Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720365230 173 DIDECTSGTHNCRTDQVCINLRGSFTCQCLPG 204
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1720365230  254 DINECDASNQCAQ--QCYNILGSFICQCNQGYElssDRLNCE 293
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT---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
                  ....*....|....*....|....*...
gi 1720365230  44 DIDECDIVPDACKGGMKCVNHYGGYLCL 71
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720365230 173 DIDECTSGTHNCRTDQVCINLRGSFTCQCLPG 204
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        40
                  ....*....|....*....|....*....|....*....|.
gi 1720365230 173 DIDECTSGtHNCRTDQVCINLRGSFTCQCLPGYqkRGEQCV 213
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY--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 1720365230 214 DIDECTVPPYC--HQRCVNTPGSFYCQCSPGFQL 245
Cdd:cd00054     1 DIDECASGNPCqnGGTCVNTVGSYRCSCPPGYTG 34

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 1720365230 254 DINECDASNQCA--QQCYNILGSFICQCNQGYELssdrLNCE 293
Cdd:cd00054     1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTG----RNCE 38

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720365230 214 DIDECTVPPY-CHQR--CVNTPGSFYCQCSPG 242
Cdd:pfam07645   1 DVDECATGTHnCPANtvCVNTIGSFECRCPDG 32

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*...
gi 1720365230  44 DIDECDIVPDACKGGMKCVNHYGGYLCL 71
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720365230 173 DIDECTSGTHNCRTDQVCINLRGSFTCQCLPG 204
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        40
                  ....*....|....*....|....*....|....*....|.
gi 1720365230 173 DIDECTSGtHNCRTDQVCINLRGSFTCQCLPGYqkRGEQCV 213
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY--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 1720365230 214 DIDECTVPPYC--HQRCVNTPGSFYCQCSPGFQL 245
Cdd:cd00054     1 DIDECASGNPCqnGGTCVNTVGSYRCSCPPGYTG 34

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 1720365230 212 CVDIDEC-TVPPYCHQRCVNTPGSFYCQCSPGFQLAANNYT 251
Cdd:cd01475   184 CVVPDLCaTLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

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 1720365230 164 EQSEHNVCQDIDECTSGTHNCrtDQVCINLRGSFTCQCLPGY 205
Cdd:cd01475   177 KKFQGKICVVPDLCATLSHVC--QQVCISTPGSYLCACTEGY 216

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 1720365230 277 CQCNQGYELSSDRLNCEDINE 297
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22

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 1720365230 252 CVDINECD-ASNQCAQQCYNILGSFICQCNQGYELSSDRLN 291
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 1720365230 236 YCQCSPGFQLAANNYTCVDINE 257
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

Epidermal growth factor-like domain;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1720365230  217 ECTVPPYCHQ-RCVNTPGSFYCQCSPGFQLAAN 248
Cdd:smart00181   1 ECASGGPCSNgTCINTPGSYTCSCPPGYTGDKR 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
                  ....*....|....*....|....*.
gi 1720365230 294 DINECETTNECREDEMCWNYHGGFRC 319
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRC 26