Laminin G domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145386553  329 FRTYDSEGIILYAESLDHSNWLLIALREGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNIN 408
Cdd:pfam00054   1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145386553  409 KLGSlfkpTDGFLD--TKIYFAGLPRKVESALIKPINPRLDGCIRG--WNLMKQG 459
Cdd:pfam00054  81 SPLG----ATTDLDvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDviVNGKPLD 131

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 145386553  168 NGGCSQTCDNTPGSYHCSCKIGFAMLTNKKDC 199
Cdd:pfam14670   5 NGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 145386553   201 DVDECSLkPSVCGT-AVCKNIPGDFECECPNGYR 233
Cdd:smart00179   1 DIDECAS-GNPCQNgGTCVNTVGSYRCECPPGYT 33

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 145386553  226 CECPNGYRYDPSSKSCKDVDE 246
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22

Laminin G domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145386553  329 FRTYDSEGIILYAESLDHSNWLLIALREGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNIN 408
Cdd:pfam00054   1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145386553  409 KLGSlfkpTDGFLD--TKIYFAGLPRKVESALIKPINPRLDGCIRG--WNLMKQG 459
Cdd:pfam00054  81 SPLG----ATTDLDvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDviVNGKPLD 131

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145386553 312 YLKFRLPDI--TRFSAEFDFRTYDSEGIILYAESLDHSNWLLIALREGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVE 389
Cdd:cd00110    9 YVRLPTLPAprTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVE 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145386553 390 ELDDSVSIKIAKEAVMNINKLGSLFkptDGFLDTKIYFAGLPRKVESALIkPINPRLDGCIRGWNL 455
Cdd:cd00110   89 RNGRSVTLSVDGERVVESGSPGGSA---LLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 145386553   46 LEETKKGNLERECIEELCNKEEAREVFENNPETDYFYPKY 85
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKY 40

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 145386553  247 CSENT--CAQLCVNYPGGYSCYCDgkKGFKLAQDQRSC 282
Cdd:pfam14670   1 CSVNNggCSHLCLNTPGGYTCSCP--EGYELQDDGRTC 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 145386553 157 DINECKDPSN-INGGcsqTCDNTPGSYHCSCKIGF 190
Cdd:cd00054    1 DIDECASGNPcQNGG---TCVNTVGSYRCSCPPGY 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 145386553 201 DVDECSLkPSVCG-TAVCKNIPGDFECECPNGYR 233
Cdd:cd00054    1 DIDECAS-GNPCQnGGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 145386553   243 DVDEC-SENTCAQ--LCVNYPGGYSCYCDGkkGFklaQDQRSCE 283
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPP--GY---TDGRNCE 39

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 145386553  226 CECPNGYRYDPSSKSCKDVDE 246
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22

Laminin G domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145386553  329 FRTYDSEGIILYAESLDHSNWLLIALREGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNIN 408
Cdd:pfam00054   1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145386553  409 KLGSlfkpTDGFLD--TKIYFAGLPRKVESALIKPINPRLDGCIRG--WNLMKQG 459
Cdd:pfam00054  81 SPLG----ATTDLDvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDviVNGKPLD 131

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145386553 312 YLKFRLPDI--TRFSAEFDFRTYDSEGIILYAESLDHSNWLLIALREGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVE 389
Cdd:cd00110    9 YVRLPTLPAprTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVE 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145386553 390 ELDDSVSIKIAKEAVMNINKLGSLFkptDGFLDTKIYFAGLPRKVESALIkPINPRLDGCIRGWNL 455
Cdd:cd00110   89 RNGRSVTLSVDGERVVESGSPGGSA---LLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 145386553   46 LEETKKGNLERECIEELCNKEEAREVFENNPETDYFYPKY 85
Cdd:pfam00594   1 LEELKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKY 40

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 145386553  168 NGGCSQTCDNTPGSYHCSCKIGFAMLTNKKDC 199
Cdd:pfam14670   5 NGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 145386553   157 DINECKDPSN-INGGcsqTCDNTPGSYHCSCKIGFamlTNKKDCK 200
Cdd:smart00179   1 DIDECASGNPcQNGG---TCVNTVGSYRCECPPGY---TDGRNCE 39

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 145386553   201 DVDECSLkPSVCGT-AVCKNIPGDFECECPNGYR 233
Cdd:smart00179   1 DIDECAS-GNPCQNgGTCVNTVGSYRCECPPGYT 33

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 145386553 241 CKDVDECSE--NTCAQLCVNYPGGYSCYCdgKKGFKLAQDQRS 281
Cdd:cd01475  184 CVVPDLCATlsHVCQQVCISTPGSYLCAC--TEGYALLEDNKT 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
                 ....*....|....*....|....*....|....*...
gi 145386553 119 DQCDPM-PCNEDGylSCKDGQGAFTCICKPGWQGDKCQ 155
Cdd:cd00054    3 DECASGnPCQNGG--TCVNTVGSYRCSCPPGYTGRNCE 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 145386553 155 QFDINECKDPS---NINGGCSQTCDNTPGSYHCSCKIGFAMLTNKK 197
Cdd:cd01475  178 KFQGKICVVPDlcaTLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223

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 145386553 243 DVDEC-SENTCA--QLCVNYPGGYSCYCDgkKGFKLaqdqRSCE 283
Cdd:cd00054    1 DIDECaSGNPCQngGTCVNTVGSYRCSCP--PGYTG----RNCE 38