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Conserved domains on  [gi|442632169|ref|NP_001261809|]
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hemolectin, isoform B [Drosophila melanogaster]

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 ...
 839-1014 3.81e-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: 133.30  E-value: 3.81e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    839 WRCTEDKCGARCGAVGDPHYQTFDGKRYDFMGKCSYHLLKT----QNTSVEAENVACSGavsesmnfaapdDPSCTKAVT 914
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcssePTFSVLLKNVPCGG------------GATCLKSVK 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    915 IRfilrDGTPSVIKLDQGLTTIVNDKPIaKLPKMLGLGEVLIRRASSTFLTVEFADGIRVWWDGVSRVYIDAPPSLRGQT 994
Cdd:smart00216   69 VE----LNGDEIELKDDNGKVTVNGQQV-SLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKT 143

                           170       180
                    ....*....|....*....|
gi 442632169    995 QGLCGTFNSNTQDDFLTPEG 1014
Cdd:smart00216  144 CGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1326-1497 1.27e-30

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: 120.20  E-value: 1.27e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   1326 WKCSKNGCESTCSVWGDSHFTTFDGHDFDFQGACDYVLAKGVFDNGDgFSITIQNVLCGTmGVTCSKSLEIALTGhaees 1405
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGG-GATCLKSVKVELNG----- 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   1406 lllsaDSAYSTDPNKTPIkklrdsVNSKGHN--------AFHIYKAGVFVVVEVIPLKLQVKWDEGTRVYVKLGNEWRQK 1477
Cdd:smart00216   74 -----DEIELKDDNGKVT------VNGQQVSlpyktsdgSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGK 142

                           170       180
                    ....*....|....*....|
gi 442632169   1478 VSGLCGNYNGNSLDDMQTPS 1497
Cdd:smart00216  143 TCGLCGNFDGEPEDDFRTPD 162
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2088-2222 9.78e-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: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 93.96  E-value: 9.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169 2088 PDSIFnASSQLAPEHGPKMARLTKEqprGSWSPSINDQMQYLELNFAKPEPFYGVVMAG--SPEFDNYVTLFKILHSHDG 2165
Cdd:cd00057    11 DDQIT-ASSSYSSGWEASRARLNSD---NAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkGGGSSEWVTSYKVQYSLDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169 2166 IAYHYLVDETEkPQMFNGPLDSRAPVQTLFKIPIEASSLRIYPLKWHGSIAMRVELL 2222
Cdd:cd00057    87 ETWTTYKDKGE-EKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELY 142
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2298-2402 2.38e-21

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: 92.80  E-value: 2.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169 2298 AWRPLANSQNEFIEFDFLEPRNISGFVTKG----GPDGWVTGYKVMFSKKKPTWnTVLSTDGQARIFEANHDAETERRHH 2373
Cdd:cd00057    36 AWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkggGSSEWVTSYKVQYSLDGETW-TTYKDKGEEKVFTGNSDGSTPVTND 114

                          90       100
                  ....*....|....*....|....*....
gi 442632169 2374 FKNPILTQYIKIVPAYWEKNINMRIEPLG 2402
Cdd:cd00057   115 FPPPIVARYIRILPTTWNGNISLRLELYG 143
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2702-2857 9.69e-21

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: 91.66  E-value: 9.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2702 CEISGKS-FTTFDGTVFKY-GPCSHILARDIHS-SSWSISVH-QQCSDETRKVCHKVITIQdteAGNELILLPH-LKLKF 2776
Cdd:pfam00094    1 CSVSGDPhYVTFDGVKYTFpGTCTYVLAKDCSEePDFSFSVTnKNCNGGASGVCLKSVTVI---VGDLEITLQKgGTVLV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2777 NGYEftvqqlINSPICKASFVVSQPGKTLLAVSTKYGFWVQL--DDIGIVKVGISSKFIRTVDGLCGYYNGNQKDDKRSP 2854
Cdd:pfam00094   78 NGQK------VSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVdgDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151


                   ...
gi 442632169  2855 DGQ 2857
Cdd:pfam00094  152 DGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 484-635 1.85e-19

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: 87.81  E-value: 1.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   484 CTTWGGINMKTFDGLVFKAPLSCSHTLITDKVSGT---FDIILKACPYGSGYGCAHTLKILWQSVLYTfenLNGTMQLTT 560
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdfsFSVTNKNCNGGASGVCLKSVTVIVGDLEIT---LQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169   561 PIKKLPMPVQVMGMKV-MPVAQHVQIDLES-VGLKLDWDHRQYVSVQAGPQMWGKVGGLCGTLDGDPNTDLTSRTGK 635
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVeILGSGFVVVDLSPgVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD super family cl47498
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 3034-3197 5.84e-19

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: 86.66  E-value: 5.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  3034 CNSLGASKYMTYDRKSFSFNGNCTYLLSRDVvlPGVHTFQVYVSMDDCKKlGQPtpvegGSCAKSLHILNGDHVIHVQRV 3113
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDC--SEEPDFSFSVTNKNCNG-GAS-----GVCLKSVTVIVGDLEITLQKG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  3114 pqkpksLQVLVDGFEVkKIPYKDSWISLRQVVGKELVLSLPeSHVELTASFEDLIFSLGVPSIKYGSKMEGLCGDCNGNA 3193
Cdd:pfam00094   73 ------GTVLVNGQKV-SLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQ 144


                   ....
gi 442632169  3194 GNDL 3197
Cdd:pfam00094  145 EDDF 148
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1120 1.27e-15

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: 74.30  E-value: 1.27e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632169   1053 KAQAEKFCDWILQD--IFQDCHFLVEPEQFYEDCLYDTCACKDeMSKCFCPILSAYGTECMRQGVK-TGWR 1120
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGG-DCECLCDALAAYAAACAEAGVCiSPWR 70
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1130-1184 4.72e-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: 63.49  E-value: 4.72e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169 1130 CPLGQVFDECGDGCALSCDDLPSKGSCKRECVEGCRCPHGEYVNEDGECVPKKMC 1184
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 3247-3312 1.01e-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: 62.78  E-value: 1.01e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169  3247 CLQFYNAELFGKCPLAVDPIAYVSACQQDICKPGNTQQGVCVALAAYAKECNQHGIC-TNWRRPQLC 3312
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCiGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1534-1608 2.59e-11

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: 61.97  E-value: 2.59e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169   1534 ETWAQLKCGALKSDL--FKECHAEVPLERFWKRCIFDTCACdqGGDCECLCTAVAAYADACAQKGINIR-WRSQHFCP 1608
Cdd:smart00832    1 KYYACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 683-753 6.36e-06

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: 46.22  E-value: 6.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632169   683 CERLLANEKLGDCIKPFNYDALIRTCMADYCNCANrehPESCNCDAIAMLAKECAFKGIKLEHgWRNLEIC 753
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGG---DDECLCAALAAYARACQAAGVCIGD-WRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2973-3029 1.06e-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: 45.46  E-value: 1.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169  2973 CPSPLVHTDCyKRRCEPSCDNVHGDDCPVLPdaCFPGCYCPEGTVR-KGPNCVPISEC 3029
Cdd:pfam01826    1 CPANEVYSEC-GSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1244-1297 4.20e-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: 43.53  E-value: 4.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442632169  1244 PYAEFTKCAPKEPKTCKNMDKYVADSSDCLPGCVCMEGYVYDTSRlACVLPANC 1297
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGG-KCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 757-810 7.00e-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: 43.07  E-value: 7.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169  757 CGFGRVYQACGPNVEPTCDSDLALPASKGACNEGCFCPEGTV-QYKEACITRELC 810
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVrNSGGKCVPPSQC 55
GHB_like super family cl21545
Glycoprotein hormone beta chain homologues; This family of cystine-knot hormones includes the ...
 3754-3812 8.80e-05

Glycoprotein hormone beta chain homologues; This family of cystine-knot hormones includes the beta chains of gonadotropins, thyrotropins, follitropins, choriogonadotropins and more. The members are reproductive hormones that consist of two glycosylated chains (alpha and beta), which form a tightly bound dimer.


The actual alignment was detected with superfamily member smart00041:

Pssm-ID: 473907  Cd Length: 82  Bit Score: 43.55  E-value: 8.80e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 442632169   3754 CEGACSSGSKYNTLTDMHekFCTCCSIKSYHPISVKMICDDGHTFTQKHEVPSNCGCSP 3812
Cdd:smart00041   23 CEGKCGSASSYSIQDVQH--SCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGCEP 79
TIL super family cl20226
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1937-2004 7.87e-03

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


The actual alignment was detected with superfamily member pfam01826:

Pssm-ID: 473303  Cd Length: 55  Bit Score: 37.37  E-value: 7.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169  1937 CPPGKIKSECANQCENTCHYygsiLKKRGLCqvGEHCKPGCVdelrpdCPKlGKFWRDEDTCVHADEC 2004
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN----LSPPDVC--PEPCVEGCV------CPP-GFVRNSGGKCVPPSDC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 3396-3450 8.22e-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 smart00214:

Pssm-ID: 450195  Cd Length: 59  Bit Score: 37.50  E-value: 8.22e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169   3396 HLPDEKWKKDKCTECQCDSKGKTTCVEKKCQvEENICAegyRPETIVSVDECCPR 3450
Cdd:smart00214    8 YNDGETWKPDPCQICTCLDGTTVLCDPVECP-PPPDCP---NPERVKPPGECCPR 58
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 839-1014 3.81e-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: 133.30  E-value: 3.81e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    839 WRCTEDKCGARCGAVGDPHYQTFDGKRYDFMGKCSYHLLKT----QNTSVEAENVACSGavsesmnfaapdDPSCTKAVT 914
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcssePTFSVLLKNVPCGG------------GATCLKSVK 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    915 IRfilrDGTPSVIKLDQGLTTIVNDKPIaKLPKMLGLGEVLIRRASSTFLTVEFADGIRVWWDGVSRVYIDAPPSLRGQT 994
Cdd:smart00216   69 VE----LNGDEIELKDDNGKVTVNGQQV-SLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKT 143

                           170       180
                    ....*....|....*....|
gi 442632169    995 QGLCGTFNSNTQDDFLTPEG 1014
Cdd:smart00216  144 CGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1326-1497 1.27e-30

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: 120.20  E-value: 1.27e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   1326 WKCSKNGCESTCSVWGDSHFTTFDGHDFDFQGACDYVLAKGVFDNGDgFSITIQNVLCGTmGVTCSKSLEIALTGhaees 1405
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGG-GATCLKSVKVELNG----- 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   1406 lllsaDSAYSTDPNKTPIkklrdsVNSKGHN--------AFHIYKAGVFVVVEVIPLKLQVKWDEGTRVYVKLGNEWRQK 1477
Cdd:smart00216   74 -----DEIELKDDNGKVT------VNGQQVSlpyktsdgSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGK 142

                           170       180
                    ....*....|....*....|
gi 442632169   1478 VSGLCGNYNGNSLDDMQTPS 1497
Cdd:smart00216  143 TCGLCGNFDGEPEDDFRTPD 162
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 850-1014 1.58e-30

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: 119.78  E-value: 1.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   850 CGAVGDPHYQTFDGKRYDFMGKCSYHLLKTQNTSVEAEnvacsgaVSESMNFAAPDDPS-CTKAVTIrfILRDGTpsvIK 928
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-------FSVTNKNCNGGASGvCLKSVTV--IVGDLE---IT 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   929 LDQGLTTIVNDKPIAkLPKMLGLGEVLIRRASSTFLTVEFADGIRVWWDGVSRVYIDAPPSLRGQTQGLCGTFNSNTQDD 1008
Cdd:pfam00094   69 LQKGGTVLVNGQKVS-LPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDD 147


                   ....*.
gi 442632169  1009 FLTPEG 1014
Cdd:pfam00094  148 FMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1337-1497 3.41e-27

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: 110.15  E-value: 3.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  1337 CSVWGDSHFTTFDGHDFDFQGACDYVLAKGV-FDNGDGFSITIQNVLCGTMGVtCSKSLEIaLTGHAEESLLLSADSAYS 1415
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGV-CLKSVTV-IVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  1416 TDPNKTPIKKLRDSVNskghnafhIYKAGVFVVVEVIPLKLQVKWDEGTRVYVKLGNEWRQKVSGLCGNYNGNSLDDMQT 1495
Cdd:pfam00094   79 GQKVSLPYKSDGGEVE--------ILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMT 150


                   ..
gi 442632169  1496 PS 1497
Cdd:pfam00094  151 PD 152
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2088-2222 9.78e-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: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 93.96  E-value: 9.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169 2088 PDSIFnASSQLAPEHGPKMARLTKEqprGSWSPSINDQMQYLELNFAKPEPFYGVVMAG--SPEFDNYVTLFKILHSHDG 2165
Cdd:cd00057    11 DDQIT-ASSSYSSGWEASRARLNSD---NAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkGGGSSEWVTSYKVQYSLDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169 2166 IAYHYLVDETEkPQMFNGPLDSRAPVQTLFKIPIEASSLRIYPLKWHGSIAMRVELL 2222
Cdd:cd00057    87 ETWTTYKDKGE-EKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELY 142
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2298-2402 2.38e-21

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: 92.80  E-value: 2.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169 2298 AWRPLANSQNEFIEFDFLEPRNISGFVTKG----GPDGWVTGYKVMFSKKKPTWnTVLSTDGQARIFEANHDAETERRHH 2373
Cdd:cd00057    36 AWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkggGSSEWVTSYKVQYSLDGETW-TTYKDKGEEKVFTGNSDGSTPVTND 114

                          90       100
                  ....*....|....*....|....*....
gi 442632169 2374 FKNPILTQYIKIVPAYWEKNINMRIEPLG 2402
Cdd:cd00057   115 FPPPIVARYIRILPTTWNGNISLRLELYG 143
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2702-2857 9.69e-21

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: 91.66  E-value: 9.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2702 CEISGKS-FTTFDGTVFKY-GPCSHILARDIHS-SSWSISVH-QQCSDETRKVCHKVITIQdteAGNELILLPH-LKLKF 2776
Cdd:pfam00094    1 CSVSGDPhYVTFDGVKYTFpGTCTYVLAKDCSEePDFSFSVTnKNCNGGASGVCLKSVTVI---VGDLEITLQKgGTVLV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2777 NGYEftvqqlINSPICKASFVVSQPGKTLLAVSTKYGFWVQL--DDIGIVKVGISSKFIRTVDGLCGYYNGNQKDDKRSP 2854
Cdd:pfam00094   78 NGQK------VSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVdgDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151


                   ...
gi 442632169  2855 DGQ 2857
Cdd:pfam00094  152 DGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 484-635 1.85e-19

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: 87.81  E-value: 1.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   484 CTTWGGINMKTFDGLVFKAPLSCSHTLITDKVSGT---FDIILKACPYGSGYGCAHTLKILWQSVLYTfenLNGTMQLTT 560
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdfsFSVTNKNCNGGASGVCLKSVTVIVGDLEIT---LQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169   561 PIKKLPMPVQVMGMKV-MPVAQHVQIDLES-VGLKLDWDHRQYVSVQAGPQMWGKVGGLCGTLDGDPNTDLTSRTGK 635
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVeILGSGFVVVDLSPgVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 3034-3197 5.84e-19

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: 86.66  E-value: 5.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  3034 CNSLGASKYMTYDRKSFSFNGNCTYLLSRDVvlPGVHTFQVYVSMDDCKKlGQPtpvegGSCAKSLHILNGDHVIHVQRV 3113
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDC--SEEPDFSFSVTNKNCNG-GAS-----GVCLKSVTVIVGDLEITLQKG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  3114 pqkpksLQVLVDGFEVkKIPYKDSWISLRQVVGKELVLSLPeSHVELTASFEDLIFSLGVPSIKYGSKMEGLCGDCNGNA 3193
Cdd:pfam00094   73 ------GTVLVNGQKV-SLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQ 144


                   ....
gi 442632169  3194 GNDL 3197
Cdd:pfam00094  145 EDDF 148
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2093-2221 1.14e-18

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: 84.81  E-value: 1.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2093 NASSQLAPEHGPKmARLTKEqPRGSWSPSINDQMQYLELNFAKPEPFYGVVMAGSP-EFDNYVTLFKILHSHDGIAYHYL 2171
Cdd:pfam00754    3 TASSSYSGEGPAA-AALDGD-PNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQdGSNGYVTSYKIEYSLDGENWTTV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 442632169  2172 VDETEKpqmfnGPLDSRAPVQTLFKIPIEASSLRIYPLKWHGS--IAMRVEL 2221
Cdd:pfam00754   81 KDEKIP-----GNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2690-2856 7.68e-18

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: 83.61  E-value: 7.68e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2690 YSCVLRPNkDDVCEISGKS-FTTFDGTVFKY-GPCSHILARDIHSS-SWSISVhQQCSDETRKVCHKVITIQDTEaGNEL 2766
Cdd:smart00216    1 WCCTQEEC-SPTCSVSGDPhYTTFDGVAYTFpGNCYYVLAQDCSSEpTFSVLL-KNVPCGGGATCLKSVKVELNG-DEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2767 ILLPHLKLKFNGYEFTVQQLINSpickaSFVVSQPGKTLLAVSTKYGFW-VQLDDIGIVKVGISSKFIRTVDGLCGYYNG 2845
Cdd:smart00216   78 LKDDNGKVTVNGQQVSLPYKTSD-----GSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDG 152

                           170
                    ....*....|.
gi 442632169   2846 NQKDDKRSPDG 2856
Cdd:smart00216  153 EPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 478-634 1.08e-17

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: 83.22  E-value: 1.08e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    478 TPRPALCTTWGGINMKTFDGLVFKAPLSCSHTLITDKVS-GTFDIILKACPYGSGYGCAHTLKILWQSVLYTFENLNGTM 556
Cdd:smart00216    6 EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSePTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKV 85

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169    557 QLTTPIKKLPMPVQVMGMKVMPVAQHVQIDLESVGLKLDWDHRQYVSVQAGPQMWGKVGGLCGTLDGDPNTDLTSRTG 634
Cdd:smart00216   86 TVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2298-2403 1.11e-17

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: 82.17  E-value: 1.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2298 AWRPLANSQNEFIEFDFLEPRNISGFVT-KGGPDGWVTGYKVMFSKKKPTWNTVlsTDGQARIFEANHDAETERRHHFKN 2376
Cdd:smart00231   35 GWCPAKNDLPPWIQVDLGRLRTVTGVITgRRHGNGDWVTYKLEYSDDGVNWTTY--KDGNSKVFPGNSDAGTVVLNDFPP 112

                            90       100
                    ....*....|....*....|....*..
gi 442632169   2377 PILTQYIKIVPAYWEKNINMRIEPLGC 2403
Cdd:smart00231  113 PIVARYVRILPTGWNGNIILRVELLGC 139
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 3032-3198 1.31e-17

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: 82.83  E-value: 1.31e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   3032 CVCNSLGASKYMTYDRKSFSFNGNCTYLLSRDvvLPGVHTFQVYVSMDDCKKlgqptpveGGSCAKSLHILNGDHVIHVq 3111
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD--CSSEPTFSVLLKNVPCGG--------GATCLKSVKVELNGDEIEL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   3112 rvpqKPKSLQVLVDGfEVKKIPYKDSWISLRQVVGKELVLSLPESHVeLTASFEDLI-FSLGVPSiKYGSKMEGLCGDCN 3190
Cdd:smart00216   79 ----KDDNGKVTVNG-QQVSLPYKTSDGSIQIRSSGGYLVVITSLGL-IQVTFDGLTlLSVQLPS-KYRGKTCGLCGNFD 151


                    ....*...
gi 442632169   3191 GNAGNDLQ 3198
Cdd:smart00216  152 GEPEDDFR 159
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2298-2399 1.38e-17

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: 81.72  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2298 AWRPLANSQNEFIEFDFLEPRNISGFVTKGGPD---GWVTGYKVMFSKKKPTWNTVLSTDgqariFEANHDAETERRHHF 2374
Cdd:pfam00754   25 AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDgsnGYVTSYKIEYSLDGENWTTVKDEK-----IPGNNDNNTPVTNTF 99

                           90       100
                   ....*....|....*....|....*..
gi 442632169  2375 KNPILTQYIKIVPAYW--EKNINMRIE 2399
Cdd:pfam00754  100 DPPIKARYVRIVPTSWngGNGIALRAE 126
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1120 1.27e-15

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: 74.30  E-value: 1.27e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632169   1053 KAQAEKFCDWILQD--IFQDCHFLVEPEQFYEDCLYDTCACKDeMSKCFCPILSAYGTECMRQGVK-TGWR 1120
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGG-DCECLCDALAAYAAACAEAGVCiSPWR 70
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2103-2224 1.23e-12

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: 67.92  E-value: 1.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2103 GPKMARLTKEQPRGsWSPSINDQMQYLELNFAKPEPFYGVVmAGSPEFDNYVTLFKILHSHDGIAYHYLVDETEKpqMFN 2182
Cdd:smart00231   22 AAKIARLNGGSDGG-WCPAKNDLPPWIQVDLGRLRTVTGVI-TGRRHGNGDWVTYKLEYSDDGVNWTTYKDGNSK--VFP 97

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 442632169   2183 GPLDSRAPVQTLFKIPIEASSLRIYPLKWHGSIAMRVELLIC 2224
Cdd:smart00231   98 GNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1059-1120 4.15e-12

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: 63.94  E-value: 4.15e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632169  1059 FCDWIL-QDIFQDCHFLVEPEQFYEDCLYDTCACKDEmSKCFCPILSAYGTECMRQGVK-TGWR 1120
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGD-DECLCAALAAYARACQAAGVCiGDWR 63
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1130-1184 4.72e-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: 63.49  E-value: 4.72e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169 1130 CPLGQVFDECGDGCALSCDDLPSKGSCKRECVEGCRCPHGEYVNEDGECVPKKMC 1184
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 3247-3312 1.01e-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: 62.78  E-value: 1.01e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169  3247 CLQFYNAELFGKCPLAVDPIAYVSACQQDICKPGNTQQGVCVALAAYAKECNQHGIC-TNWRRPQLC 3312
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCiGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1130-1184 2.46e-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: 61.25  E-value: 2.46e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169  1130 CPLGQVFDECGDGCALSCDDLPSKGSCKRECVEGCRCPHGEYVNEDGECVPKKMC 1184
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1534-1608 2.59e-11

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: 61.97  E-value: 2.59e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169   1534 ETWAQLKCGALKSDL--FKECHAEVPLERFWKRCIFDTCACdqGGDCECLCTAVAAYADACAQKGINIR-WRSQHFCP 1608
Cdd:smart00832    1 KYYACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 3256-3313 1.68e-09

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: 56.97  E-value: 1.68e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 442632169   3256 FGKCPLAVDPIAYVSACQQDICKPGNTQQGVCVALAAYAKECNQHGIC-TNWRRPQLCP 3313
Cdd:smart00832   18 FAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCiSPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1540-1607 8.99e-09

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: 54.31  E-value: 8.99e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  1540 KCGALK-SDLFKECHAEVPLERFWKRCIFDTCACdqGGDCECLCTAVAAYADACAQKGINIR-WRSQHFC 1607
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 683-753 6.36e-06

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: 46.22  E-value: 6.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632169   683 CERLLANEKLGDCIKPFNYDALIRTCMADYCNCANrehPESCNCDAIAMLAKECAFKGIKLEHgWRNLEIC 753
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGG---DDECLCAALAAYARACQAAGVCIGD-WRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2973-3029 1.06e-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: 45.46  E-value: 1.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169  2973 CPSPLVHTDCyKRRCEPSCDNVHGDDCPVLPdaCFPGCYCPEGTVR-KGPNCVPISEC 3029
Cdd:pfam01826    1 CPANEVYSEC-GSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1244-1297 4.20e-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: 43.53  E-value: 4.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442632169  1244 PYAEFTKCAPKEPKTCKNMDKYVADSSDCLPGCVCMEGYVYDTSRlACVLPANC 1297
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGG-KCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1247-1297 4.37e-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: 43.46  E-value: 4.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442632169 1247 EFTKCAPKEPKTCKNMDKYVADSSDCLPGCVCMEGYVYDTSRlACVLPANC 1297
Cdd:cd19941     6 VYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 757-810 7.00e-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: 43.07  E-value: 7.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169  757 CGFGRVYQACGPNVEPTCDSDLALPASKGACNEGCFCPEGTV-QYKEACITRELC 810
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVrNSGGKCVPPSQC 55
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 3754-3812 8.80e-05

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: 43.55  E-value: 8.80e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 442632169   3754 CEGACSSGSKYNTLTDMHekFCTCCSIKSYHPISVKMICDDGHTFTQKHEVPSNCGCSP 3812
Cdd:smart00041   23 CEGKCGSASSYSIQDVQH--SCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGCEP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2973-3029 1.12e-04

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.30  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169 2973 CPSPLVHTDCyKRRCEPSCDNVHGDdcPVLPDACFPGCYCPEGTVR-KGPNCVPISEC 3029
Cdd:cd19941     1 CPPNEVYSEC-GSACPPTCANPNAP--PPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 757-810 3.37e-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: 41.22  E-value: 3.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169   757 CGFGRVYQACGPNVEPTCDSDLALPASKGACNEGCFCPEGTV-QYKEACITRELC 810
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVrNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 708-754 2.63e-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: 39.25  E-value: 2.63e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 442632169    708 CMADYCNCANREHpesCNCDAIAMLAKECAFKGIKLeHGWRNLEICP 754
Cdd:smart00832   34 CVYDTCACGGDCE---CLCDALAAYAAACAEAGVCI-SPWRTPTFCP 76
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1937-2004 7.87e-03

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: 37.37  E-value: 7.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169  1937 CPPGKIKSECANQCENTCHYygsiLKKRGLCqvGEHCKPGCVdelrpdCPKlGKFWRDEDTCVHADEC 2004
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN----LSPPDVC--PEPCVEGCV------CPP-GFVRNSGGKCVPPSDC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
3396-3450 8.22e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.50  E-value: 8.22e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169   3396 HLPDEKWKKDKCTECQCDSKGKTTCVEKKCQvEENICAegyRPETIVSVDECCPR 3450
Cdd:smart00214    8 YNDGETWKPDPCQICTCLDGTTVLCDPVECP-PPPDCP---NPERVKPPGECCPR 58
 
Name Accession Description Interval E-value
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 839-1014 3.81e-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: 133.30  E-value: 3.81e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    839 WRCTEDKCGARCGAVGDPHYQTFDGKRYDFMGKCSYHLLKT----QNTSVEAENVACSGavsesmnfaapdDPSCTKAVT 914
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcssePTFSVLLKNVPCGG------------GATCLKSVK 68

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    915 IRfilrDGTPSVIKLDQGLTTIVNDKPIaKLPKMLGLGEVLIRRASSTFLTVEFADGIRVWWDGVSRVYIDAPPSLRGQT 994
Cdd:smart00216   69 VE----LNGDEIELKDDNGKVTVNGQQV-SLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKT 143

                           170       180
                    ....*....|....*....|
gi 442632169    995 QGLCGTFNSNTQDDFLTPEG 1014
Cdd:smart00216  144 CGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1326-1497 1.27e-30

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: 120.20  E-value: 1.27e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   1326 WKCSKNGCESTCSVWGDSHFTTFDGHDFDFQGACDYVLAKGVFDNGDgFSITIQNVLCGTmGVTCSKSLEIALTGhaees 1405
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGG-GATCLKSVKVELNG----- 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   1406 lllsaDSAYSTDPNKTPIkklrdsVNSKGHN--------AFHIYKAGVFVVVEVIPLKLQVKWDEGTRVYVKLGNEWRQK 1477
Cdd:smart00216   74 -----DEIELKDDNGKVT------VNGQQVSlpyktsdgSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGK 142

                           170       180
                    ....*....|....*....|
gi 442632169   1478 VSGLCGNYNGNSLDDMQTPS 1497
Cdd:smart00216  143 TCGLCGNFDGEPEDDFRTPD 162
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 850-1014 1.58e-30

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: 119.78  E-value: 1.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   850 CGAVGDPHYQTFDGKRYDFMGKCSYHLLKTQNTSVEAEnvacsgaVSESMNFAAPDDPS-CTKAVTIrfILRDGTpsvIK 928
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-------FSVTNKNCNGGASGvCLKSVTV--IVGDLE---IT 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   929 LDQGLTTIVNDKPIAkLPKMLGLGEVLIRRASSTFLTVEFADGIRVWWDGVSRVYIDAPPSLRGQTQGLCGTFNSNTQDD 1008
Cdd:pfam00094   69 LQKGGTVLVNGQKVS-LPYKSDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDD 147


                   ....*.
gi 442632169  1009 FLTPEG 1014
Cdd:pfam00094  148 FMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1337-1497 3.41e-27

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: 110.15  E-value: 3.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  1337 CSVWGDSHFTTFDGHDFDFQGACDYVLAKGV-FDNGDGFSITIQNVLCGTMGVtCSKSLEIaLTGHAEESLLLSADSAYS 1415
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGV-CLKSVTV-IVGDLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  1416 TDPNKTPIKKLRDSVNskghnafhIYKAGVFVVVEVIPLKLQVKWDEGTRVYVKLGNEWRQKVSGLCGNYNGNSLDDMQT 1495
Cdd:pfam00094   79 GQKVSLPYKSDGGEVE--------ILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMT 150


                   ..
gi 442632169  1496 PS 1497
Cdd:pfam00094  151 PD 152
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2088-2222 9.78e-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: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 93.96  E-value: 9.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169 2088 PDSIFnASSQLAPEHGPKMARLTKEqprGSWSPSINDQMQYLELNFAKPEPFYGVVMAG--SPEFDNYVTLFKILHSHDG 2165
Cdd:cd00057    11 DDQIT-ASSSYSSGWEASRARLNSD---NAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkGGGSSEWVTSYKVQYSLDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169 2166 IAYHYLVDETEkPQMFNGPLDSRAPVQTLFKIPIEASSLRIYPLKWHGSIAMRVELL 2222
Cdd:cd00057    87 ETWTTYKDKGE-EKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELY 142
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2298-2402 2.38e-21

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: 92.80  E-value: 2.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169 2298 AWRPLANSQNEFIEFDFLEPRNISGFVTKG----GPDGWVTGYKVMFSKKKPTWnTVLSTDGQARIFEANHDAETERRHH 2373
Cdd:cd00057    36 AWTPAVNDPPQWLQVDLGKTRRVTGIQTQGrkggGSSEWVTSYKVQYSLDGETW-TTYKDKGEEKVFTGNSDGSTPVTND 114

                          90       100
                  ....*....|....*....|....*....
gi 442632169 2374 FKNPILTQYIKIVPAYWEKNINMRIEPLG 2402
Cdd:cd00057   115 FPPPIVARYIRILPTTWNGNISLRLELYG 143
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2702-2857 9.69e-21

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: 91.66  E-value: 9.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2702 CEISGKS-FTTFDGTVFKY-GPCSHILARDIHS-SSWSISVH-QQCSDETRKVCHKVITIQdteAGNELILLPH-LKLKF 2776
Cdd:pfam00094    1 CSVSGDPhYVTFDGVKYTFpGTCTYVLAKDCSEePDFSFSVTnKNCNGGASGVCLKSVTVI---VGDLEITLQKgGTVLV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2777 NGYEftvqqlINSPICKASFVVSQPGKTLLAVSTKYGFWVQL--DDIGIVKVGISSKFIRTVDGLCGYYNGNQKDDKRSP 2854
Cdd:pfam00094   78 NGQK------VSLPYKSDGGEVEILGSGFVVVDLSPGVGLQVdgDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151


                   ...
gi 442632169  2855 DGQ 2857
Cdd:pfam00094  152 DGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 484-635 1.85e-19

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: 87.81  E-value: 1.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   484 CTTWGGINMKTFDGLVFKAPLSCSHTLITDKVSGT---FDIILKACPYGSGYGCAHTLKILWQSVLYTfenLNGTMQLTT 560
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPdfsFSVTNKNCNGGASGVCLKSVTVIVGDLEIT---LQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169   561 PIKKLPMPVQVMGMKV-MPVAQHVQIDLES-VGLKLDWDHRQYVSVQAGPQMWGKVGGLCGTLDGDPNTDLTSRTGK 635
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVeILGSGFVVVDLSPgVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 3034-3197 5.84e-19

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: 86.66  E-value: 5.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  3034 CNSLGASKYMTYDRKSFSFNGNCTYLLSRDVvlPGVHTFQVYVSMDDCKKlGQPtpvegGSCAKSLHILNGDHVIHVQRV 3113
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDC--SEEPDFSFSVTNKNCNG-GAS-----GVCLKSVTVIVGDLEITLQKG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  3114 pqkpksLQVLVDGFEVkKIPYKDSWISLRQVVGKELVLSLPeSHVELTASFEDLIFSLGVPSIKYGSKMEGLCGDCNGNA 3193
Cdd:pfam00094   73 ------GTVLVNGQKV-SLPYKSDGGEVEILGSGFVVVDLS-PGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQ 144


                   ....
gi 442632169  3194 GNDL 3197
Cdd:pfam00094  145 EDDF 148
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2093-2221 1.14e-18

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: 84.81  E-value: 1.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2093 NASSQLAPEHGPKmARLTKEqPRGSWSPSINDQMQYLELNFAKPEPFYGVVMAGSP-EFDNYVTLFKILHSHDGIAYHYL 2171
Cdd:pfam00754    3 TASSSYSGEGPAA-AALDGD-PNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQdGSNGYVTSYKIEYSLDGENWTTV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 442632169  2172 VDETEKpqmfnGPLDSRAPVQTLFKIPIEASSLRIYPLKWHGS--IAMRVEL 2221
Cdd:pfam00754   81 KDEKIP-----GNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2690-2856 7.68e-18

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: 83.61  E-value: 7.68e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2690 YSCVLRPNkDDVCEISGKS-FTTFDGTVFKY-GPCSHILARDIHSS-SWSISVhQQCSDETRKVCHKVITIQDTEaGNEL 2766
Cdd:smart00216    1 WCCTQEEC-SPTCSVSGDPhYTTFDGVAYTFpGNCYYVLAQDCSSEpTFSVLL-KNVPCGGGATCLKSVKVELNG-DEIE 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2767 ILLPHLKLKFNGYEFTVQQLINSpickaSFVVSQPGKTLLAVSTKYGFW-VQLDDIGIVKVGISSKFIRTVDGLCGYYNG 2845
Cdd:smart00216   78 LKDDNGKVTVNGQQVSLPYKTSD-----GSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDG 152

                           170
                    ....*....|.
gi 442632169   2846 NQKDDKRSPDG 2856
Cdd:smart00216  153 EPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 478-634 1.08e-17

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: 83.22  E-value: 1.08e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169    478 TPRPALCTTWGGINMKTFDGLVFKAPLSCSHTLITDKVS-GTFDIILKACPYGSGYGCAHTLKILWQSVLYTFENLNGTM 556
Cdd:smart00216    6 EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSePTFSVLLKNVPCGGGATCLKSVKVELNGDEIELKDDNGKV 85

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169    557 QLTTPIKKLPMPVQVMGMKVMPVAQHVQIDLESVGLKLDWDHRQYVSVQAGPQMWGKVGGLCGTLDGDPNTDLTSRTG 634
Cdd:smart00216   86 TVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2298-2403 1.11e-17

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: 82.17  E-value: 1.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2298 AWRPLANSQNEFIEFDFLEPRNISGFVT-KGGPDGWVTGYKVMFSKKKPTWNTVlsTDGQARIFEANHDAETERRHHFKN 2376
Cdd:smart00231   35 GWCPAKNDLPPWIQVDLGRLRTVTGVITgRRHGNGDWVTYKLEYSDDGVNWTTY--KDGNSKVFPGNSDAGTVVLNDFPP 112

                            90       100
                    ....*....|....*....|....*..
gi 442632169   2377 PILTQYIKIVPAYWEKNINMRIEPLGC 2403
Cdd:smart00231  113 PIVARYVRILPTGWNGNIILRVELLGC 139
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 3032-3198 1.31e-17

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: 82.83  E-value: 1.31e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   3032 CVCNSLGASKYMTYDRKSFSFNGNCTYLLSRDvvLPGVHTFQVYVSMDDCKKlgqptpveGGSCAKSLHILNGDHVIHVq 3111
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD--CSSEPTFSVLLKNVPCGG--------GATCLKSVKVELNGDEIEL- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   3112 rvpqKPKSLQVLVDGfEVKKIPYKDSWISLRQVVGKELVLSLPESHVeLTASFEDLI-FSLGVPSiKYGSKMEGLCGDCN 3190
Cdd:smart00216   79 ----KDDNGKVTVNG-QQVSLPYKTSDGSIQIRSSGGYLVVITSLGL-IQVTFDGLTlLSVQLPS-KYRGKTCGLCGNFD 151


                    ....*...
gi 442632169   3191 GNAGNDLQ 3198
Cdd:smart00216  152 GEPEDDFR 159
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2298-2399 1.38e-17

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: 81.72  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  2298 AWRPLANSQNEFIEFDFLEPRNISGFVTKGGPD---GWVTGYKVMFSKKKPTWNTVLSTDgqariFEANHDAETERRHHF 2374
Cdd:pfam00754   25 AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDgsnGYVTSYKIEYSLDGENWTTVKDEK-----IPGNNDNNTPVTNTF 99

                           90       100
                   ....*....|....*....|....*..
gi 442632169  2375 KNPILTQYIKIVPAYW--EKNINMRIE 2399
Cdd:pfam00754  100 DPPIKARYVRIVPTSWngGNGIALRAE 126
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1053-1120 1.27e-15

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: 74.30  E-value: 1.27e-15
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632169   1053 KAQAEKFCDWILQD--IFQDCHFLVEPEQFYEDCLYDTCACKDeMSKCFCPILSAYGTECMRQGVK-TGWR 1120
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGG-DCECLCDALAAYAAACAEAGVCiSPWR 70
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2103-2224 1.23e-12

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: 67.92  E-value: 1.23e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169   2103 GPKMARLTKEQPRGsWSPSINDQMQYLELNFAKPEPFYGVVmAGSPEFDNYVTLFKILHSHDGIAYHYLVDETEKpqMFN 2182
Cdd:smart00231   22 AAKIARLNGGSDGG-WCPAKNDLPPWIQVDLGRLRTVTGVI-TGRRHGNGDWVTYKLEYSDDGVNWTTYKDGNSK--VFP 97

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 442632169   2183 GPLDSRAPVQTLFKIPIEASSLRIYPLKWHGSIAMRVELLIC 2224
Cdd:smart00231   98 GNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1059-1120 4.15e-12

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: 63.94  E-value: 4.15e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632169  1059 FCDWIL-QDIFQDCHFLVEPEQFYEDCLYDTCACKDEmSKCFCPILSAYGTECMRQGVK-TGWR 1120
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGGD-DECLCAALAAYARACQAAGVCiGDWR 63
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1130-1184 4.72e-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: 63.49  E-value: 4.72e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169 1130 CPLGQVFDECGDGCALSCDDLPSKGSCKRECVEGCRCPHGEYVNEDGECVPKKMC 1184
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 3247-3312 1.01e-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: 62.78  E-value: 1.01e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632169  3247 CLQFYNAELFGKCPLAVDPIAYVSACQQDICKPGNTQQGVCVALAAYAKECNQHGIC-TNWRRPQLC 3312
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCiGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1130-1184 2.46e-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: 61.25  E-value: 2.46e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169  1130 CPLGQVFDECGDGCALSCDDLPSKGSCKRECVEGCRCPHGEYVNEDGECVPKKMC 1184
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1534-1608 2.59e-11

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: 61.97  E-value: 2.59e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169   1534 ETWAQLKCGALKSDL--FKECHAEVPLERFWKRCIFDTCACdqGGDCECLCTAVAAYADACAQKGINIR-WRSQHFCP 1608
Cdd:smart00832    1 KYYACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 3256-3313 1.68e-09

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: 56.97  E-value: 1.68e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 442632169   3256 FGKCPLAVDPIAYVSACQQDICKPGNTQQGVCVALAAYAKECNQHGIC-TNWRRPQLCP 3313
Cdd:smart00832   18 FAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCiSPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1540-1607 8.99e-09

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: 54.31  E-value: 8.99e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632169  1540 KCGALK-SDLFKECHAEVPLERFWKRCIFDTCACdqGGDCECLCTAVAAYADACAQKGINIR-WRSQHFC 1607
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 683-753 6.36e-06

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: 46.22  E-value: 6.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632169   683 CERLLANEKLGDCIKPFNYDALIRTCMADYCNCANrehPESCNCDAIAMLAKECAFKGIKLEHgWRNLEIC 753
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGG---DDECLCAALAAYARACQAAGVCIGD-WRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2973-3029 1.06e-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: 45.46  E-value: 1.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169  2973 CPSPLVHTDCyKRRCEPSCDNVHGDDCPVLPdaCFPGCYCPEGTVR-KGPNCVPISEC 3029
Cdd:pfam01826    1 CPANEVYSEC-GSACPPTCANLSPPDVCPEP--CVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1244-1297 4.20e-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: 43.53  E-value: 4.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442632169  1244 PYAEFTKCAPKEPKTCKNMDKYVADSSDCLPGCVCMEGYVYDTSRlACVLPANC 1297
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGG-KCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1247-1297 4.37e-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: 43.46  E-value: 4.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442632169 1247 EFTKCAPKEPKTCKNMDKYVADSSDCLPGCVCMEGYVYDTSRlACVLPANC 1297
Cdd:cd19941     6 VYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGG-KCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 757-810 7.00e-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: 43.07  E-value: 7.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169  757 CGFGRVYQACGPNVEPTCDSDLALPASKGACNEGCFCPEGTV-QYKEACITRELC 810
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVrNSGGKCVPPSQC 55
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 3754-3812 8.80e-05

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: 43.55  E-value: 8.80e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 442632169   3754 CEGACSSGSKYNTLTDMHekFCTCCSIKSYHPISVKMICDDGHTFTQKHEVPSNCGCSP 3812
Cdd:smart00041   23 CEGKCGSASSYSIQDVQH--SCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGCEP 79
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2973-3029 1.12e-04

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 42.30  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169 2973 CPSPLVHTDCyKRRCEPSCDNVHGDdcPVLPDACFPGCYCPEGTVR-KGPNCVPISEC 3029
Cdd:cd19941     1 CPPNEVYSEC-GSACPPTCANPNAP--PPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 757-810 3.37e-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: 41.22  E-value: 3.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169   757 CGFGRVYQACGPNVEPTCDSDLALPASKGACNEGCFCPEGTV-QYKEACITRELC 810
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVrNSGGKCVPPSDC 55
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
812-865 7.38e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 40.62  E-value: 7.38e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 442632169    812 CSLRGKEFKPESTVKKNCNTCTCKNGQWRCTEDKCGARCGAVGDPHYQTFDGKR 865
Cdd:smart00215    1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKPCLLHNLSGECPLGQG 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 708-754 2.63e-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: 39.25  E-value: 2.63e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 442632169    708 CMADYCNCANREHpesCNCDAIAMLAKECAFKGIKLeHGWRNLEICP 754
Cdd:smart00832   34 CVYDTCACGGDCE---CLCDALAAYAAACAEAGVCI-SPWRTPTFCP 76
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1937-2004 7.87e-03

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: 37.37  E-value: 7.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632169  1937 CPPGKIKSECANQCENTCHYygsiLKKRGLCqvGEHCKPGCVdelrpdCPKlGKFWRDEDTCVHADEC 2004
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN----LSPPDVC--PEPCVEGCV------CPP-GFVRNSGGKCVPPSDC 55
VWC smart00214
von Willebrand factor (vWF) type C domain;
3396-3450 8.22e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.50  E-value: 8.22e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442632169   3396 HLPDEKWKKDKCTECQCDSKGKTTCVEKKCQvEENICAegyRPETIVSVDECCPR 3450
Cdd:smart00214    8 YNDGETWKPDPCQICTCLDGTTVLCDPVECP-PPPDCP---NPERVKPPGECCPR 58
 
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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