Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 124487159  953 GYLCPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:cd01327     2 VFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 124487159    573 FCTRENDPVRGPDGKTHGNKCAMCKAVFKKENEERKRKEGE 613
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGP 45

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 124487159    312 FCTRENDPIRGLDGKTHGNLCSMCQAFFKTEAEEKKAEAG 351
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDG 44

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
                    ....*....|....*....|....*
gi 124487159    176 CTRESDPILGPDGRTHGNRCAMCAE 200
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKA 30

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
                    ....*....|....*....|....*.
gi 124487159    715 CTRESDPTRGPDGAMHGNKCAMCKER 740
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKAA 31

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 124487159  953 GYLCPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:cd01327     2 VFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45

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 124487159   956 CPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 124487159    956 CPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:smart00280    6 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. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 124487159   111 ICPSDTSSVCGTDGKTYRSRCELCAENAKSQNHVDVKSEGEC 152
Cdd:pfam00050    8 ACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 124487159    312 FCTRENDPIRGLDGKTHGNLCSMCQAFFKTEAEEKKAEAG 351
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDG 44

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

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 124487159    783 ICTRENDPVRDADGKMHVNKCAMCQMMFEREANERKMRE 821
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHD 43

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 124487159   176 CTRESDPILGPDGRTHGNRCAMCAelflkeakENATRNRESRIRRDAE 223
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCA--------ENGKRGTNLHKVHDGE 48

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

                            10        20
                    ....*....|....*....|....*.
gi 124487159    715 CTRESDPTRGPDGAMHGNKCAMCKER 740
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKAA 31

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 124487159  574 CTRENDPVRGPDGKTHGNKCAMCKAVFKKENEERKRKEGE 613
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGE 44

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

                            10        20
                    ....*....|....*....|....*
gi 124487159    648 CTRESDPVRGVDGEHYNNKCVMCKE 672
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKA 30

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 124487159  953 GYLCPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:cd01327     2 VFGCPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45

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 124487159   956 CPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 124487159    956 CPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:smart00280    6 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 124487159  956 CPKNLNPVCGDDGQTYSNPCMLCHENLMRQTNTRIHKQGAC 996
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 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. Alignment also includes a single domain from transporters in the OATP/PGT family.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 124487159   111 ICPSDTSSVCGTDGKTYRSRCELCAENAKSQNHVDVKSEGEC 152
Cdd:pfam00050    8 ACPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49

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

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 124487159    240 FCTRESDPIRGPDGKMHGNKCALCAEIFMRQFTEEK 275
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEV 40

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 124487159    312 FCTRENDPIRGLDGKTHGNLCSMCQAFFKTEAEEKKAEAG 351
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDG 44

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

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 124487159    783 ICTRENDPVRDADGKMHVNKCAMCQMMFEREANERKMRE 821
Cdd:smart00280    5 ACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHD 43

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 124487159   176 CTRESDPILGPDGRTHGNRCAMCAelflkeakENATRNRESRIRRDAE 223
Cdd:pfam00050    9 CPRIYDPVCGTDGKTYSNECLFCA--------ENGKRGTNLHKVHDGE 48

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

                            10        20
                    ....*....|....*....|....*.
gi 124487159    715 CTRESDPTRGPDGAMHGNKCAMCKER 740
Cdd:smart00280    6 CPREYDPVCGSDGVTYSNECHLCKAA 31

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 124487159  574 CTRENDPVRGPDGKTHGNKCAMCKAVFKKENEERKRKEGE 613
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGE 44

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 124487159  574 CTRENDPVRGPDGKTHGNKCAMCKAVFKKENEERKRKEGE 613
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGP 40

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
                   ....*....|....*....|....*....|....*...
gi 124487159   427 CSEFRNQArngmlmCTRENDPVVGPDGKRHSNKCAMCA 464
Cdd:pfam00050    1 CSDYPSGA------CPRIYDPVCGTDGKTYSNECLFCA 32