NCBI Conserved Domain Search

NCBI

3D Macromolecular Structures

Conserved Domains

Conserved domains on [gi|1734337774|ref|NP_001360620|]

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Follistatin-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

trypsin inhibitor-like cysteine-rich domain-containing protein( domain architecture ID 15330973)

trypsin inhibitor-like (TIL) cysteine-rich domain-containing protein similar to serine protease inhibitors

CATH: 2.10.25.110

Gene Ontology: GO:0004867|GO:0005576

SCOP: 4003491

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

26-80

1.14e-08

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

:

Pssm-ID: 410995 Cd Length: 55 Bit Score: 51.55 E-value: 1.14e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774  26 CKENESFQTCGTACEPTCG-LPTPTFCTLQCVMGCQCNSGFFRRtSDNRCVEQKDC 80
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnPNAPPPCTKQCVEGCFCPEGYVRN-SGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

523-578

2.25e-07

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

:

Pssm-ID: 460351 Cd Length: 55 Bit Score: 48.15 E-value: 2.25e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774 523 CAKNQTMSDCLNTCsEDKCPGMSKSMMCTKHCGQGCACASGYLRSSDGECYKPKDC 578
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

99-155

2.68e-07

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

:

Pssm-ID: 460351 Cd Length: 55 Bit Score: 47.77 E-value: 2.68e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774  99 CPVNEVSNECHNPCtEKKCPQKNAPQVnCLMACQVGCSCMDGFVRNNQGVCVKEAEC 155
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

163-219

1.48e-05

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

:

Pssm-ID: 460351 Cd Length: 55 Bit Score: 42.76 E-value: 1.48e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 163 CGTNEEPNQCHNACfEKKCPvKPQPLVNCMEKCDIGCSCKKGFLRNRQGQCVNPTEC 219
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCA-NLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

645-701

4.50e-05

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

:

Pssm-ID: 460351 Cd Length: 55 Bit Score: 41.60 E-value: 4.50e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 645 CLGTQEYTDCMPKCQQLCSGAQQceTGMEIAMCTPGCVCRPNYKLDSNGDCVHNRHC 701
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSP--PDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

707-761

8.04e-04

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

:

Pssm-ID: 460351 Cd Length: 55 Bit Score: 38.14 E-value: 8.04e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734337774 707 CPDNEEWSKCLSndnQCDlASISMIANKD----QCFSGCVCADGFARNNNGTCVASDKC 761
Cdd:pfam01826   1 CPANEVYSECGS---ACP-PTCANLSPPDvcpePCVEGCVCPPGFVRNSGGKCVPPSDC 55

Name

Accession

Description

Interval

E-value

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

26-80

1.14e-08

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 51.55 E-value: 1.14e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774  26 CKENESFQTCGTACEPTCG-LPTPTFCTLQCVMGCQCNSGFFRRtSDNRCVEQKDC 80
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnPNAPPPCTKQCVEGCFCPEGYVRN-SGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

26-80

1.94e-08

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 51.23 E-value: 1.94e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774  26 CKENESFQTCGTACEPTCG-LPTPTFCTLQCVMGCQCNSGFFRRtSDNRCVEQKDC 80
Cdd:pfam01826   1 CPANEVYSECGSACPPTCAnLSPPDVCPEPCVEGCVCPPGFVRN-SGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

523-578

2.25e-07

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 48.15 E-value: 2.25e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774 523 CAKNQTMSDCLNTCsEDKCPGMSKSMMCTKHCGQGCACASGYLRSSDGECYKPKDC 578
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

99-155

2.68e-07

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 47.77 E-value: 2.68e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774  99 CPVNEVSNECHNPCtEKKCPQKNAPQVnCLMACQVGCSCMDGFVRNNQGVCVKEAEC 155
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

99-155

6.25e-06

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 43.84 E-value: 6.25e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774  99 CPVNEVSNECHNPCtEKKCPQKNAPQvNCLMACQVGCSCMDGFVRNNQGVCVKEAEC 155
Cdd:cd19941     1 CPPNEVYSECGSAC-PPTCANPNAPP-PCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

163-219

1.48e-05

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 42.76 E-value: 1.48e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 163 CGTNEEPNQCHNACfEKKCPvKPQPLVNCMEKCDIGCSCKKGFLRNRQGQCVNPTEC 219
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCA-NLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

523-578

2.57e-05

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 42.30 E-value: 2.57e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774 523 CAKNQTMSDCLNTCsEDKCPGMSKSMMCTKHCGQGCACASGYLRSSDGECYKPKDC 578
Cdd:cd19941     1 CPPNEVYSECGSAC-PPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

645-701

4.50e-05

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 41.60 E-value: 4.50e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 645 CLGTQEYTDCMPKCQQLCSGAQQceTGMEIAMCTPGCVCRPNYKLDSNGDCVHNRHC 701
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSP--PDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

163-219

2.75e-04

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 39.22 E-value: 2.75e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 163 CGTNEEPNQCHNACfEKKCpVKPQPLVNCMEKCDIGCSCKKGFLRNRQGQCVNPTEC 219
Cdd:cd19941     1 CPPNEVYSECGSAC-PPTC-ANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

707-761

8.04e-04

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 38.14 E-value: 8.04e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734337774 707 CPDNEEWSKCLSndnQCDlASISMIANKD----QCFSGCVCADGFARNNNGTCVASDKC 761
Cdd:pfam01826   1 CPANEVYSECGS---ACP-PTCANLSPPDvcpePCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

645-701

2.78e-03

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 36.53 E-value: 2.78e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 645 CLGTQEYTDCMPKCQQLCSGAQQceTGMEIAMCTPGCVCRPNYKLDSNGDCVHNRHC 701
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNA--PPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

Name

Accession

Description

Interval

E-value

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

26-80

1.14e-08

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 51.55 E-value: 1.14e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774  26 CKENESFQTCGTACEPTCG-LPTPTFCTLQCVMGCQCNSGFFRRtSDNRCVEQKDC 80
Cdd:cd19941     1 CPPNEVYSECGSACPPTCAnPNAPPPCTKQCVEGCFCPEGYVRN-SGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

26-80

1.94e-08

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 51.23 E-value: 1.94e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774  26 CKENESFQTCGTACEPTCG-LPTPTFCTLQCVMGCQCNSGFFRRtSDNRCVEQKDC 80
Cdd:pfam01826   1 CPANEVYSECGSACPPTCAnLSPPDVCPEPCVEGCVCPPGFVRN-SGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

523-578

2.25e-07

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 48.15 E-value: 2.25e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774 523 CAKNQTMSDCLNTCsEDKCPGMSKSMMCTKHCGQGCACASGYLRSSDGECYKPKDC 578
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

99-155

2.68e-07

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 47.77 E-value: 2.68e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774  99 CPVNEVSNECHNPCtEKKCPQKNAPQVnCLMACQVGCSCMDGFVRNNQGVCVKEAEC 155
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCANLSPPDV-CPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

99-155

6.25e-06

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 43.84 E-value: 6.25e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774  99 CPVNEVSNECHNPCtEKKCPQKNAPQvNCLMACQVGCSCMDGFVRNNQGVCVKEAEC 155
Cdd:cd19941     1 CPPNEVYSECGSAC-PPTCANPNAPP-PCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

163-219

1.48e-05

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 42.76 E-value: 1.48e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 163 CGTNEEPNQCHNACfEKKCPvKPQPLVNCMEKCDIGCSCKKGFLRNRQGQCVNPTEC 219
Cdd:pfam01826   1 CPANEVYSECGSAC-PPTCA-NLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

523-578

2.57e-05

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 42.30 E-value: 2.57e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734337774 523 CAKNQTMSDCLNTCsEDKCPGMSKSMMCTKHCGQGCACASGYLRSSDGECYKPKDC 578
Cdd:cd19941     1 CPPNEVYSECGSAC-PPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

645-701

4.50e-05

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 41.60 E-value: 4.50e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 645 CLGTQEYTDCMPKCQQLCSGAQQceTGMEIAMCTPGCVCRPNYKLDSNGDCVHNRHC 701
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSP--PDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

163-219

2.75e-04

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 39.22 E-value: 2.75e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 163 CGTNEEPNQCHNACfEKKCpVKPQPLVNCMEKCDIGCSCKKGFLRNRQGQCVNPTEC 219
Cdd:cd19941     1 CPPNEVYSECGSAC-PPTC-ANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

TIL

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...

707-761

8.04e-04

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.

Pssm-ID: 460351 Cd Length: 55 Bit Score: 38.14 E-value: 8.04e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734337774 707 CPDNEEWSKCLSndnQCDlASISMIANKD----QCFSGCVCADGFARNNNGTCVASDKC 761
Cdd:pfam01826   1 CPANEVYSECGS---ACP-PTCANLSPPDvcpePCVEGCVCPPGFVRNSGGKCVPPSDC 55

TIL

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...

645-701

2.78e-03

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.

Pssm-ID: 410995 Cd Length: 55 Bit Score: 36.53 E-value: 2.78e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337774 645 CLGTQEYTDCMPKCQQLCSGAQQceTGMEIAMCTPGCVCRPNYKLDSNGDCVHNRHC 701
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNA--PPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55

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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of the residues that compose this conserved feature have been mapped to the query sequence.

Click on the triangle to view details about the feature, including a multiple sequence alignment of your query sequence and the protein sequences used to curate the domain model, where hash marks (#) above the aligned sequences show the location of the conserved feature residues.

The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions. Click on the triangle for interactive 3D structure viewing options.

Functional characterization of the conserved domain architecture found on the query. Click here to see more details.

This image shows a graphical summary of conserved domains identified on the query sequence. The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits (labeled illustration) or all hits (labeled illustration).
Domains are color coded according to superfamilies to which they have been assigned. Hits with scores that pass a domain-specific threshold (specific hits) are drawn in bright colors. Others (non-specific hits) and superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features), they are mapped to the query sequence and indicated through sets of triangles with the same color and shade of the domain or superfamily that provides the annotation.
Mouse over the colored bars or triangles to see descriptions of the domains and features. click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.

The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores. Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.

To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page, or click on the triangles, if present, that represent functional sites (conserved features) mapped to the query sequence.

Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence. (labeled illustration)
Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence. (labeled illustration)
Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance. (labeled illustration)
Four types of hits can be shown, as available, for each region on the query sequence:

specific hits meet or exceed a domain-specific e-value threshold (illustrated example) and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains

The CD-Search help document provides more detail about the tool and its features.

Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool (CDART).

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