Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412955480 1295 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 1374
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1412955480 1375 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 1426
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412955480  1025 ATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFD 1104
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1412955480  1105 PTTAfrAPDVARALLRQIQVSrRRSLGVRRplQEHVRFMDFDWFP 1149
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQA-AYSLKITN--VNVVDVLDPDSAD 120

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1412955480   384 ECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPC 429
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1412955480   599 VCDFSCQSVPgSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 645
Cdd:smart00280    1 DCPEACPREY-DPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1412955480   514 VCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPC 559
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1412955480  742 CSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG 778
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1412955480   167 CPATCRGAPEgTVCGSDGADYPGECQLLRRACARQENVFKKFDGPC 212
Cdd:smart00280    2 CPEACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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 1412955480 1720 ASGHPCLNGASCVPREAAYVCLCPGGFSGPHCE 1752
Cdd:cd00054      6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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
                   ....*....|....*....|....*....|.
gi 1412955480 1450 PNPCHGGAPCQNLEaGRFHCQCPPGRVGPTC 1480
Cdd:cd00054      8 GNPCQNGGTCVNTV-GSYRCSCPPGYTGRNC 37

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412955480 1295 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 1374
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1412955480 1375 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 1426
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412955480 1563 FLARGPSGLLLYNGQKTDGkgDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVL 1642
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1412955480 1643 GESPKSRKvphTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLL 1698
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 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 1412955480 1765 TLAFDGRTFVEYLNavteSEKALQSNHFELSLRTEATQGLVLWSGKATeRADYVALAIVDGHLQLSYNLGSQPVVLRSTV 1844
Cdd:cd00110      1 GVSFSGSSYVRLPT----LPAPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1412955480 1845 PVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVV 1921
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150

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 1412955480 1535 FNGFSHLELRGLHTFARDlgekMALEVVFLARGPSGLLLYNGQKTdgKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPV 1614
Cdd:cd00110      4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1412955480 1615 TLGAWTRVSLERNGRKGALRVgDGPRVLgESPKSRKVPHtvLNLKEPLYVGGAPDFSKLaRAAAVSSGFDGAIQLVSL 1692
Cdd:cd00110     78 NDGQWHSVSVERNGRSVTLSV-DGERVV-ESGSPGGSAL--LNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412955480  1025 ATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFD 1104
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1412955480  1105 PTTAfrAPDVARALLRQIQVSrRRSLGVRRplQEHVRFMDFDWFP 1149
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQA-AYSLKITN--VNVVDVLDPDSAD 120

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1412955480  687 ACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNF 728
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1412955480   384 ECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPC 429
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1412955480   449 VCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPC 494
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1412955480  389 CSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPC 429
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1412955480   97 CPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPC 137
Cdd:cd00104      1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1412955480  450 CPSECvalaQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPC 494
Cdd:cd00104      1 CPKEY----DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1412955480   817 VCPMlTCPEANAtKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPC 864
Cdd:smart00280    1 DCPE-ACPREYD-PVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1412955480  610 SPVCGSDGVTYSTECELKKARCESQRGLYVAAQGAC 645
Cdd:cd00104      6 DPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1412955480  741 PCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDG---RALGPAGCE 787
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGyygLPSQGGGCQ 50

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1412955480   311 CDRVtCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPC 356
Cdd:smart00280    2 CPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1412955480  600 CDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGL 637
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 39

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1412955480  244 CPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQC 284
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1412955480  384 ECLQACS-SLYDPVCGSDGVTYGSACELEATACTLGREIQ---VARKGPC 429
Cdd:pfam07648    1 NCNCQCPkTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1412955480  513 CVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARA---GPC 559
Cdd:pfam07648    1 NCNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKVkydGSC 50

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1412955480   97 CPSVV-APVCGSDASTYSNECELQRAQCSQQRRIR---LLSRGPC 137
Cdd:pfam07648    6 CPKTEyEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1412955480  179 VCGSDGADYPGECQLLRRACARQENVFKKFDGPC 212
Cdd:cd00104      8 VCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1412955480  822 TCPEANATKVCGSDGVTYGNECQLKTIACRQGLQIS---IQSLGPC 864
Cdd:pfam07648    5 QCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50

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 1412955480 1450 PNPCHGGAPCQNLEaGRFHCQCPPGRVGPTC 1480
Cdd:cd00054      8 GNPCQNGGTCVNTV-GSYRCSCPPGYTGRNC 37

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1412955480  167 CPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFK---KFDGPC 212
Cdd:pfam07648    2 CNCQCPKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEekvKYDGSC 50

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 1412955480 1228 CDSQ-PCFHGGTCQDwaLGGGFTCSCPAGRGGAVCE 1262
Cdd:cd00054      5 CASGnPCQNGGTCVN--TVGSYRCSCPPGYTGRNCE 38

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412955480 1295 FRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGE 1374
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1412955480 1375 SPSGTDG-LNLDTDLFVGGVPEDqaAVALERTFVGAGLRGCIRLLDVNNQRLE 1426
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1412955480 1563 FLARGPSGLLLYNGQKTDGkgDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVL 1642
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTER--DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1412955480 1643 GESPKSRKvphTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLL 1698
Cdd:pfam00054   79 GESPLGAT---TDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 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 1412955480 1765 TLAFDGRTFVEYLNavteSEKALQSNHFELSLRTEATQGLVLWSGKATeRADYVALAIVDGHLQLSYNLGSQPVVLRSTV 1844
Cdd:cd00110      1 GVSFSGSSYVRLPT----LPAPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1412955480 1845 PVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPkaYGTGFVGCLRDVVV 1921
Cdd:cd00110     76 PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150