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Conserved domains on  [gi|24371216|ref|NP_082748|]
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BMP-binding endothelial regulator protein precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 364-508 2.72e-36

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.65  E-value: 2.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24371216   364 CTVFGDPHYNTFDGRTFNFQGTCQYVLTKDCSSPASP-FQVLVKNDARRTRSfSWTKSVELMLGESTVSLQQHLTVRWNG 442
Cdd:pfam00094   1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTVLVNG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216   443 SRIALPCHTPHFHID-LDGYLLKVTTRAGLEIS--WDGDSFVEVMAAPHLKGKLCGLCGNYNGHKRDDL 508
Cdd:pfam00094  80 QKVSLPYKSDGGEVEiLGSGFVVVDLSPGVGLQvdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDF 148
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 560-624 9.50e-13

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: 63.55  E-value: 9.50e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24371216   560 CQKLKSWE-FQTCHSTVDYTTFYRSCVTDMCECPVHKNCYCESFLAYTRACQREGIKV-HWEPQQSC 624
Cdd:pfam08742   2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 629-682 2.00e-09

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: 53.86  E-value: 2.00e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24371216 629 CKHGAVYDTCGPGCVKTCDNWNEIGPCNKPCIAGCHCPANLVLH-KGRCIKPVLC 682
Cdd:cd19941   1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 166-224 7.18e-08

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


:

Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 7.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216   166 CVFEGVQYREGEEFQPEgnKCITCSCVGGRTQCVREVCPILSCPQHLSHTPSGQCCPKC 224
Cdd:pfam00093   1 CVQNGVVYENGETWKPD--LCTICTCDDGKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 301-357 5.70e-06

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


The actual alignment was detected with superfamily member pfam00093:

Pssm-ID: 450195  Cd Length: 57  Bit Score: 43.95  E-value: 5.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24371216   301 CKFGSKIFRDGEMWSSVNCSICACVKGKTECRKKQCvPVSSCPQGKILNRKG-CCPIC 357
Cdd:pfam00093   1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIIC-PPLDCPNPRLEIPPGeCCPVC 57
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 364-508 2.72e-36

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.65  E-value: 2.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24371216   364 CTVFGDPHYNTFDGRTFNFQGTCQYVLTKDCSSPASP-FQVLVKNDARRTRSfSWTKSVELMLGESTVSLQQHLTVRWNG 442
Cdd:pfam00094   1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTVLVNG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216   443 SRIALPCHTPHFHID-LDGYLLKVTTRAGLEIS--WDGDSFVEVMAAPHLKGKLCGLCGNYNGHKRDDL 508
Cdd:pfam00094  80 QKVSLPYKSDGGEVEiLGSGFVVVDLSPGVGLQvdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDF 148
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 353-508 3.07e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 127.90  E-value: 3.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24371216    353 CCpICTEKPGVCTVFGDPHYNTFDGRTFNFQGTCQYVLTKDCSSPASpFQVLVKNDARRTRSfSWTKSVELMLGESTVSL 432
Cdd:smart00216   2 CC-TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGGGA-TCLKSVKVELNGDEIEL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24371216    433 QQH-LTVRWNGSRIALPCHTPHFHID---LDGYLLKVTTRAGLEISWDGDSFVEVMAAPHLKGKLCGLCGNYNGHKRDDL 508
Cdd:smart00216  79 KDDnGKVTVNGQQVSLPYKTSDGSIQirsSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 560-624 9.50e-13

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: 63.55  E-value: 9.50e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24371216   560 CQKLKSWE-FQTCHSTVDYTTFYRSCVTDMCECPVHKNCYCESFLAYTRACQREGIKV-HWEPQQSC 624
Cdd:pfam08742   2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 568-625 1.26e-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: 60.82  E-value: 1.26e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216    568 FQTCHSTVDYTTFYRSCVTDMCECPVHKNCYCESFLAYTRACQREGIKVH-WEPQQSCA 625
Cdd:smart00832  18 FAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 629-682 2.00e-09

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: 53.86  E-value: 2.00e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24371216 629 CKHGAVYDTCGPGCVKTCDNWNEIGPCNKPCIAGCHCPANLVLH-KGRCIKPVLC 682
Cdd:cd19941   1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 629-682 8.52e-09

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: 52.00  E-value: 8.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24371216   629 CKHGAVYDTCGPGCVKTCDNWNEIGPCNKPCIAGCHCPANLVLHK-GRCIKPVLC 682
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSgGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 166-224 7.18e-08

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 7.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216   166 CVFEGVQYREGEEFQPEgnKCITCSCVGGRTQCVREVCPILSCPQHLSHTPSGQCCPKC 224
Cdd:pfam00093   1 CVQNGVVYENGETWKPD--LCTICTCDDGKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 301-357 5.70e-06

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 43.95  E-value: 5.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24371216   301 CKFGSKIFRDGEMWSSVNCSICACVKGKTECRKKQCvPVSSCPQGKILNRKG-CCPIC 357
Cdd:pfam00093   1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIIC-PPLDCPNPRLEIPPGeCCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
301-357 2.99e-05

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 42.12  E-value: 2.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216    301 CKFGSKIFRDGEMWSSVNCSICACVKGKTE-CRKKQCVPVSSCPQGKILNRKG-CCPIC 357
Cdd:smart00214   1 CVHNGRVYNDGETWKPDPCQICTCLDGTTVlCDPVECPPPPDCPNPERVKPPGeCCPRC 59
VWC smart00214
von Willebrand factor (vWF) type C domain;
166-224 7.59e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 38.27  E-value: 7.59e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24371216    166 CVFEGVQYREGEEFQPegNKCITCSCVGGRT-QCVREVCPI-LSCPQHLSHTPSGQCCPKC 224
Cdd:smart00214   1 CVHNGRVYNDGETWKP--DPCQICTCLDGTTvLCDPVECPPpPDCPNPERVKPPGECCPRC 59
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 364-508 2.72e-36

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.65  E-value: 2.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24371216   364 CTVFGDPHYNTFDGRTFNFQGTCQYVLTKDCSSPASP-FQVLVKNDARRTRSfSWTKSVELMLGESTVSLQQHLTVRWNG 442
Cdd:pfam00094   1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTVLVNG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216   443 SRIALPCHTPHFHID-LDGYLLKVTTRAGLEIS--WDGDSFVEVMAAPHLKGKLCGLCGNYNGHKRDDL 508
Cdd:pfam00094  80 QKVSLPYKSDGGEVEiLGSGFVVVDLSPGVGLQvdGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDF 148
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 353-508 3.07e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 127.90  E-value: 3.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24371216    353 CCpICTEKPGVCTVFGDPHYNTFDGRTFNFQGTCQYVLTKDCSSPASpFQVLVKNDARRTRSfSWTKSVELMLGESTVSL 432
Cdd:smart00216   2 CC-TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCGGGA-TCLKSVKVELNGDEIEL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24371216    433 QQH-LTVRWNGSRIALPCHTPHFHID---LDGYLLKVTTRAGLEISWDGDSFVEVMAAPHLKGKLCGLCGNYNGHKRDDL 508
Cdd:smart00216  79 KDDnGKVTVNGQQVSLPYKTSDGSIQirsSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 560-624 9.50e-13

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: 63.55  E-value: 9.50e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24371216   560 CQKLKSWE-FQTCHSTVDYTTFYRSCVTDMCECPVHKNCYCESFLAYTRACQREGIKV-HWEPQQSC 624
Cdd:pfam08742   2 CGLLSDSGpFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 568-625 1.26e-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: 60.82  E-value: 1.26e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216    568 FQTCHSTVDYTTFYRSCVTDMCECPVHKNCYCESFLAYTRACQREGIKVH-WEPQQSCA 625
Cdd:smart00832  18 FAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 629-682 2.00e-09

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: 53.86  E-value: 2.00e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24371216 629 CKHGAVYDTCGPGCVKTCDNWNEIGPCNKPCIAGCHCPANLVLH-KGRCIKPVLC 682
Cdd:cd19941   1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 629-682 8.52e-09

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: 52.00  E-value: 8.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24371216   629 CKHGAVYDTCGPGCVKTCDNWNEIGPCNKPCIAGCHCPANLVLHK-GRCIKPVLC 682
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSgGKCVPPSDC 55
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 166-224 7.18e-08

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 49.35  E-value: 7.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216   166 CVFEGVQYREGEEFQPEgnKCITCSCVGGRTQCVREVCPILSCPQHLSHTPSGQCCPKC 224
Cdd:pfam00093   1 CVQNGVVYENGETWKPD--LCTICTCDDGKVLCDKIICPPLDCPNPRLEIPPGECCPVC 57
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 301-357 5.70e-06

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


Pssm-ID: 278520  Cd Length: 57  Bit Score: 43.95  E-value: 5.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24371216   301 CKFGSKIFRDGEMWSSVNCSICACVKGKTECRKKQCvPVSSCPQGKILNRKG-CCPIC 357
Cdd:pfam00093   1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIIC-PPLDCPNPRLEIPPGeCCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
301-357 2.99e-05

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 42.12  E-value: 2.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24371216    301 CKFGSKIFRDGEMWSSVNCSICACVKGKTE-CRKKQCVPVSSCPQGKILNRKG-CCPIC 357
Cdd:smart00214   1 CVHNGRVYNDGETWKPDPCQICTCLDGTTVlCDPVECPPPPDCPNPERVKPPGeCCPRC 59
VWC smart00214
von Willebrand factor (vWF) type C domain;
166-224 7.59e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 38.27  E-value: 7.59e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24371216    166 CVFEGVQYREGEEFQPegNKCITCSCVGGRT-QCVREVCPI-LSCPQHLSHTPSGQCCPKC 224
Cdd:smart00214   1 CVHNGRVYNDGETWKP--DPCQICTCLDGTTvLCDPVECPPpPDCPNPERVKPPGECCPRC 59
 
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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