Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564354450  1398 FRALETEGLLLYNGNARGKDFLALALLDGRVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGETPVVGE 1477
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564354450  1478 SPSGTDG-LNLDTNLYVGGIPEEqvAMVLDRTSVGVGLKGCIRMLDINNQQLE 1529
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564354450  1896 RTEATQGLVLWIGKAAERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRIRAHREHREGSLQVGNEAPVTGS 1975
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564354450  1976 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 2026
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 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 564354450   1130 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSVRLRELGPGKLVRAIVDVHFD 1209
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 564354450   1210 PTTAfqASDVGQALLRQIQVSRpWALAVRRplQEHVRFLDFDWFP 1254
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITN--VNVVDVLDPDSAD 120

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564354450    491 ECQRVCSGIYDPVCGSDGVTYGSVCELESMACTLGREIQVARRGPC 536
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 564354450    198 VCKKNaCPATVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564354450    621 VCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEAHAGPC 666
Cdd:smart00280    1 DCPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 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. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 564354450   351 CPAQHTPICGDDGVTYENDCVMSRIGATRGLLLQKVRSGQC 391
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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 564354450  423 CDGSYRPVCAQDGHTYNNDCWRQQAECRQQRAIPPKHQGPC 463
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

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 564354450 1819 ALGNPCLNGGSCVPREATYECLCPGGFSGLHCE 1851
Cdd:cd00054     6 ASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564354450  1398 FRALETEGLLLYNGNARGKDFLALALLDGRVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGETPVVGE 1477
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564354450  1478 SPSGTDG-LNLDTNLYVGGIPEEqvAMVLDRTSVGVGLKGCIRMLDINNQQLE 1529
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564354450  1896 RTEATQGLVLWIGKAAERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRIRAHREHREGSLQVGNEAPVTGS 1975
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564354450  1976 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 2026
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 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 564354450 1375 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGRVQFRFDTGSGPAVLTSLVPVEPGRWH 1453
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564354450 1454 RLELSRHWRQGTLSVDGETPVVGESPSGTDGLNLDTNLYVGGIPEEQvamVLDRTSVGVGLKGCIRMLDIN 1524
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL---KSPGLPVSPGFVGCIRDLKVN 151

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 564354450 1638 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFCYDLGKGAAVIRSKEPI 1717
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564354450 1718 ALGTWVRVFLERNGRKGALQVGDGPRVLGESPVPHTMLNLKEPLYIGGAPDFSKLaRGAAVSSGFNGVIQLVSL 1791
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150

Laminin G domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564354450   1662 LEMVFLARGPSGLLLYNGQKtdGKGDFVSLALHNRHLEFCYDLGKGAAVIRSK-EPIALGTWVRVFLERNGRKGALQVGD 1740
Cdd:smart00282    2 ISFSFRTTSPNGLLLYAGSK--GGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDG 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 564354450   1741 GPRVLGESPVPHTMLNLKEPLYIGGAPDFSKLARGaAVSSGFNGVIQLVSLRGH 1794
Cdd:smart00282   80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132

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 564354450   1130 ATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSVRLRELGPGKLVRAIVDVHFD 1209
Cdd:smart00200    1 PTQSFGVSLSVLSVEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGSVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 564354450   1210 PTTAfqASDVGQALLRQIQVSRpWALAVRRplQEHVRFLDFDWFP 1254
Cdd:smart00200   81 GVTN--GQDVEEDLLQVIKQAA-YSLKITN--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 564354450  795 CHCNPHGSYSGTCDPATGQCSCRPGVGGLRCDRCEPGFWNF 835
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42

Laminin-type epidermal growth factor-like domai;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 564354450    795 CHCNPHGSYSGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRG 837
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 564354450    198 VCKKNaCPATVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:smart00280    1 DCPEA-CPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 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 564354450  496 CSGIYDPVCGSDGVTYGSVCELESMACTLGREIQVARRGPC 536
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 564354450  204 CPATVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564354450    274 CPTTCFGAPDgTVCGSDGVDYPSECQLLSHACASQEHIFKKFNGPC 319
Cdd:smart00280    2 CPEACPREYD-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        40
                  ....*....|....*....|....*....|....*....|.
gi 564354450  561 CVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHC 601
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41

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

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 564354450   849 CSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDG 885
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPG 37

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 564354450    924 ICPTlTCPEaNSTKVCGSDGVTYGNECQLKAIACRQRLDISTQSLGPC 971
Cdd:smart00280    1 DCPE-ACPR-EYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 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 564354450  930 CPEaNSTKVCGSDGVTYGNECQLKAIACRQRLDISTQSLGPC 971
Cdd:cd00104     1 CPK-EYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 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 564354450  711 CQSVPRsPVCGSDGVTYGTECDLKKARCESQQELYVAAQGAC 752
Cdd:cd00104     1 CPKEYD-PVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 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
                  ....*....|....*....|....*....|....
gi 564354450  286 VCGSDGVDYPSECQLLSHACASQEHIFKKFNGPC 319
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        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 564354450   620 CVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEA---HAGPC 666
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. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 564354450   200 KKNACPATVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPC 244
Cdd:pfam00050    5 PSGACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 564354450    348 PENCPAQHTPICGDDGVTYENDCVMSRIGATRGLLLQKVRSGQC 391
Cdd:smart00280    3 PEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 564354450   1819 ALGNPCLNGGSCVPREATYECLCPGGFS-GLHCE 1851
Cdd:smart00179    6 ASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564354450   554 RCVCPsecVESAQPVCGSDGHTYASECELHVHACTHQISL 593
Cdd:pfam07648    3 NCQCP---KTEYEPVCGSDGVTYPSPCALCAAGCKLGKEV 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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564354450   416 CSCDRVTcdgsYRPVCAQDGHTYNNDCWRQQAECRQQR---AIPPKHQGPC 463
Cdd:pfam07648    4 CQCPKTE----YEPVCGSDGVTYPSPCALCAAGCKLGKevkEEKVKYDGSC 50

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564354450  1398 FRALETEGLLLYNGNARGKDFLALALLDGRVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGETPVVGE 1477
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564354450  1478 SPSGTDG-LNLDTNLYVGGIPEEqvAMVLDRTSVGVGLKGCIRMLDINNQQLE 1529
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSL--GVKKRRLAISPSFDGCIRDVIVNGKPLD 131

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564354450  1896 RTEATQGLVLWIGKAAERaDYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRIRAHREHREGSLQVGNEAPVTGS 1975
Cdd:pfam00054    2 RTTEPSGLLLYNGTQTER-DFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564354450  1976 SPLGATQ-LDTDGALWLGGLQKLPVgQALPKAYGTGFVGCLRDVVVGHRQLH 2026
Cdd:pfam00054   81 SPLGATTdLDVDGPLYVGGLPSLGV-KKRRLAISPSFDGCIRDVIVNGKPLD 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 564354450 1375 FKGHSFLAFPTLRA-YHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGRVQFRFDTGSGPAVLTSLVPVEPGRWH 1453
Cdd:cd00110     4 FSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564354450 1454 RLELSRHWRQGTLSVDGETPVVGESPSGTDGLNLDTNLYVGGIPEEQvamVLDRTSVGVGLKGCIRMLDIN 1524
Cdd:cd00110    84 SVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDL---KSPGLPVSPGFVGCIRDLKVN 151

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 564354450 1638 FNGFSYLELKGLHTFERDlgekMALEMVFLARGPSGLLLYNGQKTdgKGDFVSLALHNRHLEFCYDLGKGAAVIRSKEPI 1717
Cdd:cd00110     4 FSGSSYVRLPTLPAPRTR----LSISFSFRTTSPNGLLLYAGSQN--GGDFLALELEDGRLVLRYDLGSGSLVLSSKTPL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564354450 1718 ALGTWVRVFLERNGRKGALQVGDGPRVLGESPVPHTMLNLKEPLYIGGAPDFSKLaRGAAVSSGFNGVIQLVSL 1791
Cdd:cd00110    78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKS-PGLPVSPGFVGCIRDLKV 150