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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193208545   291 CGANEQYSACFSSCQPSCQDPSTPACPAPGCQPGCICLPGYIRrdsSPRSACVPRGLC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVR---NSGGKCVPPSDC 55

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208545   897 GRFTFSQLTSTALRIHGEVYTLPVGRHAVVLHQFGDSSEGCSRVGA---PFSK------SLSPSLGDI-------TETGK 960
Cdd:pfam00080    3 GTVTFTQAGGGPVRVTGNLTGLTPGKHGFHIHEFGDCTNGCTSAGGhfnPTGKqhggpnDDGRHVGDLgnitadaDGVAT 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 193208545   961 F----DRIVEWPVIDVVGRAVVIysfstaewslraH-----FGEKP-------LACGTI 1003
Cdd:pfam00080   83 VeftdSLISLSGGNSIIGRALVV------------HagpddLGTQPtgnagarIACGVI 129

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193208545  782 CPdKHAVWSSCGTLCPEYCGQPSVP-VCSGTCSAGCHCAPGFVRARNDVtapCVPRE 837
Cdd:cd19941     1 CP-PNEVYSECGSACPPTCANPNAPpPCTKQCVEGCFCPEGYVRNSGGK---CVPPS 53

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 193208545   629 PTKEFMTCGSSCPMGCDN-RHPKNC-APCQTGCFCKNGLVFENS 670
Cdd:pfam01826    3 ANEVYSECGSACPPTCANlSPPDVCpEPCVEGCVCPPGFVRNSG 46

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193208545   291 CGANEQYSACFSSCQPSCQDPSTPACPAPGCQPGCICLPGYIRrdsSPRSACVPRGLC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVR---NSGGKCVPPSDC 55

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 193208545  291 CGANEQYSACFSSCQPSCQDPSTP-ACPAPgCQPGCICLPGYIRrdsSPRSACVPRGLC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPpPCTKQ-CVEGCFCPEGYVR---NSGGKCVPPSQC 55

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 193208545   130 MRRRELLDELRSLEIVGQAIPLCEESGLaWRRRQCLAGTEVCWCVTRYGRRLSGKESKD 188
Cdd:pfam00086    4 ERARALEQAASGRPASGLYIPNCDEDGF-YKPVQCHGSTGYCWCVDPEGQEIPGTRTRG 61

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193208545  782 CPdKHAVWSSCGTLCPEYCGQPSVP-VCSGTCSAGCHCAPGFVRARNDVtapCVPRE 837
Cdd:cd19941     1 CP-PNEVYSECGSACPPTCANPNAPpPCTKQCVEGCFCPEGYVRNSGGK---CVPPS 53

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 193208545   782 CPdKHAVWSSCGTLCPEYCGQPSVP-VCSGTCSAGCHCAPGFVRARNDVtapCVPRE 837
Cdd:pfam01826    1 CP-ANEVYSECGSACPPTCANLSPPdVCPEPCVEGCVCPPGFVRNSGGK---CVPPS 53

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 193208545   490 YQSCGSKCPASCDRPlsqAASIDCALSCEPGCFCRLPYVLadskDPNSTCILPQLC 545
Cdd:pfam01826    7 YSECGSACPPTCANL---SPPDVCPEPCVEGCVCPPGFVR----NSGGKCVPPSDC 55

copper, zinc superoxide dismutase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208545  901 FSQLTSTALRIHGEVYTLPVGRHAVVLHQFGDSSEGCSRVGAPFSKSLSPS----LGDI-----TETGKFD---RIVEWP 968
Cdd:PLN02957   98 FAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPSDDDTdeepLGDLgtleaDENGEATfsgTKEKLK 177

                          90
                  ....*....|..
gi 193208545  969 VIDVVGRAVVIY 980
Cdd:PLN02957  178 VWDLIGRSLAVY 189

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 193208545  632 EFMTCGSSCPMGCDNRH-PKNC-APCQTGCFCKNGLVFENS 670
Cdd:cd19941     6 VYSECGSACPPTCANPNaPPPCtKQCVEGCFCPEGYVRNSG 46

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 193208545   291 CGANEQYSACFSSCQPSCQDPSTPACPAPGCQPGCICLPGYIRrdsSPRSACVPRGLC 348
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVR---NSGGKCVPPSDC 55

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 193208545  291 CGANEQYSACFSSCQPSCQDPSTP-ACPAPgCQPGCICLPGYIRrdsSPRSACVPRGLC 348
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPpPCTKQ-CVEGCFCPEGYVR---NSGGKCVPPSQC 55

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 193208545   130 MRRRELLDELRSLEIVGQAIPLCEESGLaWRRRQCLAGTEVCWCVTRYGRRLSGKESKD 188
Cdd:pfam00086    4 ERARALEQAASGRPASGLYIPNCDEDGF-YKPVQCHGSTGYCWCVDPEGQEIPGTRTRG 61

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 193208545  782 CPdKHAVWSSCGTLCPEYCGQPSVP-VCSGTCSAGCHCAPGFVRARNDVtapCVPRE 837
Cdd:cd19941     1 CP-PNEVYSECGSACPPTCANPNAPpPCTKQCVEGCFCPEGYVRNSGGK---CVPPS 53

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 193208545   782 CPdKHAVWSSCGTLCPEYCGQPSVP-VCSGTCSAGCHCAPGFVRARNDVtapCVPRE 837
Cdd:pfam01826    1 CP-ANEVYSECGSACPPTCANLSPPdVCPEPCVEGCVCPPGFVRNSGGK---CVPPS 53

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.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 193208545   490 YQSCGSKCPASCDRPlsqAASIDCALSCEPGCFCRLPYVLadskDPNSTCILPQLC 545
Cdd:pfam01826    7 YSECGSACPPTCANL---SPPDVCPEPCVEGCVCPPGFVR----NSGGKCVPPSDC 55

copper, zinc superoxide dismutase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193208545  901 FSQLTSTALRIHGEVYTLPVGRHAVVLHQFGDSSEGCSRVGAPFSKSLSPS----LGDI-----TETGKFD---RIVEWP 968
Cdd:PLN02957   98 FAQVSMELARIEAAFSGLSPGTHGWSINEYGDLTRGAASTGKVYNPSDDDTdeepLGDLgtleaDENGEATfsgTKEKLK 177

                          90
                  ....*....|..
gi 193208545  969 VIDVVGRAVVIY 980
Cdd:PLN02957  178 VWDLIGRSLAVY 189

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 193208545  632 EFMTCGSSCPMGCDNRH-PKNC-APCQTGCFCKNGLVFENS 670
Cdd:cd19941     6 VYSECGSACPPTCANPNaPPPCtKQCVEGCFCPEGYVRNSG 46