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 1847916741 275 CQHECVNQPGTYFCSCPPGYILLDDNRSC 303
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 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 1847916741 192 GYCQQLCANVPGSYSCTCNPGFTLNEDGRSC 222
Cdd:pfam14670   6 GGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 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
                  ....*....|....*....|....*....
gi 1847916741 275 CQHECVNQPGTYFCSCPPGYILLDDNRSC 303
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

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 1847916741 224 DVNECATENPCV--QTCVNTYGSFICRCDPGYEL 255
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 1847916741 262 CSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRS 302
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1847916741  144 DVDECATDsHQCNPTQICINTEGGYTCSCTDGY 176
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32

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 1847916741 228 CATEN-PCVQTCVNTYGSFICRCDPGYELEEDGVHC 262
Cdd:pfam14670   1 CSVNNgGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1847916741  264 DMDECSfSEFLCQH--ECVNQPGTYFCSCPPGYIlldDNRSCQ 304
Cdd:smart00179   1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

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 1847916741 275 CQHECVNQPGTYFCSCPPGYILLDDNRSC 303
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

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 1847916741 224 DVNECATENPCV--QTCVNTYGSFICRCDPGYEL 255
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 1847916741 262 CSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRS 302
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 1847916741 213 FTLNEDGRSCQDVNECATENP-CVQTCVNTYGSFICRCDPGYELEEDGV 260
Cdd:cd01475   175 LTKKFQGKICVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDNK 223

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1847916741  144 DVDECATDsHQCNPTQICINTEGGYTCSCTDGY 176
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 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 1847916741 178 LLEGQCLDIDECRYG--YCQQLCANVPGSYSCTCNPGFTLNEDGRS 221
Cdd:cd01475   179 FQGKICVVPDLCATLshVCQQVCISTPGSYLCACTEGYALLEDNKT 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 1847916741 288 CSCPPGYILLDDNRSCQDINE 308
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1847916741 224 DVNECATE-NPCVQ--TCVNTYGSFICRCDPG 252
Cdd:pfam07645   1 DVDECATGtHNCPAntVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1847916741  264 DMDECSfSEFLCQH--ECVNQPGTYFCSCPPGYIlldDNRSCQ 304
Cdd:smart00179   1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1847916741 227 ECATENPCV--QTCVNTYGSFICRCDPGYELE 256
Cdd:cd00053     1 ECAASNPCSngGTCVNTPGSYRCVCPPGYTGD 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
                  ....*....|....*....|....*...
gi 1847916741 195 QQLCANVPGSYSCTCNPGFTLneDGRSC 222
Cdd:pfam12947  11 NATCTNTGGSFTCTCNDGYTG--DGVTC 36