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Conserved domains on  [gi|15012095|gb|AAH10952|]
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Peptidase inhibitor 3, skin-derived [Homo sapiens]

Protein Classification

Cementoin and WAP domain-containing protein( domain architecture ID 11187140)

Cementoin and WAP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WAP smart00217
Four-disulfide core domains;
72-117 1.66e-14

Four-disulfide core domains;


:

Pssm-ID: 197580 [Multi-domain]  Cd Length: 47  Bit Score: 62.39  E-value: 1.66e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 15012095     72 KPGSCP-IILIRCAMLNPPNRCLKDTDCPGIKKCCEGSCGMACFVPQ 117
Cdd:smart00217   1 KPGSCPwPTIASCPLGNPPNKCSSDSQCPGVKKCCFNGCGKSCLTPV 47
Cementoin pfam10511
Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has ...
 31-47 1.66e-04

Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.


:

Pssm-ID: 371104  Cd Length: 17  Bit Score: 36.11  E-value: 1.66e-04
                          10
                  ....*....|....*..
gi 15012095    31 GQDTVKGRVPFNGQDPV 47
Cdd:pfam10511   1 GQDTVKGQVPVKGQDPV 17
Cementoin pfam10511
Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has ...
 55-71 1.71e-03

Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.


:

Pssm-ID: 371104  Cd Length: 17  Bit Score: 33.41  E-value: 1.71e-03
                          10
                  ....*....|....*..
gi 15012095    55 GQDKVKAQEPVKGPVST 71
Cdd:pfam10511   1 GQDTVKGQVPVKGQDPV 17
 
Name Accession Description Interval E-value
WAP smart00217
Four-disulfide core domains;
72-117 1.66e-14

Four-disulfide core domains;


Pssm-ID: 197580 [Multi-domain]  Cd Length: 47  Bit Score: 62.39  E-value: 1.66e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 15012095     72 KPGSCP-IILIRCAMLNPPNRCLKDTDCPGIKKCCEGSCGMACFVPQ 117
Cdd:smart00217   1 KPGSCPwPTIASCPLGNPPNKCSSDSQCPGVKKCCFNGCGKSCLTPV 47
WAP cd00199
whey acidic protein-type four-disulfide core domains. Members of the family include whey ...
 67-117 1.20e-12

whey acidic protein-type four-disulfide core domains. Members of the family include whey acidic protein, elafin (elastase-specific inhibitor), caltrin-like protein (a calcium transport inhibitor) and other extracellular proteinase inhibitors. A group of proteins containing 8 characteristically-spaced cysteine residuesforming disulphide bonds, have been termed '4-disulphide core' proteins. Protease inhibition occurs by insertion of the inhibitory loop into the active site pocket and interference with the catalytic residues of the protease.


Pssm-ID: 238120 [Multi-domain]  Cd Length: 60  Bit Score: 57.85  E-value: 1.20e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15012095  67 GPVSTKPGSCPI---ILIRCAMLN------PPNRCLKDTDCPGIKKCCEGSCGMACFVPQ 117
Cdd:cd00199   1 GNNMTKPGSCPRpveKPGRCPMVNppslgiPPNRCSSDSDCPGDKKCCENGCGKSCLTPV 60
WAP pfam00095
WAP-type (Whey Acidic Protein) 'four-disulfide core'; WAP belongs to the group of Elafin or ...
 72-116 2.18e-08

WAP-type (Whey Acidic Protein) 'four-disulfide core'; WAP belongs to the group of Elafin or elastase-specific inhibitors.


Pssm-ID: 459672 [Multi-domain]  Cd Length: 42  Bit Score: 46.65  E-value: 2.18e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15012095    72 KPGSCPIILIRCamlNPPNRCLKDTDCPGIKKCCEGSCGMACFVP 116
Cdd:pfam00095   1 KPGCCPRLGARG---CCRSCCSSDDDCPGRQKCCSNGCGSVCVPP 42
Cementoin pfam10511
Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has ...
 31-47 1.66e-04

Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.


Pssm-ID: 371104  Cd Length: 17  Bit Score: 36.11  E-value: 1.66e-04
                          10
                  ....*....|....*..
gi 15012095    31 GQDTVKGRVPFNGQDPV 47
Cdd:pfam10511   1 GQDTVKGQVPVKGQDPV 17
Cementoin pfam10511
Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has ...
 55-71 1.71e-03

Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.


Pssm-ID: 371104  Cd Length: 17  Bit Score: 33.41  E-value: 1.71e-03
                          10
                  ....*....|....*..
gi 15012095    55 GQDKVKAQEPVKGPVST 71
Cdd:pfam10511   1 GQDTVKGQVPVKGQDPV 17
 
Name Accession Description Interval E-value
WAP smart00217
Four-disulfide core domains;
72-117 1.66e-14

Four-disulfide core domains;


Pssm-ID: 197580 [Multi-domain]  Cd Length: 47  Bit Score: 62.39  E-value: 1.66e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 15012095     72 KPGSCP-IILIRCAMLNPPNRCLKDTDCPGIKKCCEGSCGMACFVPQ 117
Cdd:smart00217   1 KPGSCPwPTIASCPLGNPPNKCSSDSQCPGVKKCCFNGCGKSCLTPV 47
WAP cd00199
whey acidic protein-type four-disulfide core domains. Members of the family include whey ...
 67-117 1.20e-12

whey acidic protein-type four-disulfide core domains. Members of the family include whey acidic protein, elafin (elastase-specific inhibitor), caltrin-like protein (a calcium transport inhibitor) and other extracellular proteinase inhibitors. A group of proteins containing 8 characteristically-spaced cysteine residuesforming disulphide bonds, have been termed '4-disulphide core' proteins. Protease inhibition occurs by insertion of the inhibitory loop into the active site pocket and interference with the catalytic residues of the protease.


Pssm-ID: 238120 [Multi-domain]  Cd Length: 60  Bit Score: 57.85  E-value: 1.20e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15012095  67 GPVSTKPGSCPI---ILIRCAMLN------PPNRCLKDTDCPGIKKCCEGSCGMACFVPQ 117
Cdd:cd00199   1 GNNMTKPGSCPRpveKPGRCPMVNppslgiPPNRCSSDSDCPGDKKCCENGCGKSCLTPV 60
WAP pfam00095
WAP-type (Whey Acidic Protein) 'four-disulfide core'; WAP belongs to the group of Elafin or ...
 72-116 2.18e-08

WAP-type (Whey Acidic Protein) 'four-disulfide core'; WAP belongs to the group of Elafin or elastase-specific inhibitors.


Pssm-ID: 459672 [Multi-domain]  Cd Length: 42  Bit Score: 46.65  E-value: 2.18e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15012095    72 KPGSCPIILIRCamlNPPNRCLKDTDCPGIKKCCEGSCGMACFVP 116
Cdd:pfam00095   1 KPGCCPRLGARG---CCRSCCSSDDDCPGRQKCCSNGCGSVCVPP 42
Cementoin pfam10511
Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has ...
 31-47 1.66e-04

Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.


Pssm-ID: 371104  Cd Length: 17  Bit Score: 36.11  E-value: 1.66e-04
                          10
                  ....*....|....*..
gi 15012095    31 GQDTVKGRVPFNGQDPV 47
Cdd:pfam10511   1 GQDTVKGQVPVKGQDPV 17
Cementoin pfam10511
Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has ...
 55-71 1.71e-03

Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.


Pssm-ID: 371104  Cd Length: 17  Bit Score: 33.41  E-value: 1.71e-03
                          10
                  ....*....|....*..
gi 15012095    55 GQDKVKAQEPVKGPVST 71
Cdd:pfam10511   1 GQDTVKGQVPVKGQDPV 17
Cementoin pfam10511
Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has ...
 43-59 6.00e-03

Trappin protein transglutaminase binding domain; Trappin-2, itself a protease inhibitor, has this unique N-terminal domain that enables it to become cross-linked to extracellular matrix proteins by transglutaminase. This domain contains several repeated motifs with the the consensus sequence Gly-Gln-Asp-Pro-Val-Lys, and these together can anchor the whole molecule to extracellular matrix proteins, such as laminin, fibronectin, beta-crystallin, collagen IV, fibrinogen, and elastin, by transglutaminase-catalyzed cross-links. The whole domain is rich in glutamine and lysine, thus allowing and transglutaminase(s) to catalyze the formation of an intermolecular epsilon-(gamma-glutamyl)lysine isopeptide bond. Cementoin is associated with the WAP family, pfam00095, at the C-terminus.


Pssm-ID: 371104  Cd Length: 17  Bit Score: 32.25  E-value: 6.00e-03
                          10
                  ....*....|....*..
gi 15012095    43 GQDPVKGQVSVKGQDKV 59
Cdd:pfam10511   1 GQDTVKGQVPVKGQDPV 17
 
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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