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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462526741 699 GHFYNTTTHRCIRCPVGTYQPEFGKNNCVSCPGNTTTDFDGSTNITQC 746
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741  48 CAQGLDDCHADALCQNTPTSYKCSCKPGYQGEGRQC 83
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741 406 CSINNGGCQQVCVNTVGSYECQCHPGYKLHWNKKDC 441
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462526741 311 FTLQLDGKTCKDIDECQTRNGGCDHFCKNIVGSFDCGCKKGFKLLTDEKS 360
Cdd:cd01475   175 LTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741 216 CNHGNGGCQHSCDDTADGPECSCHPQYKMHTDGRSC 251
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462526741 176 CMNKDHGCSHICKEAPrGSVACECRPGFELAKNQRDC 212
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526741 751 CGGELGDFTGYIESPNYPGNYPANTECTWTINPPPKRRILIVVPEIFLPIEDDCG-DYLVMRKTSSSNSVTTYETCqTYE 829
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462526741 830 RPIAFTSRSKKLWIQFKSNEGNSARGFQVPY 860
Cdd:pfam00431  80 IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462526741 699 GHFYNTTTHRCIRCPVGTYQPEFGKNNCVSCPGNTTTDFDGSTNITQC 746
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741  48 CAQGLDDCHADALCQNTPTSYKCSCKPGYQGEGRQC 83
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741 406 CSINNGGCQQVCVNTVGSYECQCHPGYKLHWNKKDC 441
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462526741 311 FTLQLDGKTCKDIDECQTRNGGCDHFCKNIVGSFDCGCKKGFKLLTDEKS 360
Cdd:cd01475   175 LTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741 216 CNHGNGGCQHSCDDTADGPECSCHPQYKMHTDGRSC 251
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462526741  44 DVDECAQGlDDCHADALCQNTPTSYKCSCKPGYqgEGRQCE 84
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462526741  94 NGGCVHDCLNIPGNYRCTCFDGFMLAHDGHNC 125
Cdd:pfam14670   5 NGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462526741 125 CLDVDECLENNGGCQHTCVNVMGSYECCCKEGFFLSDNQHT 165
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462526741 176 CMNKDHGCSHICKEAPrGSVACECRPGFELAKNQRDC 212
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462526741   85 DIDECgnELNGGCVHD--CLNIPGNYRCTCFDGFmlaHDGHNC 125
Cdd:smart00179   1 DIDEC--ASGNPCQNGgtCVNTVGSYRCECPPGY---TDGRNC 38

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462526741  322 DIDECQTRNGgCDH--FCKNIVGSFDCGCKKGFkllTDEKSCQ 362
Cdd:smart00179   1 DIDECASGNP-CQNggTCVNTVGSYRCECPPGY---TDGRNCE 39

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462526741 751 CGGELGDFTGYIESPNYPGNYPANTECTWTINPPPKRRILIVVPEIFLPIEDDCG-DYLVMRKTSSSNSVTTYETCqTYE 829
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462526741 830 RPIAFTSRSKKLWIQFKSNEGNSARGFQVPY 860
Cdd:pfam00431  80 IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462526741 699 GHFYNTTTHRCIRCPVGTYQPEFGKNNCVSCPGNTTTDFDGSTNITQC 746
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741  48 CAQGLDDCHADALCQNTPTSYKCSCKPGYQGEGRQC 83
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741 406 CSINNGGCQQVCVNTVGSYECQCHPGYKLHWNKKDC 441
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462526741 311 FTLQLDGKTCKDIDECQTRNGGCDHFCKNIVGSFDCGCKKGFKLLTDEKS 360
Cdd:cd01475   175 LTKKFQGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741 216 CNHGNGGCQHSCDDTADGPECSCHPQYKMHTDGRSC 251
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462526741 326 CQTRNGGCDHFCKNIVGSFDCGCKKGFKLLTDEKSC 361
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462526741   44 DVDECAQGlDDCHADALCQNTPTSYKCSCKPGYQgEGRQCE 84
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462526741 400 CGDTNECSINNGGCQQVCVNTVGSYECQCHPGYKLHWNKK 439
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462526741  402 DTNECSINNG-GCQQVCVNTVGSYECQCHPGY 432
Cdd:smart00179   1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY 32

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462526741 402 DTNECSINNG-GCQQVCVNTVGSYECQCHPGYKLH 435
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTGR 35

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462526741 176 CMNKDHGCSHICKEAPrGSVACECRPGFELAKNQRDC 212
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                          10        20
                  ....*....|....*....|..
gi 2462526741 109 RCTCFDGFMLAHDGHNCLDVDE 130
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462526741  363 DVDECSLDRTCDH--SCINHPGTFACACNRGYT 393
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462526741  47 ECAQGlDDCHADALCQNTPTSYKCSCKPGYQGEGR 81
Cdd:cd00053     1 ECAAS-NPCSNGGTCVNTPGSYRCVCPPGYTGDRS 34

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462526741 402 DTNECSINNGGCQQ--VCVNTVGSYECQCHPG 431
Cdd:pfam07645   1 DVDECATGTHNCPAntVCVNTIGSFECRCPDG 32