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 148666879  420 PRGDLDGSTKD-LIETCCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCCISYLKEKSC 479
Cdd:cd00017     1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDE 61

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 148666879  505 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 553
Cdd:cd00017    11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 148666879    848 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRdafGRTCI 890
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD---GRNCE 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 148666879   903 CQHTCENTPGSYRCSCAAGFLLAADGKHC 931
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 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
                   ....*....|....*....|....*....
gi 148666879   942 CSQECANIYGSYQCYCRQGYQLAEDGHTC 970
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 148666879   709 DINECVTDLHTCTRAEHCVNTPGSFQCykalTCEPG 744
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 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 148666879   692 CSCFPGYAIMADGVSCEDINE 712
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22

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 148666879  420 PRGDLDGSTKD-LIETCCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCCISYLKEKSC 479
Cdd:cd00017     1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDE 61

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 148666879  505 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 553
Cdd:cd00017    11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 148666879    848 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRdafGRTCI 890
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        40
                  ....*....|....*....|....*....|....*....|...
gi 148666879  848 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQrdafGRTCI 890
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 148666879    891 DVNECwvSPGRLCQH--TCENTPGSYRCSCAAGFLlaaDGKHCE 932
Cdd:smart00179    1 DIDEC--ASGNPCQNggTCVNTVGSYRCECPPGYT---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 a three-fold repeat in fibulins.

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 148666879    435 CCAAGQQWAIDNDECQEIPENGAQSDiCRIAQRQCC 470
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINSGD-CRKAFLQCC 35

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 148666879    800 DINECTSLlEPCRSGFSCINTVGSYTCQrnplvCGRGYH 838
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCE-----CPPGYT 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 148666879   709 DINECVTDLHTCTRAEHCVNTPGSFQCykalTCEPG 744
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 32

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 148666879   848 DVNECETGVHRCGEGQLCYNLPGSYRCDCKPG 879
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32

Calcium-binding EGF domain;

                           10        20
                   ....*....|....*....|....*...
gi 148666879   800 DINECTSLLEPCRSGFSCINTVGSYTCQ 827
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR 28

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 148666879   435 CCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCC 470
Cdd:pfam01821    1 CCLDGMKRNPMGRSCEQRAARIKEGPRCRKAFLQCC 36

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 148666879    709 DINECVTDlHTCTRAEHCVNTPGSFQCykalTCEPGY 745
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRC----ECPPGY 32

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 148666879    511 CCGLGLRVRAEGQSCESNPNLGY--PCNHVMLSCC 543
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 148666879  972 DIDECAQGAGILCTFRCVNVPGSYQCACPEqGYTmmanGRSCK 1014
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPP-GYT----GRNCE 38

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 148666879   692 CSCFPGYAIMADGVSCEDINE 712
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 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 148666879   675 DNGPCRQVCRVVGDTAMCSCFPGYAIMADGVSC 707
Cdd:pfam14670    4 NNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

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 148666879  420 PRGDLDGSTKD-LIETCCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCCISYLKEKSC 479
Cdd:cd00017     1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDE 61

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 148666879  505 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 553
Cdd:cd00017    11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 148666879    848 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRdafGRTCI 890
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        40
                  ....*....|....*....|....*....|....*....|...
gi 148666879  848 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQrdafGRTCI 890
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 148666879    891 DVNECwvSPGRLCQH--TCENTPGSYRCSCAAGFLlaaDGKHCE 932
Cdd:smart00179    1 DIDEC--ASGNPCQNggTCVNTVGSYRCECPPGYT---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 a three-fold repeat in fibulins.

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 148666879    435 CCAAGQQWAIDNDECQEIPENGAQSDiCRIAQRQCC 470
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINSGD-CRKAFLQCC 35

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 148666879   954 QCYCRQGYQLAEDGHTCTDIDE 975
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 148666879  891 DVNECwvSPGRLCQH--TCENTPGSYRCSCAAGFLlaadGKHCE 932
Cdd:cd00054     1 DIDEC--ASGNPCQNggTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 148666879   709 DINECVTDLHTCTRAEHCVNTPGSFQCykalTCEPG 744
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 32

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 148666879   848 DVNECETGVHRCGEGQLCYNLPGSYRCDCKPG 879
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 148666879    972 DIDECAQGAGILCTFRCVNVPGSYQCACPEqGYTmmaNGRSCK 1014
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPP-GYT---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
                  ....*....|....*....|....*....|....*....
gi 148666879  800 DINECTSLlEPCRSGFSCINTVGSYTCQrnplvCGRGYH 838
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCS-----CPPGYT 33

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 148666879   915 RCSCAAGFLLAADGKHCEDVNE 936
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 148666879    709 DINECVTDlHTCTRAEHCVNTPGSFQCykalTCEPGY 745
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRC----ECPPGY 32

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 148666879    754 DVDECVTGtHNCQAGFSCQNTKGSFYCQarqrCMDGF 790
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCE----CPPGY 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 148666879  594 DQDECLMLPGELCQHLCINTVGSYRCACFPGFElqgdGRTC 634
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNC 37

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 148666879  972 DIDECAQGAGILCTFRCVNVPGSYQCACPEqGYTmmanGRSCK 1014
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPP-GYT----GRNCE 38

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 148666879   692 CSCFPGYAIMADGVSCEDINE 712
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 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 148666879  754 DVDECVTGtHNCQAGFSCQNTKGSFYCQarqrCMDGF 790
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCS----CPPGY 32

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 148666879  851 ECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRD 883
Cdd:cd00053     1 ECAAS-NPCSNGGTCVNTPGSYRCVCPPGYTGD 32