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 31377568   696 GQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDC 743
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 31377568    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 31377568   240 CAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTC 275
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 31377568   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 31377568 313 ERNCQDIDECS-FDRTCDHICVNTPGSFQCLCHRGYLL 349
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 31377568   161 CMNKNHGCAHICRETPkGGIACECRPGFELTKNQRDC 197
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377568   804 CGGELGEFTGYIESPNYPGNYPAGVECIWNINPPPKRKILIVVPEIFLPSEDECG-DVLVMRKNSSPSSITTYETCqTYE 882
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 31377568   883 RPIAFTARSRKLWINFKTSEANSARGFQIPY 913
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 31377568   696 GQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDC 743
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 31377568    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 31377568   240 CAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTC 275
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 31377568   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 31377568   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 31377568 313 ERNCQDIDECS-FDRTCDHICVNTPGSFQCLCHRGYLL 349
Cdd:cd01475 181 GKICVVPDLCAtLSHVCQQVCISTPGSYLCACTEGYAL 218

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 31377568     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 31377568 273 KTCKDIDECRLNNGGCDHICRNTVGSFECSCKKGYKLLINERN 315
Cdd:cd01475 182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 31377568    357 DVDECSINrGGCRFG--CINTPGSYQCTCPAGqgrlHWNGKDCT 398
Cdd:smart00179   1 DIDECASG-NPCQNGgtCVNTVGSYRCECPPG----YTDGRNCE 39

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 31377568    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 31377568  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 31377568 357 DVDECSINrGGCRFG--CINTPGSYQCTCPAG 386
Cdd:cd00054   1 DIDECASG-NPCQNGgtCVNTVGSYRCSCPPG 31

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377568   804 CGGELGEFTGYIESPNYPGNYPAGVECIWNINPPPKRKILIVVPEIFLPSEDECG-DVLVMRKNSSPSSITTYETCqTYE 882
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 31377568   883 RPIAFTARSRKLWINFKTSEANSARGFQIPY 913
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 31377568   696 GQHSVDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAISFQDC 743
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 31377568    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 31377568   240 CAVNNGGCDSKCHDAATGVHCTCPVGFMLQPDRKTC 275
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 31377568   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 31377568 110 CLDVDECAEGNGGCQQSCVNMMGSYECHCREGFFLSDNQHT 150
Cdd:cd01475 184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 31377568     29 DVDECVEGtDNCHIDAICQNTPRSYKCICKSGYTgDGKHCK 69
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 31377568    318 DIDECSFDRTCDH--ICVNTPGSFQCLCHRGY 347
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 31377568  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 31377568 318 DIDECSFDRTCDH--ICVNTPGSFQCLCHRGY 347
Cdd:cd00054   1 DIDECASGNPCQNggTCVNTVGSYRCSCPPGY 32

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 31377568    357 DVDECSINrGGCRFG--CINTPGSYQCTCPAGqgrlHWNGKDCT 398
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 31377568 277 DIDECRLNNG-GCDHICRNTVGSFECSCKKGYKLlineRNCQ 317
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 31377568   281 CRLNNGGCDH--ICRNTVGSFECSCKKGYK 308
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 31377568   259 HCTCPVGFMLQPDRKTCKDIDE 280
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 31377568    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 31377568 357 DVDECSINrGGCRFG--CINTPGSYQCTCPAG 386
Cdd:cd00054   1 DIDECASG-NPCQNGgtCVNTVGSYRCSCPPG 31

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 31377568   357 DVDECSINRGGCRFG--CINTPGSYQCTCPAG 386
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 31377568  52 SYKCICKSGYTGDGKHCKDVDECEREDNaGCVHDCVNIPGNYRCTCYDGFHLAHDG 107
Cdd:cd01475 168 DFSTIEELTKKFQGKICVVPDLCATLSH-VCQQVCISTPGSYLCACTEGYALLEDN 222