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Conserved domains on  [gi|194380162|dbj|BAG63848|]
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unnamed protein product [Homo sapiens]

Protein Classification

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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 ...
 119-272 2.31e-48

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: 169.09  E-value: 2.31e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   119 CTASGDPHYLTFDGALHHFMGTCTYVLTRPCWSRSQDSyFVVSATNENRGGilEVSYIKAVHVTVFDLSISLLRGCKVML 198
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGA--SGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   199 NGHRVALPVWLAQGRVTIRLS-SNLVLLYTNFGLQVRYDGSHLVEVTVPSSYGGQLCGLCGNYNNNSLDDNLRPD 272
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 442-595 5.57e-39

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 142.12  E-value: 5.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   442 CQLPGESHYVSFDGSNHSIPDACTLVLVKVCHPamaLPLFKISAKHEKEEGGTEAFRLHEVYIDIYDAQVTLQKGHRVLI 521
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE---EPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   522 NSKQVTLPAISQIPGVSVKSS-SIYTIVNIKIGVQVKFDGNHLLEIEIPTTYYGKVCGMCGNFNDEEEDELMMPS 595
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 314-386 1.27e-20

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: 87.01  E-value: 1.27e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194380162    314 AWNKNCAILINPQGPFSQCHQVVPPQSSFASCVHGQCGTKGDTTALCRSLQAYASLCAQAGQAP-AWRNRTFCP 386
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 805-923 3.39e-20

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: 88.58  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   805 CSVYGDPRYLTFDGFSYRLQGRMTYVLIKTVDVLPegvEPLLVEGRNKMDPPRSSIFLQEVITTVYGYKVQLQAGLELVV 884
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 194380162   885 NNQKMAVPY-RPNEHLRVTLRGQ-RLYLVTDFELVVSFGGR 923
Cdd:pfam00094   78 NGQKVSLPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGR 118
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 743-794 4.59e-16

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 4.59e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194380162   743 CKDAHGGSIPLGKSWVSSGCTEKCVCTGGAIQCGDFRCPSGSHCQLTSDNSN 794
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3-56 5.96e-13

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 64.26  E-value: 5.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162    3 CPPNSKYSLCAKPCPDTCHSGFSGMFCSDRCVEACECNPGFVLS-GLECIPRSQC 56
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 58-112 1.83e-11

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 60.01  E-value: 1.83e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162    58 CLHPAGSYFKVGERWYKPGCKELCVCESNNrIRCQPWRCRAQEFCGQQDGIYGCH 112
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1035-1079 2.00e-07

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 48.84  E-value: 2.00e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 194380162  1035 LGSSFLTEDCSQRCTCASSRILlCEPFSCRAGEVCTLGNHTQGCF 1079
Cdd:pfam12714   11 AGKTWFSSGCTQSCTCTGGNIQ-CQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 685-741 3.89e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 45.07  E-value: 3.89e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 194380162   685 CPAYSSYTNYLPSCSPSCWDLDGRcegAKVPSACAEGCICQPGYVLSED-KCVPRSRC 741
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPP---DVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1084-1112 3.00e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.29  E-value: 3.00e-04
                           10        20
                   ....*....|....*....|....*....
gi 194380162  1084 CLQNPCQNDGQCREQGATFTCECEVGYGG 1112
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 119-272 2.31e-48

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: 169.09  E-value: 2.31e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   119 CTASGDPHYLTFDGALHHFMGTCTYVLTRPCWSRSQDSyFVVSATNENRGGilEVSYIKAVHVTVFDLSISLLRGCKVML 198
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGA--SGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   199 NGHRVALPVWLAQGRVTIRLS-SNLVLLYTNFGLQVRYDGSHLVEVTVPSSYGGQLCGLCGNYNNNSLDDNLRPD 272
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 111-272 6.40e-40

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: 145.24  E-value: 6.40e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    111 CHAQGAATCTASGDPHYLTFDGALHHFMGTCTYVLTRPCWSRSQdsyFVVSATNENRGGilEVSYIKAVHVTVFDLSISL 190
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT---FSVLLKNVPCGG--GATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    191 LR-GCKVMLNGHRVALPVWLAQGRVTIRLSSNLVLLYTNFGL-QVRYDGSHLVEVTVPSSYGGQLCGLCGNYNNNSLDDN 268
Cdd:smart00216   79 KDdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....
gi 194380162    269 LRPD 272
Cdd:smart00216  159 RTPD 162
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 442-595 5.57e-39

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 142.12  E-value: 5.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   442 CQLPGESHYVSFDGSNHSIPDACTLVLVKVCHPamaLPLFKISAKHEKEEGGTEAFRLHEVYIDIYDAQVTLQKGHRVLI 521
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE---EPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   522 NSKQVTLPAISQIPGVSVKSS-SIYTIVNIKIGVQVKFDGNHLLEIEIPTTYYGKVCGMCGNFNDEEEDELMMPS 595
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 440-595 9.19e-31

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: 119.04  E-value: 9.19e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    440 GVCQLPGESHYVSFDGSNHSIPDACTLVLVKVCHPamaLPLFKISAKHEKEEGGteAFRLHEVYIDIYDAQVTLQKGHR- 518
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS---EPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDDNGk 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194380162    519 VLINSKQVTLPAISQIPGVSVKSSSIYTIVNIKIGV-QVKFDGNHLLEIEIPTTYYGKVCGMCGNFNDEEEDELMMPS 595
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 314-386 1.27e-20

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: 87.01  E-value: 1.27e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194380162    314 AWNKNCAILINPQGPFSQCHQVVPPQSSFASCVHGQCGTKGDTTALCRSLQAYASLCAQAGQAP-AWRNRTFCP 386
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 805-923 3.39e-20

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: 88.58  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   805 CSVYGDPRYLTFDGFSYRLQGRMTYVLIKTVDVLPegvEPLLVEGRNKMDPPRSSIFLQEVITTVYGYKVQLQAGLELVV 884
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 194380162   885 NNQKMAVPY-RPNEHLRVTLRGQ-RLYLVTDFELVVSFGGR 923
Cdd:pfam00094   78 NGQKVSLPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGR 118
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 322-385 1.23e-16

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: 75.49  E-value: 1.23e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   322 LINPQGPFSQCHQVVPPQSSFASCVHGQCGTKGDTTALCRSLQAYASLCAQAGQAPA-WRNRTFC 385
Cdd:pfam08742    4 LLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 743-794 4.59e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 4.59e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194380162   743 CKDAHGGSIPLGKSWVSSGCTEKCVCTGGAIQCGDFRCPSGSHCQLTSDNSN 794
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3-56 5.96e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 64.26  E-value: 5.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162    3 CPPNSKYSLCAKPCPDTCHSGFSGMFCSDRCVEACECNPGFVLS-GLECIPRSQC 56
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3-56 8.84e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 61.25  E-value: 8.84e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162     3 CPPNSKYSLCAKPCPDTCHSGFSGMFCSDRCVEACECNPGFVLSGL-ECIPRSQC 56
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 58-112 1.83e-11

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 60.01  E-value: 1.83e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162    58 CLHPAGSYFKVGERWYKPGCKELCVCESNNrIRCQPWRCRAQEFCGQQDGIYGCH 112
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 805-925 1.88e-11

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 63.57  E-value: 1.88e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    805 CSVYGDPRYLTFDGFSYRLQGRMTYVLIKTVDVLPEgvepLLVEGRNKMDPPRSSIfLQEVITTVYGYKVQL-QAGLELV 883
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATC-LKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 194380162    884 VNNQKMAVPY-RPNEHLRVTLRGQRLYLVTDFELV-VSFGGRKN 925
Cdd:smart00216   87 VNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL 130
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1035-1079 2.00e-07

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 48.84  E-value: 2.00e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 194380162  1035 LGSSFLTEDCSQRCTCASSRILlCEPFSCRAGEVCTLGNHTQGCF 1079
Cdd:pfam12714   11 AGKTWFSSGCTQSCTCTGGNIQ-CQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 685-741 3.89e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 45.07  E-value: 3.89e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 194380162   685 CPAYSSYTNYLPSCSPSCWDLDGRcegAKVPSACAEGCICQPGYVLSED-KCVPRSRC 741
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPP---DVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 685-741 1.52e-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: 1.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162  685 CPAYSSYTNYLPSCSPSCWDLD--GRCegakvPSACAEGCICQPGYVLSED-KCVPRSRC 741
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-----TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1084-1112 3.00e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.29  E-value: 3.00e-04
                           10        20
                   ....*....|....*....|....*....
gi 194380162  1084 CLQNPCQNDGQCREQGATFTCECEVGYGG 1112
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1087-1115 7.47e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.31  E-value: 7.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 194380162 1087 NPCQNDGQCREQGATFTCECEVGYGGGLC 1115
Cdd:cd00054     9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 119-272 2.31e-48

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: 169.09  E-value: 2.31e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   119 CTASGDPHYLTFDGALHHFMGTCTYVLTRPCWSRSQDSyFVVSATNENRGGilEVSYIKAVHVTVFDLSISLLRGCKVML 198
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGA--SGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   199 NGHRVALPVWLAQGRVTIRLS-SNLVLLYTNFGLQVRYDGSHLVEVTVPSSYGGQLCGLCGNYNNNSLDDNLRPD 272
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 111-272 6.40e-40

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: 145.24  E-value: 6.40e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    111 CHAQGAATCTASGDPHYLTFDGALHHFMGTCTYVLTRPCWSRSQdsyFVVSATNENRGGilEVSYIKAVHVTVFDLSISL 190
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT---FSVLLKNVPCGG--GATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    191 LR-GCKVMLNGHRVALPVWLAQGRVTIRLSSNLVLLYTNFGL-QVRYDGSHLVEVTVPSSYGGQLCGLCGNYNNNSLDDN 268
Cdd:smart00216   79 KDdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....
gi 194380162    269 LRPD 272
Cdd:smart00216  159 RTPD 162
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 442-595 5.57e-39

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 142.12  E-value: 5.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   442 CQLPGESHYVSFDGSNHSIPDACTLVLVKVCHPamaLPLFKISAKHEKEEGGTEAFRLHEVYIDIYDAQVTLQKGHRVLI 521
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE---EPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   522 NSKQVTLPAISQIPGVSVKSS-SIYTIVNIKIGVQVKFDGNHLLEIEIPTTYYGKVCGMCGNFNDEEEDELMMPS 595
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 440-595 9.19e-31

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: 119.04  E-value: 9.19e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    440 GVCQLPGESHYVSFDGSNHSIPDACTLVLVKVCHPamaLPLFKISAKHEKEEGGteAFRLHEVYIDIYDAQVTLQKGHR- 518
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS---EPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDDNGk 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194380162    519 VLINSKQVTLPAISQIPGVSVKSSSIYTIVNIKIGV-QVKFDGNHLLEIEIPTTYYGKVCGMCGNFNDEEEDELMMPS 595
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 314-386 1.27e-20

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: 87.01  E-value: 1.27e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194380162    314 AWNKNCAILINPQGPFSQCHQVVPPQSSFASCVHGQCGTKGDTTALCRSLQAYASLCAQAGQAP-AWRNRTFCP 386
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 805-923 3.39e-20

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: 88.58  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162   805 CSVYGDPRYLTFDGFSYRLQGRMTYVLIKTVDVLPegvEPLLVEGRNKMDPPRSSIFLQEVITTVYGYKVQLQAGLELVV 884
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 194380162   885 NNQKMAVPY-RPNEHLRVTLRGQ-RLYLVTDFELVVSFGGR 923
Cdd:pfam00094   78 NGQKVSLPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGR 118
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 322-385 1.23e-16

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: 75.49  E-value: 1.23e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194380162   322 LINPQGPFSQCHQVVPPQSSFASCVHGQCGTKGDTTALCRSLQAYASLCAQAGQAPA-WRNRTFC 385
Cdd:pfam08742    4 LLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 743-794 4.59e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 4.59e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194380162   743 CKDAHGGSIPLGKSWVSSGCTEKCVCTGGAIQCGDFRCPSGSHCQLTSDNSN 794
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3-56 5.96e-13

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 64.26  E-value: 5.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162    3 CPPNSKYSLCAKPCPDTCHSGFSGMFCSDRCVEACECNPGFVLS-GLECIPRSQC 56
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3-56 8.84e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 61.25  E-value: 8.84e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162     3 CPPNSKYSLCAKPCPDTCHSGFSGMFCSDRCVEACECNPGFVLSGL-ECIPRSQC 56
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 58-112 1.83e-11

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 60.01  E-value: 1.83e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 194380162    58 CLHPAGSYFKVGERWYKPGCKELCVCESNNrIRCQPWRCRAQEFCGQQDGIYGCH 112
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 805-925 1.88e-11

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 63.57  E-value: 1.88e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162    805 CSVYGDPRYLTFDGFSYRLQGRMTYVLIKTVDVLPEgvepLLVEGRNKMDPPRSSIfLQEVITTVYGYKVQL-QAGLELV 883
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATC-LKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 194380162    884 VNNQKMAVPY-RPNEHLRVTLRGQRLYLVTDFELV-VSFGGRKN 925
Cdd:smart00216   87 VNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTL 130
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1035-1079 2.00e-07

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 48.84  E-value: 2.00e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 194380162  1035 LGSSFLTEDCSQRCTCASSRILlCEPFSCRAGEVCTLGNHTQGCF 1079
Cdd:pfam12714   11 AGKTWFSSGCTQSCTCTGGNIQ-CQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 685-741 3.89e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 45.07  E-value: 3.89e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 194380162   685 CPAYSSYTNYLPSCSPSCWDLDGRcegAKVPSACAEGCICQPGYVLSED-KCVPRSRC 741
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPP---DVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 685-741 1.52e-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: 1.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194380162  685 CPAYSSYTNYLPSCSPSCWDLD--GRCegakvPSACAEGCICQPGYVLSED-KCVPRSRC 741
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-----TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1084-1112 3.00e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.29  E-value: 3.00e-04
                           10        20
                   ....*....|....*....|....*....
gi 194380162  1084 CLQNPCQNDGQCREQGATFTCECEVGYGG 1112
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1087-1115 7.47e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.31  E-value: 7.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 194380162 1087 NPCQNDGQCREQGATFTCECEVGYGGGLC 1115
Cdd:cd00054     9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
 
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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