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 578820667  786 GHFYNTTTHRCIRCPVGTYQPEFGKNNCVSCPGNTTTDFDGSTNITQC 833
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

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        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578820667  673 GTYYDGARERCILCPNGTFQNEEGQMTCEPCPRPGNSgalKTPEAWNMSEC 723
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTT---DSPGATSISDC 48

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 578820667  286 CAVNNGGCDRTCKDTSTGVHCSCPVGFTLQLDGKTC 321
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 578820667  132 CLENNGGCQHTCVNVMGSYECCCKEGFFLSDNQHTC 167
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
                 ....*....|....*....|....*....|....*...
gi 578820667 359 EKSCQDVDECS-LDRTCDHSCINHPGTFACACNRGYTL 395
Cdd:cd01475  181 GKICVVPDLCAtLSHVCQQVCISTPGSYLCACTEGYAL 218

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 578820667   95 NGGCVHDCLNIPGNYRCTCFDGFMLAHDGHNC 126
Cdd:pfam14670   5 NGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578820667  838 CGGELGDFTGYIESPNYPGNYPANTECTWTINPPPKRRILIVVPEIFLPIEDDCG-DYLVMRKTSSSNSVTTYETCqTYE 916
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 578820667  917 RPIAFTSRSKKLWIQFKSNEGNSARGFQVPY 947
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 578820667  786 GHFYNTTTHRCIRCPVGTYQPEFGKNNCVSCPGNTTTDFDGSTNITQC 833
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

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        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578820667  673 GTYYDGARERCILCPNGTFQNEEGQMTCEPCPRPGNSgalKTPEAWNMSEC 723
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTT---DSPGATSISDC 48

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 578820667  286 CAVNNGGCDRTCKDTSTGVHCSCPVGFTLQLDGKTC 321
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 578820667  132 CLENNGGCQHTCVNVMGSYECCCKEGFFLSDNQHTC 167
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
                 ....*....|....*....|....*....|....*...
gi 578820667 359 EKSCQDVDECS-LDRTCDHSCINHPGTFACACNRGYTL 395
Cdd:cd01475  181 GKICVVPDLCAtLSHVCQQVCISTPGSYLCACTEGYAL 218

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 578820667  327 CQTRNGGCDHFCKNIVGSFDCGCKKGFKLLTDEKSC 362
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 578820667   95 NGGCVHDCLNIPGNYRCTCFDGFMLAHDGHNC 126
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 578820667 401 CGDTNECSINNGGCQQVCVNTVGSYECQCHPGYKLHWNKK 440
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 578820667   403 DTNECSINNG-GCQQVCVNTVGSYECQCHPGY 433
Cdd:smart00179   1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY 32

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 578820667   128 DVDECLENNGgCQH--TCVNVMGSYECCCKEGF 158
Cdd:smart00179   1 DIDECASGNP-CQNggTCVNTVGSYRCECPPGY 32

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 578820667    86 DIDECgnELNGGCVHD--CLNIPGNYRCTCFDGFmlaHDGHNC 126
Cdd:smart00179   1 DIDEC--ASGNPCQNGgtCVNTVGSYRCECPPGY---TDGRNC 38

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578820667  838 CGGELGDFTGYIESPNYPGNYPANTECTWTINPPPKRRILIVVPEIFLPIEDDCG-DYLVMRKTSSSNSVTTYETCqTYE 916
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 578820667  917 RPIAFTSRSKKLWIQFKSNEGNSARGFQVPY 947
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 578820667  786 GHFYNTTTHRCIRCPVGTYQPEFGKNNCVSCPGNTTTDFDGSTNITQC 833
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

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        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578820667  673 GTYYDGARERCILCPNGTFQNEEGQMTCEPCPRPGNSgalKTPEAWNMSEC 723
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTT---DSPGATSISDC 48

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 578820667  286 CAVNNGGCDRTCKDTSTGVHCSCPVGFTLQLDGKTC 321
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 578820667  132 CLENNGGCQHTCVNVMGSYECCCKEGFFLSDNQHTC 167
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
                 ....*....|....*....|....*....|....*...
gi 578820667 359 EKSCQDVDECS-LDRTCDHSCINHPGTFACACNRGYTL 395
Cdd:cd01475  181 GKICVVPDLCAtLSHVCQQVCISTPGSYLCACTEGYAL 218

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 578820667  217 CNHGNGGCQHSCDDTADGPECSCHPQYKMHTDGRSC 252
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 578820667    45 DVDECAQGlDDCHADALCQNTPTSYKCSCKPGYQgEGRQCE 85
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39

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 578820667  45 DVDECAQGlDDCHADALCQNTPTSYKCSCKPGYqgEGRQCE 85
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38

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 578820667 126 CLDVDECLENNGGCQHTCVNVMGSYECCCKEGFFLSDNQHT 166
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

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 578820667  305 HCSCPVGFTLQLDGKTCKDIDE 326
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

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 578820667  407 CSINNGGC--QQVCVNTVGSYECQCHPGYK 434
Cdd:pfam12947   1 CSDNNGGChpNATCTNTGGSFTCTCNDGYT 30

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 578820667  110 RCTCFDGFMLAHDGHNCLDVDE 131
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 578820667   364 DVDECSLDRTCDH--SCINHPGTFACACNRGYT 394
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33

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 578820667 364 DVDECSLDRTCDHS--CINHPGTFACACNRGYTL 395
Cdd:cd00054    1 DIDECASGNPCQNGgtCVNTVGSYRCSCPPGYTG 34