von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    305 CTYYPCPAVCTVYGDRHYHSFDGLEYDYISDCQVFLIKS-TDDSDISVISQNKKCfDNDIVCSKSVLISIGDTEIYLNDA 383
Cdd:smart00216    3 CTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcSSEPTFSVLLKNVPC-GGGATCLKSVKVELNGDEIELKDD 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    384 P----YKQKRSGF-FLESRPEYQLWKAGFYIVIYFPEEDITILWDEKTTIHIKVGPQWKNKLAGLCGNFDKCTSNDMTTS 458
Cdd:smart00216   82 NgkvtVNGQQVSLpYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161

                    ..
gi 568968159    459 NN 460
Cdd:smart00216  162 DG 163

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    873 CCPEWECPCRCSMLSELSIITFDGNSAALSSMASYILVR--VPGEIVVVHIDKCSMNQNGHalkkpasfgrisglCFKKL 950
Cdd:smart00216    2 CCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQdcSSEPTFSVLLKNVPCGGGAT--------------CLKSV 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    951 NV---TTSIHKILINRVVRkVDVDSIVVPLPFSSHELFIEDSGTMYVITTPAGLI-IKWAHLTGIidihfgpQFNLSSY- 1025
Cdd:smart00216   68 KVelnGDEIELKDDNGKVT-VNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLL-------SVQLPSKy 139

                           170       180
                    ....*....|....*....|....
gi 568968159   1026 ---TEGLCGICNDNPDDDLRMQNG 1046
Cdd:smart00216  140 rgkTCGLCGNFDGEPEDDFRTPDG 163

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968159    43 HCDVI-HQELFAPCHVYVSPGLYYQLCRHDACKCG--SPCLCNALAHYAYLCGQRGVPIDFRAHISFC 107
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGgdDECLCAALAAYARACQAAGVCIGDWRTPTFC 68

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 568968159  111 CQKGMLYHHCSSLCLRSCTSLSSPEQCKDDCAEGCNCPEGkFYEETLNFCVPIYHC 166
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEG-YVRNSGGKCVPPSQC 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 568968159   742 YEPCATPCFKTCSDPEALACTFLPPVEGClpYCPKNMILDETTlKCVHPEDC 793
Cdd:pfam01826    7 YSECGSACPPTCANLSPPDVCPEPCVEGC--VCPPGFVRNSGG-KCVPPSDC 55

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    305 CTYYPCPAVCTVYGDRHYHSFDGLEYDYISDCQVFLIKS-TDDSDISVISQNKKCfDNDIVCSKSVLISIGDTEIYLNDA 383
Cdd:smart00216    3 CTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcSSEPTFSVLLKNVPC-GGGATCLKSVKVELNGDEIELKDD 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    384 P----YKQKRSGF-FLESRPEYQLWKAGFYIVIYFPEEDITILWDEKTTIHIKVGPQWKNKLAGLCGNFDKCTSNDMTTS 458
Cdd:smart00216   82 NgkvtVNGQQVSLpYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161

                    ..
gi 568968159    459 NN 460
Cdd:smart00216  162 DG 163

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968159    495 FPYAKRECSILYSD--VFAPCRNVIDVTSFAKNCHEDTCNCnlGGDCECLCTSVAAYAYKCCQEGVPVH-WRSPTVCA 569
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968159   1080 TEYDCSHCIELLNREG-FIPCHDKVSPRDFCEKMWI---NYTYFWSYECDAISAYVALCNKFDICIQ-WRTPDYCP 1150
Cdd:smart00832    1 KYYACSQCGILLSPRGpFAACHSVVDPEPFFENCVYdtcACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568968159   502 CSIL-YSDVFAPCRNVIDVTSFAKNCHEDTCNCnlGGDCECLCTSVAAYAYKCCQEGVPV-HWRSPTVC 568
Cdd:pfam08742    2 CGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968159   1627 QDCVSqSSISVASCDGKCPSATIYNINVESHlrFCKCCRENGVRNVTVPLHCSgNGTEVMYTLQEPIDCTCQWN 1700
Cdd:smart00041   11 NGCTS-VTVKNAFCEGKCGSASSYSIQDVQH--SCSCCQPHKTKTRQVRLRCP-DGSTVKKTVMHIEECGCEPN 80

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 568968159  111 CQKGMLYHHCSSLCLRSCTSLSSPEQCKDDCAEGCNCPEGkFYEETLNFCVPIYHC 166
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEG-YVRNSGGKCVPPSQC 55

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968159  1086 HCIELLNREGFIPCHDKVSPRDFCEKMWINYTYFWSYE---CDAISAYVALCNKFDICIQ-WRTPDYC 1149
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDeclCAALAAYARACQAAGVCIGdWRTPTFC 68

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968159  209 CPEGKEYFDCrfpdpalpagGINCETTCANLAMNFTCapSSPCISGCVCAAGMAEH-KGKCYVPESC 274
Cdd:cd19941     1 CPPNEVYSEC----------GSACPPTCANPNAPPPC--TKQCVEGCFCPEGYVRNsGGKCVPPSQC 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 568968159  742 YEPCATPCFKTCSDPEA-LACTfLPPVEGClpYCPKNMILDETTlKCVHPEDC 793
Cdd:cd19941     7 YSECGSACPPTCANPNApPPCT-KQCVEGC--FCPEGYVRNSGG-KCVPPSQC 55

Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The OTOG family includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOG or OTOGL gene may cause hearing loss. Members of this family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159  579 LGEGPYMLASYGQSGLVLGANMTSRSVFSLPRsNNRGNLFFIFMITPGLFKEKTSslaLVSLESAERPNYFLYVHDNDTL 658
Cdd:cd23398     1 LGEGPYKLSSYNYPGYLLGANDDSGVVSLIPT-ENSPSGGVSFMVTPGLNGDKAN---LVSFESAERPNYFLCVQANGTL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968159  659 SLKLWRANSEFHQRATFFHHQGLWIPGYSAFELYSKKGYFIVFMGSSVKASKYDDSEEFKQSSSFSI 725
Cdd:cd23398    77 KLVKWENSALFRNAASFFLRQGTWIPGYVAFESTSKPGYFIRHSNSSLKLQKYDHTEEFRRSSSFKL 143

Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159  579 LGEGPYMLASYGQSGLVLGANMTSRSVFSLPrsnNRGNLFFIFMITPGLFKEKTsslalVSLESAERPNYFLyVHDNDTL 658
Cdd:cd23265     1 DGGTPVRLRSASDPGYYIRHDGGSGSVTSDD---DDSAEDAFFRVVPGLAGEGT-----VSFESVDKPGYYL-RHRGGEL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968159  659 SLKLWRANSEFHQRATFFHHQGLWIPGYSAFELYSKKGYFIVFMGSSVKASKYdDSEEFKQSSSF 723
Cdd:cd23265    72 RLEKNDGSAAFREDATFRPRPGLADPGGVSFESVNYPGYYLRHRNNRLVLGKV-DSTAFKEDATF 135

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159   314 CTVYGDRHYHSFDGLEYDYISDCQVFLIKS-TDDSDISVISQNKKC-FDNDIVCSKSVLISIGDTEIYLNDA-------- 383
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDcSEEPDFSFSVTNKNCnGGASGVCLKSVTVIVGDLEITLQKGgtvlvngq 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159   384 ----PYKqkrsgfflESRPEYQLWKAGFYIVIYFPEEDITILWDEKTTIHIKVGPQWKNKLAGLCGNFDKCTSNDMTTSN 459
Cdd:pfam00094   81 kvslPYK--------SDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152

                   .
gi 568968159   460 N 460
Cdd:pfam00094  153 G 153

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    873 CCPEWECPCRCSMLSELSIITFDGNSAALSSMASYILVR--VPGEIVVVHIDKCSMNQNGHalkkpasfgrisglCFKKL 950
Cdd:smart00216    2 CCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQdcSSEPTFSVLLKNVPCGGGAT--------------CLKSV 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159    951 NV---TTSIHKILINRVVRkVDVDSIVVPLPFSSHELFIEDSGTMYVITTPAGLI-IKWAHLTGIidihfgpQFNLSSY- 1025
Cdd:smart00216   68 KVelnGDEIELKDDNGKVT-VNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLL-------SVQLPSKy 139

                           170       180
                    ....*....|....*....|....
gi 568968159   1026 ---TEGLCGICNDNPDDDLRMQNG 1046
Cdd:smart00216  140 rgkTCGLCGNFDGEPEDDFRTPDG 163

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159   883 CSMLSELSIITFDGNSAALSSMASYILVRVPGE----IVVVHIDKCSMNQNGhalkkpasfgrisgLCFKKLNVTTSIHK 958
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEepdfSFSVTNKNCNGGASG--------------VCLKSVTVIVGDLE 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159   959 ILINRVvRKVDVDSIVVPLPFSSH--ELFIEDSGTMYVITTPA-GLIIKWAHLtGIIDIHFGPQFNlsSYTEGLCGICND 1035
Cdd:pfam00094   67 ITLQKG-GTVLVNGQKVSLPYKSDggEVEILGSGFVVVDLSPGvGLQVDGDGR-GQLFVTLSPSYQ--GKTCGLCGNYNG 142

                          170
                   ....*....|..
gi 568968159  1036 NPDDDLRMQNGT 1047
Cdd:pfam00094  143 NQEDDFMTPDGT 154

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968159    43 HCDVI-HQELFAPCHVYVSPGLYYQLCRHDACKCG--SPCLCNALAHYAYLCGQRGVPIDFRAHISFC 107
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGgdDECLCAALAAYARACQAAGVCIGDWRTPTFC 68

Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF B) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. The family also includes Hungateiclostridium thermocellum anti-sigma-I factor RsgI5. It negatively regulates SigI5 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI5 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI5. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968159  619 FIFMITPGLfkektSSLALVSLESAERPNYFLyVHDNDTLSLklwRANSE---FHQRATFFHHQGLWIPGYSAFELYSKK 695
Cdd:cd23399    40 ATFKVVPGL-----ADSGCVSFESVNYPGYYL-RHYNFRLRL---DKNDGsalFKEDATFCPRPGLADGGGVSFRSYNYP 110

                          90       100
                  ....*....|....*....|....*...
gi 568968159  696 GYFIVFMGSSVKASKYDDSEEFKQSSSF 723
Cdd:cd23399   111 GRYIRHRNFELWLDPNDGTALFRQDATF 138

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568968159  111 CQKGMLYHHCSSLCLRSCTSLSSPEQCKDDCAEGCNCPEGkFYEETLNFCVPIYHC 166
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEG-YVRNSGGKCVPPSQC 55

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.

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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968159  1086 HCIELLNREGFIPCHDKVSPRDFCEKMWINYTYFWSYE---CDAISAYVALCNKFDICIQ-WRTPDYC 1149
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDeclCAALAAYARACQAAGVCIGdWRTPTFC 68

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968159  209 CPEGKEYFDCrfpdpalpagGINCETTCANLAMNFTCapSSPCISGCVCAAGMAEH-KGKCYVPESC 274
Cdd:cd19941     1 CPPNEVYSEC----------GSACPPTCANPNAPPPC--TKQCVEGCFCPEGYVRNsGGKCVPPSQC 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 568968159  742 YEPCATPCFKTCSDPEA-LACTfLPPVEGClpYCPKNMILDETTlKCVHPEDC 793
Cdd:cd19941     7 YSECGSACPPTCANPNApPPCT-KQCVEGC--FCPEGYVRNSGG-KCVPPSQC 55