRVT-DVTSTSVTLSWEPPPDDGITGYIVG---YRVEYREE--------GSEWKEVNVTP--SSTSYTLTGLKP 66

                           90
                   ....*....|....
gi 568928965   418 GARYTVRVAALNGV 431
Cdd:smart00060  67 GTEYEFRVRAVNGA 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 338-430 2.54e-05

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: 43.25  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 338 PSAPRDLQYSlSRSPLALRLRWLPPADSGGRSDvTYSLLClrcgRDGPAGACQPCGPRVAfvprqaglRERAATLLHLRP 417
Cdd:cd00063    1 PSPPTNLRVT-DVTSTSVTLSWTPPEDDGGPIT-GYVVEY----REKGSGDWKEVEVTPG--------SETSYTLTGLKP 66

                         90
                 ....*....|...
gi 568928965 418 GARYTVRVAALNG 430
Cdd:cd00063   67 GTEYEFRVRAVNG 79
 
Name Accession Description Interval E-value
EphR_LBD_A10 cd10487
Ligand Binding Domain of Ephrin type-A Receptor 10; Ephrin receptors (EphRs) comprise the ...
 35-210 2.45e-126

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: 369.35  E-value: 2.45e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10487    1 EVVLLDSKESQAELGWTSLPSNGWEEISGVDEHYKPIRTYQVCNVMEPNQNNWLQTGWISRGRGQRIFIELQFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGRgrpRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQD 194
Cdd:cd10487   81 IPGVAGTCKETFNLYYAESDADLGR---RLRESRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGHLSRRGFHLAFQD 157

                        170
                 ....*....|....*.
gi 568928965 195 VGACVALVSVRVYYKQ 210
Cdd:cd10487  158 VGACVALVSVRVYYKQ 173
EphR_LBD_A cd10473
Ligand Binding Domain of Ephrin type-A Receptors; Ephrin receptors (EphRs) comprise the ...
 35-210 1.18e-106

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: 319.00  E-value: 1.18e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10473    1 EVVLLDSKTAQGELGWITYPPNGWEEISEMDEDYTPIRTYQVCNVMEPNQNNWLRTNWIYRGEAQRIYIELKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGRgrpRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQD 194
Cdd:cd10473   81 FPGVLGTCKETFNLYYMESDLDLGR---NIRENQFTKIDTIAADESFTQGDLGDRIMKLNTEVREVGPLTKKGFYLAFQD 157

                        170
                 ....*....|....*.
gi 568928965 195 VGACVALVSVRVYYKQ 210
Cdd:cd10473  158 VGACVALVSVRVYYKK 173
EphR_LBD_A7 cd10485
Ligand Binding Domain of Ephrin type-A Receptor 7; Ephrin receptors (EphRs) comprise the ...
 33-211 1.43e-98

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: 298.10  E-value: 1.43e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  33 AEEVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDC 112
Cdd:cd10485    1 AKEVILLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 113 SSIPGATGTCKETFNAYYLETETDLGRGrprLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAF 192
Cdd:cd10485   81 NSLPGVLGTCKETFNLYYYETDYDTGRN---IRENQYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAF 157

                        170
                 ....*....|....*....
gi 568928965 193 QDVGACVALVSVRVYYKQC 211
Cdd:cd10485  158 QDVGACIALVSVKVYYKKC 176
EPH_lbd smart00615
Ephrin receptor ligand binding domain;
35-209 1.58e-94

Ephrin receptor ligand binding domain;


Pssm-ID: 128877  Cd Length: 177  Bit Score: 287.64  E-value: 1.58e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965    35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:smart00615   1 EVVLLDTKTETGELGWTTYPPEGWEEVSGMDENGTPIRTYQVCNVQEGNQNNWLRTNFIRRRGAQRIYVELKFTVRDCSS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   115 IPGATGTCKETFNAYYLETETDLGRG-RPRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:smart00615  81 LPGVGGSCKETFNLYYYESDTDTATNtLPNWMENPYTKVDTIAADESFTGGDVGKRNVKLNTEVRSLGPLSKKGFYLAFQ 160

                          170
                   ....*....|....*.
gi 568928965   194 DVGACVALVSVRVYYK 209
Cdd:smart00615 161 DQGACVALVSVRVFYK 176
EphR_LBD_A3 cd10481
Ligand Binding Domain of Ephrin type-A Receptor 3; Ephrin receptors (EphRs) comprise the ...
 35-210 3.12e-89

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: 273.85  E-value: 3.12e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10481    1 EVNLLDSKAIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWIPRNSAQKIYVELKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDlgrgrprlGGNRPR-----KIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFH 189
Cdd:cd10481   81 IPLVLGTCKETFNLYYMESDED--------QGVKFRehqftKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSKKGFY 152

                        170       180
                 ....*....|....*....|.
gi 568928965 190 LAFQDVGACVALVSVRVYYKQ 210
Cdd:cd10481  153 LAFQDVGACVALVSVRVYFKK 173
Ephrin_lbd pfam01404
Ephrin receptor ligand binding domain; The Eph receptors, which bind to ephrins pfam00812 are ...
 36-211 1.07e-87

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: 269.92  E-value: 1.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   36 VILLDSKASQAELGWTALP-STGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:pfam01404   1 EVLLDTTSATSDLGWTTYPyDGGWEEVSGLDENGRTIRTYQVCNVEEPNQNNWLRTPFIPRGGASRVYVELKFTVRDCSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  115 IPGATGTCKETFNAYYLETETDLG-RGRPRLGGNRPRKIDTIAADESFTQGDlGERKMKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:pfam01404  81 IPGVSGTCKETFNLYYYESDADAAtATPPAWRENPYKKIDTIAADESFTDTG-KGRVMKLNTETRSIGPLSKRGFYLAFQ 159

                         170
                  ....*....|....*...
gi 568928965  194 DVGACVALVSVRVYYKQC 211
Cdd:pfam01404 160 DQGACIALLSVRVFYKKC 177
EphR_LBD_A6 cd10484
Ligand Binding Domain of Ephrin type-A Receptor 6; Ephrin receptors (EphRs) comprise the ...
 35-210 3.81e-84

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: 260.72  E-value: 3.81e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10484    1 QVVLLDTTMVLGELNWKTYPCNGWDAITEMDEYNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGrgrPRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQD 194
Cdd:cd10484   81 IPWVVGTCKETFNLHYMESDEAHA---VKFKPNQYSKIDTIAADESFTQMDLGDRILKLNTEVREVGPITRKGFYLAFQD 157

                        170
                 ....*....|....*.
gi 568928965 195 VGACVALVSVRVYYKQ 210
Cdd:cd10484  158 IGACIALVSVRVYYKK 173
EphR_LBD_A5 cd10483
Ligand Binding Domain of Ephrin type-A Receptor 5; Ephrin receptors (EphRs) comprise the ...
 35-210 1.05e-82

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: 257.26  E-value: 1.05e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10483    1 EVNLLDSRSVMGDLGWIAYPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGRgrpRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQD 194
Cdd:cd10483   81 LPGGLGTCKETFNVYYFESNDEDGR---NIRENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLTKKGFYLAFQD 157

                        170
                 ....*....|....*.
gi 568928965 195 VGACVALVSVRVYYKQ 210
Cdd:cd10483  158 LGACIALVSVRVYYKK 173
EphR_LBD_A4 cd10482
Ligand Binding Domain of Ephrin type-A Receptor 4; Ephrin receptors (EphRs) comprise the ...
 35-210 4.51e-82

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: 255.35  E-value: 4.51e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTG-WEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCS 113
Cdd:cd10482    1 EVTLLDSRSVQGELGWIASPLEGgWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWIPREGAQRVYIEIKFTLRDCN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 114 SIPGATGTCKETFNAYYLETETDLGRgrpRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:cd10482   81 SLPGVMGTCKETFNLYYYESNNDKER---FIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEVRDVGPLSKKGFYLAFQ 157

                        170
                 ....*....|....*..
gi 568928965 194 DVGACVALVSVRVYYKQ 210
Cdd:cd10482  158 DVGACIALVSVRVFYKK 174
EphR_LBD_B cd10472
Ligand Binding Domain of Ephrin type-B receptors; Ephrin receptors (EphRs) comprise the ...
 37-210 1.36e-81

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


Pssm-ID: 198440  Cd Length: 176  Bit Score: 254.42  E-value: 1.36e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  37 ILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSSIP 116
Cdd:cd10472    2 TLMDTRTATAELGWTAHPPSGWEEVSGYDENMNTIRTYQVCNVFESNQNNWLRTKFIRRRGAHRVYVEMKFTVRDCSSIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 117 GATGTCKETFNAYYLETETDLGRGR-PRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQDV 195
Cdd:cd10472   82 NVPGSCKETFNLYYYESDSDIATKTsPFWMENPYVKVDTIAADESFSQVDLGGRVMKVNTEVRSFGPLSRNGFYLAFQDY 161

                        170
                 ....*....|....*
gi 568928965 196 GACVALVSVRVYYKQ 210
Cdd:cd10472  162 GACMSLISVRVFYKK 176
EphR_LBD_A8 cd10486
Ligand Binding Domain of Ephrin type-A Receptor 8; Ephrin receptors (EphRs) comprise the ...
 35-210 1.66e-80

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: 251.49  E-value: 1.66e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10486    1 EVNLLDTSTISGDWGWLTYPSHGWDSINEMDEYFSPIHTYQVCNVMSPNQNNWLRTNWVQRDGARRVYAEIKFTLRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGRGRPRlggNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQD 194
Cdd:cd10486   81 MPGVLGTCKETFNLYYYESDRDLGTSTWE---SQFLKIDTIAADESFTNVDLGVRRLKLNTEVRGVGPLSKRGFYLAFQD 157

                        170
                 ....*....|....*.
gi 568928965 195 VGACVALVSVRVYYKQ 210
Cdd:cd10486  158 IGACIAIVSVRVYYKK 173
EphR_LBD_B1 cd10476
Ligand Binding Domain of Ephrin type-B Receptor 1; Ephrin receptors (EphRs) comprise the ...
 38-210 2.41e-76

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


Pssm-ID: 198444  Cd Length: 176  Bit Score: 240.73  E-value: 2.41e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  38 LLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSSIPG 117
Cdd:cd10476    3 LMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 118 ATGTCKETFNAYYLETETDLGRGRPRLGGNRPR-KIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQDVG 196
Cdd:cd10476   83 VPGSCKETFNLYYYETDSVIATKKSAFWTEAPYlKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYG 162

                        170
                 ....*....|....
gi 568928965 197 ACVALVSVRVYYKQ 210
Cdd:cd10476  163 ACMSLLSVRVFFKK 176
EphR_LBD cd10319
Ligand Binding Domain of Ephrin Receptors; Ephrin receptors (EphRs) comprise the largest ...
 36-209 1.41e-74

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: 1.41e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  36 VILLDSKASQAELGWTALP--STGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCS 113
Cdd:cd10319    1 VVLLDTTLATSDLGWLTYPygHGGWDEESGLDPDGANIRTYVVCNVAMPNQDNWLRTPFIERRGAQRIYVELKFTVRDCE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 114 SIPGATGTCKETFNAYYLETETDLG-RGRPRLGGNRPRKIDTIAADESFTQGDlGERKMKLNTEVREIGPLSRQGFHLAF 192
Cdd:cd10319   81 SFPGNARSCKETFNLYYYESDHDTAtKEFPPWNEDPYTKIDTIAADESFKSSN-EDTTEKLNTETRSIGPLTKRGFYLAF 159

                        170
                 ....*....|....*..
gi 568928965 193 QDVGACVALVSVRVYYK 209
Cdd:cd10319  160 QDQGACMSLLSVKVYYK 176
EphR_LBD_B3 cd10478
Ligand Binding Domain of Ephrin type-B Receptor 3; Ephrin receptors (EphRs) comprise the ...
 35-210 1.06e-73

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: 233.75  E-value: 1.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10478    1 EETLMDTKWVTSELAWTTHPESGWEEVSGYDEAMNPIRTYQVCNVRESNQNNWLRTGFIPRRDVQRVYVELKFTVRDCNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLGRG-RPRLGGNRPRKIDTIAADESFTQGDLGerkmKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:cd10478   81 IPNIPGSCKETFNLFYYESDSDSASAsSPFWMENPYVKVDTIAPDESFSRLDSG----RVNTKVRSFGPLSKAGFYLAFQ 156

                        170
                 ....*....|....*..
gi 568928965 194 DVGACVALVSVRVYYKQ 210
Cdd:cd10478  157 DLGACMSLISVRAFFKK 173
EphR_LBD_B2 cd10477
Ligand Binding Domain of Ephrin type-B Receptor 2; Ephrin receptors (EphRs) comprise the ...
 35-210 3.16e-72

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: 229.95  E-value: 3.16e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCSS 114
Cdd:cd10477    2 EETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKYIRRRGAHRIHVEMKFSVRDCSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 115 IPGATGTCKETFNAYYLETETDLG-RGRPRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:cd10477   82 IPSVPGSCKETFNLYYYESDFDSAtKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRNGFYLAFQ 161

                        170
                 ....*....|....*..
gi 568928965 194 DVGACVALVSVRVYYKQ 210
Cdd:cd10477  162 DYGGCMSLIAVRVFYRK 178
EphR_LBD_A2 cd10480
Ligand Binding Domain of Ephrin type-A Receptor 2; EphRs comprise the largest subfamily of ...
 35-211 6.76e-69

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: 221.26  E-value: 6.76e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALP-STGWEEISGVdEHDRPIRTYQVCNVLEPNQDNWLQTGWISRGRGQRIFVELQFTLRDCS 113
Cdd:cd10480    1 EVVLLDFAAAGGELGWLTHPyGKGWDLMQNV-MNDSPIYMYSVCNVMSGEQDNWLRTNWIYRSEAERIFIELKFTVRDCN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 114 SIPGATGTCKETFNAYYLETETDLGRGRPRlggNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHLAFQ 193
Cdd:cd10480   80 SFPGGAGSCKETFNLYYAESDVDYGTNFQK---RQFRKIDTIAPDEITVSSDFETRNVKLNVEERSVGPLTRKGFYLAFQ 156

                        170
                 ....*....|....*...
gi 568928965 194 DVGACVALVSVRVYYKQC 211
Cdd:cd10480  157 DIGACVALLSVRVYYKKC 174
EphR_LBD_A1 cd10479
Ligand Binding Domain of Ephrin type-A Receptor 1; Ephrin receptors (EphRs) comprise the ...
 35-210 4.03e-55

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: 184.85  E-value: 4.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTA-LPSTGWEEISGVdEHDRPIRTYQVCNVLEP-NQDNWLQTGWISRGR-GQRIFVELQFTLRD 111
Cdd:cd10479    1 EVTLMDTSTAQGELGWLLdPPEVGWSEVQQM-LNGTPLYMYQDCPVQSEgDTDHWLRSNWIYRGEeASRIYVELQFTVRD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 112 CSSIPGATG--TCKETFNAYYLETETDLGrgrprLGGNRP--RKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQG 187
Cdd:cd10479   80 CKSFPGGAGplGCKETFNLYYMESDQDVG-----IQLRRPlfQKVTTVAADQSFTIRDLASGSVKLNVERCSLGKLTRRG 154

                        170       180
                 ....*....|....*....|...
gi 568928965 188 FHLAFQDVGACVALVSVRVYYKQ 210
Cdd:cd10479  155 LYLAFHNPGACVALVSVRVFYQR 177
EphR_LBD_B6 cd10475
Ligand Binding Domain of Ephrin type-B Receptor 6; Ephrin receptors (EphRs) comprise the ...
 35-208 6.72e-53

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: 178.97  E-value: 6.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTGWEEISGVDEHDRPIRTYQVCNV--LEPNQDNWLQTGWISRGRGQRIFVELQFTLRDC 112
Cdd:cd10475    1 EEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEVCNVaaQGPGQDNWLRTHFIERRGAHRVHVRLHFSVRDC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 113 SSIPGATGTCKETFNAYYLET-ETDLGRGRPRLGGNRPRKIDTIAADESFTQGDLGERK-MKLNTEVREIGPLSRQGFHL 190
Cdd:cd10475   81 ASLGVPGGTCRETFTLYYRQAdEPDEPADKSEWHEGPWTKVDTIAADESFPASLGKGGQgLQMNVKERSFGPLTQRGFYL 160

                        170
                 ....*....|....*...
gi 568928965 191 AFQDVGACVALVSVRVYY 208
Cdd:cd10475  161 AFQDSGACLSLVAVKVFF 178
EphR_LBD_B4 cd10474
Ligand Binding Domain of Ephrin type-B Receptor 4; Ephrin receptors (EphRs) comprise the ...
 35-210 1.72e-52

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: 177.85  E-value: 1.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  35 EVILLDSKASQAELGWTALPSTG--WEEISGVDEHDRPIRTYQVCNV-LEPNQDNWLQTGWISRGRGQRIFVELQFTLRD 111
Cdd:cd10474    1 EETLLNTKLETADLKWVTYPQVDgqWEELSGLDEEQHSVRTYEVCDAqRAGGQAHWLRTGWVPRRGAVHVYATLRFTMLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 112 CSSIPGATGTCKETFNAYYLETETDLGRGR-PRLGGNRPRKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSRQGFHL 190
Cdd:cd10474   81 CLSLPRAGRSCKETFTVFYYESDADTATAHtPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYL 160

                        170       180
                 ....*....|....*....|
gi 568928965 191 AFQDVGACVALVSVRVYYKQ 210
Cdd:cd10474  161 AFQDQGACMALLSLHLFYKK 180
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 465-551 1.23e-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: 58.28  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 465 VEPQSVSLSWREPVPAGAPGTNsteYEIRYYEKGQSE-QTYSTVKTGAPAVTVTNLKPATRYVFQIRAASPGplwEAQSF 543
Cdd:cd00063   12 VTSTSVTLSWTPPEDDGGPITG---YVVEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG---GESPP 85


                 ....*...
gi 568928965 544 SPSIEVQT 551
Cdd:cd00063   86 SESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 451-531 1.37e-09

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.93  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   451 PGAPWEedeIRRDRVEPQSVSLSWREPVPAGaPGTNSTEYEIRYYEKGQSEQTYsTVKTGAPAVTVTNLKPATRYVFQIR 530
Cdd:smart00060   1 PSPPSN---LRVTDVTSTSVTLSWEPPPDDG-ITGYIVGYRVEYREEGSEWKEV-NVTPSSTSYTLTGLKPGTEYEFRVR 75


                   .
gi 568928965   531 A 531
Cdd:smart00060  76 A 76
fn3 pfam00041
Fibronectin type III domain;
469-533 3.35e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.96  E-value: 3.35e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568928965  469 SVSLSWREPVPAGAPGTNsteYEIRYYEKG-QSEQTYSTVKTGAPAVTVTNLKPATRYVFQIRAAS 533
Cdd:pfam00041  15 SLTVSWTPPPDGNGPITG---YEVEYRPKNsGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
415-584 1.76e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 54.24  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 415 LRPGARYTVRVAALNG---VSGPAAAagatyaqVTVSTGPGAPWEEDEIRRDRVEPQSVSLSWrepvpAGAPGTNSTEYE 491
Cdd:COG3401  292 LTNGTTYYYRVTAVDAagnESAPSNV-------VSVTTDLTPPAAPSGLTATAVGSSSITLSW-----TASSDADVTGYN 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 492 IryYEKGQSEQTYSTVKTGAPAV--TVTNLKPATRYVFQIRAASPGPLWEAQSFSPSIEVQTPGEGTPNTcaswcAPPWR 569
Cdd:COG3401  360 V--YRSTSGGGTYTKIAETVTTTsyTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLT-----ASVDA 432

                        170
                 ....*....|....*
gi 568928965 570 MPSLIKIASLWTLLD 584
Cdd:COG3401  433 VPLTDVAGATAAASA 447
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
417-531 1.75e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.16  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 417 PGARYTVRVAALNgvSGPAAAAGATYAQVTVSTGPGAPweeDEIRRDRVEPQSVSLSWREpvpagAPGTNSTEYEIryYE 496
Cdd:COG3401  201 PGTTYYYRVAATD--TGGESAPSNEVSVTTPTTPPSAP---TGLTATADTPGSVTLSWDP-----VTESDATGYRV--YR 268

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568928965 497 KGQSEQTYSTVKTGAPAV-TVTNLKPATRYVFQIRA 531
Cdd:COG3401  269 SNSGDGPFTKVATVTTTSyTDTGLTNGTTYYYRVTA 304
fn3 pfam00041
Fibronectin type III domain;
339-431 5.97e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.71  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965  339 SAPRDLQYSlSRSPLALRLRWLPPADSGGrSDVTYSLLCLRCGRDGPagacqpcgPRVAFVPRQaglrERAATLLHLRPG 418
Cdd:pfam00041   1 SAPSNLTVT-DVTSTSLTVSWTPPPDGNG-PITGYEVEYRPKNSGEP--------WNEITVPGT----TTSVTLTGLKPG 66

                          90
                  ....*....|...
gi 568928965  419 ARYTVRVAALNGV 431
Cdd:pfam00041  67 TEYEVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 338-431 2.10e-05

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: 42.99  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965   338 PSAPRDLQYSlSRSPLALRLRWLPPADSGGRSDVTYsllCLRCGRDGpagacqpcGPRVAFVPRQAglRERAATLLHLRP 417
Cdd:smart00060   1 PSPPSNLRVT-DVTSTSVTLSWEPPPDDGITGYIVG---YRVEYREE--------GSEWKEVNVTP--SSTSYTLTGLKP 66

                           90
                   ....*....|....
gi 568928965   418 GARYTVRVAALNGV 431
Cdd:smart00060  67 GTEYEFRVRAVNGA 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 338-430 2.54e-05

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: 43.25  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 338 PSAPRDLQYSlSRSPLALRLRWLPPADSGGRSDvTYSLLClrcgRDGPAGACQPCGPRVAfvprqaglRERAATLLHLRP 417
Cdd:cd00063    1 PSPPTNLRVT-DVTSTSVTLSWTPPEDDGGPIT-GYVVEY----REKGSGDWKEVEVTPG--------SETSYTLTGLKP 66

                         90
                 ....*....|...
gi 568928965 418 GARYTVRVAALNG 430
Cdd:cd00063   67 GTEYEFRVRAVNG 79
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
465-563 9.69e-05

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 45.15  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 465 VEPQSVSLSWRepvpAGAPGTNSTEYEIryYEKGQSEQTYstvkTGAPAVTVTNLKPATRYVFQIRAASPGPLWEAQSF- 543
Cdd:COG3979   14 VTSSSVSLSWD----ASTDNVGVTGYDV--YRGGDQVATV----TGLTAWTVTGLTPGTEYTFTVGACDAAGNVSAASGt 83

                         90       100
                 ....*....|....*....|..
gi 568928965 544 --SPSIEVQTPGEGTPNTCASW 563
Cdd:COG3979   84 stAMFGGSSTTLGSAEGVADTS 105
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 467-533 1.86e-04

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: 40.86  E-value: 1.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568928965  467 PQSVSLSWREPVPAGAP----GTNSTEY------EIRYYEKGQSEQTYSTVktgapaVTVTNLKPATRYVFQIRAAS 533
Cdd:pfam16656  12 STSMTVSWVTPSAVTSPvvqyGTSSSALtstataTSSTYTTGDGGTGYIHR------ATLTGLEPGTTYYYRVGDDN 82
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
420-532 1.09e-03

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


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 42.24  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928965 420 RYTVRVAALN--GVSGPaaAAGATYAQVTVSTG-PGAPweeDEIrrdRVEPQ--SVSLSWREPVpagapGTNSTEYEIRY 494
Cdd:COG4733  598 DYEVRVRAINalGVSSA--WAASSETTVTGKTApPPAP---TGL---TATGGlgGITLSWSFPV-----DADTLRTEIRY 664

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568928965 495 YEKGQ-SEQTYSTVKTGAPAVTVTNLKPATRYVFQIRAA 532
Cdd:COG4733  665 STTGDwASATVAQALYPGNTYTLAGLKAGQTYYYRARAV 703
 
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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