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 1622855660  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 1622855660 1492 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1534
Cdd:pfam00683    2 RCSNPLPG-NVTKSECCCTSvGRAWGSPCELCPPPGTDEFRELC 44

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1622855660  1121 DIDECQHHHLCAHG-QCRNTEGSFQCVCDQGYRAsglGDHCE 1161
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYTD---GRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1622855660  1039 DVDECLEPNVCTNG-DCSNLEGSYMCSCHKGYTrtpDHKHCK 1079
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 1622855660   627 DINECQLQGVCPNG-ECLNTMGSYRCTCKIGF 657
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGY 32

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1622855660  1619 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1653
Cdd:smart00179    1 DIDECASGNP----CQNgGTCVNTVGSYRCECPPGY 32

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
                   ....*....|....*....|....*....|....*..
gi 1622855660  568 QCGKALPG-LSKQEDCCGTVGTSWGfNKCQKCPKKPS 603
Cdd:pfam00683    2 RCSNPLPGnVTKSECCCTSVGRAWG-SPCELCPPPGT 37

Calcium-binding EGF-like domain;

                            10        20
                    ....*....|....*....|....*...
gi 1622855660  1424 DMDECQDPSSCIDG-QCVNTEGSYNCFC 1450
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCEC 28

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 1622855660  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 1622855660 1492 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1534
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 1622855660 1203 DINECEHPGLCGPQGECLNTEGSFHCVCQQGFSisadGRTCE 1244
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 1622855660 1121 DIDECQHHHLC-AHGQCRNTEGSFQCVCDQGYRasglGDHCE 1161
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 1622855660 1080 DIDECQQGNLCVN-GQCKNTEGSFRCTCGQGYQL 1112
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1622855660   916 DIDECTQVqHLCSQG-RCENTEGSFLCICPAGFmasEEGTNCI 957
Cdd:smart00179    1 DIDECASG-NPCQNGgTCVNTVGSYRCECPPGY---TDGRNCE 39

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855660 1162 DINECLEDKSVCQR-GDCINTAGSYDCTCPDG 1192
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 1622855660 1039 DVDECLEPNVCTN-GDCSNLEGSYMCSCHKGYT 1070
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1622855660  1619 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1653
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 1622855660  916 DIDECTQvQHLCS-QGRCENTEGSFLCICPAGFmaseEGTNCI 957
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 1622855660 1619 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1653
Cdd:cd00054      1 DIDECASGNP----CQNgGTCVNTVGSYRCSCPPGY 32

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
                   ....*....|....*....|....*....|....*..
gi 1622855660  568 QCGKALPG-LSKQEDCCGTVGTSWGfNKCQKCPKKPS 603
Cdd:pfam00683    2 RCSNPLPGnVTKSECCCTSVGRAWG-SPCELCPPPGT 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
                   ....*....|....*....|....*....|....
gi 1622855660  958 DVDECLRPDVCGEGH-CVNTVGAFRCEyCDSGYR 990
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 1622855660  999 DIDECLNPSTC-PDEQCVNSPGSYQCVpCTEGFRG 1032
Cdd:cd00054      1 DIDECASGNPCqNGGTCVNTVGSYRCS-CPPGYTG 34

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 1622855660   999 DIDECLNPSTC-PDEQCVNSPGSYQCVpCTEGFR 1031
Cdd:smart00179    1 DIDECASGNPCqNGGTCVNTVGSYRCE-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 1622855660 1063 CSCHKGYTRTPDHKHCKDIDE 1083
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 1622855660  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 1622855660 1492 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1534
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 1622855660 1203 DINECEHPGLCGPQGECLNTEGSFHCVCQQGFSisadGRTCE 1244
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 1622855660 1121 DIDECQHHHLC-AHGQCRNTEGSFQCVCDQGYRasglGDHCE 1161
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 1622855660 1080 DIDECQQGNLCVN-GQCKNTEGSFRCTCGQGYQL 1112
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1622855660   916 DIDECTQVqHLCSQG-RCENTEGSFLCICPAGFmasEEGTNCI 957
Cdd:smart00179    1 DIDECASG-NPCQNGgTCVNTVGSYRCECPPGY---TDGRNCE 39

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855660 1162 DINECLEDKSVCQR-GDCINTAGSYDCTCPDG 1192
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 1622855660 1039 DVDECLEPNVCTN-GDCSNLEGSYMCSCHKGYT 1070
Cdd:cd00054      1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1622855660  1619 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1653
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 1622855660  916 DIDECTQvQHLCS-QGRCENTEGSFLCICPAGFmaseEGTNCI 957
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 1622855660 1619 DVNECDELNNrmslCKN-AKCINTEGSYKCLCLPGY 1653
Cdd:cd00054      1 DIDECASGNP----CQNgGTCVNTVGSYRCSCPPGY 32

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
                   ....*....|....*....|....*....|....*..
gi 1622855660  568 QCGKALPG-LSKQEDCCGTVGTSWGfNKCQKCPKKPS 603
Cdd:pfam00683    2 RCSNPLPGnVTKSECCCTSVGRAWG-SPCELCPPPGT 37

Epidermal growth factor-like domain;

                            10        20
                    ....*....|....*....|....*....
gi 1622855660  1124 ECQHHHLCAHGQCRNTEGSFQCVCDQGYR 1152
Cdd:smart00181    1 ECASGGPCSNGTCINTPGSYTCSCPPGYT 29

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 1622855660  958 DVDECLRPDVCGEGH-CVNTVGAFRCEyCDSGYR 990
Cdd:cd00054      1 DIDECASGNPCQNGGtCVNTVGSYRCS-CPPGYT 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855660  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 1622855660 1206 ECEHPGLCGPQGECLNTEGSFHCVCQQGFS 1235
Cdd:cd00053      1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYT 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 1622855660 1227 HCVCQQGFSISADGRTCEDVNE 1248
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 1622855660 1187 CTCPDGFQLD-DNKTCQDINE 1206
Cdd:pfam12662    2 CSCPPGYQLDpDGRTCVDIDE 22

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1622855660 1203 DINECEHPG-LCGPQGECLNTEGSFHCVCQQG 1233
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 1622855660 1063 CSCHKGYTRTPDHKHCKDIDE 1083
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22