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 repeats in fibulins.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51873053  430 PRSSPEGSTKD-LIETCCAAGQQWAIDNDECLEIPESGTEDNVCRTAQRHCCVSYLQEKSCM 490
Cdd:cd00017    1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDEE 62

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 repeats in fibulins.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51873053  515 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 563
Cdd:cd00017   11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873053     905 DVNECETGvHRCGEGQVCHNLPGSYRCDCKAGFQRdafGRGCI 947
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD---GRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 51873053     857 DINECTSLSePCRPGFSCINTVGSYTCQrnpliCARGYHasdDGTKCV 904
Cdd:smart00179    1 DIDECASGN-PCQNGGTCVNTVGSYRCE-----CPPGYT---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 51873053   1011 QCYCRQGYQLAEDGHTCTDIDE 1032
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

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 51873053    685 DNGPCKQVCSTVGGSAICSCFPGYAIMADGVSC 717
Cdd:pfam14670    4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873053    1029 DIDECAQGAGILCTFRCLNVPGSYQCACPEqGYTmtaNGRSCK 1071
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPP-GYT---DGRNCE 39

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 repeats in fibulins.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51873053  430 PRSSPEGSTKD-LIETCCAAGQQWAIDNDECLEIPESGTEDNVCRTAQRHCCVSYLQEKSCM 490
Cdd:cd00017    1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDEE 62

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 repeats in fibulins.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51873053  515 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 563
Cdd:cd00017   11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873053     905 DVNECETGvHRCGEGQVCHNLPGSYRCDCKAGFQRdafGRGCI 947
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD---GRNCE 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
                 ....*....|....*....|....*....|....
gi 51873053  905 DVNECETGvHRCGEGQVCHNLPGSYRCDCKAGFQ 938
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT 33

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 51873053    960 CQHTCENTLGSYRCSCASGFLLAADGKRC 988
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 51873053     948 DVNECwaSPGRLCQH--TCENTLGSYRCSCASGFLlaaDGKRCE 989
Cdd:smart00179    1 DIDEC--ASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51873053    766 DINECVTDLHTCSRGEHCVNTLGSFHCykalTCEPG 801
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 32

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 51873053     766 DINECVTDlHTCSRGEHCVNTLGSFHCykalTCEPGY 802
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRC----ECPPGY 32

Calcium-binding EGF domain;

                           10        20
                   ....*....|....*....|....*...
gi 51873053    857 DINECTSLSEPCRPGFSCINTVGSYTCQ 884
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873053     604 DQDECLLlpGELCQH--LCINTVGSYHCACFPGFSlqdDGRTC 644
Cdd:smart00179    1 DIDECAS--GNPCQNggTCVNTVGSYRCECPPGYT---DGRNC 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 51873053    1072 DVDECALGtHNCSEAETCHNIQGSFRClrfECPPNY 1107
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRC---ECPPGY 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 51873053  766 DINECvTDLHTCSRGEHCVNTLGSFHCykalTCEPGYALK 805
Cdd:cd00054    1 DIDEC-ASGNPCQNGGTCVNTVGSYRC----SCPPGYTGR 35

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 51873053  804 LKDGECEDVDECAMGTHTCQPGflCQNTKGSFYCQARQR 842
Cdd:cd01475  179 FQGKICVVPDLCATLSHVCQQV--CISTPGSYLCACTEG 215

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 51873053     521 CCGLGLRVRAEGQSCESNPNLGY--PCNHVMLSCC 553
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINsgDCRKAFLQCC 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 51873053  604 DQDECLLLPGELCQHLCINTVGSYHCACFPGFSlqddGRTC 644
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNC 37

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 repeats in fibulins.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51873053  430 PRSSPEGSTKD-LIETCCAAGQQWAIDNDECLEIPESGTEDNVCRTAQRHCCVSYLQEKSCM 490
Cdd:cd00017    1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDEE 62

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 repeats in fibulins.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51873053  515 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 563
Cdd:cd00017   11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873053     905 DVNECETGvHRCGEGQVCHNLPGSYRCDCKAGFQRdafGRGCI 947
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD---GRNCE 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
                 ....*....|....*....|....*....|....
gi 51873053  905 DVNECETGvHRCGEGQVCHNLPGSYRCDCKAGFQ 938
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT 33

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 51873053    960 CQHTCENTLGSYRCSCASGFLLAADGKRC 988
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 51873053     948 DVNECwaSPGRLCQH--TCENTLGSYRCSCASGFLlaaDGKRCE 989
Cdd:smart00179    1 DIDEC--ASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

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 51873053    999 CSQECANIYGSYQCYCRQGYQLAEDGHTC 1027
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 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 51873053  857 DINECTSLSePCRPGFSCINTVGSYTCQrnpliCARGYH 895
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 51873053     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 51873053  948 DVNECwaSPGRLCQH--TCENTLGSYRCSCASGFLlaadGKRCE 989
Cdd:cd00054    1 DIDEC--ASGNPCQNggTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 51873053     811 DVDECAMGtHTCQPGFLCQNTKGSFYCQarqrCMDGF 847
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 51873053    685 DNGPCKQVCSTVGGSAICSCFPGYAIMADGVSC 717
Cdd:pfam14670    4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 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 51873053    972 RCSCASGFLLAADGKRCEDVNE 993
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF domain;

                           10        20
                   ....*....|....*....|....*...
gi 51873053    719 DQDECLMGAHDCSRRQFCVNTLGSFYCV 746
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 51873053    1029 DIDECAQGAGILCTFRCLNVPGSYQCACPEqGYTmtaNGRSCK 1071
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPP-GYT---DGRNCE 39

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 51873053    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        40
                 ....*....|....*....|....*....|....*....|.
gi 51873053  604 DQDECLLLPGELCQHLCINTVGSYHCACFPGFSlqddGRTC 644
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNC 37

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 51873053  717 CEDQDECLMGAHDCsrRQFCVNTLGSFYCVnhtvlCADGYILN 759
Cdd:cd01475  184 CVVPDLCATLSHVC--QQVCISTPGSYLCA-----CTEGYALL 219