Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 564332154   123 DVDECTQAiHDCRPSQDCHNLPGSYQCTCPDGYRkIGPECV 163
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*...
gi 564332154  283 DIDECETGAHQCSEAQTCVNFHGGYRCV 310
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28

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 564332154 203 DVNECDMGAPCE--QRCFNSYGTFLCRCNQGYELHR 236
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGRN 36

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 564332154   123 DVDECTQAiHDCRPSQDCHNLPGSYQCTCPDGYRkIGPECV 163
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-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        40
                 ....*....|....*....|....*....|....*....|.
gi 564332154 123 DVDECTQAiHDCRPSQDCHNLPGSYQCTCPDGYRkiGPECV 163
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*...
gi 564332154  283 DIDECETGAHQCSEAQTCVNFHGGYRCV 310
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28

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 564332154 162 CVDIDECRY--RYCQHRCVNLPGSFRCQCEPGFQLGPNNRS 200
Cdd:cd01475  184 CVVPDLCATlsHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

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 564332154 203 DVNECDMGAPCE--QRCFNSYGTFLCRCNQGYELHR 236
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGRN 36

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 564332154   203 DVNECDMGAPCEQ--RCFNSYGTFLCRCNQGYELHRD 237
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37

Calcium-binding EGF-like domain;

                           10        20
                   ....*....|....*....|....*...
gi 564332154   283 DIDECETGaHQCSEAQTCVNFHGGYRCV 310
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCE 27

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 564332154   123 DVDECTQAiHDCRPSQDCHNLPGSYQCTCPDGYRkIGPECV 163
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-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        40
                 ....*....|....*....|....*....|....*....|.
gi 564332154 123 DVDECTQAiHDCRPSQDCHNLPGSYQCTCPDGYRkiGPECV 163
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*...
gi 564332154  283 DIDECETGAHQCSEAQTCVNFHGGYRCV 310
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28

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 564332154 162 CVDIDECRY--RYCQHRCVNLPGSFRCQCEPGFQLGPNNRS 200
Cdd:cd01475  184 CVVPDLCATlsHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

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 564332154  185 RCQCEPGFQLGPNNRSCVDVNE 206
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 564332154 203 DVNECDMGAPCE--QRCFNSYGTFLCRCNQGYELHR 236
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGRN 36

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 564332154 241 CSDIDECSYSSYLCQYRCVNEPGRFSCHCPQGYQLL 276
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALL 219

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 564332154 198 NRSCVDVNECDMGAP-CEQRCFNSYGTFLCRCNQGYELHRDG 238
Cdd:cd01475  181 GKICVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDN 222

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 564332154  226 CRCNQGYELHRDGFSCSDIDE 246
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                           10        20
                   ....*....|....*....|....*...
gi 564332154   283 DIDECETGaHQCSEAQTCVNFHGGYRCV 310
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCE 27