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 530381652   712 GQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDC 759
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 530381652    33 CVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHC 68
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 530381652   256 CAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTC 291
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 530381652   116 CAEGNGGCQQSCVNMMGSYECHCREGFFLSDNQHTC 151
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 530381652  329 ERNCQDIDECS-FDRTCDHICVNTPGSFQCLCHRGYLL 365
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 530381652   161 CMNKNHGCAHICRETPkGGIACECRPGFELTKNQRDC 197
Cdd:pfam14670    1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36

CUB domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381652   820 CGGELGEFTGYIESPNYPGNYPAGVECIWNINPPPKRKILIVVPEIFLPSEDECG-DVLVMRKNSSPSSITTYETCqTYE 898
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 530381652   899 RPIAFTARSRKLWINFKTSEANSARGFQIPY 929
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 530381652   712 GQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDC 759
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 530381652    33 CVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHC 68
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 530381652   256 CAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTC 291
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 530381652   116 CAEGNGGCQQSCVNMMGSYECHCREGFFLSDNQHTC 151
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 530381652   201 CNYGNGGCQHTCDDTEQGPRCGCHIKFVLHTDGKTC 236
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 530381652  329 ERNCQDIDECS-FDRTCDHICVNTPGSFQCLCHRGYLL 365
Cdd:cd01475   181 GKICVVPDLCAtLSHVCQQVCISTPGSYLCACTEGYAL 218

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 530381652     70 DVDECEREDNAGCVHDCVNIPGNYRCTCYDGFhlaHDGHNC 110
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY---TDGRNC 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 530381652  289 KTCKDIDECRLNNGGCDHICRNTVGSFECSCKKGYKLLINERN 331
Cdd:cd01475   182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 530381652    373 DVDECSINrGGCRFG--CINTPGSYQCTCPAGqgrlHWNGKDCT 414
Cdd:smart00179    1 DIDECASG-NPCQNGgtCVNTVGSYRCECPPG----YTDGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 530381652    112 DVDECAEGNG-GCQQSCVNMMGSYECHCREGF 142
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 530381652   70 DVDECEREDNAGCVHDCVNIPGNYRCTCYDGFHLAH 105
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRN 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
                  ....*....|....*....|....*....|..
gi 530381652  373 DVDECSINrGGCRFG--CINTPGSYQCTCPAG 402
Cdd:cd00054     1 DIDECASG-NPCQNGgtCVNTVGSYRCSCPPG 31

CUB domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530381652   820 CGGELGEFTGYIESPNYPGNYPAGVECIWNINPPPKRKILIVVPEIFLPSEDECG-DVLVMRKNSSPSSITTYETCqTYE 898
Cdd:pfam00431    1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                           90       100       110
                   ....*....|....*....|....*....|.
gi 530381652   899 RPIAFTARSRKLWINFKTSEANSARGFQIPY 929
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 530381652   712 GQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDC 759
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 530381652    33 CVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHC 68
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 530381652   256 CAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTC 291
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 530381652   116 CAEGNGGCQQSCVNMMGSYECHCREGFFLSDNQHTC 151
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
                  ....*....|....*....|....*....|....*....|.
gi 530381652  110 CLDVDECAEGNGGCQQSCVNMMGSYECHCREGFFLSDNQHT 150
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 530381652     29 DVDECVEGtDNCHIDAICQNTPRSYKCICKSGYTgDGKHCK 69
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 530381652    334 DIDECSFDRTCDH--ICVNTPGSFQCLCHRGY 363
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        40
                  ....*....|....*....|....*....|....*....|.
gi 530381652   29 DVDECVEGtDNCHIDAICQNTPRSYKCICKSGYTgdGKHCK 69
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38

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 530381652  334 DIDECSFDRTCDH--ICVNTPGSFQCLCHRGY 363
Cdd:cd00054     1 DIDECASGNPCQNggTCVNTVGSYRCSCPPGY 32

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 530381652    373 DVDECSINrGGCRFG--CINTPGSYQCTCPAGqgrlHWNGKDCT 414
Cdd:smart00179    1 DIDECASG-NPCQNGgtCVNTVGSYRCECPPG----YTDGRNCE 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 530381652  293 DIDECRLNNG-GCDHICRNTVGSFECSCKKGYKLlineRNCQ 333
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTG----RNCE 38

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 530381652   297 CRLNNGGCDH--ICRNTVGSFECSCKKGYK 324
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 530381652   275 HCTCPVGFMLQPDRKTCKDIDE 296
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

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 530381652    94 RCTCYDGFHLAHDGHNCLDVDE 115
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

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 530381652  373 DVDECSINrGGCRFG--CINTPGSYQCTCPAG 402
Cdd:cd00054     1 DIDECASG-NPCQNGgtCVNTVGSYRCSCPPG 31

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 530381652   373 DVDECSINRGGCRFG--CINTPGSYQCTCPAG 402
Cdd:pfam07645    1 DVDECATGTHNCPANtvCVNTIGSFECRCPDG 32

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 530381652   52 SYKCICKSGYTGDGKHCKDVDECEREDNaGCVHDCVNIPGNYRCTCYDGFHLAHDG 107
Cdd:cd01475   168 DFSTIEELTKKFQGKICVVPDLCATLSH-VCQQVCISTPGSYLCACTEGYALLEDN 222