NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1316090325|ref|XP_014324026|]
View 

IgGFc-binding protein [Xiphophorus maculatus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
IgGFc_binding pfam17517
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
 119-413 1.02e-72

IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.


:

Pssm-ID: 465430  Cd Length: 292  Bit Score: 245.72  E-value: 1.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  119 DTSVIYPTTAWGKEYFILTPPSGPYGTSKEFAVTNGKDKNQVEIFPEALITFQGRVfNKGNKLVIDLEPYESVQLQSKYD 198
Cdd:pfam17517    1 DATLLLPVSSLGTEYYVVSWDPTPGSGPSYFQIVATEDNTTVTITPTVDVTGGGGV-YAGSPFTITLNRGEVLQLQSDGD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  199 LSGSQVTSQRPVAVFSGHTCFLL---FSKCNHVYEQLLPVSSWGTSFILSALSFQKNYDSVY---LQASQATQVSVNDGK 272
Cdd:pfam17517   80 LTGSRITSDKPVAVFSGHSCANVpsgGGACDHLVEQLPPVSSWGKEYVVVPFRRGNGDEQSIyriVAAEDNTTVTVNGAA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  273 GKTAfSLSRGTMKEIKLKHPetLFIQSDHGIQVLMLFNGvEYSWFQIYDPFFMTILPIDRFCSSYSLEALESFDNKALIV 352
Cdd:pfam17517  160 GAPA-TLNAGEVYEFSTDAP--FYVKSSKPIYVAQYMTG-GSSDGGTGDPEMVLVPPVEQYLNSYVFFTDPTYPNNYLVI 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316090325  353 AKTSATA--RLQLDNKNlPQDVQWKKVAGTDFSWAEMSYkqisGNNIHTVSSSGsSFGLYSIG 413
Cdd:pfam17517  236 VRTKSTGgfDVTLDGAL-GELTDWKPGTGGEYEYARVDL----GTGAHTVESDG-PFGVTVYG 292
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 469-625 8.81e-39

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.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 142.89  E-value: 8.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  469 CWAMGDPHYRTFDGRRFDFMGTCTYVIAKNCESNSKlPTFEVLAQNENRGSLKVsYIGLVIVKVYDTTVTVVRseNGRVR 548
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325  549 IDNSLWSLPIVLNNSKLNLFQCGR-SAVIETDFGLSVRYDWDHNLVVNLSSSFAGKTCGLCGNFNGSPADDFTTPSGT 625
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1668-1824 1.64e-37

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.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 139.43  E-value: 1.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1668 CWAWGDPHYHTFDGYNFDFQGTCKYVISKTCGTLYGLVpFSVNERNDNRGNTAVsYVREVDVLVYGYTITIRKNqiGQIM 1747
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKG--GTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325 1748 VDGELVNLPVQLGDGEVTVFQRGNA-AELQTDFGLVVTYDWNWHVVIKLPSSYYGSVCGLCGNFNGNSGDELQNPTGQ 1824
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFVvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2449-2603 7.59e-36

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.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 134.42  E-value: 7.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2449 CVASGDPHYTSFDGRRFDFQGTCIYTLAKVCDDDKGQLtpFTVTQGNEKyGNGKVAVTNAVAVTVYGYVIYIQQRLpwKV 2528
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS--FSVTNKNCN-GGASGVCLKSVTVIVGDLEITLQKGG--TV 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325 2529 IVNDELLNLPLSLEEGSLIVTQEGRNIVI-RTVFGLKVLYDTVYYVEVVVPSTYQGRMCGLCGNYNNKGSDDFMLP 2603
Cdd:pfam00094   76 LVNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1249-1409 1.83e-35

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.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.26  E-value: 1.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1249 CRASGDPHYLSFDGRKFDFQGTCTYTLSKSCGVEGTHlqAFSVQVENEQWDQmRGQKKVSVTRLVamevyGFTLIMRNKM 1328
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF--SFSVTNKNCNGGA-SGVCLKSVTVIV-----GDLEITLQKG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1329 LGVLINGEFNNLPVNLNNGAVKVYQEGRNYVI-ATDFELVVTYDLVYHVTVTVPGNYRGKVCGLCGNFNGDKNDDFQMSN 1407
Cdd:pfam00094   73 GTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152


                   ..
gi 1316090325 1408 HQ 1409
Cdd:pfam00094  153 GT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 853-1012 1.00e-34

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.


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.76  E-value: 1.00e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   853 CQALSQSTCHATGDPHYLTFDKMRFDFQGTCVYQLAALCSKDPElvpFEVLVQNDQRGSKVvSYTKLVQINVYSTSIVIT 932
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT---FSVLLKNVPCGGGA-TCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   933 NTHKDlILVNNELVNLPINLNDGQISVHKSGWDAVVTTDFGL-KVSFNWQSAAFVTLPSNYMGAVCGLCGNYNGKPQDDL 1011
Cdd:smart00216   80 DDNGK-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    .
gi 1316090325  1012 T 1012
Cdd:smart00216  159 R 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2061-2216 2.63e-34

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.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 130.18  E-value: 2.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2061 CTASGDPHYRTFDGRKYDFQGTCEYQLAGLCSQHAGLVpFNVTVQNDNRGSKAVsYTKTVKISIHGATLIISKEYpyKVL 2140
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGG--TVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 2141 LNGQLALLPL-DYNNELTVFQSGRTaVLETVAGITVSFDW--GSTVTISLPSTYQGMVCGLCGNYNGKAQDDLAMPNGQ 2216
Cdd:pfam00094   77 VNGQKVSLPYkSDGGEVEILGSGFV-VVDLSPGVGLQVDGdgRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2644-2719 7.40e-30

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.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 114.36  E-value: 7.40e-30
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  2644 LYGKPDSCGIISAPNGPFKACHSKVDPASYVSNCVFDVCATDGNKDTLCDSIQAYALACQGAGIQIQPWRSTSFCP 2719
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1055-1130 9.64e-28

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.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 108.20  E-value: 9.64e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  1055 QYEKKDFCGIIRDPNGPFQECHAKVDPADYFEDCVYDVCLYKGRKDVLCQAITSYTSACQKVGAKVHSWRTTQFCA 1130
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2256-2330 2.04e-27

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.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 107.43  E-value: 2.04e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  2256 YQATKYCGIIADKAGPFRECHSLVDPTPYMEDCVYDVCQYHGHQGSVCDAVEVYVSECQSRGITIHSWRTNTFCP 2330
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1450-1524 1.88e-25

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.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 102.03  E-value: 1.88e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  1450 FSKPTYCGIIAAANGPFVACHSKIDPQLYFDDCVFDLCASNGEGNVLCDSVAAYAYNCHLAGVDVKDWRTPSFCP 1524
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 667-741 3.51e-21

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.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 89.71  E-value: 3.51e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325   667 YGSNSYCGLIEKENGPFNKCHPVIDPQAYLENCKFDLCMGGGLRQFLCKAFEAYTEACQNAGIQVQDWRNMAKCP 741
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1871-1940 9.22e-17

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.


:

Pssm-ID: 462584  Cd Length: 68  Bit Score: 76.65  E-value: 9.22e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1871 FCGALTAktNNVFQKCNGKLDPQAFMNSCVYDMCLNKGDKKMLCQALDSYNQQCREDGIIIKNWRQTFGC 1940
Cdd:pfam08742    1 KCGLLSD--SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 744-797 6.43e-16

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: 73.89  E-value: 6.43e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  744 CPANSHYEFCGNACPATCSDPTAPSKCKHPCVETCTCDNGFVLS-GDKCVPAAKC 797
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
VWD super family cl47498
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2836-2988 6.53e-14

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.


The actual alignment was detected with superfamily member pfam00094:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 71.63  E-value: 6.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2836 CNISPVGELSSFDGMSGKIGAQGAFDLASLCNEASNqwFRVVVDVRLCRKNAPLA-VAALYVFFKDTTVVVNSEHVTWVN 2914
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD--FSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316090325 2915 GRKVSLPSKvTNELSVQI--SNRSVVIERLS-GVQVIYSMSQKVTVTVDGNLSGEICGACGNYNNNSKDDMKTADGK 2988
Cdd:pfam00094   79 GQKVSLPYK-SDGGEVEIlgSGFVVVDLSPGvGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1133-1186 1.64e-13

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: 67.34  E-value: 1.64e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1133 CPNNSHYEICATACPATCSSLAPPQGCEDICEESCACDEDYILS-GNLCVPFSQC 1186
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2333-2386 3.85e-12

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: 63.10  E-value: 3.85e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2333 CPANSHYTLCATGCPTSCASLTSFATCHRRCAEACECDQGYLLS-GETCVPVREC 2386
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1940-1997 3.17e-11

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: 60.86  E-value: 3.17e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 1940 CPMNcqrySHYEECASPCQPSCPFPEEKQMCSGTCVEACVCDMGYVLSA-GVCVPSKTC 1997
Cdd:pfam01826    1 CPAN----EVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSgGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2722-2775 3.57e-11

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: 60.41  E-value: 3.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2722 CPPHSHYEVCADTCKGTCASFLQQVTCSESCFEGCQCDAGFV-SDGIQCVPLDNC 2775
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVrNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1527-1580 8.70e-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: 50.78  E-value: 8.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1527 CFSNSHYEMCAETCSTSCPGLTEIVECPTGCTEGCECDTGFLFN-GQTCVNETEC 1580
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 799-854 1.43e-06

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 47.30  E-value: 1.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  799 CTYEGHYIPAGEaFWADQRCKRWCKCVPGtrRVECQDKGCGPGQQCKLVNGIRRCQ 854
Cdd:pfam12714    2 KDAQGNYIPAGK-TWFSSGCTQSCTCTGG--NIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2388-2442 2.36e-05

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 43.83  E-value: 2.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2388 CSYDGQYYKKGEVFYPEDkCMKKCTCGEnGAVTCQEEKCRKGEVCKLLNGVKGCH 2442
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSG-CTQSCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1191-1242 6.74e-04

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 39.98  E-value: 6.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1316090325 1191 NDRYYKIGEVFYQNGQCQlECKCTQdGEVECKNFSCGPNEKCKIENGVQKCH 1242
Cdd:pfam12714    5 QGNYIPAGKTWFSSGCTQ-SCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1582-1635 3.39e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 38.05  E-value: 3.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1316090325 1582 CYENGKTYKPGEIIYEEECNTKCTCnPATGLVCEKYSCPKDTKCMVKNGIRACH 1635
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
 
Name Accession Description Interval E-value
IgGFc_binding pfam17517
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
 119-413 1.02e-72

IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.


Pssm-ID: 465430  Cd Length: 292  Bit Score: 245.72  E-value: 1.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  119 DTSVIYPTTAWGKEYFILTPPSGPYGTSKEFAVTNGKDKNQVEIFPEALITFQGRVfNKGNKLVIDLEPYESVQLQSKYD 198
Cdd:pfam17517    1 DATLLLPVSSLGTEYYVVSWDPTPGSGPSYFQIVATEDNTTVTITPTVDVTGGGGV-YAGSPFTITLNRGEVLQLQSDGD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  199 LSGSQVTSQRPVAVFSGHTCFLL---FSKCNHVYEQLLPVSSWGTSFILSALSFQKNYDSVY---LQASQATQVSVNDGK 272
Cdd:pfam17517   80 LTGSRITSDKPVAVFSGHSCANVpsgGGACDHLVEQLPPVSSWGKEYVVVPFRRGNGDEQSIyriVAAEDNTTVTVNGAA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  273 GKTAfSLSRGTMKEIKLKHPetLFIQSDHGIQVLMLFNGvEYSWFQIYDPFFMTILPIDRFCSSYSLEALESFDNKALIV 352
Cdd:pfam17517  160 GAPA-TLNAGEVYEFSTDAP--FYVKSSKPIYVAQYMTG-GSSDGGTGDPEMVLVPPVEQYLNSYVFFTDPTYPNNYLVI 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316090325  353 AKTSATA--RLQLDNKNlPQDVQWKKVAGTDFSWAEMSYkqisGNNIHTVSSSGsSFGLYSIG 413
Cdd:pfam17517  236 VRTKSTGgfDVTLDGAL-GELTDWKPGTGGEYEYARVDL----GTGAHTVESDG-PFGVTVYG 292
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 469-625 8.81e-39

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 142.89  E-value: 8.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  469 CWAMGDPHYRTFDGRRFDFMGTCTYVIAKNCESNSKlPTFEVLAQNENRGSLKVsYIGLVIVKVYDTTVTVVRseNGRVR 548
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325  549 IDNSLWSLPIVLNNSKLNLFQCGR-SAVIETDFGLSVRYDWDHNLVVNLSSSFAGKTCGLCGNFNGSPADDFTTPSGT 625
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 455-624 1.08e-38

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 142.93  E-value: 1.08e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   455 PSCVAKPVKPqlgTCWAMGDPHYRTFDGRRFDFMGTCTYVIAKNCESNsklPTFEVLAQNENRGSlKVSYIGLVIVKVYD 534
Cdd:smart00216    1 WCCTQEECSP---TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGG-GATCLKSVKVELNG 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   535 TTVTVVrSENGRVRIDNSLWSLPIVLNNSKLNLFQCGRSAVIETDFGL-SVRYDWDHNLVVNLSSSFAGKTCGLCGNFNG 613
Cdd:smart00216   74 DEIELK-DDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDG 152

                           170
                    ....*....|.
gi 1316090325   614 SPADDFTTPSG 624
Cdd:smart00216  153 EPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1668-1824 1.64e-37

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 139.43  E-value: 1.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1668 CWAWGDPHYHTFDGYNFDFQGTCKYVISKTCGTLYGLVpFSVNERNDNRGNTAVsYVREVDVLVYGYTITIRKNqiGQIM 1747
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKG--GTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325 1748 VDGELVNLPVQLGDGEVTVFQRGNA-AELQTDFGLVVTYDWNWHVVIKLPSSYYGSVCGLCGNFNGNSGDELQNPTGQ 1824
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFVvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1666-1823 3.04e-37

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 138.69  E-value: 3.04e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  1666 GTCWAWGDPHYHTFDGYNFDFQGTCKYVISKTCGTlygLVPFSVNERNDNRGNTAvSYVREVDVLVYGYTITIRKNQiGQ 1745
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS---EPTFSVLLKNVPCGGGA-TCLKSVKVELNGDEIELKDDN-GK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325  1746 IMVDGELVNLPVQLGDGEVTVFQRGNAAELQTDFGLV-VTYDWNWHVVIKLPSSYYGSVCGLCGNFNGNSGDELQNPTG 1823
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2449-2603 7.59e-36

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 134.42  E-value: 7.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2449 CVASGDPHYTSFDGRRFDFQGTCIYTLAKVCDDDKGQLtpFTVTQGNEKyGNGKVAVTNAVAVTVYGYVIYIQQRLpwKV 2528
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS--FSVTNKNCN-GGASGVCLKSVTVIVGDLEITLQKGG--TV 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325 2529 IVNDELLNLPLSLEEGSLIVTQEGRNIVI-RTVFGLKVLYDTVYYVEVVVPSTYQGRMCGLCGNYNNKGSDDFMLP 2603
Cdd:pfam00094   76 LVNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1249-1409 1.83e-35

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.26  E-value: 1.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1249 CRASGDPHYLSFDGRKFDFQGTCTYTLSKSCGVEGTHlqAFSVQVENEQWDQmRGQKKVSVTRLVamevyGFTLIMRNKM 1328
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF--SFSVTNKNCNGGA-SGVCLKSVTVIV-----GDLEITLQKG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1329 LGVLINGEFNNLPVNLNNGAVKVYQEGRNYVI-ATDFELVVTYDLVYHVTVTVPGNYRGKVCGLCGNFNGDKNDDFQMSN 1407
Cdd:pfam00094   73 GTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152


                   ..
gi 1316090325 1408 HQ 1409
Cdd:pfam00094  153 GT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1241-1408 3.74e-35

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.91  E-value: 3.74e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  1241 CHPVGKGVCRASGDPHYLSFDGRKFDFQGTCTYTLSKSCGVEGThlqaFSVQVENEQwdqmrGQKKVSVTRLVAMEVYGF 1320
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVP-----CGGGATCLKSVKVELNGD 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  1321 TLIMRNKMLGVLINGEFNNLPVNLNNGAVKVYQEGRNYVIATDFELV-VTYDLVYHVTVTVPGNYRGKVCGLCGNFNGDK 1399
Cdd:smart00216   75 EIELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 1316090325  1400 NDDFQMSNH 1408
Cdd:smart00216  155 EDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 853-1012 1.00e-34

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.76  E-value: 1.00e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   853 CQALSQSTCHATGDPHYLTFDKMRFDFQGTCVYQLAALCSKDPElvpFEVLVQNDQRGSKVvSYTKLVQINVYSTSIVIT 932
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT---FSVLLKNVPCGGGA-TCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   933 NTHKDlILVNNELVNLPINLNDGQISVHKSGWDAVVTTDFGL-KVSFNWQSAAFVTLPSNYMGAVCGLCGNYNGKPQDDL 1011
Cdd:smart00216   80 DDNGK-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    .
gi 1316090325  1012 T 1012
Cdd:smart00216  159 R 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2061-2216 2.63e-34

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 130.18  E-value: 2.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2061 CTASGDPHYRTFDGRKYDFQGTCEYQLAGLCSQHAGLVpFNVTVQNDNRGSKAVsYTKTVKISIHGATLIISKEYpyKVL 2140
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGG--TVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 2141 LNGQLALLPL-DYNNELTVFQSGRTaVLETVAGITVSFDW--GSTVTISLPSTYQGMVCGLCGNYNGKAQDDLAMPNGQ 2216
Cdd:pfam00094   77 VNGQKVSLPYkSDGGEVEILGSGFV-VVDLSPGVGLQVDGdgRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2050-2215 6.55e-33

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 126.36  E-value: 6.55e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2050 ERACRPIsyglCTASGDPHYRTFDGRKYDFQGTCEYQLAGLCSQHAglvPFNVTVQNDNRGSKAvSYTKTVKISIHGATL 2129
Cdd:smart00216    5 QEECSPT----CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP---TFSVLLKNVPCGGGA-TCLKSVKVELNGDEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2130 IISKEYpYKVLLNGQLALLPLDYNN-ELTVFQSGRTAVLETVAGI-TVSFDWGSTVTISLPSTYQGMVCGLCGNYNGKAQ 2207
Cdd:smart00216   77 ELKDDN-GKVTVNGQQVSLPYKTSDgSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1316090325  2208 DDLAMPNG 2215
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 861-1012 1.39e-32

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.18  E-value: 1.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  861 CHATGDPHYLTFDKMRFDFQGTCVYQLAALCSKDPELVpFEVLVQNDQRGSKVVsYTKLVQINVYSTSIVITntHKDLIL 940
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQ--KGGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316090325  941 VNNELVNLPINLNDGQISVHKSGwDAVVTTDFGLKVSFNWQS--AAFVTLPSNYMGAVCGLCGNYNGKPQDDLT 1012
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSG-FVVVDLSPGVGLQVDGDGrgQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2441-2603 4.24e-32

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 124.05  E-value: 4.24e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2441 CHPEGEAKCVASGDPHYTSFDGRRFDFQGTCIYTLAKVCDDDKgqltPFTVTQGNEKYGnGKVAVTNAVAVTVYGYVIYI 2520
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP----TFSVLLKNVPCG-GGATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2521 QQRLPwKVIVNDELLNLPLSLEEGSLIVTQEGRNIVIRTVFGL-KVLYDTVYYVEVVVPSTYQGRMCGLCGNYNNKGSDD 2599
Cdd:smart00216   79 KDDNG-KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....
gi 1316090325  2600 FMLP 2603
Cdd:smart00216  158 FRTP 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2644-2719 7.40e-30

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 114.36  E-value: 7.40e-30
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  2644 LYGKPDSCGIISAPNGPFKACHSKVDPASYVSNCVFDVCATDGNKDTLCDSIQAYALACQGAGIQIQPWRSTSFCP 2719
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1055-1130 9.64e-28

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 108.20  E-value: 9.64e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  1055 QYEKKDFCGIIRDPNGPFQECHAKVDPADYFEDCVYDVCLYKGRKDVLCQAITSYTSACQKVGAKVHSWRTTQFCA 1130
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2256-2330 2.04e-27

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 107.43  E-value: 2.04e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  2256 YQATKYCGIIADKAGPFRECHSLVDPTPYMEDCVYDVCQYHGHQGSVCDAVEVYVSECQSRGITIHSWRTNTFCP 2330
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1450-1524 1.88e-25

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 102.03  E-value: 1.88e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  1450 FSKPTYCGIIAAANGPFVACHSKIDPQLYFDDCVFDLCASNGEGNVLCDSVAAYAYNCHLAGVDVKDWRTPSFCP 1524
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2651-2718 1.63e-24

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 98.99  E-value: 1.63e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325 2651 CGIISApNGPFKACHSKVDPASYVSNCVFDVCATDGNKDTLCDSIQAYALACQGAGIQIQPWRSTSFC 2718
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2261-2329 1.44e-23

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 96.30  E-value: 1.44e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 2261 YCGIIADkAGPFRECHSLVDPTPYMEDCVYDVCQYHGHQGSVCDAVEVYVSECQSRGITIHSWRTNTFC 2329
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1061-1129 3.46e-23

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 95.14  E-value: 3.46e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 1061 FCGIIRDpNGPFQECHAKVDPADYFEDCVYDVCLYKGRKDVLCQAITSYTSACQKVGAKVHSWRTTQFC 1129
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1455-1523 6.88e-22

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 91.29  E-value: 6.88e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 1455 YCGIIAAaNGPFVACHSKIDPQLYFDDCVFDLCASNGEGNVLCDSVAAYAYNCHLAGVDVKDWRTPSFC 1523
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 667-741 3.51e-21

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 89.71  E-value: 3.51e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325   667 YGSNSYCGLIEKENGPFNKCHPVIDPQAYLENCKFDLCMGGGLRQFLCKAFEAYTEACQNAGIQVQDWRNMAKCP 741
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 672-740 7.02e-20

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 85.89  E-value: 7.02e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325  672 YCGLIeKENGPFNKCHPVIDPQAYLENCKFDLCMGGGLRQFLCKAFEAYTEACQNAGIQVQDWRNMAKC 740
Cdd:pfam08742    1 KCGLL-SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1871-1940 9.22e-17

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 76.65  E-value: 9.22e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1871 FCGALTAktNNVFQKCNGKLDPQAFMNSCVYDMCLNKGDKKMLCQALDSYNQQCREDGIIIKNWRQTFGC 1940
Cdd:pfam08742    1 KCGLLSD--SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1865-1941 5.60e-16

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.07  E-value: 5.60e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316090325  1865 LYQTQAFCGALTaKTNNVFQKCNGKLDPQAFMNSCVYDMCLNKGDKKMLCQALDSYNQQCREDGIIIKNWRQTFGCP 1941
Cdd:smart00832    1 KYYACSQCGILL-SPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 744-797 6.43e-16

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: 73.89  E-value: 6.43e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  744 CPANSHYEFCGNACPATCSDPTAPSKCKHPCVETCTCDNGFVLS-GDKCVPAAKC 797
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 744-797 7.22e-16

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: 73.96  E-value: 7.22e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  744 CPANSHYEFCGNACPATCSDPTAPSKCKHPCVETCTCDNGFVLS-GDKCVPAAKC 797
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2836-2988 6.53e-14

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 71.63  E-value: 6.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2836 CNISPVGELSSFDGMSGKIGAQGAFDLASLCNEASNqwFRVVVDVRLCRKNAPLA-VAALYVFFKDTTVVVNSEHVTWVN 2914
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD--FSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316090325 2915 GRKVSLPSKvTNELSVQI--SNRSVVIERLS-GVQVIYSMSQKVTVTVDGNLSGEICGACGNYNNNSKDDMKTADGK 2988
Cdd:pfam00094   79 GQKVSLPYK-SDGGEVEIlgSGFVVVDLSPGvGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1133-1186 1.64e-13

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: 67.34  E-value: 1.64e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1133 CPNNSHYEICATACPATCSSLAPPQGCEDICEESCACDEDYILS-GNLCVPFSQC 1186
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1133-1186 9.89e-13

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: 65.10  E-value: 9.89e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1133 CPNNSHYEICATACPATCSSLAPPQGCEDICEESCACDEDYILS-GNLCVPFSQC 1186
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2333-2386 3.85e-12

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: 63.10  E-value: 3.85e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2333 CPANSHYTLCATGCPTSCASLTSFATCHRRCAEACECDQGYLLS-GETCVPVREC 2386
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2333-2386 8.57e-12

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: 62.40  E-value: 8.57e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2333 CPANSHYTLCATGCPTSCASLTSFATCHRRCAEACECDQGYLLSGE-TCVPVREC 2386
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1940-1997 3.17e-11

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: 60.86  E-value: 3.17e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 1940 CPMNcqrySHYEECASPCQPSCPFPEEKQMCSGTCVEACVCDMGYVLSA-GVCVPSKTC 1997
Cdd:pfam01826    1 CPAN----EVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSgGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1944-1997 3.50e-11

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: 60.41  E-value: 3.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1944 CQRYSHYEECASPCQPSCPFPEEKQMCSGTCVEACVCDMGYVLSA-GVCVPSKTC 1997
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2722-2775 3.57e-11

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: 60.41  E-value: 3.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2722 CPPHSHYEVCADTCKGTCASFLQQVTCSESCFEGCQCDAGFV-SDGIQCVPLDNC 2775
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVrNSGGKCVPPSQC 55
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2829-2987 3.68e-11

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 63.96  E-value: 3.68e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2829 CHVIQGHCNISPVGELSSFDGMSgkigaqgaFDLASLCNE------ASNQWFRVVVDvRLCRKNAPLAVAALYVFFKDTT 2902
Cdd:smart00216    5 QEECSPTCSVSGDPHYTTFDGVA--------YTFPGNCYYvlaqdcSSEPTFSVLLK-NVPCGGGATCLKSVKVELNGDE 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2903 VVVNSEHVT-WVNGRKVSLPsKVTNELSVQISNR---SVVIERLSGVQVIYSMSQKVTVTVDGNLSGEICGACGNYNNNS 2978
Cdd:smart00216   76 IELKDDNGKvTVNGQQVSLP-YKTSDGSIQIRSSggyLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 1316090325  2979 KDDMKTADG 2987
Cdd:smart00216  155 EDDFRTPDG 163
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2722-2775 7.43e-11

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: 59.71  E-value: 7.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2722 CPPHSHYEVCADTCKGTCASFLQQVTCSESCFEGCQCDAGFV-SDGIQCVPLDNC 2775
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVrNSGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1527-1580 8.70e-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: 50.78  E-value: 8.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1527 CFSNSHYEMCAETCSTSCPGLTEIVECPTGCTEGCECDTGFLFN-GQTCVNETEC 1580
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1527-1580 1.58e-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: 50.08  E-value: 1.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1527 CFSNSHYEMCAETCSTSCPGLTEIVECPTGCTEGCECDTGFLFN-GQTCVNETEC 1580
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 799-854 1.43e-06

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 47.30  E-value: 1.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  799 CTYEGHYIPAGEaFWADQRCKRWCKCVPGtrRVECQDKGCGPGQQCKLVNGIRRCQ 854
Cdd:pfam12714    2 KDAQGNYIPAGK-TWFSSGCTQSCTCTGG--NIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2388-2442 2.36e-05

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 43.83  E-value: 2.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2388 CSYDGQYYKKGEVFYPEDkCMKKCTCGEnGAVTCQEEKCRKGEVCKLLNGVKGCH 2442
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSG-CTQSCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1191-1242 6.74e-04

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 39.98  E-value: 6.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1316090325 1191 NDRYYKIGEVFYQNGQCQlECKCTQdGEVECKNFSCGPNEKCKIENGVQKCH 1242
Cdd:pfam12714    5 QGNYIPAGKTWFSSGCTQ-SCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1582-1635 3.39e-03

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 38.05  E-value: 3.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1316090325 1582 CYENGKTYKPGEIIYEEECNTKCTCnPATGLVCEKYSCPKDTKCMVKNGIRACH 1635
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
 
Name Accession Description Interval E-value
IgGFc_binding pfam17517
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
 119-413 1.02e-72

IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been shown to confer IgG Fc binding activity. It may play a role in immune protection and inflammation in the intestines of primates.


Pssm-ID: 465430  Cd Length: 292  Bit Score: 245.72  E-value: 1.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  119 DTSVIYPTTAWGKEYFILTPPSGPYGTSKEFAVTNGKDKNQVEIFPEALITFQGRVfNKGNKLVIDLEPYESVQLQSKYD 198
Cdd:pfam17517    1 DATLLLPVSSLGTEYYVVSWDPTPGSGPSYFQIVATEDNTTVTITPTVDVTGGGGV-YAGSPFTITLNRGEVLQLQSDGD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  199 LSGSQVTSQRPVAVFSGHTCFLL---FSKCNHVYEQLLPVSSWGTSFILSALSFQKNYDSVY---LQASQATQVSVNDGK 272
Cdd:pfam17517   80 LTGSRITSDKPVAVFSGHSCANVpsgGGACDHLVEQLPPVSSWGKEYVVVPFRRGNGDEQSIyriVAAEDNTTVTVNGAA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  273 GKTAfSLSRGTMKEIKLKHPetLFIQSDHGIQVLMLFNGvEYSWFQIYDPFFMTILPIDRFCSSYSLEALESFDNKALIV 352
Cdd:pfam17517  160 GAPA-TLNAGEVYEFSTDAP--FYVKSSKPIYVAQYMTG-GSSDGGTGDPEMVLVPPVEQYLNSYVFFTDPTYPNNYLVI 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316090325  353 AKTSATA--RLQLDNKNlPQDVQWKKVAGTDFSWAEMSYkqisGNNIHTVSSSGsSFGLYSIG 413
Cdd:pfam17517  236 VRTKSTGgfDVTLDGAL-GELTDWKPGTGGEYEYARVDL----GTGAHTVESDG-PFGVTVYG 292
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 469-625 8.81e-39

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 142.89  E-value: 8.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  469 CWAMGDPHYRTFDGRRFDFMGTCTYVIAKNCESNSKlPTFEVLAQNENRGSLKVsYIGLVIVKVYDTTVTVVRseNGRVR 548
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325  549 IDNSLWSLPIVLNNSKLNLFQCGR-SAVIETDFGLSVRYDWDHNLVVNLSSSFAGKTCGLCGNFNGSPADDFTTPSGT 625
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 455-624 1.08e-38

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 142.93  E-value: 1.08e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   455 PSCVAKPVKPqlgTCWAMGDPHYRTFDGRRFDFMGTCTYVIAKNCESNsklPTFEVLAQNENRGSlKVSYIGLVIVKVYD 534
Cdd:smart00216    1 WCCTQEECSP---TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGG-GATCLKSVKVELNG 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   535 TTVTVVrSENGRVRIDNSLWSLPIVLNNSKLNLFQCGRSAVIETDFGL-SVRYDWDHNLVVNLSSSFAGKTCGLCGNFNG 613
Cdd:smart00216   74 DEIELK-DDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDG 152

                           170
                    ....*....|.
gi 1316090325   614 SPADDFTTPSG 624
Cdd:smart00216  153 EPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1668-1824 1.64e-37

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 139.43  E-value: 1.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1668 CWAWGDPHYHTFDGYNFDFQGTCKYVISKTCGTLYGLVpFSVNERNDNRGNTAVsYVREVDVLVYGYTITIRKNqiGQIM 1747
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKG--GTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325 1748 VDGELVNLPVQLGDGEVTVFQRGNA-AELQTDFGLVVTYDWNWHVVIKLPSSYYGSVCGLCGNFNGNSGDELQNPTGQ 1824
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFVvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1666-1823 3.04e-37

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 138.69  E-value: 3.04e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  1666 GTCWAWGDPHYHTFDGYNFDFQGTCKYVISKTCGTlygLVPFSVNERNDNRGNTAvSYVREVDVLVYGYTITIRKNQiGQ 1745
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS---EPTFSVLLKNVPCGGGA-TCLKSVKVELNGDEIELKDDN-GK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325  1746 IMVDGELVNLPVQLGDGEVTVFQRGNAAELQTDFGLV-VTYDWNWHVVIKLPSSYYGSVCGLCGNFNGNSGDELQNPTG 1823
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2449-2603 7.59e-36

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 134.42  E-value: 7.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2449 CVASGDPHYTSFDGRRFDFQGTCIYTLAKVCDDDKGQLtpFTVTQGNEKyGNGKVAVTNAVAVTVYGYVIYIQQRLpwKV 2528
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS--FSVTNKNCN-GGASGVCLKSVTVIVGDLEITLQKGG--TV 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325 2529 IVNDELLNLPLSLEEGSLIVTQEGRNIVI-RTVFGLKVLYDTVYYVEVVVPSTYQGRMCGLCGNYNNKGSDDFMLP 2603
Cdd:pfam00094   76 LVNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1249-1409 1.83e-35

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.26  E-value: 1.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1249 CRASGDPHYLSFDGRKFDFQGTCTYTLSKSCGVEGTHlqAFSVQVENEQWDQmRGQKKVSVTRLVamevyGFTLIMRNKM 1328
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF--SFSVTNKNCNGGA-SGVCLKSVTVIV-----GDLEITLQKG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1329 LGVLINGEFNNLPVNLNNGAVKVYQEGRNYVI-ATDFELVVTYDLVYHVTVTVPGNYRGKVCGLCGNFNGDKNDDFQMSN 1407
Cdd:pfam00094   73 GTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152


                   ..
gi 1316090325 1408 HQ 1409
Cdd:pfam00094  153 GT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1241-1408 3.74e-35

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.91  E-value: 3.74e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  1241 CHPVGKGVCRASGDPHYLSFDGRKFDFQGTCTYTLSKSCGVEGThlqaFSVQVENEQwdqmrGQKKVSVTRLVAMEVYGF 1320
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVP-----CGGGATCLKSVKVELNGD 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  1321 TLIMRNKMLGVLINGEFNNLPVNLNNGAVKVYQEGRNYVIATDFELV-VTYDLVYHVTVTVPGNYRGKVCGLCGNFNGDK 1399
Cdd:smart00216   75 EIELKDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 1316090325  1400 NDDFQMSNH 1408
Cdd:smart00216  155 EDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 853-1012 1.00e-34

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.76  E-value: 1.00e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   853 CQALSQSTCHATGDPHYLTFDKMRFDFQGTCVYQLAALCSKDPElvpFEVLVQNDQRGSKVvSYTKLVQINVYSTSIVIT 932
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT---FSVLLKNVPCGGGA-TCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325   933 NTHKDlILVNNELVNLPINLNDGQISVHKSGWDAVVTTDFGL-KVSFNWQSAAFVTLPSNYMGAVCGLCGNYNGKPQDDL 1011
Cdd:smart00216   80 DDNGK-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    .
gi 1316090325  1012 T 1012
Cdd:smart00216  159 R 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2061-2216 2.63e-34

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 130.18  E-value: 2.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2061 CTASGDPHYRTFDGRKYDFQGTCEYQLAGLCSQHAGLVpFNVTVQNDNRGSKAVsYTKTVKISIHGATLIISKEYpyKVL 2140
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGG--TVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 2141 LNGQLALLPL-DYNNELTVFQSGRTaVLETVAGITVSFDW--GSTVTISLPSTYQGMVCGLCGNYNGKAQDDLAMPNGQ 2216
Cdd:pfam00094   77 VNGQKVSLPYkSDGGEVEILGSGFV-VVDLSPGVGLQVDGdgRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2050-2215 6.55e-33

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 126.36  E-value: 6.55e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2050 ERACRPIsyglCTASGDPHYRTFDGRKYDFQGTCEYQLAGLCSQHAglvPFNVTVQNDNRGSKAvSYTKTVKISIHGATL 2129
Cdd:smart00216    5 QEECSPT----CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP---TFSVLLKNVPCGGGA-TCLKSVKVELNGDEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2130 IISKEYpYKVLLNGQLALLPLDYNN-ELTVFQSGRTAVLETVAGI-TVSFDWGSTVTISLPSTYQGMVCGLCGNYNGKAQ 2207
Cdd:smart00216   77 ELKDDN-GKVTVNGQQVSLPYKTSDgSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1316090325  2208 DDLAMPNG 2215
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 861-1012 1.39e-32

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 125.18  E-value: 1.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  861 CHATGDPHYLTFDKMRFDFQGTCVYQLAALCSKDPELVpFEVLVQNDQRGSKVVsYTKLVQINVYSTSIVITntHKDLIL 940
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQ--KGGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316090325  941 VNNELVNLPINLNDGQISVHKSGwDAVVTTDFGLKVSFNWQS--AAFVTLPSNYMGAVCGLCGNYNGKPQDDLT 1012
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSG-FVVVDLSPGVGLQVDGDGrgQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2441-2603 4.24e-32

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 124.05  E-value: 4.24e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2441 CHPEGEAKCVASGDPHYTSFDGRRFDFQGTCIYTLAKVCDDDKgqltPFTVTQGNEKYGnGKVAVTNAVAVTVYGYVIYI 2520
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP----TFSVLLKNVPCG-GGATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2521 QQRLPwKVIVNDELLNLPLSLEEGSLIVTQEGRNIVIRTVFGL-KVLYDTVYYVEVVVPSTYQGRMCGLCGNYNNKGSDD 2599
Cdd:smart00216   79 KDDNG-KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....
gi 1316090325  2600 FMLP 2603
Cdd:smart00216  158 FRTP 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2644-2719 7.40e-30

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 114.36  E-value: 7.40e-30
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  2644 LYGKPDSCGIISAPNGPFKACHSKVDPASYVSNCVFDVCATDGNKDTLCDSIQAYALACQGAGIQIQPWRSTSFCP 2719
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1055-1130 9.64e-28

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 108.20  E-value: 9.64e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  1055 QYEKKDFCGIIRDPNGPFQECHAKVDPADYFEDCVYDVCLYKGRKDVLCQAITSYTSACQKVGAKVHSWRTTQFCA 1130
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2256-2330 2.04e-27

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 107.43  E-value: 2.04e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  2256 YQATKYCGIIADKAGPFRECHSLVDPTPYMEDCVYDVCQYHGHQGSVCDAVEVYVSECQSRGITIHSWRTNTFCP 2330
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1450-1524 1.88e-25

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 102.03  E-value: 1.88e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  1450 FSKPTYCGIIAAANGPFVACHSKIDPQLYFDDCVFDLCASNGEGNVLCDSVAAYAYNCHLAGVDVKDWRTPSFCP 1524
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2651-2718 1.63e-24

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 98.99  E-value: 1.63e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316090325 2651 CGIISApNGPFKACHSKVDPASYVSNCVFDVCATDGNKDTLCDSIQAYALACQGAGIQIQPWRSTSFC 2718
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2261-2329 1.44e-23

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 96.30  E-value: 1.44e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 2261 YCGIIADkAGPFRECHSLVDPTPYMEDCVYDVCQYHGHQGSVCDAVEVYVSECQSRGITIHSWRTNTFC 2329
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1061-1129 3.46e-23

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 95.14  E-value: 3.46e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 1061 FCGIIRDpNGPFQECHAKVDPADYFEDCVYDVCLYKGRKDVLCQAITSYTSACQKVGAKVHSWRTTQFC 1129
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1455-1523 6.88e-22

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 91.29  E-value: 6.88e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 1455 YCGIIAAaNGPFVACHSKIDPQLYFDDCVFDLCASNGEGNVLCDSVAAYAYNCHLAGVDVKDWRTPSFC 1523
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 667-741 3.51e-21

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 89.71  E-value: 3.51e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325   667 YGSNSYCGLIEKENGPFNKCHPVIDPQAYLENCKFDLCMGGGLRQFLCKAFEAYTEACQNAGIQVQDWRNMAKCP 741
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 672-740 7.02e-20

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 85.89  E-value: 7.02e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325  672 YCGLIeKENGPFNKCHPVIDPQAYLENCKFDLCMGGGLRQFLCKAFEAYTEACQNAGIQVQDWRNMAKC 740
Cdd:pfam08742    1 KCGLL-SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1871-1940 9.22e-17

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.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 76.65  E-value: 9.22e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 1871 FCGALTAktNNVFQKCNGKLDPQAFMNSCVYDMCLNKGDKKMLCQALDSYNQQCREDGIIIKNWRQTFGC 1940
Cdd:pfam08742    1 KCGLLSD--SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1865-1941 5.60e-16

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.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.07  E-value: 5.60e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316090325  1865 LYQTQAFCGALTaKTNNVFQKCNGKLDPQAFMNSCVYDMCLNKGDKKMLCQALDSYNQQCREDGIIIKNWRQTFGCP 1941
Cdd:smart00832    1 KYYACSQCGILL-SPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 744-797 6.43e-16

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: 73.89  E-value: 6.43e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  744 CPANSHYEFCGNACPATCSDPTAPSKCKHPCVETCTCDNGFVLS-GDKCVPAAKC 797
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 744-797 7.22e-16

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: 73.96  E-value: 7.22e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325  744 CPANSHYEFCGNACPATCSDPTAPSKCKHPCVETCTCDNGFVLS-GDKCVPAAKC 797
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2836-2988 6.53e-14

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.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 71.63  E-value: 6.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325 2836 CNISPVGELSSFDGMSGKIGAQGAFDLASLCNEASNqwFRVVVDVRLCRKNAPLA-VAALYVFFKDTTVVVNSEHVTWVN 2914
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD--FSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316090325 2915 GRKVSLPSKvTNELSVQI--SNRSVVIERLS-GVQVIYSMSQKVTVTVDGNLSGEICGACGNYNNNSKDDMKTADGK 2988
Cdd:pfam00094   79 GQKVSLPYK-SDGGEVEIlgSGFVVVDLSPGvGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1133-1186 1.64e-13

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: 67.34  E-value: 1.64e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1133 CPNNSHYEICATACPATCSSLAPPQGCEDICEESCACDEDYILS-GNLCVPFSQC 1186
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1133-1186 9.89e-13

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: 65.10  E-value: 9.89e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1133 CPNNSHYEICATACPATCSSLAPPQGCEDICEESCACDEDYILS-GNLCVPFSQC 1186
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2333-2386 3.85e-12

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: 63.10  E-value: 3.85e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2333 CPANSHYTLCATGCPTSCASLTSFATCHRRCAEACECDQGYLLS-GETCVPVREC 2386
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2333-2386 8.57e-12

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: 62.40  E-value: 8.57e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2333 CPANSHYTLCATGCPTSCASLTSFATCHRRCAEACECDQGYLLSGE-TCVPVREC 2386
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1940-1997 3.17e-11

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: 60.86  E-value: 3.17e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1316090325 1940 CPMNcqrySHYEECASPCQPSCPFPEEKQMCSGTCVEACVCDMGYVLSA-GVCVPSKTC 1997
Cdd:pfam01826    1 CPAN----EVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSgGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1944-1997 3.50e-11

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: 60.41  E-value: 3.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1944 CQRYSHYEECASPCQPSCPFPEEKQMCSGTCVEACVCDMGYVLSA-GVCVPSKTC 1997
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2722-2775 3.57e-11

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: 60.41  E-value: 3.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2722 CPPHSHYEVCADTCKGTCASFLQQVTCSESCFEGCQCDAGFV-SDGIQCVPLDNC 2775
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVrNSGGKCVPPSQC 55
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2829-2987 3.68e-11

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.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 63.96  E-value: 3.68e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2829 CHVIQGHCNISPVGELSSFDGMSgkigaqgaFDLASLCNE------ASNQWFRVVVDvRLCRKNAPLAVAALYVFFKDTT 2902
Cdd:smart00216    5 QEECSPTCSVSGDPHYTTFDGVA--------YTFPGNCYYvlaqdcSSEPTFSVLLK-NVPCGGGATCLKSVKVELNGDE 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316090325  2903 VVVNSEHVT-WVNGRKVSLPsKVTNELSVQISNR---SVVIERLSGVQVIYSMSQKVTVTVDGNLSGEICGACGNYNNNS 2978
Cdd:smart00216   76 IELKDDNGKvTVNGQQVSLP-YKTSDGSIQIRSSggyLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEP 154


                    ....*....
gi 1316090325  2979 KDDMKTADG 2987
Cdd:smart00216  155 EDDFRTPDG 163
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2722-2775 7.43e-11

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: 59.71  E-value: 7.43e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2722 CPPHSHYEVCADTCKGTCASFLQQVTCSESCFEGCQCDAGFV-SDGIQCVPLDNC 2775
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVrNSGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1527-1580 8.70e-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: 50.78  E-value: 8.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1527 CFSNSHYEMCAETCSTSCPGLTEIVECPTGCTEGCECDTGFLFN-GQTCVNETEC 1580
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1527-1580 1.58e-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: 50.08  E-value: 1.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 1527 CFSNSHYEMCAETCSTSCPGLTEIVECPTGCTEGCECDTGFLFN-GQTCVNETEC 1580
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 799-854 1.43e-06

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 47.30  E-value: 1.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1316090325  799 CTYEGHYIPAGEaFWADQRCKRWCKCVPGtrRVECQDKGCGPGQQCKLVNGIRRCQ 854
Cdd:pfam12714    2 KDAQGNYIPAGK-TWFSSGCTQSCTCTGG--NIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2388-2442 2.36e-05

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 43.83  E-value: 2.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1316090325 2388 CSYDGQYYKKGEVFYPEDkCMKKCTCGEnGAVTCQEEKCRKGEVCKLLNGVKGCH 2442
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSG-CTQSCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1191-1242 6.74e-04

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 39.98  E-value: 6.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1316090325 1191 NDRYYKIGEVFYQNGQCQlECKCTQdGEVECKNFSCGPNEKCKIENGVQKCH 1242
Cdd:pfam12714    5 QGNYIPAGKTWFSSGCTQ-SCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1582-1635 3.39e-03

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 38.05  E-value: 3.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1316090325 1582 CYENGKTYKPGEIIYEEECNTKCTCnPATGLVCEKYSCPKDTKCMVKNGIRACH 1635
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH