Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 71989803    304 DIDECVTGHNCGAGEECVNTPGSFRCQqkgnlCAHGYE 341
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE-----CPPGYT 33

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 71989803    476 DIDECSIWAGSGNDlcmGGCINTKGSYLCQCPPGYKiqpDGRTCV 520
Cdd:smart00179   1 DIDECASGNPCQNG---GTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 71989803    351 DVNECQQ-GVCGSM-ECINLPGTYKCKCGPGYEfndAKKRCE 390
Cdd:smart00179   1 DIDECASgNPCQNGgTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 71989803    391 DVDECIkfAGHVCDLSAECINTIGSFECKCKPGFQlasDGRRCE 434
Cdd:smart00179   1 DIDECA--SGNPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39

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 71989803 430 GRRCEDVNECTTGIAACEQKCVNIPGSYQCICDRGFALGPDG 471
Cdd:cd01475 181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222

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 71989803 391 DVDECikFAGHVCDLSAECINTIGSFECKCKPGFQlasdGRRCE 434
Cdd:cd00054   1 DIDEC--ASGNPCQNGGTCVNTVGSYRCSCPPGYT----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 71989803   504 CQCPPGYKIQPDGRTCVDVDE 524
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 71989803 474 CEDIDECSiwagSGNDLCMGGCINTKGSYLCQCPPGYKIQPDGRT 518
Cdd:cd01475 184 CVVPDLCA----TLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 71989803   435 DVNECTTGIAACEQ--KCVNIPGSYQCICDRG 464
Cdd:pfam07645   1 DVDECATGTHNCPAntVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 71989803    351 DVNECQQ-GVCGSM-ECINLPGTYKCKCGPGYEfndAKKRCE 390
Cdd:smart00179   1 DIDECASgNPCQNGgTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 71989803    391 DVDECIkfAGHVCDLSAECINTIGSFECKCKPGFQlasDGRRCE 434
Cdd:smart00179   1 DIDECA--SGNPCQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39

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 71989803 430 GRRCEDVNECTTGIAACEQKCVNIPGSYQCICDRGFALGPDG 471
Cdd:cd01475 181 GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDN 222

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 71989803 391 DVDECikFAGHVCDLSAECINTIGSFECKCKPGFQlasdGRRCE 434
Cdd:cd00054   1 DIDEC--ASGNPCQNGGTCVNTVGSYRCSCPPGYT----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 71989803   504 CQCPPGYKIQPDGRTCVDVDE 524
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 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 71989803   418 CKCKPGFQLASDGRRCEDVNE 438
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 71989803 474 CEDIDECSiwagSGNDLCMGGCINTKGSYLCQCPPGYKIQPDGRT 518
Cdd:cd01475 184 CVVPDLCA----TLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 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        40
                ....*....|....*....|....*....|....*....|....*..
gi 71989803 476 DIDECSIwagsgNDLCMGG--CINTKGSYLCQCPPGYKiqpdGRTCV 520
Cdd:cd00054   1 DIDECAS-----GNPCQNGgtCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 71989803   435 DVNECTTGIAACEQ--KCVNIPGSYQCICDRG 464
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 71989803   458 QCICDRGFALGPDGTKCEDIDE 479
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 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
                  ....*....|....*....|....*....
gi 71989803   446 CEQKCVNIPGSYQCICDRGFALGPDGTKC 474
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36