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Conserved domains on  [gi|2462624602|ref|XP_054218893|]
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insulin-like growth factor-binding protein-like 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KAZAL_FS super family cl00097
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
114-151 2.24e-04

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.


The actual alignment was detected with superfamily member smart00280:

Pssm-ID: 412159  Cd Length: 46  Bit Score: 37.27  E-value: 2.24e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462624602  114 VCGSDGRSYPSVCALRLRARHTPRahpgHLHKARDGPC 151
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACESGK----SIEVKHDGPC 46
 
Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
114-151 2.24e-04

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 37.27  E-value: 2.24e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462624602  114 VCGSDGRSYPSVCALRLRARHTPRahpgHLHKARDGPC 151
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACESGK----SIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
114-151 3.75e-03

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: 33.78  E-value: 3.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462624602 114 VCGSDGRSYPSVCALRLRARHTPRahpgHLHKARDGPC 151
Cdd:cd00104     8 VCGSDGKTYSNECHLGCAACRSGR----SITVAHNGPC 41
 
Name Accession Description Interval E-value
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
114-151 2.24e-04

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


Pssm-ID: 197624  Cd Length: 46  Bit Score: 37.27  E-value: 2.24e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462624602  114 VCGSDGRSYPSVCALRLRARHTPRahpgHLHKARDGPC 151
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAACESGK----SIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
114-151 3.75e-03

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: 33.78  E-value: 3.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462624602 114 VCGSDGRSYPSVCALRLRARHTPRahpgHLHKARDGPC 151
Cdd:cd00104     8 VCGSDGKTYSNECHLGCAACRSGR----SITVAHNGPC 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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