TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622855656  689 QCMHPLSVHLTKQLCCC-SVGKAWGPHCEKCPLPGTAAFKEIC 730
Cdd:pfam00683    2 RCSNPLPGNVTKSECCCtSVGRAWGSPCELCPPPGTDEFRELC 44

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1622855656 1533 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1575
Cdd:pfam00683    2 RCSNPLPG-NVTKSECCCTSvGRAWGSPCELCPPPGTDEFRELC 44

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1622855656  1120 DIDECQHHHLCAHG-QCRNTEGSFQCVCDQGYRAsglGDHCE 1160
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYTD---GRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1622855656  1244 DIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFqapQDGQGCV 1285
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY---TDGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622855656   627 DINECQLQGVCPNG-ECLNTMGSYRCTCKIGF 657
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGY 32

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855656 1161 DINECLEDKSVCQR-GDCINTAGSYDCTCPDG 1191
Cdd:pfam07645    1 DVDECATGTHNCPAnTVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1622855656   957 DVDECLRPDVCGEG-HCVNTVGAFRCEyCDSGYrmTQRGRCE 997
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCE-CPPGY--TDGRNCE 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 1622855656  998 DIDECLNPSTC-PDEQCVNSPGSYQCVpCTEGFRG 1031
Cdd:cd00054      1 DIDECASGNPCqNGGTCVNTVGSYRCS-CPPGYTG 34

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622855656  689 QCMHPLSVHLTKQLCCC-SVGKAWGPHCEKCPLPGTAAFKEIC 730
Cdd:pfam00683    2 RCSNPLPGNVTKSECCCtSVGRAWGSPCELCPPPGTDEFRELC 44

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1622855656 1533 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1575
Cdd:pfam00683    2 RCSNPLPG-NVTKSECCCTSvGRAWGSPCELCPPPGTDEFRELC 44

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 1622855656 1202 DINECEHPGLCGPQGECLNTEGSFHCVCQQGFSisadGRTCE 1243
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----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        40
                   ....*....|....*....|....*....|....*....|..
gi 1622855656 1120 DIDECQHHHLC-AHGQCRNTEGSFQCVCDQGYRasglGDHCE 1160
Cdd:cd00054      1 DIDECASGNPCqNGGTCVNTVGSYRCSCPPGYT----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 1622855656 1079 DIDECQQGNLCVN-GQCKNTEGSFRCTCGQGYQL 1111
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1622855656  1038 DVDECLEPNVCTNG-DCSNLEGSYMCSCHKGYTrtpDHKHCK 1078
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622855656   627 DINECQLQGVCPNG-ECLNTMGSYRCTCKIGF 657
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGY 32

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855656 1161 DINECLEDKSVCQR-GDCINTAGSYDCTCPDG 1191
Cdd:pfam07645    1 DVDECATGTHNCPAnTVCVNTIGSFECRCPDG 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 1622855656  627 DINECQLQGVCPN-GECLNTMGSYRCTCKIGF 657
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGY 32

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1622855656  1660 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1694
Cdd:smart00179    1 DIDECASGNP----CQNgGTCVNTVGSYRCECPPGY 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 1622855656  915 DIDECTQvQHLCS-QGRCENTEGSFLCICPAGFmaseEGTNCI 956
Cdd:cd00054      1 DIDECAS-GNPCQnGGTCVNTVGSYRCSCPPGY----TGRNCE 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 1622855656 1660 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1694
Cdd:cd00054      1 DIDECASGNP----CQNgGTCVNTVGSYRCSCPPGY 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 1622855656 1161 DINEClEDKSVCQR-GDCINTAGSYDCTCPDGFQLddnKTCQ 1201
Cdd:cd00054      1 DIDEC-ASGNPCQNgGTCVNTVGSYRCSCPPGYTG---RNCE 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 1622855656 1226 HCVCQQGFSISADGRTCEDIDE 1247
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 1622855656  957 DVDECLRPDVCGEGH-CVNTVGAFRCEyCDSGYR 989
Cdd:cd00054      1 DIDECASGNPCQNGGtCVNTVGSYRCS-CPPGYT 33

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 1622855656  998 DIDECLNPSTC-PDEQCVNSPGSYQCVpCTEGFRG 1031
Cdd:cd00054      1 DIDECASGNPCqNGGTCVNTVGSYRCS-CPPGYTG 34

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 1622855656 1062 CSCHKGYTRTPDHKHCKDIDE 1082
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622855656  689 QCMHPLSVHLTKQLCCC-SVGKAWGPHCEKCPLPGTAAFKEIC 730
Cdd:pfam00683    2 RCSNPLPGNVTKSECCCtSVGRAWGSPCELCPPPGTDEFRELC 44

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1622855656 1533 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1575
Cdd:pfam00683    2 RCSNPLPG-NVTKSECCCTSvGRAWGSPCELCPPPGTDEFRELC 44

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 1622855656 1202 DINECEHPGLCGPQGECLNTEGSFHCVCQQGFSisadGRTCE 1243
Cdd:cd00054      1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----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        40
                   ....*....|....*....|....*....|....*....|..
gi 1622855656 1120 DIDECQHHHLC-AHGQCRNTEGSFQCVCDQGYRasglGDHCE 1160
Cdd:cd00054      1 DIDECASGNPCqNGGTCVNTVGSYRCSCPPGYT----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 1622855656 1079 DIDECQQGNLCVN-GQCKNTEGSFRCTCGQGYQL 1111
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1622855656  1038 DVDECLEPNVCTNG-DCSNLEGSYMCSCHKGYTrtpDHKHCK 1078
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622855656   627 DINECQLQGVCPNG-ECLNTMGSYRCTCKIGF 657
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGY 32

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855656 1161 DINECLEDKSVCQR-GDCINTAGSYDCTCPDG 1191
Cdd:pfam07645    1 DVDECATGTHNCPAnTVCVNTIGSFECRCPDG 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 1622855656  627 DINECQLQGVCPN-GECLNTMGSYRCTCKIGF 657
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGY 32

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1622855656  1660 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1694
Cdd:smart00179    1 DIDECASGNP----CQNgGTCVNTVGSYRCECPPGY 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 1622855656  915 DIDECTQvQHLCS-QGRCENTEGSFLCICPAGFmaseEGTNCI 956
Cdd:cd00054      1 DIDECAS-GNPCQnGGTCVNTVGSYRCSCPPGY----TGRNCE 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 1622855656 1660 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1694
Cdd:cd00054      1 DIDECASGNP----CQNgGTCVNTVGSYRCSCPPGY 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 1622855656 1161 DINEClEDKSVCQR-GDCINTAGSYDCTCPDGFQLddnKTCQ 1201
Cdd:cd00054      1 DIDEC-ASGNPCQNgGTCVNTVGSYRCSCPPGYTG---RNCE 38

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855656 1244 DIDECVNNT-VCDSHGFCDNTAGSFRCLCYQG 1274
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 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 1622855656 1226 HCVCQQGFSISADGRTCEDIDE 1247
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

Epidermal growth factor-like domain;

                            10        20        30
                    ....*....|....*....|....*....|...
gi 1622855656   630 ECQLQGVCPNGECLNTMGSYRCTCKIGFGPDPT 662
Cdd:smart00181    1 ECASGGPCSNGTCINTPGSYTCSCPPGYTGDKR 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855656  627 DINEC-QLQGVCP-NGECLNTMGSYRCTCKIG 656
Cdd:pfam07645    1 DVDECaTGTHNCPaNTVCVNTIGSFECRCPDG 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 1622855656 1205 ECEHPGLCGPQGECLNTEGSFHCVCQQGFS 1234
Cdd:cd00053      1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYT 30

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 1622855656   998 DIDECLNPSTC-PDEQCVNSPGSYQCVpCTEGFR 1030
Cdd:smart00179    1 DIDECASGNPCqNGGTCVNTVGSYRCE-CPPGYT 33

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 1622855656  909 QQRKCVDIDECTQVQHLCSQGrCENTEGSFLCICPAGFMASEEG 952
Cdd:cd01475    180 QGKICVVPDLCATLSHVCQQV-CISTPGSYLCACTEGYALLEDN 222

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855656 1202 DINECEHPG-LCGPQGECLNTEGSFHCVCQQG 1232
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32