Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 51873055   1025 DVDECALGTHNCSEAETCHNIQGSFRCLrfeCPPN 1059
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 32

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
                   ....*....|....*....|....*....
gi 51873055    616 CQHLCINTVGSYHCACFPGFSLQDDGRTC 644
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51873055    764 DVDECAMGTHTCQPGFLCQNTKGSFYCqarqRCMDG 799
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 32

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
                   ....*....|....*....|....*....
gi 51873055    913 CQHTCENTLGSYRCSCASGFLLAADGKRC 941
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51873055    719 DINECVTDLHTCSRGEHCVNTLGSFHCykalTCEPG 754
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 32

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873055     982 DIDECAQGAGILCTFRCLNVPGSYQCACPEqGYTmtaNGRSCK 1024
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPP-GYT---DGRNCE 39

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 51873055   1025 DVDECALGTHNCSEAETCHNIQGSFRCLrfeCPPN 1059
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 32

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
                   ....*....|....*....|....*....
gi 51873055    616 CQHLCINTVGSYHCACFPGFSLQDDGRTC 644
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51873055    764 DVDECAMGTHTCQPGFLCQNTKGSFYCqarqRCMDG 799
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 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 51873055  858 DVNECETGvHRCGEGQVCHNLPGSYRCDCKAGFQ 891
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 51873055     901 DVNECwaSPGRLCQH--TCENTLGSYRCSCASGFLlaaDGKRCE 942
Cdd:smart00179    1 DIDEC--ASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

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 51873055    964 QCYCRQGYQLAEDGHTCTDIDE 985
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 51873055  810 DINECTSLSePCRPGFSCINTVGSYTCQrnpliCARGYH 848
Cdd:cd00054    1 DIDECASGN-PCQNGGTCVNTVGSYRCS-----CPPGYT 33

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 51873055     445 CCAAGQQWAIDNDECLEIPESGTEDNvCRTAQRHCC 480
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINSGD-CRKAFLQCC 35

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 51873055  901 DVNECwaSPGRLCQH--TCENTLGSYRCSCASGFLlaadGKRCE 942
Cdd:cd00054    1 DIDEC--ASGNPCQNggTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 51873055     764 DVDECAMGtHTCQPGFLCQNTKGSFYCQarqrCMDGF 800
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCE----CPPGY 32

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 51873055    685 DNGPCKQVCSTVGGSAICSCFPGYAIMADGVSC 717
Cdd:pfam14670    4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873055     982 DIDECAQGAGILCTFRCLNVPGSYQCACPEqGYTmtaNGRSCK 1024
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPP-GYT---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
                 ....*....|....*....|....*....|....*....
gi 51873055  757 LKDGECEDVDECAMGTHTCQPGflCQNTKGSFYCQARQR 795
Cdd:cd01475  179 FQGKICVVPDLCATLSHVCQQV--CISTPGSYLCACTEG 215

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 51873055  604 DQDECLLLPGELCQHLCINTVGSYHCACFPGFSlqddGRTC 644
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNC 37

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 51873055   1025 DVDECALGTHNCSEAETCHNIQGSFRCLrfeCPPN 1059
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 32

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
                   ....*....|....*....|....*....
gi 51873055    616 CQHLCINTVGSYHCACFPGFSLQDDGRTC 644
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51873055    764 DVDECAMGTHTCQPGFLCQNTKGSFYCqarqRCMDG 799
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 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 51873055  858 DVNECETGvHRCGEGQVCHNLPGSYRCDCKAGFQ 891
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 51873055     901 DVNECwaSPGRLCQH--TCENTLGSYRCSCASGFLlaaDGKRCE 942
Cdd:smart00179    1 DIDEC--ASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

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 51873055    964 QCYCRQGYQLAEDGHTCTDIDE 985
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51873055    719 DINECVTDLHTCSRGEHCVNTLGSFHCykalTCEPG 754
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 32

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 51873055     719 DINECVTDlHTCSRGEHCVNTLGSFHCykalTCEPGY 755
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRC----ECPPGY 32

Calcium-binding EGF domain;

                           10        20
                   ....*....|....*....|....*...
gi 51873055    810 DINECTSLSEPCRPGFSCINTVGSYTCQ 837
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873055     604 DQDECLLlpGELCQH--LCINTVGSYHCACFPGFSlqdDGRTC 644
Cdd:smart00179    1 DIDECAS--GNPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 51873055    1025 DVDECALGtHNCSEAETCHNIQGSFRClrfECPPNY 1060
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRC---ECPPGY 32

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 51873055    925 RCSCASGFLLAADGKRCEDVNE 946
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        40
                 ....*....|....*....|....*....|....*....|
gi 51873055  719 DINECvTDLHTCSRGEHCVNTLGSFHCykalTCEPGYALK 758
Cdd:cd00054    1 DIDEC-ASGNPCQNGGTCVNTVGSYRC----SCPPGYTGR 35

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                            10        20        30
                    ....*....|....*....|....*....|....*
gi 51873055     521 CCGLGLRVRAEGQSCESNPNLGY--PCNHVMLSCC 553
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINsgDCRKAFLQCC 35

Anaphylotoxin-like domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51873055    445 CCAAGQQWAIDNDECLEIPESGTEDNVCRTAQRHCC 480
Cdd:pfam01821    1 CCLDGMKRNPMGRSCEQRAARIKEGPRCRKAFLQCC 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 51873055  764 DVDECAMGtHTCQPGFLCQNTKGSFYCQarqrCMDGF 800
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCS----CPPGY 32

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 51873055    702 CSCFPGYAIMADGVSCEDINE 722
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22