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Conserved domains on  [gi|2117997536|ref|XP_044291191|]
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IgGFc-binding protein-like [Varanus komodoensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgGFc_binding pfam17517
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
 82-372 2.44e-68

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


:

Pssm-ID: 465430  Cd Length: 292  Bit Score: 232.24  E-value: 2.44e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   82 ATTAVYPVQQLGKEYYAITPMGDRANTFKEFAILAYTFPTRVDVHLKGSVIFKGQVYpAGSRLVVDLDSFQAIQLQSSVD 161
Cdd:pfam17517    1 DATLLLPVSSLGTEYYVVSWDPTPGSGPSYFQIVATEDNTTVTITPTVDVTGGGGVY-AGSPFTITLNRGEVLQLQSDGD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  162 LSGSRIESKEPVAVLSGHSCA---WKFTSCDHVVEQLLPVSSWGNTSIVPPL-PFYSRLDTLY--IIASKVTCIKIQsGN 235
Cdd:pfam17517   80 LTGSRITSDKPVAVFSGHSCAnvpSGGGACDHLVEQLPPVSSWGKEYVVVPFrRGNGDEQSIYriVAAEDNTTVTVN-GA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  236 NHNSHNVVAGQVLKLDeqLSHPIYVSADAGIQIIFFFPGSTRENEVYDPFMINIPALTSYCMSYHIDGMAHFHNYAVLIA 315
Cdd:pfam17517  159 AGAPATLNAGEVYEFS--TDAPFYVKSSKPIYVAQYMTGGSSDGGTGDPEMVLVPPVEQYLNSYVFFTDPTYPNNYLVIV 236

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536  316 NTSESSG--ITIQKEAIMNVQWKPVQGTQYSWGDYSLGTEATSLsvqHPSTPFGLLVLG 372
Cdd:pfam17517  237 RTKSTGGfdVTLDGALGELTDWKPGTGGEYEYARVDLGTGAHTV---ESDGPFGVTVYG 292
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 806-969 7.19e-42

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: 151.40  E-value: 7.19e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   806 CYPTSYA-TCSASGDPHYITFDGLKFDFQGTCVYQFTGLCekrTDLVDFLVLVQNDHRGSQAvSFTRDVEIYVYETSIVI 884
Cdd:smart00216    3 CTQEECSpTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGA-TCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   885 SRRNpAKVMVNGLLTNLPYYTESKRISIHRQGQEAVIETDFGL-TVTFDWQSRVTVTVPSTYANTLCGLCGNFNGNKQDE 963
Cdd:smart00216   79 KDDN-GKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 2117997536   964 LTMKNG 969
Cdd:smart00216  158 FRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 422-577 6.76e-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: 142.51  E-value: 6.76e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  422 CWAQGDPHYYTFDGRKFDFMGTCTYIIARTCGQDvSLPSFSIVAKNENRGNPHVsYIALVTATIYNVTISVARyeVGFVR 501
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEE-PDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2117997536  502 VNNQRTRLPISLNDGKLRLYQ-YGGSAFIETDFSLRVSYDWNSYLVVKISSSFWESVCGLCGNYNGDPTDDFRTPEG 577
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGsGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1200-1356 1.35e-36

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 135.96  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536 1200 CSASGDPHYLSFDGLAFDFQGTCTYTLAKaNGDNQTLVPFVVNVENEPWGNGQVSVtKMVSVKIYGITLTLlqKKKGQVK 1279
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAK-DCSEEPDFSFSVTNKNCNGGASGVCL-KSVTVIVGDLEITL--QKGGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2117997536 1280 VNGISQSLPVSFSTGMVTVTQQGSNIVI-KADIGLIVNYDLFYSVKVMVPSTYQGRMQGLCGNYNGQKEDEFLLPDGT 1356
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1399-1473 2.92e-30

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 114.75  E-value: 2.92e-30
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536  1399 FKQRNYCGILTASDGPFRACHSKVDPSVYFDNCVYDVCLGNGESLILCQSIQSYVSACQEAGVSVEPWRNPSFCP 1473
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 617-692 8.89e-23

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: 93.56  E-value: 8.89e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536   617 KYKDEPFCGWISKvGDGPFSQCHSVVDPSIFLENCVYDLCLNDGLKHVLCEALKNYAEACQKEGAAVSDWRSLTGC 692
Cdd:smart00832    1 KYYACSQCGILLS-PRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1013-1082 1.36e-17

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: 78.54  E-value: 1.36e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  1013 KECGLILAKDGPFRECHSKIDPEGYFQDCVYDYCFFEGQQTVICQLISSYAAACQAAGAVLYEWRSDTFC 1082
Cdd:smart00832    6 SQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1086-1139 1.88e-16

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 74.66  E-value: 1.88e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1086 CTPNSHYELCAQGCPQTCSSLYAPAPCPAQCREGCVCNEDFVLS-GDQCVPLSQC 1139
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 696-750 1.69e-15

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: 71.96  E-value: 1.69e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  696 CPENSHYEACGPPCPTTCNAQAGPQNCsTLPCVETCQCNGGFVLDA-GRCVPESAC 750
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1476-1529 8.12e-14

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: 67.41  E-value: 8.12e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1476 CPANSHYQLCADLCSTSCAKITDPQPCPETCTEGCQCDDGFFFDGLG-CVRAESC 1529
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1144-1193 6.71e-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: 47.68  E-value: 6.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2117997536 1144 QGQYYLAGET-FYPTCQERCVCqAGGTVQCMAFSCGPHEECRLLDGIQKCY 1193
Cdd:pfam12714    5 QGNYIPAGKTwFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 752-807 5.43e-06

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 44.99  E-value: 5.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  752 CLFEGKLYSPGEQfWGDAACTKRCTCdaETKQVTCQATGCKSGEQCRVEDGIQNCY 807
Cdd:pfam12714    2 KDAQGNYIPAGKT-WFSSGCTQSCTC--TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
 
Name Accession Description Interval E-value
IgGFc_binding pfam17517
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
 82-372 2.44e-68

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


Pssm-ID: 465430  Cd Length: 292  Bit Score: 232.24  E-value: 2.44e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   82 ATTAVYPVQQLGKEYYAITPMGDRANTFKEFAILAYTFPTRVDVHLKGSVIFKGQVYpAGSRLVVDLDSFQAIQLQSSVD 161
Cdd:pfam17517    1 DATLLLPVSSLGTEYYVVSWDPTPGSGPSYFQIVATEDNTTVTITPTVDVTGGGGVY-AGSPFTITLNRGEVLQLQSDGD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  162 LSGSRIESKEPVAVLSGHSCA---WKFTSCDHVVEQLLPVSSWGNTSIVPPL-PFYSRLDTLY--IIASKVTCIKIQsGN 235
Cdd:pfam17517   80 LTGSRITSDKPVAVFSGHSCAnvpSGGGACDHLVEQLPPVSSWGKEYVVVPFrRGNGDEQSIYriVAAEDNTTVTVN-GA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  236 NHNSHNVVAGQVLKLDeqLSHPIYVSADAGIQIIFFFPGSTRENEVYDPFMINIPALTSYCMSYHIDGMAHFHNYAVLIA 315
Cdd:pfam17517  159 AGAPATLNAGEVYEFS--TDAPFYVKSSKPIYVAQYMTGGSSDGGTGDPEMVLVPPVEQYLNSYVFFTDPTYPNNYLVIV 236

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536  316 NTSESSG--ITIQKEAIMNVQWKPVQGTQYSWGDYSLGTEATSLsvqHPSTPFGLLVLG 372
Cdd:pfam17517  237 RTKSTGGfdVTLDGALGELTDWKPGTGGEYEYARVDLGTGAHTV---ESDGPFGVTVYG 292
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 806-969 7.19e-42

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: 151.40  E-value: 7.19e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   806 CYPTSYA-TCSASGDPHYITFDGLKFDFQGTCVYQFTGLCekrTDLVDFLVLVQNDHRGSQAvSFTRDVEIYVYETSIVI 884
Cdd:smart00216    3 CTQEECSpTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGA-TCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   885 SRRNpAKVMVNGLLTNLPYYTESKRISIHRQGQEAVIETDFGL-TVTFDWQSRVTVTVPSTYANTLCGLCGNFNGNKQDE 963
Cdd:smart00216   79 KDDN-GKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 2117997536   964 LTMKNG 969
Cdd:smart00216  158 FRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 422-577 6.76e-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: 142.51  E-value: 6.76e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  422 CWAQGDPHYYTFDGRKFDFMGTCTYIIARTCGQDvSLPSFSIVAKNENRGNPHVsYIALVTATIYNVTISVARyeVGFVR 501
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEE-PDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2117997536  502 VNNQRTRLPISLNDGKLRLYQ-YGGSAFIETDFSLRVSYDWNSYLVVKISSSFWESVCGLCGNYNGDPTDDFRTPEG 577
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGsGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 814-970 7.52e-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: 7.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  814 CSASGDPHYITFDGLKFDFQGTCVYQFTGLCEKRTDLVdFLVLVQNDHRGSQAVsFTRDVEIYVYETSIVISRRNpaKVM 893
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGG--TVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536  894 VNGLLTNLPYYTESKRISIHRQGQeAVIETDFGLTVTFDWQSR--VTVTVPSTYANTLCGLCGNFNGNKQDELTMKNGT 970
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGF-VVVDLSPGVGLQVDGDGRgqLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 412-577 1.32e-37

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 139.07  E-value: 1.32e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   412 PVCVPESE-STCWAQGDPHYYTFDGRKFDFMGTCTYIIARTCGqdvSLPSFSIVAKNENRGnPHVSYIALVTATIYNVTI 490
Cdd:smart00216    1 WCCTQEECsPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS---SEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   491 SVArYEVGFVRVNNQRTRLPISLNDGKLRLYQYGGSAFIETDFSL-RVSYDWNSYLVVKISSSFWESVCGLCGNYNGDPT 569
Cdd:smart00216   77 ELK-DDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 2117997536   570 DDFRTPEG 577
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1200-1356 1.35e-36

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 135.96  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536 1200 CSASGDPHYLSFDGLAFDFQGTCTYTLAKaNGDNQTLVPFVVNVENEPWGNGQVSVtKMVSVKIYGITLTLlqKKKGQVK 1279
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAK-DCSEEPDFSFSVTNKNCNGGASGVCL-KSVTVIVGDLEITL--QKGGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2117997536 1280 VNGISQSLPVSFSTGMVTVTQQGSNIVI-KADIGLIVNYDLFYSVKVMVPSTYQGRMQGLCGNYNGQKEDEFLLPDGT 1356
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1198-1355 4.01e-36

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: 134.84  E-value: 4.01e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  1198 ATCSASGDPHYLSFDGLAFDFQGTCTYTLAKANGDNQTlvpFVVNVENEPWGnGQVSVTKMVSVKIYGITLtLLQKKKGQ 1277
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT---FSVLLKNVPCG-GGATCLKSVKVELNGDEI-ELKDDNGK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536  1278 VKVNGISQSLPVSFSTGMVTVTQQGSNIVIKADIGLI-VNYDLFYSVKVMVPSTYQGRMQGLCGNYNGQKEDEFLLPDG 1355
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1399-1473 2.92e-30

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 114.75  E-value: 2.92e-30
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536  1399 FKQRNYCGILTASDGPFRACHSKVDPSVYFDNCVYDVCLGNGESLILCQSIQSYVSACQEAGVSVEPWRNPSFCP 1473
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1404-1472 4.48e-26

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: 102.46  E-value: 4.48e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536 1404 YCGILTASdGPFRACHSKVDPSVYFDNCVYDVCLGNGESLILCQSIQSYVSACQEAGVSVEPWRNPSFC 1472
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 617-692 8.89e-23

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: 93.56  E-value: 8.89e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536   617 KYKDEPFCGWISKvGDGPFSQCHSVVDPSIFLENCVYDLCLNDGLKHVLCEALKNYAEACQKEGAAVSDWRSLTGC 692
Cdd:smart00832    1 KYYACSQCGILLS-PRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 623-692 1.99e-22

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 92.06  E-value: 1.99e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  623 FCGWISKvgDGPFSQCHSVVDPSIFLENCVYDLCLNDGLKHVLCEALKNYAEACQKEGAAVSDWRSLTGC 692
Cdd:pfam08742    1 KCGLLSD--SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1013-1082 1.36e-17

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: 78.54  E-value: 1.36e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  1013 KECGLILAKDGPFRECHSKIDPEGYFQDCVYDYCFFEGQQTVICQLISSYAAACQAAGAVLYEWRSDTFC 1082
Cdd:smart00832    6 SQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1086-1139 1.88e-16

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 74.66  E-value: 1.88e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1086 CTPNSHYELCAQGCPQTCSSLYAPAPCPAQCREGCVCNEDFVLS-GDQCVPLSQC 1139
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1086-1139 2.15e-16

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 74.73  E-value: 2.15e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1086 CTPNSHYELCAQGCPQTCSSLYAPAPCPAQCREGCVCNEDFVLS-GDQCVPLSQC 1139
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 696-750 1.69e-15

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: 71.96  E-value: 1.69e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  696 CPENSHYEACGPPCPTTCNAQAGPQNCsTLPCVETCQCNGGFVLDA-GRCVPESAC 750
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1015-1082 6.84e-15

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: 70.87  E-value: 6.84e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2117997536 1015 CGLILaKDGPFRECHSKIDPEGYFQDCVYDYCFFEGQQTVICQLISSYAAACQAAGAVLYEWRSDTFC 1082
Cdd:pfam08742    2 CGLLS-DSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1476-1529 8.12e-14

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: 67.41  E-value: 8.12e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1476 CPANSHYQLCADLCSTSCAKITDPQPCPETCTEGCQCDDGFFFDGLG-CVRAESC 1529
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1476-1529 9.50e-14

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: 66.96  E-value: 9.50e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1476 CPANSHYQLCADLCSTSCAKITDPQPCPETCTEGCQCDDGFFFDGLG-CVRAESC 1529
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 696-750 1.25e-13

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 66.64  E-value: 1.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  696 CPENSHYEACGPPCPTTCNAQAGPQNCsTLPCVETCQCNGGFVLDA-GRCVPESAC 750
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRNSgGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1144-1193 6.71e-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: 47.68  E-value: 6.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2117997536 1144 QGQYYLAGET-FYPTCQERCVCqAGGTVQCMAFSCGPHEECRLLDGIQKCY 1193
Cdd:pfam12714    5 QGNYIPAGKTwFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 752-807 5.43e-06

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 44.99  E-value: 5.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  752 CLFEGKLYSPGEQfWGDAACTKRCTCdaETKQVTCQATGCKSGEQCRVEDGIQNCY 807
Cdd:pfam12714    2 KDAQGNYIPAGKT-WFSSGCTQSCTC--TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC smart00214
von Willebrand factor (vWF) type C domain;
1141-1183 2.58e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.50  E-value: 2.58e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2117997536  1141 CIHQGQYYLAGETFYPTCQERCVCQAGGTVQCMAFSCGPHEEC 1183
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTTVLCDPVECPPPPDC 43
 
Name Accession Description Interval E-value
IgGFc_binding pfam17517
IgGFc binding protein; This domain is found at the N terminal of Swiss:Q9Y6R7 and has been ...
 82-372 2.44e-68

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


Pssm-ID: 465430  Cd Length: 292  Bit Score: 232.24  E-value: 2.44e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   82 ATTAVYPVQQLGKEYYAITPMGDRANTFKEFAILAYTFPTRVDVHLKGSVIFKGQVYpAGSRLVVDLDSFQAIQLQSSVD 161
Cdd:pfam17517    1 DATLLLPVSSLGTEYYVVSWDPTPGSGPSYFQIVATEDNTTVTITPTVDVTGGGGVY-AGSPFTITLNRGEVLQLQSDGD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  162 LSGSRIESKEPVAVLSGHSCA---WKFTSCDHVVEQLLPVSSWGNTSIVPPL-PFYSRLDTLY--IIASKVTCIKIQsGN 235
Cdd:pfam17517   80 LTGSRITSDKPVAVFSGHSCAnvpSGGGACDHLVEQLPPVSSWGKEYVVVPFrRGNGDEQSIYriVAAEDNTTVTVN-GA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  236 NHNSHNVVAGQVLKLDeqLSHPIYVSADAGIQIIFFFPGSTRENEVYDPFMINIPALTSYCMSYHIDGMAHFHNYAVLIA 315
Cdd:pfam17517  159 AGAPATLNAGEVYEFS--TDAPFYVKSSKPIYVAQYMTGGSSDGGTGDPEMVLVPPVEQYLNSYVFFTDPTYPNNYLVIV 236

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536  316 NTSESSG--ITIQKEAIMNVQWKPVQGTQYSWGDYSLGTEATSLsvqHPSTPFGLLVLG 372
Cdd:pfam17517  237 RTKSTGGfdVTLDGALGELTDWKPGTGGEYEYARVDLGTGAHTV---ESDGPFGVTVYG 292
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 806-969 7.19e-42

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: 151.40  E-value: 7.19e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   806 CYPTSYA-TCSASGDPHYITFDGLKFDFQGTCVYQFTGLCekrTDLVDFLVLVQNDHRGSQAvSFTRDVEIYVYETSIVI 884
Cdd:smart00216    3 CTQEECSpTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGA-TCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   885 SRRNpAKVMVNGLLTNLPYYTESKRISIHRQGQEAVIETDFGL-TVTFDWQSRVTVTVPSTYANTLCGLCGNFNGNKQDE 963
Cdd:smart00216   79 KDDN-GKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157


                    ....*.
gi 2117997536   964 LTMKNG 969
Cdd:smart00216  158 FRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 422-577 6.76e-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: 142.51  E-value: 6.76e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  422 CWAQGDPHYYTFDGRKFDFMGTCTYIIARTCGQDvSLPSFSIVAKNENRGNPHVsYIALVTATIYNVTISVARyeVGFVR 501
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEE-PDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2117997536  502 VNNQRTRLPISLNDGKLRLYQ-YGGSAFIETDFSLRVSYDWNSYLVVKISSSFWESVCGLCGNYNGDPTDDFRTPEG 577
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGsGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 814-970 7.52e-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: 7.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  814 CSASGDPHYITFDGLKFDFQGTCVYQFTGLCEKRTDLVdFLVLVQNDHRGSQAVsFTRDVEIYVYETSIVISRRNpaKVM 893
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGG--TVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536  894 VNGLLTNLPYYTESKRISIHRQGQeAVIETDFGLTVTFDWQSR--VTVTVPSTYANTLCGLCGNFNGNKQDELTMKNGT 970
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGF-VVVDLSPGVGLQVDGDGRgqLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 412-577 1.32e-37

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 139.07  E-value: 1.32e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   412 PVCVPESE-STCWAQGDPHYYTFDGRKFDFMGTCTYIIARTCGqdvSLPSFSIVAKNENRGnPHVSYIALVTATIYNVTI 490
Cdd:smart00216    1 WCCTQEECsPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS---SEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEI 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536   491 SVArYEVGFVRVNNQRTRLPISLNDGKLRLYQYGGSAFIETDFSL-RVSYDWNSYLVVKISSSFWESVCGLCGNYNGDPT 569
Cdd:smart00216   77 ELK-DDNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155


                    ....*...
gi 2117997536   570 DDFRTPEG 577
Cdd:smart00216  156 DDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1200-1356 1.35e-36

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 135.96  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536 1200 CSASGDPHYLSFDGLAFDFQGTCTYTLAKaNGDNQTLVPFVVNVENEPWGNGQVSVtKMVSVKIYGITLTLlqKKKGQVK 1279
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAK-DCSEEPDFSFSVTNKNCNGGASGVCL-KSVTVIVGDLEITL--QKGGTVL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2117997536 1280 VNGISQSLPVSFSTGMVTVTQQGSNIVI-KADIGLIVNYDLFYSVKVMVPSTYQGRMQGLCGNYNGQKEDEFLLPDGT 1356
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFVVVDlSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1198-1355 4.01e-36

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: 134.84  E-value: 4.01e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  1198 ATCSASGDPHYLSFDGLAFDFQGTCTYTLAKANGDNQTlvpFVVNVENEPWGnGQVSVTKMVSVKIYGITLtLLQKKKGQ 1277
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT---FSVLLKNVPCG-GGATCLKSVKVELNGDEI-ELKDDNGK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536  1278 VKVNGISQSLPVSFSTGMVTVTQQGSNIVIKADIGLI-VNYDLFYSVKVMVPSTYQGRMQGLCGNYNGQKEDEFLLPDG 1355
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1399-1473 2.92e-30

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 114.75  E-value: 2.92e-30
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536  1399 FKQRNYCGILTASDGPFRACHSKVDPSVYFDNCVYDVCLGNGESLILCQSIQSYVSACQEAGVSVEPWRNPSFCP 1473
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1404-1472 4.48e-26

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: 102.46  E-value: 4.48e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2117997536 1404 YCGILTASdGPFRACHSKVDPSVYFDNCVYDVCLGNGESLILCQSIQSYVSACQEAGVSVEPWRNPSFC 1472
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 617-692 8.89e-23

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: 93.56  E-value: 8.89e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536   617 KYKDEPFCGWISKvGDGPFSQCHSVVDPSIFLENCVYDLCLNDGLKHVLCEALKNYAEACQKEGAAVSDWRSLTGC 692
Cdd:smart00832    1 KYYACSQCGILLS-PRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 623-692 1.99e-22

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 92.06  E-value: 1.99e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  623 FCGWISKvgDGPFSQCHSVVDPSIFLENCVYDLCLNDGLKHVLCEALKNYAEACQKEGAAVSDWRSLTGC 692
Cdd:pfam08742    1 KCGLLSD--SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1013-1082 1.36e-17

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: 78.54  E-value: 1.36e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117997536  1013 KECGLILAKDGPFRECHSKIDPEGYFQDCVYDYCFFEGQQTVICQLISSYAAACQAAGAVLYEWRSDTFC 1082
Cdd:smart00832    6 SQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1086-1139 1.88e-16

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 74.66  E-value: 1.88e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1086 CTPNSHYELCAQGCPQTCSSLYAPAPCPAQCREGCVCNEDFVLS-GDQCVPLSQC 1139
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1086-1139 2.15e-16

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 74.73  E-value: 2.15e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1086 CTPNSHYELCAQGCPQTCSSLYAPAPCPAQCREGCVCNEDFVLS-GDQCVPLSQC 1139
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 696-750 1.69e-15

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: 71.96  E-value: 1.69e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  696 CPENSHYEACGPPCPTTCNAQAGPQNCsTLPCVETCQCNGGFVLDA-GRCVPESAC 750
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1015-1082 6.84e-15

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: 70.87  E-value: 6.84e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2117997536 1015 CGLILaKDGPFRECHSKIDPEGYFQDCVYDYCFFEGQQTVICQLISSYAAACQAAGAVLYEWRSDTFC 1082
Cdd:pfam08742    2 CGLLS-DSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1476-1529 8.12e-14

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: 67.41  E-value: 8.12e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1476 CPANSHYQLCADLCSTSCAKITDPQPCPETCTEGCQCDDGFFFDGLG-CVRAESC 1529
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1476-1529 9.50e-14

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: 66.96  E-value: 9.50e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2117997536 1476 CPANSHYQLCADLCSTSCAKITDPQPCPETCTEGCQCDDGFFFDGLG-CVRAESC 1529
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 696-750 1.25e-13

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 66.64  E-value: 1.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  696 CPENSHYEACGPPCPTTCNAQAGPQNCsTLPCVETCQCNGGFVLDA-GRCVPESAC 750
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-PEPCVEGCVCPPGFVRNSgGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1144-1193 6.71e-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: 47.68  E-value: 6.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2117997536 1144 QGQYYLAGET-FYPTCQERCVCqAGGTVQCMAFSCGPHEECRLLDGIQKCY 1193
Cdd:pfam12714    5 QGNYIPAGKTwFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 752-807 5.43e-06

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 44.99  E-value: 5.43e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2117997536  752 CLFEGKLYSPGEQfWGDAACTKRCTCdaETKQVTCQATGCKSGEQCRVEDGIQNCY 807
Cdd:pfam12714    2 KDAQGNYIPAGKT-WFSSGCTQSCTC--TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC smart00214
von Willebrand factor (vWF) type C domain;
1141-1183 2.58e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 37.50  E-value: 2.58e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2117997536  1141 CIHQGQYYLAGETFYPTCQERCVCQAGGTVQCMAFSCGPHEEC 1183
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGTTVLCDPVECPPPPDC 43
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 217-250 8.92e-03

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 35.45  E-value: 8.92e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2117997536  217 DTLYIIASK--VTCIKIQSGNNHNSHNVVAGQVLKL 250
Cdd:pfam01476    7 DTLSSIAKRygITVEQLAELNGLSSPNLYVGQKLKI 42
 
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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