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Conserved domains on  [gi|1346296|sp|P98092|]
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RecName: Full=Hemocytin; AltName: Full=Humoral lectin; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 238-396 4.07e-46

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: 164.50  E-value: 4.07e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      238 WSCTQRKCAGVCGAWGDSHVNTFDGTQYDFEGVCTYLLAKGAMDGTDgFDVEIQNVPCGTtGATCSKSVTLKVGG----- 312
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGG-GATCLKSVKVELNGdeiel 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      313 -AGNEEIVSLTKNAPIPDISKLKRIKMRKAGAYVFLDVPSLGMSLQWDRGLRVYVKIDTMWQGRVKGLCGNYNGDMRDDF 391
Cdd:smart00216   79 kDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1346296      392 QTPSG 396
Cdd:smart00216  159 RTPDG 163
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1118-1253 4.57e-43

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 154.82  E-value: 4.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296  1118 EPLGLIGELPLENIQVSS-NSEEKDYLSINGNR--GWKPLYNTPG-WVMFDFTGPRNITGILTKGGN----DGWVTSYKV 1189
Cdd:cd00057    1 EPLGMESGLADDQITASSsYSSGWEASRARLNSdnAWTPAVNDPPqWLQVDLGKTRRVTGIQTQGRKgggsSEWVTSYKV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1346296  1190 LYTSDFETFNPVIDKdGKEKIFPANFDGIVSVTNEFHPPIRARYLKVLPQKWNKNIELRIEPIG 1253
Cdd:cd00057   81 QYSLDGETWTTYKDK-GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1953-2115 3.34e-31

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: 121.32  E-value: 3.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1953 CTGVGTPaKYTTFEGDDLPFLGNCTYLASRDRNQTGEHKyqVYATNGPCDDNANIVCTKIVHLIYEKNVIHISKDpttkk 2032
Cdd:pfam00094    1 CSVSGDP-HYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS--FSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKG----- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    2033 lRTVIGKTAVFKYPVKENWGTISLLNGQDVSVTLPdIHVELTVSQLNLEFAVRVPTFLYGNRTEGLCGVCAG-YQDFLVT 2111
Cdd:pfam00094   73 -GTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGnQEDDFMT 150


                   ....
gi 1346296    2112 SNGT 2115
Cdd:pfam00094  151 PDGT 154
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 955-1094 4.17e-30

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 117.84  E-value: 4.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296   955 LPDTAFSASSEFSEIFAPHNARLNRGptnsgaGSWNPKVNNDKQYIQVELPRREPIYGVVLQG--SPIFDQYVTSYEIMY 1032
Cdd:cd00057    9 LADDQITASSSYSSGWEASRARLNSD------NAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkGGGSSEWVTSYKVQY 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346296  1033 GDDGNTFSTVDGPdGKPKIFRGPIDNTHPVKQMISPPIEAKVVRIRPLTWHDEISLRLEIIG 1094
Cdd:cd00057   83 SLDGETWTTYKDK-GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1621-1771 3.96e-26

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: 106.69  E-value: 3.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1621 CNMTG-RTFNTFDGMEYKYD-VCFHMLARD--NKFDAWLIIVRKNCRLDG---CTNELIVMQDDQLIQVKPNMMVTYNNY 1693
Cdd:pfam00094    1 CSVSGdPHYVTFDGVKYTFPgTCTYVLAKDcsEEPDFSFSVTNKNCNGGAsgvCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1694 EYTIEqtkkicFQKNSFDVDRLGNGISITSRKYNFTVLFNKEGD--VKIGVLKKHMGGVDGLCGAYDGSLANERRLPDGR 1771
Cdd:pfam00094   81 KVSLP------YKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRgqLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2173-2226 1.33e-12

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: 65.44  E-value: 1.33e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296     2173 FGACHALVEPQPYVESCEADECGGHG----PCDALQRYAAACAELGLCLPDWRRE-LCP 2226
Cdd:smart00832   18 FAACHSVVDPEPFFENCVYDTCACGGdcecLCDALAAYAAACAEAGVCISPWRTPtFCP 76
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 40-96 2.55e-10

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: 58.17  E-value: 2.55e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296      40 CTGGQQYTVCADSCLRKCSDtaLAASGQCKPVCVEGCACSPSQLLDDNGVCVPVAKC 96
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 3018-3074 4.75e-09

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


:

Pssm-ID: 214482  Cd Length: 82  Bit Score: 55.49  E-value: 4.75e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296     3018 GSCDSGTIYNNQTGTHEsaCECCQAAKYSGVSVRLTCEDGTVRPHRVATPARCHCAA 3074
Cdd:smart00041   25 GKCGSASSYSIQDVQHS--CSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGCEP 79
Mucin2_WxxW super family cl16239
Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. ...
 648-736 1.12e-06

Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. The function is not known, but the repeat can be present in up to 32 copies, as in Swiss:C3Y5K5, from Branchiostoma floridae. The region carries a highly conserved WxxW sequence motif and also has at least six well conserved cysteine residues.


The actual alignment was detected with superfamily member pfam13330:

Pssm-ID: 463846 [Multi-domain]  Cd Length: 85  Bit Score: 48.87  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     648 WTPWINRG-PAeiGPDGQSVEseplPKPNELQIGKPMCKPEmmkKIECRTVNDHKTP-KETGLNVECSLENGLVC---EE 722
Cdd:pfam13330    1 WTPWFDVDnPS--GSGGGDFE----TLENLRAYGKFCENPT---DIECRAEPPTGVPaSETGQVVTCDVTTGLVCrnaDQ 71

                           90
                   ....*....|....
gi 1346296     723 PEKTCPDFEIKVYC 736
Cdd:pfam13330   72 QPDGCLDYEVRFLC 85
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 156-209 1.16e-06

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.70  E-value: 1.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1346296   156 NMEFTTCETSEPLTCKNMHLPPSTqTAECRPGCQCKKGQVLDtASKRCVPATQC 209
Cdd:cd19941    4 NEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRN-SGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2229-2285 1.93e-06

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 1.93e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296  2229 CEEPFVYRACVD-CERTCDNYEQlqtsPEKCTNKPVEGCFCPEGKVR-VNNTCIEPGKC 2285
Cdd:cd19941    1 CPPNEVYSECGSaCPPTCANPNA----PPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1890-1948 1.28e-05

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 1.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296  1890 CPPPLVHYDCYRKrCEETCApYPNAARACPAQegqCSPGCYCPDGKLR-KGDQCVLPADC 1948
Cdd:cd19941    1 CPPNEVYSECGSA-CPPTCA-NPNAPPPCTKQ---CVEGCFCPEGYVRnSGGKCVPPSQC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2293-2349 1.63e-04

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 41.73  E-value: 1.63e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1346296     2293 HYAGDEWQEDASTLCACarspHGTALVGCRATSCAP-PVCAHGEDlrtaPPPPGQCCP 2349
Cdd:smart00214    8 YNDGETWKPDPCQICTC----LDGTTVLCDPVECPPpPDCPNPER----VKPPGECCP 57
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1809-1886 2.98e-04

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: 41.60  E-value: 2.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296    1809 LCNVI-AEEPFSQCGKVLNLDKWRHICLEKICECTDlvvngtkrtEEQCRCLVLQQMAAEClaADAGVDLASWRLMMDC 1886
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGG---------DDECLCAALAAYARAC--QAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 770-837 5.36e-04

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 40.45  E-value: 5.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1346296     770 CPPGEVYQACAYKCDRLCDHFKKTLIakgrCiSEMCVDGCVdesvasngCEGSSRWRDERTCVPVKDC 837
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV----C-PEPCVEGCV--------CPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 434-506 1.48e-03

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: 39.63  E-value: 1.48e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1346296      434 KEWAQSVCGALK--RYPFSLCAGEVGAGAYVARCERDACDAGADCECACAALAAYAHACAHRGVTF-NWRTNDLCP 506
Cdd:smart00832    1 KYYACSQCGILLspRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 238-396 4.07e-46

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: 164.50  E-value: 4.07e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      238 WSCTQRKCAGVCGAWGDSHVNTFDGTQYDFEGVCTYLLAKGAMDGTDgFDVEIQNVPCGTtGATCSKSVTLKVGG----- 312
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGG-GATCLKSVKVELNGdeiel 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      313 -AGNEEIVSLTKNAPIPDISKLKRIKMRKAGAYVFLDVPSLGMSLQWDRGLRVYVKIDTMWQGRVKGLCGNYNGDMRDDF 391
Cdd:smart00216   79 kDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1346296      392 QTPSG 396
Cdd:smart00216  159 RTPDG 163
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1118-1253 4.57e-43

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 154.82  E-value: 4.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296  1118 EPLGLIGELPLENIQVSS-NSEEKDYLSINGNR--GWKPLYNTPG-WVMFDFTGPRNITGILTKGGN----DGWVTSYKV 1189
Cdd:cd00057    1 EPLGMESGLADDQITASSsYSSGWEASRARLNSdnAWTPAVNDPPqWLQVDLGKTRRVTGIQTQGRKgggsSEWVTSYKV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1346296  1190 LYTSDFETFNPVIDKdGKEKIFPANFDGIVSVTNEFHPPIRARYLKVLPQKWNKNIELRIEPIG 1253
Cdd:cd00057   81 QYSLDGETWTTYKDK-GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 249-396 4.02e-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: 135.19  E-value: 4.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     249 CGAWGDSHVNTFDGTQYDFEGVCTYLLAKGAMDGTDG-FDVEIQNVPCGTTGaTCSKSVTLKVGGAGNEEIVSLT---KN 324
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTvlvNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1346296     325 APIPD--ISKLKRIKMRKAGaYVFLDV-PSLGMSLQWDRGLRVYVKIDTMWQGRVKGLCGNYNGDMRDDFQTPSG 396
Cdd:pfam00094   80 QKVSLpyKSDGGEVEILGSG-FVVVDLsPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1953-2115 3.34e-31

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: 121.32  E-value: 3.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1953 CTGVGTPaKYTTFEGDDLPFLGNCTYLASRDRNQTGEHKyqVYATNGPCDDNANIVCTKIVHLIYEKNVIHISKDpttkk 2032
Cdd:pfam00094    1 CSVSGDP-HYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS--FSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKG----- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    2033 lRTVIGKTAVFKYPVKENWGTISLLNGQDVSVTLPdIHVELTVSQLNLEFAVRVPTFLYGNRTEGLCGVCAG-YQDFLVT 2111
Cdd:pfam00094   73 -GTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGnQEDDFMT 150


                   ....
gi 1346296    2112 SNGT 2115
Cdd:pfam00094  151 PDGT 154
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 955-1094 4.17e-30

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 117.84  E-value: 4.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296   955 LPDTAFSASSEFSEIFAPHNARLNRGptnsgaGSWNPKVNNDKQYIQVELPRREPIYGVVLQG--SPIFDQYVTSYEIMY 1032
Cdd:cd00057    9 LADDQITASSSYSSGWEASRARLNSD------NAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkGGGSSEWVTSYKVQY 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346296  1033 GDDGNTFSTVDGPdGKPKIFRGPIDNTHPVKQMISPPIEAKVVRIRPLTWHDEISLRLEIIG 1094
Cdd:cd00057   83 SLDGETWTTYKDK-GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1116-1254 1.32e-29

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 116.07  E-value: 1.32e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1116 CTEPLGLIGElplENIQVSSNSEEKDYLSING--NRGWKPLYNT-PGWVMFDFTGPRNITGILTKGGN-DGWVTSYKVLY 1191
Cdd:smart00231    2 CNEPLGLESD---SQITASSSYWAAKIARLNGgsDGGWCPAKNDlPPWIQVDLGRLRTVTGVITGRRHgNGDWVTYKLEY 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1346296     1192 TSDFETFNPVidKDGKEKIFPANFDGIVSVTNEFHPPIRARYLKVLPQKWNKNIELRIEPIGC 1254
Cdd:smart00231   79 SDDGVNWTTY--KDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1621-1771 3.96e-26

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: 106.69  E-value: 3.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1621 CNMTG-RTFNTFDGMEYKYD-VCFHMLARD--NKFDAWLIIVRKNCRLDG---CTNELIVMQDDQLIQVKPNMMVTYNNY 1693
Cdd:pfam00094    1 CSVSGdPHYVTFDGVKYTFPgTCTYVLAKDcsEEPDFSFSVTNKNCNGGAsgvCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1694 EYTIEqtkkicFQKNSFDVDRLGNGISITSRKYNFTVLFNKEGD--VKIGVLKKHMGGVDGLCGAYDGSLANERRLPDGR 1771
Cdd:pfam00094   81 KVSLP------YKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRgqLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 959-1092 1.92e-24

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 100.98  E-value: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     959 AFSASSEFSEIFaPHNARLNrGPTNSGagsWNPKVNNDKQYIQVELPRREPIYGVVLQGSP-IFDQYVTSYEIMYGDDGN 1037
Cdd:pfam00754    1 QITASSSYSGEG-PAAAALD-GDPNTA---WSAWSGDDPQWIQVDLGKPKKITGVVTQGRQdGSNGYVTSYKIEYSLDGE 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296    1038 TFSTVDGPDGKpkifrGPIDNTHPVKQMISPPIEAKVVRIRPLTWHDE--ISLRLEI 1092
Cdd:pfam00754   76 NWTTVKDEKIP-----GNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1941-2114 5.96e-23

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: 97.86  E-value: 5.96e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1941 QCVLPADClDCTCTGVGTPaKYTTFEGDDLPFLGNCTYLASRDRnqTGEHKYQVYATNGPCDDNAniVCTKIVHLIYEKN 2020
Cdd:smart00216    1 WCCTQEEC-SPTCSVSGDP-HYTTFDGVAYTFPGNCYYVLAQDC--SSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGD 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     2021 VIHISKDPTTKKLRTVIgktavFKYPVKENWGTISLLNGQDVSVTLPDIHV-ELTVSQLNLeFAVRVPTfLYGNRTEGLC 2099
Cdd:smart00216   75 EIELKDDNGKVTVNGQQ-----VSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTL-LSVQLPS-KYRGKTCGLC 147

                           170
                    ....*....|....*.
gi 1346296     2100 GVCAGYQ-DFLVTSNG 2114
Cdd:smart00216  148 GNFDGEPeDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1609-1770 1.08e-22

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: 97.09  E-value: 1.08e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1609 YECVPPLERPVfCNMTG-RTFNTFDGMEYKYD-VCFHMLARDNK-FDAWLIIVRKNCRLDG--CTNELIVMQDDQLIQ-V 1682
Cdd:smart00216    1 WCCTQEECSPT-CSVSGdPHYTTFDGVAYTFPgNCYYVLAQDCSsEPTFSVLLKNVPCGGGatCLKSVKVELNGDEIElK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1683 KPNMMVTYNNYEYTIEQTKKICfqknSFDVDRLGNGISITSRKYNFTVLFNKEGDVKIGVLKKHMGGVDGLCGAYDGSLA 1762
Cdd:smart00216   80 DDNGKVTVNGQQVSLPYKTSDG----SIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1346296     1763 NERRLPDG 1770
Cdd:smart00216  156 DDFRTPDG 163
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 957-1095 5.75e-22

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 94.50  E-value: 5.75e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      957 DTAFSASSEFSeifAPHNARLNRGPtnsgAGSWNPKVNNDKQYIQVELPRREPIYGVVLQGsPIFDQYVTSYEIMYGDDG 1036
Cdd:smart00231   11 DSQITASSSYW---AAKIARLNGGS----DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGR-RHGNGDWVTYKLEYSDDG 82

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296     1037 NTFSTVDgpDGKPKIFRGPIDNTHPVKQMISPPIEAKVVRIRPLTWHDEISLRLEIIGC 1095
Cdd:smart00231   83 VNWTTYK--DGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1130-1250 1.48e-21

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 92.51  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1130 NIQVSSN--SEEKDYLSINGNR--GWKPLYNTPG-WVMFDFTGPRNITGILTKGGND---GWVTSYKVLYTSDFETFNPV 1201
Cdd:pfam00754    1 QITASSSysGEGPAAAALDGDPntAWSAWSGDDPqWIQVDLGKPKKITGVVTQGRQDgsnGYVTSYKIEYSLDGENWTTV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1346296    1202 idkdgKEKIFPANFDGIVSVTNEFHPPIRARYLKVLPQKWN--KNIELRIE 1250
Cdd:pfam00754   81 -----KDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNggNGIALRAE 126
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2173-2226 1.33e-12

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: 65.44  E-value: 1.33e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296     2173 FGACHALVEPQPYVESCEADECGGHG----PCDALQRYAAACAELGLCLPDWRRE-LCP 2226
Cdd:smart00832   18 FAACHSVVDPEPFFENCVYDTCACGGdcecLCDALAAYAAACAEAGVCISPWRTPtFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2164-2225 6.20e-11

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: 60.47  E-value: 6.20e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1346296    2164 CYHLYNADRFGACHALVEPQPYVESCEADECGGHGP----CDALQRYAAACAELGLCLPDWRRELC 2225
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDdeclCAALAAYARACQAAGVCIGDWRTPTF 67
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 40-96 2.55e-10

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: 58.17  E-value: 2.55e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296      40 CTGGQQYTVCADSCLRKCSDtaLAASGQCKPVCVEGCACSPSQLLDDNGVCVPVAKC 96
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 3018-3074 4.75e-09

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


Pssm-ID: 214482  Cd Length: 82  Bit Score: 55.49  E-value: 4.75e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296     3018 GSCDSGTIYNNQTGTHEsaCECCQAAKYSGVSVRLTCEDGTVRPHRVATPARCHCAA 3074
Cdd:smart00041   25 GKCGSASSYSIQDVQHS--CSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGCEP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 40-96 2.41e-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: 52.70  E-value: 2.41e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296    40 CTGGQQYTVCADSCLRKCSDtaLAASGQCKPVCVEGCACSPSQLLDDNGVCVPVAKC 96
Cdd:cd19941    1 CPPNEVYSECGSACPPTCAN--PNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
Mucin2_WxxW pfam13330
Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. ...
 648-736 1.12e-06

Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. The function is not known, but the repeat can be present in up to 32 copies, as in Swiss:C3Y5K5, from Branchiostoma floridae. The region carries a highly conserved WxxW sequence motif and also has at least six well conserved cysteine residues.


Pssm-ID: 463846 [Multi-domain]  Cd Length: 85  Bit Score: 48.87  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     648 WTPWINRG-PAeiGPDGQSVEseplPKPNELQIGKPMCKPEmmkKIECRTVNDHKTP-KETGLNVECSLENGLVC---EE 722
Cdd:pfam13330    1 WTPWFDVDnPS--GSGGGDFE----TLENLRAYGKFCENPT---DIECRAEPPTGVPaSETGQVVTCDVTTGLVCrnaDQ 71

                           90
                   ....*....|....
gi 1346296     723 PEKTCPDFEIKVYC 736
Cdd:pfam13330   72 QPDGCLDYEVRFLC 85
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 156-209 1.16e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.70  E-value: 1.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1346296   156 NMEFTTCETSEPLTCKNMHLPPSTqTAECRPGCQCKKGQVLDtASKRCVPATQC 209
Cdd:cd19941    4 NEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRN-SGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2229-2285 1.93e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 1.93e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296  2229 CEEPFVYRACVD-CERTCDNYEQlqtsPEKCTNKPVEGCFCPEGKVR-VNNTCIEPGKC 2285
Cdd:cd19941    1 CPPNEVYSECGSaCPPTCANPNA----PPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 156-209 3.76e-06

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: 46.23  E-value: 3.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1346296     156 NMEFTTCETSEPLTCKNMHlPPSTQTAECRPGCQCKKGQVLDTaSKRCVPATQC 209
Cdd:pfam01826    4 NEVYSECGSACPPTCANLS-PPDVCPEPCVEGCVCPPGFVRNS-GGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1890-1948 1.28e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 1.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296  1890 CPPPLVHYDCYRKrCEETCApYPNAARACPAQegqCSPGCYCPDGKLR-KGDQCVLPADC 1948
Cdd:cd19941    1 CPPNEVYSECGSA-CPPTCA-NPNAPPPCTKQ---CVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2229-2285 6.42e-05

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 42.76  E-value: 6.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296    2229 CEEPFVYRACVD-CERTCDNYEQLQTSPEKCtnkpVEGCFCPEGKVR-VNNTCIEPGKC 2285
Cdd:pfam01826    1 CPANEVYSECGSaCPPTCANLSPPDVCPEPC----VEGCVCPPGFVRnSGGKCVPPSDC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2293-2349 1.63e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 41.73  E-value: 1.63e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1346296     2293 HYAGDEWQEDASTLCACarspHGTALVGCRATSCAP-PVCAHGEDlrtaPPPPGQCCP 2349
Cdd:smart00214    8 YNDGETWKPDPCQICTC----LDGTTVLCDPVECPPpPDCPNPER----VKPPGECCP 57
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1890-1948 1.80e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.60  E-value: 1.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1890 CPPPLVHYDCYRKrCEETCApYPNAARACPAQegqCSPGCYCPDGKLR-KGDQCVLPADC 1948
Cdd:pfam01826    1 CPANEVYSECGSA-CPPTCA-NLSPPDVCPEP---CVEGCVCPPGFVRnSGGKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1809-1886 2.98e-04

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: 41.60  E-value: 2.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296    1809 LCNVI-AEEPFSQCGKVLNLDKWRHICLEKICECTDlvvngtkrtEEQCRCLVLQQMAAEClaADAGVDLASWRLMMDC 1886
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGG---------DDECLCAALAAYARAC--QAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 770-837 5.36e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 40.45  E-value: 5.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1346296     770 CPPGEVYQACAYKCDRLCDHFKKTLIakgrCiSEMCVDGCVdesvasngCEGSSRWRDERTCVPVKDC 837
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV----C-PEPCVEGCV--------CPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 434-506 1.48e-03

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: 39.63  E-value: 1.48e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1346296      434 KEWAQSVCGALK--RYPFSLCAGEVGAGAYVARCERDACDAGADCECACAALAAYAHACAHRGVTF-NWRTNDLCP 506
Cdd:smart00832    1 KYYACSQCGILLspRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 238-396 4.07e-46

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: 164.50  E-value: 4.07e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      238 WSCTQRKCAGVCGAWGDSHVNTFDGTQYDFEGVCTYLLAKGAMDGTDgFDVEIQNVPCGTtGATCSKSVTLKVGG----- 312
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGG-GATCLKSVKVELNGdeiel 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      313 -AGNEEIVSLTKNAPIPDISKLKRIKMRKAGAYVFLDVPSLGMSLQWDRGLRVYVKIDTMWQGRVKGLCGNYNGDMRDDF 391
Cdd:smart00216   79 kDDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1346296      392 QTPSG 396
Cdd:smart00216  159 RTPDG 163
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1118-1253 4.57e-43

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 154.82  E-value: 4.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296  1118 EPLGLIGELPLENIQVSS-NSEEKDYLSINGNR--GWKPLYNTPG-WVMFDFTGPRNITGILTKGGN----DGWVTSYKV 1189
Cdd:cd00057    1 EPLGMESGLADDQITASSsYSSGWEASRARLNSdnAWTPAVNDPPqWLQVDLGKTRRVTGIQTQGRKgggsSEWVTSYKV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1346296  1190 LYTSDFETFNPVIDKdGKEKIFPANFDGIVSVTNEFHPPIRARYLKVLPQKWNKNIELRIEPIG 1253
Cdd:cd00057   81 QYSLDGETWTTYKDK-GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 249-396 4.02e-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: 135.19  E-value: 4.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     249 CGAWGDSHVNTFDGTQYDFEGVCTYLLAKGAMDGTDG-FDVEIQNVPCGTTGaTCSKSVTLKVGGAGNEEIVSLT---KN 324
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTvlvNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1346296     325 APIPD--ISKLKRIKMRKAGaYVFLDV-PSLGMSLQWDRGLRVYVKIDTMWQGRVKGLCGNYNGDMRDDFQTPSG 396
Cdd:pfam00094   80 QKVSLpyKSDGGEVEILGSG-FVVVDLsPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1953-2115 3.34e-31

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: 121.32  E-value: 3.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1953 CTGVGTPaKYTTFEGDDLPFLGNCTYLASRDRNQTGEHKyqVYATNGPCDDNANIVCTKIVHLIYEKNVIHISKDpttkk 2032
Cdd:pfam00094    1 CSVSGDP-HYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS--FSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKG----- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    2033 lRTVIGKTAVFKYPVKENWGTISLLNGQDVSVTLPdIHVELTVSQLNLEFAVRVPTFLYGNRTEGLCGVCAG-YQDFLVT 2111
Cdd:pfam00094   73 -GTVLVNGQKVSLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGnQEDDFMT 150


                   ....
gi 1346296    2112 SNGT 2115
Cdd:pfam00094  151 PDGT 154
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 955-1094 4.17e-30

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 117.84  E-value: 4.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296   955 LPDTAFSASSEFSEIFAPHNARLNRGptnsgaGSWNPKVNNDKQYIQVELPRREPIYGVVLQG--SPIFDQYVTSYEIMY 1032
Cdd:cd00057    9 LADDQITASSSYSSGWEASRARLNSD------NAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkGGGSSEWVTSYKVQY 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1346296  1033 GDDGNTFSTVDGPdGKPKIFRGPIDNTHPVKQMISPPIEAKVVRIRPLTWHDEISLRLEIIG 1094
Cdd:cd00057   83 SLDGETWTTYKDK-GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1116-1254 1.32e-29

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 116.07  E-value: 1.32e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1116 CTEPLGLIGElplENIQVSSNSEEKDYLSING--NRGWKPLYNT-PGWVMFDFTGPRNITGILTKGGN-DGWVTSYKVLY 1191
Cdd:smart00231    2 CNEPLGLESD---SQITASSSYWAAKIARLNGgsDGGWCPAKNDlPPWIQVDLGRLRTVTGVITGRRHgNGDWVTYKLEY 78

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1346296     1192 TSDFETFNPVidKDGKEKIFPANFDGIVSVTNEFHPPIRARYLKVLPQKWNKNIELRIEPIGC 1254
Cdd:smart00231   79 SDDGVNWTTY--KDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1621-1771 3.96e-26

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: 106.69  E-value: 3.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1621 CNMTG-RTFNTFDGMEYKYD-VCFHMLARD--NKFDAWLIIVRKNCRLDG---CTNELIVMQDDQLIQVKPNMMVTYNNY 1693
Cdd:pfam00094    1 CSVSGdPHYVTFDGVKYTFPgTCTYVLAKDcsEEPDFSFSVTNKNCNGGAsgvCLKSVTVIVGDLEITLQKGGTVLVNGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1694 EYTIEqtkkicFQKNSFDVDRLGNGISITSRKYNFTVLFNKEGD--VKIGVLKKHMGGVDGLCGAYDGSLANERRLPDGR 1771
Cdd:pfam00094   81 KVSLP------YKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRgqLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 959-1092 1.92e-24

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 100.98  E-value: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     959 AFSASSEFSEIFaPHNARLNrGPTNSGagsWNPKVNNDKQYIQVELPRREPIYGVVLQGSP-IFDQYVTSYEIMYGDDGN 1037
Cdd:pfam00754    1 QITASSSYSGEG-PAAAALD-GDPNTA---WSAWSGDDPQWIQVDLGKPKKITGVVTQGRQdGSNGYVTSYKIEYSLDGE 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296    1038 TFSTVDGPDGKpkifrGPIDNTHPVKQMISPPIEAKVVRIRPLTWHDE--ISLRLEI 1092
Cdd:pfam00754   76 NWTTVKDEKIP-----GNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1941-2114 5.96e-23

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: 97.86  E-value: 5.96e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1941 QCVLPADClDCTCTGVGTPaKYTTFEGDDLPFLGNCTYLASRDRnqTGEHKYQVYATNGPCDDNAniVCTKIVHLIYEKN 2020
Cdd:smart00216    1 WCCTQEEC-SPTCSVSGDP-HYTTFDGVAYTFPGNCYYVLAQDC--SSEPTFSVLLKNVPCGGGA--TCLKSVKVELNGD 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     2021 VIHISKDPTTKKLRTVIgktavFKYPVKENWGTISLLNGQDVSVTLPDIHV-ELTVSQLNLeFAVRVPTfLYGNRTEGLC 2099
Cdd:smart00216   75 EIELKDDNGKVTVNGQQ-----VSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTL-LSVQLPS-KYRGKTCGLC 147

                           170
                    ....*....|....*.
gi 1346296     2100 GVCAGYQ-DFLVTSNG 2114
Cdd:smart00216  148 GNFDGEPeDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1609-1770 1.08e-22

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: 97.09  E-value: 1.08e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1609 YECVPPLERPVfCNMTG-RTFNTFDGMEYKYD-VCFHMLARDNK-FDAWLIIVRKNCRLDG--CTNELIVMQDDQLIQ-V 1682
Cdd:smart00216    1 WCCTQEECSPT-CSVSGdPHYTTFDGVAYTFPgNCYYVLAQDCSsEPTFSVLLKNVPCGGGatCLKSVKVELNGDEIElK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     1683 KPNMMVTYNNYEYTIEQTKKICfqknSFDVDRLGNGISITSRKYNFTVLFNKEGDVKIGVLKKHMGGVDGLCGAYDGSLA 1762
Cdd:smart00216   80 DDNGKVTVNGQQVSLPYKTSDG----SIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 1346296     1763 NERRLPDG 1770
Cdd:smart00216  156 DDFRTPDG 163
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 957-1095 5.75e-22

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 94.50  E-value: 5.75e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296      957 DTAFSASSEFSeifAPHNARLNRGPtnsgAGSWNPKVNNDKQYIQVELPRREPIYGVVLQGsPIFDQYVTSYEIMYGDDG 1036
Cdd:smart00231   11 DSQITASSSYW---AAKIARLNGGS----DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGR-RHGNGDWVTYKLEYSDDG 82

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296     1037 NTFSTVDgpDGKPKIFRGPIDNTHPVKQMISPPIEAKVVRIRPLTWHDEISLRLEIIGC 1095
Cdd:smart00231   83 VNWTTYK--DGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1130-1250 1.48e-21

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 92.51  E-value: 1.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1130 NIQVSSN--SEEKDYLSINGNR--GWKPLYNTPG-WVMFDFTGPRNITGILTKGGND---GWVTSYKVLYTSDFETFNPV 1201
Cdd:pfam00754    1 QITASSSysGEGPAAAALDGDPntAWSAWSGDDPqWIQVDLGKPKKITGVVTQGRQDgsnGYVTSYKIEYSLDGENWTTV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1346296    1202 idkdgKEKIFPANFDGIVSVTNEFHPPIRARYLKVLPQKWN--KNIELRIE 1250
Cdd:pfam00754   81 -----KDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNggNGIALRAE 126
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2173-2226 1.33e-12

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: 65.44  E-value: 1.33e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296     2173 FGACHALVEPQPYVESCEADECGGHG----PCDALQRYAAACAELGLCLPDWRRE-LCP 2226
Cdd:smart00832   18 FAACHSVVDPEPFFENCVYDTCACGGdcecLCDALAAYAAACAEAGVCISPWRTPtFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2164-2225 6.20e-11

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: 60.47  E-value: 6.20e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1346296    2164 CYHLYNADRFGACHALVEPQPYVESCEADECGGHGP----CDALQRYAAACAELGLCLPDWRRELC 2225
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDdeclCAALAAYARACQAAGVCIGDWRTPTF 67
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 40-96 2.55e-10

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: 58.17  E-value: 2.55e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296      40 CTGGQQYTVCADSCLRKCSDtaLAASGQCKPVCVEGCACSPSQLLDDNGVCVPVAKC 96
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 3018-3074 4.75e-09

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


Pssm-ID: 214482  Cd Length: 82  Bit Score: 55.49  E-value: 4.75e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296     3018 GSCDSGTIYNNQTGTHEsaCECCQAAKYSGVSVRLTCEDGTVRPHRVATPARCHCAA 3074
Cdd:smart00041   25 GKCGSASSYSIQDVQHS--CSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGCEP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 40-96 2.41e-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: 52.70  E-value: 2.41e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1346296    40 CTGGQQYTVCADSCLRKCSDtaLAASGQCKPVCVEGCACSPSQLLDDNGVCVPVAKC 96
Cdd:cd19941    1 CPPNEVYSECGSACPPTCAN--PNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
Mucin2_WxxW pfam13330
Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. ...
 648-736 1.12e-06

Mucin-2 protein WxxW repeating region; This family is repeating region found on mucins 2 and 5. The function is not known, but the repeat can be present in up to 32 copies, as in Swiss:C3Y5K5, from Branchiostoma floridae. The region carries a highly conserved WxxW sequence motif and also has at least six well conserved cysteine residues.


Pssm-ID: 463846 [Multi-domain]  Cd Length: 85  Bit Score: 48.87  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296     648 WTPWINRG-PAeiGPDGQSVEseplPKPNELQIGKPMCKPEmmkKIECRTVNDHKTP-KETGLNVECSLENGLVC---EE 722
Cdd:pfam13330    1 WTPWFDVDnPS--GSGGGDFE----TLENLRAYGKFCENPT---DIECRAEPPTGVPaSETGQVVTCDVTTGLVCrnaDQ 71

                           90
                   ....*....|....
gi 1346296     723 PEKTCPDFEIKVYC 736
Cdd:pfam13330   72 QPDGCLDYEVRFLC 85
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 156-209 1.16e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.70  E-value: 1.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1346296   156 NMEFTTCETSEPLTCKNMHLPPSTqTAECRPGCQCKKGQVLDtASKRCVPATQC 209
Cdd:cd19941    4 NEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRN-SGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2229-2285 1.93e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 1.93e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296  2229 CEEPFVYRACVD-CERTCDNYEQlqtsPEKCTNKPVEGCFCPEGKVR-VNNTCIEPGKC 2285
Cdd:cd19941    1 CPPNEVYSECGSaCPPTCANPNA----PPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 156-209 3.76e-06

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: 46.23  E-value: 3.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1346296     156 NMEFTTCETSEPLTCKNMHlPPSTQTAECRPGCQCKKGQVLDTaSKRCVPATQC 209
Cdd:pfam01826    4 NEVYSECGSACPPTCANLS-PPDVCPEPCVEGCVCPPGFVRNS-GGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1890-1948 1.28e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 1.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296  1890 CPPPLVHYDCYRKrCEETCApYPNAARACPAQegqCSPGCYCPDGKLR-KGDQCVLPADC 1948
Cdd:cd19941    1 CPPNEVYSECGSA-CPPTCA-NPNAPPPCTKQ---CVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2229-2285 6.42e-05

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 42.76  E-value: 6.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296    2229 CEEPFVYRACVD-CERTCDNYEQLQTSPEKCtnkpVEGCFCPEGKVR-VNNTCIEPGKC 2285
Cdd:pfam01826    1 CPANEVYSECGSaCPPTCANLSPPDVCPEPC----VEGCVCPPGFVRnSGGKCVPPSDC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
2293-2349 1.63e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 41.73  E-value: 1.63e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1346296     2293 HYAGDEWQEDASTLCACarspHGTALVGCRATSCAP-PVCAHGEDlrtaPPPPGQCCP 2349
Cdd:smart00214    8 YNDGETWKPDPCQICTC----LDGTTVLCDPVECPPpPDCPNPER----VKPPGECCP 57
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1890-1948 1.80e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 41.60  E-value: 1.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1346296    1890 CPPPLVHYDCYRKrCEETCApYPNAARACPAQegqCSPGCYCPDGKLR-KGDQCVLPADC 1948
Cdd:pfam01826    1 CPANEVYSECGSA-CPPTCA-NLSPPDVCPEP---CVEGCVCPPGFVRnSGGKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1809-1886 2.98e-04

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: 41.60  E-value: 2.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1346296    1809 LCNVI-AEEPFSQCGKVLNLDKWRHICLEKICECTDlvvngtkrtEEQCRCLVLQQMAAEClaADAGVDLASWRLMMDC 1886
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGG---------DDECLCAALAAYARAC--QAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 770-837 5.36e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 40.45  E-value: 5.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1346296     770 CPPGEVYQACAYKCDRLCDHFKKTLIakgrCiSEMCVDGCVdesvasngCEGSSRWRDERTCVPVKDC 837
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDV----C-PEPCVEGCV--------CPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 434-506 1.48e-03

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: 39.63  E-value: 1.48e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1346296      434 KEWAQSVCGALK--RYPFSLCAGEVGAGAYVARCERDACDAGADCECACAALAAYAHACAHRGVTF-NWRTNDLCP 506
Cdd:smart00832    1 KYYACSQCGILLspRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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