Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317613  97 DNASLEATFV-KRCCHCCLLGRAAQAQGQSCEYSL---MVGYQCGQVFQACCVKSQETGD 152
Cdd:cd00017     1 KNSEKAAQYKdKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRD 60

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1676317613  356 DVDECAPPAePCGKGHRCVNSPGSFRCECKTGYY 389
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33

Calcium-binding EGF domain;

                          10        20
                  ....*....|....*....|....*...
gi 1676317613 262 DIDECESGIHNCLPDFICQNTLGSFRCR 289
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1676317613  308 DINECLSISaPCPIGHTCINTEGSYTCQknvpnCGRGYHlneEGTRCV 355
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCE-----CPPGYT---DGRNCE 39

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317613  97 DNASLEATFV-KRCCHCCLLGRAAQAQGQSCEYSL---MVGYQCGQVFQACCVKSQETGD 152
Cdd:cd00017     1 KNSEKAAQYKdKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRD 60

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1676317613  356 DVDECAPPAePCGKGHRCVNSPGSFRCECKTGYY 389
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1676317613 525 DIDECVTGIHNCSINETCFNIQGGFRCLafeCPEN 559
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 32

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 1676317613 479 CEDIDECAlpTGGHICSYRCINIPGSFQCSCpSSGYRLAPNGRN 522
Cdd:cd01475   184 CVVPDLCA--TLSHVCQQVCISTPGSYLCAC-TEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1676317613  308 DINECLSISaPCPIGHTCINTEGSYTCQknvpnCGRGYHlneEGTRCV 355
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCE-----CPPGYT---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 1676317613 308 DINECLSISaPCPIGHTCINTEGSYTCQknvpnCGRGYHL 347
Cdd:cd00054     1 DIDECASGN-PCQNGGTCVNTVGSYRCS-----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 1676317613 506 QCSCPSsGYRLAPNGRNCQDIDE 528
Cdd:pfam12662   1 TCSCPP-GYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1676317613  262 DIDECESGiHNCLPDFICQNTLGSFRCrpklQCKSGF 298
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRC----ECPPGY 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 1676317613 424 CSCSVGFRLSVDGRSCEDINE 444
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676317613  97 DNASLEATFV-KRCCHCCLLGRAAQAQGQSCEYSL---MVGYQCGQVFQACCVKSQETGD 152
Cdd:cd00017     1 KNSEKAAQYKdKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRD 60

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1676317613  356 DVDECAPPAePCGKGHRCVNSPGSFRCECKTGYY 389
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1676317613 525 DIDECVTGIHNCSINETCFNIQGGFRCLafeCPEN 559
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 32

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 1676317613 479 CEDIDECAlpTGGHICSYRCINIPGSFQCSCpSSGYRLAPNGRN 522
Cdd:cd01475   184 CVVPDLCA--TLSHVCQQVCISTPGSYLCAC-TEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1676317613  308 DINECLSISaPCPIGHTCINTEGSYTCQknvpnCGRGYHlneEGTRCV 355
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCE-----CPPGYT---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 1676317613 308 DINECLSISaPCPIGHTCINTEGSYTCQknvpnCGRGYHL 347
Cdd:cd00054     1 DIDECASGN-PCQNGGTCVNTVGSYRCS-----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 1676317613 506 QCSCPSsGYRLAPNGRNCQDIDE 528
Cdd:pfam12662   1 TCSCPP-GYQLDPDGRTCVDIDE 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
                  ....*....|....*....|....*....|....*
gi 1676317613 354 CVDVDECAppAEPCGKGHRCVNSPGSFRCECKTGY 388
Cdd:cd01475   184 CVVPDLCA--TLSHVCQQVCISTPGSYLCACTEGY 216

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 1676317613 399 DVNECQRYPGRLCGHKCENTLGSYLCSCSVGFRlsvdGRSCE 440
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38

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 1676317613 395 RMCVDVNECQRYPgRLCGHKCENTLGSYLCSCSVGFRLSVDGRS 438
Cdd:cd01475   182 KICVVPDLCATLS-HVCQQVCISTPGSYLCACTEGYALLEDNKT 224