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follistatin isoform X1 [Homo sapiens]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||
KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
117-164 | 4.12e-09 | ||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 51.91 E-value: 4.12e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
283-329 | 2.87e-08 | ||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 49.21 E-value: 2.87e-08
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
192-239 | 5.28e-08 | ||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. : Pssm-ID: 197624 Cd Length: 46 Bit Score: 48.44 E-value: 5.28e-08
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FOLN | smart00274 | Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ... |
94-117 | 1.12e-03 | ||
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence : Pssm-ID: 128570 Cd Length: 24 Bit Score: 36.10 E-value: 1.12e-03
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FOLN | smart00274 | Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ... |
167-190 | 3.71e-03 | ||
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence : Pssm-ID: 128570 Cd Length: 24 Bit Score: 34.56 E-value: 3.71e-03
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Name | Accession | Description | Interval | E-value | |||
KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
117-164 | 4.12e-09 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 51.91 E-value: 4.12e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
283-329 | 2.87e-08 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 49.21 E-value: 2.87e-08
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FSL_SPARC | cd01328 | Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ... |
95-166 | 4.74e-08 | |||
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238649 [Multi-domain] Cd Length: 86 Bit Score: 50.17 E-value: 4.74e-08
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
192-239 | 5.28e-08 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 48.44 E-value: 5.28e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
207-239 | 3.11e-07 | |||
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. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 46.49 E-value: 3.11e-07
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
294-329 | 7.59e-07 | |||
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. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 45.34 E-value: 7.59e-07
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
118-164 | 1.34e-05 | |||
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. Pssm-ID: 400135 Cd Length: 50 Bit Score: 42.09 E-value: 1.34e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
283-329 | 5.80e-05 | |||
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. Pssm-ID: 400135 Cd Length: 50 Bit Score: 40.17 E-value: 5.80e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
192-239 | 6.53e-05 | |||
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. Pssm-ID: 400135 Cd Length: 50 Bit Score: 40.17 E-value: 6.53e-05
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FOLN | smart00274 | Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ... |
94-117 | 1.12e-03 | |||
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence Pssm-ID: 128570 Cd Length: 24 Bit Score: 36.10 E-value: 1.12e-03
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FOLN | pfam09289 | Follistatin/Osteonectin-like EGF domain; Members of this family are predominantly found in ... |
95-116 | 2.63e-03 | |||
Follistatin/Osteonectin-like EGF domain; Members of this family are predominantly found in osteonectin and follistatin and adopt an EGF-like fold. Pssm-ID: 462743 Cd Length: 22 Bit Score: 34.76 E-value: 2.63e-03
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FOLN | smart00274 | Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ... |
167-190 | 3.71e-03 | |||
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence Pssm-ID: 128570 Cd Length: 24 Bit Score: 34.56 E-value: 3.71e-03
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Name | Accession | Description | Interval | E-value | |||
KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
117-164 | 4.12e-09 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 51.91 E-value: 4.12e-09
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
283-329 | 2.87e-08 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 49.21 E-value: 2.87e-08
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FSL_SPARC | cd01328 | Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ... |
95-166 | 4.74e-08 | |||
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238649 [Multi-domain] Cd Length: 86 Bit Score: 50.17 E-value: 4.74e-08
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KAZAL | smart00280 | Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ... |
192-239 | 5.28e-08 | |||
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains. Pssm-ID: 197624 Cd Length: 46 Bit Score: 48.44 E-value: 5.28e-08
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
207-239 | 3.11e-07 | |||
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. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 46.49 E-value: 3.11e-07
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
130-164 | 3.33e-07 | |||
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. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 46.11 E-value: 3.33e-07
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KAZAL_FS | cd00104 | Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ... |
294-329 | 7.59e-07 | |||
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. Pssm-ID: 238052 [Multi-domain] Cd Length: 41 Bit Score: 45.34 E-value: 7.59e-07
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
118-164 | 1.34e-05 | |||
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. Pssm-ID: 400135 Cd Length: 50 Bit Score: 42.09 E-value: 1.34e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
283-329 | 5.80e-05 | |||
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. Pssm-ID: 400135 Cd Length: 50 Bit Score: 40.17 E-value: 5.80e-05
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Kazal_2 | pfam07648 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
192-239 | 6.53e-05 | |||
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. Pssm-ID: 400135 Cd Length: 50 Bit Score: 40.17 E-value: 6.53e-05
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FSL_SPARC | cd01328 | Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ... |
168-227 | 4.67e-04 | |||
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins. Pssm-ID: 238649 [Multi-domain] Cd Length: 86 Bit Score: 38.61 E-value: 4.67e-04
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KAZAL_PSTI | cd01327 | Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ... |
130-164 | 5.92e-04 | |||
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. Pssm-ID: 238648 Cd Length: 45 Bit Score: 37.26 E-value: 5.92e-04
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FOLN | smart00274 | Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ... |
94-117 | 1.12e-03 | |||
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence Pssm-ID: 128570 Cd Length: 24 Bit Score: 36.10 E-value: 1.12e-03
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FOLN | pfam09289 | Follistatin/Osteonectin-like EGF domain; Members of this family are predominantly found in ... |
95-116 | 2.63e-03 | |||
Follistatin/Osteonectin-like EGF domain; Members of this family are predominantly found in osteonectin and follistatin and adopt an EGF-like fold. Pssm-ID: 462743 Cd Length: 22 Bit Score: 34.76 E-value: 2.63e-03
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Kazal_1 | pfam00050 | Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ... |
130-164 | 3.64e-03 | |||
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. Pssm-ID: 395004 Cd Length: 49 Bit Score: 34.95 E-value: 3.64e-03
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FOLN | smart00274 | Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ... |
167-190 | 3.71e-03 | |||
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence Pssm-ID: 128570 Cd Length: 24 Bit Score: 34.56 E-value: 3.71e-03
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Blast search parameters | ||||
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