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        30
                   ....*....|....*....|....*....|....*.
gi 442630815   754 CQKQNGGCSHRCSNTEGSFKCSCPPGYELDSDQKTC 789
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

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        30
                   ....*....|....*....|....*....|....*.
gi 442630815   296 CLESNGGCSEICENLPGEYKCSCQEGYYLDESGKSC 331
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630815  919 CPRFQAPRNGKSHCNRYRHKqklfYYSRCRISCNSGYILQGPEIKSCDANGIWEGPETKCV 979
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYS----YGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

104 kDa microneme/rhoptry antigen; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630815  826 EIPTASSLPESPKielkTPKYPdftelsnEIPENPKKPAEfdypePKFPSLPKWEGLPKLPPLADIPTSkapvPLRPEVP 905
Cdd:PTZ00449  571 KIPTLSKKPEFPK----DPKHP-------KDPEEPKKPKR-----PRSAQRPTRPKSPKLPELLDIPKS----PKRPESP 630

                  ..
gi 442630815  906 KS 907
Cdd:PTZ00449  631 KS 632

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630815  1277 CPPSIEVYLKENQNLRSVVWDEPRFE---GKLLKIYKSHFPGSLFKVGDHAIKYEATTTDGKTLSCTFFIYV 1345
Cdd:pfam02494   10 CPNNIVRTVELGTSTVRVFFTEPTAFdnsGQAILVSRTAQPGDFFPVGTTTVTYVAYDNSGNRASCTFTVTV 81

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        30
                   ....*....|....*....|....*....|
gi 442630815   476 CAHECQDLPeGSYRCVCPKGYELSEDQHSC 505
Cdd:pfam14670    8 CSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36

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 442630815   396 TCNSGFQLSADGTDCQDINE 415
Cdd:pfam12662    3 SCPPGYQLDPDGRTCVDIDE 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        30
                   ....*....|....*....|....*....|....*.
gi 442630815   754 CQKQNGGCSHRCSNTEGSFKCSCPPGYELDSDQKTC 789
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

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        30
                   ....*....|....*....|....*....|....*.
gi 442630815   296 CLESNGGCSEICENLPGEYKCSCQEGYYLDESGKSC 331
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630815  919 CPRFQAPRNGKSHCNRYRHKqklfYYSRCRISCNSGYILQGPEIKSCDANGIWEGPETKCV 979
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYS----YGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630815    919 CPRFQAPRNGKSHCnryrHKQKLFYYSRCRISCNSGYILQGPEIKSCDANGIWEGPETKC 978
Cdd:smart00032    1 CPPPPDIENGTVTS----SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

104 kDa microneme/rhoptry antigen; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630815  826 EIPTASSLPESPKielkTPKYPdftelsnEIPENPKKPAEfdypePKFPSLPKWEGLPKLPPLADIPTSkapvPLRPEVP 905
Cdd:PTZ00449  571 KIPTLSKKPEFPK----DPKHP-------KDPEEPKKPKR-----PRSAQRPTRPKSPKLPELLDIPKS----PKRPESP 630

                  ..
gi 442630815  906 KS 907
Cdd:PTZ00449  631 KS 632

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 442630815  750 DIDECQKQNG-GCSHRCSNTEGSFKCSCPPGYELDS 784
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTGRN 36

HYR domain; This domain is known as the HYR (Hyalin Repeat) domain, after the protein hyalin that is composed exclusively of this repeat. This domain probably corresponds to a new superfamily in the immunoglobulin fold. The function of this domain is uncertain it may be involved in cell adhesion.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630815  1277 CPPSIEVYLKENQNLRSVVWDEPRFE---GKLLKIYKSHFPGSLFKVGDHAIKYEATTTDGKTLSCTFFIYV 1345
Cdd:pfam02494   10 CPNNIVRTVELGTSTVRVFFTEPTAFdnsGQAILVSRTAQPGDFFPVGTTTVTYVAYDNSGNRASCTFTVTV 81

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 442630815   552 DIDECAEDTHLC--SHTCQNTPGGYQCQCPEG 581
Cdd:pfam07645    1 DVDECATGTHNCpaNTVCVNTIGSFECRCPDG 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 442630815  290 CLDIDECLESNGGCSEICENLPGEYKCSCQEGYYLDESGKS 330
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 442630815    412 DINECEVDGPedldnnavCQQ--KCENTIGSFRCTCVEGYHlleDQRSC 458
Cdd:smart00179    1 DIDECASGNP--------CQNggTCVNTVGSYRCECPPGYT---DGRNC 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 442630815  412 DINECEVDGPedldnnavCQ--QKCENTIGSFRCTCVEGYHL 451
Cdd:cd00054     1 DIDECASGNP--------CQngGTCVNTVGSYRCSCPPGYTG 34

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442630815  992 CPALKPAQNGVIlpaSCTQGPSRFGDVCRLQCNAGFVSTGSLLTACMMLQGWS 1044
Cdd:cd00033     1 CPPPPVPENGTV---TGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWS 50

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 442630815  671 CLDVDECAgLLSGGCSHECINKAGTFECGCPLGYILNDDGRS 712
Cdd:cd01475   184 CVVPDLCA-TLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

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        30
                   ....*....|....*....|....*....|....*.
gi 442630815   754 CQKQNGGCSHRCSNTEGSFKCSCPPGYELDSDQKTC 789
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

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        30
                   ....*....|....*....|....*....|....*.
gi 442630815   296 CLESNGGCSEICENLPGEYKCSCQEGYYLDESGKSC 331
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630815  919 CPRFQAPRNGKSHCNRYRHKqklfYYSRCRISCNSGYILQGPEIKSCDANGIWEGPETKCV 979
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYS----YGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630815    919 CPRFQAPRNGKSHCnryrHKQKLFYYSRCRISCNSGYILQGPEIKSCDANGIWEGPETKC 978
Cdd:smart00032    1 CPPPPDIENGTVTS----SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

104 kDa microneme/rhoptry antigen; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630815  826 EIPTASSLPESPKielkTPKYPdftelsnEIPENPKKPAEfdypePKFPSLPKWEGLPKLPPLADIPTSkapvPLRPEVP 905
Cdd:PTZ00449  571 KIPTLSKKPEFPK----DPKHP-------KDPEEPKKPKR-----PRSAQRPTRPKSPKLPELLDIPKS----PKRPESP 630

                  ..
gi 442630815  906 KS 907
Cdd:PTZ00449  631 KS 632

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 442630815  750 DIDECQKQNG-GCSHRCSNTEGSFKCSCPPGYELDS 784
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTGRN 36

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 442630815   773 KCSCPPGYELDSDQKTCQDIDE 794
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        30
                   ....*....|....*....|....*....|....
gi 442630815   425 DNNAVCQQKCENTIGSFRCTCVEGYHLLEDQRSC 458
Cdd:pfam14670    3 VNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 442630815   552 DIDECAEDTHLC--SHTCQNTPGGYQCQCPEG 581
Cdd:pfam07645    1 DVDECATGTHNCpaNTVCVNTIGSFECRCPDG 32

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20        30
                   ....*....|....*....|....*....|..
gi 442630815   754 CQKQNGGCSH--RCSNTEGSFKCSCPPGYELD 783
Cdd:pfam12947    1 CSDNNGGCHPnaTCTNTGGSFTCTCNDGYTGD 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 442630815  552 DIDECAEDtHLCSH--TCQNTPGGYQCQCPEG 581
Cdd:cd00054     1 DIDECASG-NPCQNggTCVNTVGSYRCSCPPG 31

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 442630815  290 CLDIDECLESNGGCSEICENLPGEYKCSCQEGYYLDESGKS 330
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 442630815    412 DINECEVDGPedldnnavCQQ--KCENTIGSFRCTCVEGYHlleDQRSC 458
Cdd:smart00179    1 DIDECASGNP--------CQNggTCVNTVGSYRCECPPGYT---DGRNC 38

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 442630815   412 DINECeVDGPEDLDNNAVCqqkcENTIGSFRCTCVEG 448
Cdd:pfam07645    1 DVDEC-ATGTHNCPANTVC----VNTIGSFECRCPDG 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 442630815   315 KCSCQEGYYLDESGKSCVDINE 336
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        40
                  ....*....|....*....|....*....|....*....|..
gi 442630815  412 DINECEVDGPedldnnavCQ--QKCENTIGSFRCTCVEGYHL 451
Cdd:cd00054     1 DIDECASGNP--------CQngGTCVNTVGSYRCSCPPGYTG 34

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 442630815   556 CAEDTHLCSHTCQNTPGGYQCQCPEGLNL 584
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYEL 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        40
                  ....*....|....*....|....*....|....*....|...
gi 442630815  292 DIDEClESNGGCSE--ICENLPGEYKCSCQEGYyldeSGKSCV 332
Cdd:cd00054     1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGY----TGRNCE 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 442630815  410 CQDINECEVdgpEDLDnnavCQQKCENTIGSFRCTCVEGYHLLEDQRS 457
Cdd:cd01475   184 CVVPDLCAT---LSHV----CQQVCISTPGSYLCACTEGYALLEDNKT 224

Epidermal growth factor-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 442630815    753 ECQkQNGGCSH-RCSNTEGSFKCSCPPGYELDsdqKTCQ 790
Cdd:smart00181    1 ECA-SGGPCSNgTCINTPGSYTCSCPPGYTGD---KRCE 35

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20
                   ....*....|....*....|....*...
gi 442630815   556 CAEDTHLCSH--TCQNTPGGYQCQCPEG 581
Cdd:pfam12947    1 CSDNNGGCHPnaTCTNTGGSFTCTCNDG 28