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Conserved domains on  [gi|2119003705|ref|XP_043926711|]
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IgGFc-binding protein-like [Protopterus annectens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
2608-2761 1.21e-54

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


:

Pssm-ID: 99706  Cd Length: 157  Bit Score: 189.51  E-value: 1.21e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2608 CDFDTDFCEWEQSTTDSFDWQRNRGPTPSLNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPSCPA-YGPHCFRFWYH 2686
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSFWYH 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 2687 MYGvAQNMALKVYLVEKGSPFLK--WVQTGNQGNKWRPVEVDLQ-LKGNFQIIIEGVRGSDYRSDVAVDDVTFNAGCC 2761
Cdd:cd06263     81 MYG-SGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
3833-3986 1.48e-54

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


:

Pssm-ID: 99706  Cd Length: 157  Bit Score: 189.13  E-value: 1.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3833 CDFDTDFCEWEQSTTDSFDWQRNSGPTPSLNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPSCPA-YGPHCFRFWYH 3911
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSFWYH 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 3912 MYGvAQNMALKVYLVEKGAAFLK--WVQTGNQGNKWRPVEVDLQ-LKGNFQIIIEGVRGSDYRSDVAVDDVTFSAGCC 3986
Cdd:cd06263     81 MYG-SGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
1340-1497 1.72e-51

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


:

Pssm-ID: 99706  Cd Length: 157  Bit Score: 180.27  E-value: 1.72e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1340 CDFDIDYCGWAQSSSDSFDWLRYKGPTPSLNTGPPYDHTSAEeevdGYYVYIEGDFAKPGDVAHLLSPSCPA-YGPHCFR 1418
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGS----GHYLYVESSSGREGQKARLLSPLLPPpRSSHCLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1419 FWYHMYGvAQNMALKLYLVQKGVPV--LMWSQTGNQGNKWRLVEVELQ-LRGSFQIIIEGVRGSDYRSDVAVDDITFKAG 1495
Cdd:cd06263     77 FWYHMYG-SGVGTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPG 155

                   ..
gi 2119003705 1496 CC 1497
Cdd:cd06263    156 PC 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
5700-5854 7.66e-40

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: 147.13  E-value: 7.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5700 CTASGDPHYNTFDGRVHHFMGNCTYVLTKLCNESSgLPLFEVTTTNEHRGSNTKvsYVNSVHVNVYGNSISLLKNKKVNV 5779
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP-DFSFSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 5780 NGKRVNPPYSI-KDQIKVYFSGN-YLYLETDFRLVVRFDGNHYVDVSVSRNFNGLLCGMCGNSNGNPKDDIIKPDGT 5854
Cdd:pfam00094   78 NGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2790-2943 2.08e-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: 145.59  E-value: 2.08e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2790 CSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCDvNSSLPYFNVEAANENRGGNThvSYVKSVTVDVYSYRIILEKSKVVKV 2869
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 2870 NGQVQLFPLTlSPGVNIIISGQYVMLTS---DFGLRVKYDGNHRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 2943
Cdd:pfam00094   78 NGQKVSLPYK-SDGGEVEILGSGFVVVDlspGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4022-4175 2.91e-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: 145.21  E-value: 2.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4022 CSVHSDPHYHTFDGQPHTFMGTCTYTLSKLCDViSTLPYFNVEAANEHRGGNThvSYVKSVTVDVYSHRIILEKNKVVKI 4101
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 4102 NGQVQLLPLTlSPGVNIIISGQYVMLTS---DFGLRVKYDGNQRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 4175
Cdd:pfam00094   78 NGQKVSLPYK-SDGGEVEILGSGFVVVDlspGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4795-4945 2.53e-38

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: 2.53e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4795 CDIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSNY-FTITTRNEHRGNPSWtAINSVALNVNGVHIVLRKNKIVYVNG 4873
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4874 IPVTLPTSPMpGVAISLNGAY-VLVQTNFGLHLKFNGDQKLLVNVT--ERYKGQLCGLCGTYNGDQKDDFMRPDG 4945
Cdd:pfam00094   80 QKVSLPYKSD-GGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTlsPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
271-425 9.71e-38

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: 140.97  E-value: 9.71e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  271 CSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCDvNSTLPYFNVEAANENRGGNThvSYVKSVTVDVYSYRIILEKNKVVKV 350
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  351 NGiaQLIPLPLTPD---VTITQSGQ-YAMVMTSFGLRVKYDGNQRAEVTLPSTFQGKVCGMCGNYNSIRNDDFLNPDGK 425
Cdd:pfam00094   78 NG--QKVSLPYKSDggeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
6085-6238 4.94e-37

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: 139.04  E-value: 4.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 6085 CHVAGDPHYFTFDKVMHTFIGTCTYVLVQVCdkSNVIDLKVSG--KNEQRGLPfSSYLKEVYIDVYNTRITIQRSKALLL 6162
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDC--SEEPDFSFSVtnKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 6163 NGGRVHTPVENQIRGITINTNGI-YTIVETDFGMMVKFDGNHHLEISLPDSYFSKVCGLCGNYNMKKDDEFLMPSGQ 6238
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4408-4564 4.94e-37

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: 139.04  E-value: 4.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4408 CRVWGDPHYSTFDKETHHFMGNCTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKkeASRVL 4487
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 4488 IDDIWTNLPASLVKGAVTVDRSG-SYVLLETDFLLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNNLRADDFMKPDGS 4564
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3562-3713 8.83e-37

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: 138.27  E-value: 8.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3562 CHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSD-HFTVTTRNEHRGNPtWTAINSVALTVNGVHIALRKNRIVYVND 3640
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDfSFSVTNKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3641 ILVTLP-TSPIPDVTISLSG-AYVLVQTSFGLRLQFSGDHELLVNVTERYKGKLCGLCGTYTGKQQDDFMRPDGV 3713
Cdd:pfam00094   80 QKVSLPyKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3176-3332 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: 137.89  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3176 CRVWGDPHYSTFDKETHHFMGICTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKRETsrVL 3255
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGT--VL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 3256 VDNTWRTLPVTLVGGAVTVKRSGN-YVLLETDFLLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNKLRADDFMKPDGS 3332
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1060-1220 2.56e-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: 137.15  E-value: 2.56e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1060 WGC-HVANAAMCHIYGDPHYITFDGKLYHFQGACNYSVTQTCRNSAvNFSVTSRNEHRGSpKWSALNSVAFTISGLHIIL 1138
Cdd:smart00216    1 WCCtQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP-TFSVLLKNVPCGG-GATCLKSVKVELNGDEIEL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1139 KK-NNKVSVNGVNISLPYN-NGHGILVSKDGPYLVLQTHFGL-KLKYNGDHELFVHVNENFKGQLCGLCGTYNDDQLDDF 1215
Cdd:smart00216   79 KDdNGKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158

                    ....*
gi 2119003705  1216 TRPDG 1220
Cdd:smart00216  159 RTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
684-840 1.03e-35

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 135.19  E-value: 1.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  684 CRVHNDPHYNTFDKETHHFMGTCTYTVAKVCANTTSlPYFNIETKNEHRGNPSVsYVQKVHVDVYGHRVSIIKkePSRVL 763
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  764 VDGvwQKLSVSLADGALLVRQSGRY---VQLETDFGLSVSYDTDHSVEVKVPSTYFNLTCGMCGNFNNLRKDDFMMPNGT 840
Cdd:pfam00094   77 VNG--QKVSLPYKSDGGEVEILGSGfvvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
108-267 1.62e-35

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


:

Pssm-ID: 99706  Cd Length: 157  Bit Score: 134.81  E-value: 1.62e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  108 CDFNnnyQPFCDWVQpCDGDDGDWIRTKHATPTPETGPIGDYPGGNGYFIYQEASNFIPLGTNRLESPSL-GVLGDICIE 186
Cdd:cd06263      1 CDFE---DGLCGWTQ-DSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLpPPRSSHCLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  187 FWYHMLGSeNHNKLKVIIKDNA--TEAVIWSRTGNQSSFWLNASVPVTiSVEKHIKVIFEAVRGWTEYGDTAVDNVAVQK 264
Cdd:cd06263     77 FWYHMYGS-GVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLS-ASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154

                   ...
gi 2119003705  265 GPC 267
Cdd:cd06263    155 GPC 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1945-2106 2.20e-35

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: 134.42  E-value: 2.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1945 CRVWGDPHYSTFDKETHHFMGICTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKNQRTLlh 2024
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2025 lgsymVDNIWRTLPVTLVGGAVTVKRSG-SYVLLETDFLLSVYYDSDHTADVKVPSTYFNQTCGICGNYNNLRADDFMKP 2103
Cdd:pfam00094   77 -----VNGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151

                   ...
gi 2119003705 2104 DGS 2106
Cdd:pfam00094  152 DGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2337-2487 2.42e-35

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: 134.04  E-value: 2.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2337 CHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSD-HFTVTTRNEHRGNPtWTAINSVALTVNGVHIALRKNRIVYVND 2415
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDfSFSVTNKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 2416 ILVTLP-TSPIPDVTISLSGaYVLVQTSFGLHLRFSGDHELLVNVT--ERYKGELCGLCGTYTGKQQDDFMRPDG 2487
Cdd:pfam00094   80 QKVSLPyKSDGGEVEILGSG-FVVVDLSPGVGLQVDGDGRGQLFVTlsPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
6377-6532 1.99e-30

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 120.17  E-value: 1.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 6377 CAITGDPHYLTFDGLSHHFQGKYTYItaasLTDIPNTLQEFSIQGKNEPMQTNNKITYLKEISTHVYGHVVQFKQKKNVV 6456
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYV----LAKDCSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 6457 LDGEKIKPPAQPHDG-LRIFQKAT-RVYLETDFGLSVSFDGSENADITLPNTYKAKVGGLCGNFDGKYKNDFTKPDGT 6532
Cdd:pfam00094   77 VNGQKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
877-952 1.22e-29

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: 1.22e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705   877 LYEGNDYCGIITKADGHFAVCHSVVNPSSFFDSCVFDLCALNGDRQRLCNALETYAHACQSAGVSIPPWRNETFCP 952
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4601-4676 1.18e-28

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: 112.05  E-value: 1.18e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  4601 KYESSSYCGLITSKEGPFANCLHVVSPNSFFDSCVFDLCALNGSQDALCDSLQSYAVACQKAGVIIPPWRNSTFCP 4676
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1528-1713 1.82e-28

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: 114.39  E-value: 1.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1528 CSVHSDPHYHTFDGLAHTYMGNCSHLLSTICANSTLPyyEVAAANEFRGGNTHVSYVKSVSIDVNSYSIVLDKGKVVKda 1607
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF--SFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1608 rshmeiqnmpenhklkktkperrkcecsseVNGKVQQLPVTL-KSDINITFSGQ-YVMVSTDFGLRVKYDGNHRVEVTLP 1685
Cdd:pfam00094   77 ------------------------------VNGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLS 126
                          170       180
                   ....*....|....*....|....*...
gi 2119003705 1686 SKFKGNVFGMCGNYDGNKTDDLLNCEGK 1713
Cdd:pfam00094  127 PSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3369-3444 2.98e-28

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: 110.89  E-value: 2.98e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  3369 KYESSSYCGLITSKEGPFANCLHVVSPNSFFESCVFDLCALNGSQDTLCDSLQSYADACQKAGVIIPPWKNSTFCP 3444
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2143-2217 2.36e-27

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: 108.20  E-value: 2.36e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2143 KYESSSYCGLITSKEGPFANCLHVVGPDSFFESCVFDLCALNGSQTALCDSLQSYADACQKAGVIVPPWRNSTFC 2217
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4215-4288 6.88e-27

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: 107.04  E-value: 6.88e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705  4215 ESNSYCGIITDTNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVTIETWRNQTFCP 4288
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2983-3056 1.59e-26

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: 105.89  E-value: 1.59e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705  2983 ESNSYCGIITDTNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVIIHPWRNQTFCP 3056
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
464-537 5.90e-26

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: 104.34  E-value: 5.90e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705   464 ESNSYCGIITDTNGPFRQCHSVIDPKDYFDDCAYDLCELNMDTGALCSNLQAYADACQSEGVTIRPWRNETFCA 537
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1752-1824 1.53e-25

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: 103.19  E-value: 1.53e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119003705  1752 QSNSYCGIITDTNGPFKQCHSVIDPKDYFNDCAYDLCALNMDTGALCSNLQAYADACQSKGVTIEPWRNQTFC 1824
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
5898-5965 1.49e-24

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: 100.49  E-value: 1.49e-24
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  5898 CGMIKDPTGVFKDCHAVIPPENFFENCVIDFCASSGDSVSLCYALQSYASMCAEAGICV-AWRNSTFCP 5965
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2525-2599 7.51e-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: 95.49  E-value: 7.51e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2525 EQAAAEHCKIVLDSNGPFAECHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYVAACEEAGVDLGDWRKDTVC 2599
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3750-3824 1.08e-22

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: 95.10  E-value: 1.08e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  3750 EQAAEEHCRIVLDSNGPFVNCHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYAAACEEAGVDLGDWRKDTVC 3824
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4983-5057 5.42e-22

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: 93.17  E-value: 5.42e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  4983 EQAATEHCRIVSDSNGPFAKCHGHISPELYFVSCVYDQCATNGSSEQLCNALESYAATCEEAGVDLGDWRKDTVC 5057
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1263-1331 2.96e-21

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: 90.52  E-value: 2.96e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 1263 QCQIIMaSNGPFGSCHWYIPPQLYFESCVFDFCATNGSLEYFCSALESYATACAAAGVHVGDWKKETFC 1331
Cdd:pfam08742    1 KCGLLS-DSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
6587-6658 2.32e-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: 88.55  E-value: 2.32e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119003705  6587 GTDYCGSLINPKGPFRACHNVFPPDAYLENCLYDLCAAFDNIALLCTNLEQYALTCQSEGVTLENWRKGTIC 6658
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
6283-6348 1.78e-19

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: 85.51  E-value: 1.78e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 6283 QCNVLLSN-AFVPCHSLVDPDLFIESCVYDMCKYDGKQSTLCDIVQAYVDICKNEGVTI-HWRNSTFC 6348
Cdd:pfam08742    1 KCGLLSDSgPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
1828-1881 1.17e-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: 76.97  E-value: 1.17e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 1828 CKPKSHYKQCGPACPATCANPNAPSSCSLPCVEGCICDSGYML-YHDQCVPSTQC 1881
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
3059-3112 1.70e-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: 76.59  E-value: 1.70e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3059 CKPNSHYEHCGHACPATCANPNSPSSCSLPCVEGCICNSGYML-YHDQCVPSTQC 3112
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
4291-4344 3.56e-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: 75.82  E-value: 3.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4291 CKPNSHYEQCGSACPATCMNPNAPSTCSLPCVESCVCDSGYML-YHDRCVPNTQC 4344
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
567-620 5.26e-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: 75.43  E-value: 5.26e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  567 CKPNTHYQQCGPACPATCTNPNAPSSCSLPCVEDCVCDSGYLL-YHDRCVPSTQC 620
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
955-1008 1.41e-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: 73.89  E-value: 1.41e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  955 CPSNSHYNVCGSACPATCTDMSAPNNCSKPCVEGCHCDHEFVLS-GQTCVSVHDC 1008
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
3447-3500 1.85e-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: 70.81  E-value: 1.85e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3447 CPDNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDTGFVLS-GSTCVNVADC 3500
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
5968-6021 3.89e-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: 70.04  E-value: 3.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 5968 CPAGSHYENCATGCPATCANTSPPSSCNASPAEGCICDDGYILS-GNKCVQQSDC 6021
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
6662-6715 5.86e-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: 69.27  E-value: 5.86e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 6662 CPLNSKYDMCTSACPATCGDLTAPSECDLPCLEGCECLPGYVMS-GFDCVPYKEC 6715
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
2224-2275 2.74e-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: 67.34  E-value: 2.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 2224 PNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDSGFVLS-GNTCVNVADC 2275
Cdd:cd19941      3 PNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
4682-4733 4.25e-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: 66.96  E-value: 4.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4682 PNSHYEPCSSACPATCLDQFAPLNCSKPCVEACECDSGFVLS-GSTCVNVADC 4733
Cdd:cd19941      3 PNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
6023-6078 5.13e-10

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: 58.08  E-value: 5.13e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705 6023 CVDGDNNYYTVGESWYSyDNCTERCTCnSNNNITCQQWECGLLESCKIQDGVLGCY 6078
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
6717-6770 3.05e-05

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: 44.60  E-value: 3.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 6717 CMYENKYYEVGEHFITEDCSQSCVCTeSSSVSCEKNQCKLEELCATSNFVRGCY 6770
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
3114-3169 5.71e-05

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: 43.83  E-value: 5.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705 3114 CWQDGKHYPVGsEFWTDDSCSTKCRCPsaGSKLECFPASCPTGHYCGIKNGVPGCY 3169
Cdd:pfam12714    2 KDAQGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 super family cl31530
BDLF3; Provisional
5173-5374 1.14e-04

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 47.59  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5173 TTSVDNVINTPHITSVTLQTSTHAASPSTSSPSGETKTTTKAPVTdiftsatsPSTSPSTSIPPVITSGigktTAKPDIE 5252
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT--------TTAILSTNTTTVTSTG----TTVTPVP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5253 TTSADNVINTphITSVTLQTSTHAaspstsspsgETKTTTKAPVTDiftsatspstspstsippiitsgiGKTTAKPdiE 5332
Cdd:PHA03255    93 TTSNASTINV--TTKVTAQNITAT----------EAGTGTSTGVTS------------------------NVTTRSS--S 134
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2119003705 5333 TTSAdniinTPHITLVTlqtsTHAPSPST-SPSGETKTTTKAP 5374
Cdd:PHA03255   135 TTSA-----TTRITNAT----TLAPTLSSkGTSNATKTTAELP 168
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
4735-4788 1.18e-04

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: 43.06  E-value: 1.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 4735 CWYQGKYYEKNEITMTENCEQQCKCLGNNdMHCTPTSCEPDKICKVKDGVLDCV 4788
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
2277-2330 6.41e-04

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: 41.14  E-value: 6.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 2277 CWYQGKYYEKHEDTMTENCEQQCQCSGNNdMNCTPTSCEPDKICKVEDGTLGCF 2330
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
3502-3555 6.41e-04

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: 41.14  E-value: 6.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 3502 CWYQGKYYEKHEDTMTENCEQQCQCSGNNdMNCTPTSCEPDKICKVEDGTLGCF 3555
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
4349-4401 1.06e-03

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 40.36  E-value: 1.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4349 DGKHYPVGsEFWTDDSCSTKCSCPsrGGQLACVNASCPKDHYCGINNGVPGCY 4401
Cdd:pfam12714    5 QGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
622-677 1.46e-03

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 39.98  E-value: 1.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  622 CWQDGKHYPVGsEFWTDDSCSTKCSCPsrGSQLVCVNASCPKDHYCGINNGVPGCY 677
Cdd:pfam12714    2 KDAQGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 super family cl31530
BDLF3; Provisional
5571-5706 2.11e-03

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 43.74  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5571 TTSADNIINTPHITSVTLQTSTHAASPSASSQSGETKTTTKAPVTdifTSATSPSISPSTSIPPiitsgigktTAKPDIE 5650
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT---TTAILSTNTTTVTSTG---------TTVTPVP 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119003705 5651 TTSADNVINTphITSVTLQTSTHA------ASPSTSSQSGETKTTTKAPVTDHHVCTASGDP 5706
Cdd:PHA03255    93 TTSNASTINV--TTKVTAQNITATeagtgtSTGVTSNVTTRSSSTTSATTRITNATTLAPTL 152
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
1013-1063 9.79e-03

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 37.67  E-value: 9.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2119003705 1013 NGKYHEKGHTFWEENCEHKCTCYGNNhLNCTAAKCESNEICKVQNGEWGCH 1063
Cdd:pfam12714    5 QGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
2608-2761 1.21e-54

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 189.51  E-value: 1.21e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2608 CDFDTDFCEWEQSTTDSFDWQRNRGPTPSLNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPSCPA-YGPHCFRFWYH 2686
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSFWYH 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 2687 MYGvAQNMALKVYLVEKGSPFLK--WVQTGNQGNKWRPVEVDLQ-LKGNFQIIIEGVRGSDYRSDVAVDDVTFNAGCC 2761
Cdd:cd06263     81 MYG-SGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
3833-3986 1.48e-54

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 189.13  E-value: 1.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3833 CDFDTDFCEWEQSTTDSFDWQRNSGPTPSLNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPSCPA-YGPHCFRFWYH 3911
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSFWYH 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 3912 MYGvAQNMALKVYLVEKGAAFLK--WVQTGNQGNKWRPVEVDLQ-LKGNFQIIIEGVRGSDYRSDVAVDDVTFSAGCC 3986
Cdd:cd06263     81 MYG-SGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
1340-1497 1.72e-51

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 180.27  E-value: 1.72e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1340 CDFDIDYCGWAQSSSDSFDWLRYKGPTPSLNTGPPYDHTSAEeevdGYYVYIEGDFAKPGDVAHLLSPSCPA-YGPHCFR 1418
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGS----GHYLYVESSSGREGQKARLLSPLLPPpRSSHCLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1419 FWYHMYGvAQNMALKLYLVQKGVPV--LMWSQTGNQGNKWRLVEVELQ-LRGSFQIIIEGVRGSDYRSDVAVDDITFKAG 1495
Cdd:cd06263     77 FWYHMYG-SGVGTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPG 155

                   ..
gi 2119003705 1496 CC 1497
Cdd:cd06263    156 PC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
2608-2762 5.48e-48

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 170.62  E-value: 5.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2608 CDFDTD-FCEWEQSTTDSFDWQRNRGPTPslNTGPPYDHT--SADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 2683
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTqgTGSGHFMYVDTSSGAPGQTARLLSPLlPPSRSPQCLRF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2684 WYHMYGVAQNmALKVYLVEKGSPF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFNAGC 2760
Cdd:pfam00629   79 WYHMSGSGVG-TLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISLSSGP 157

                   ..
gi 2119003705 2761 CS 2762
Cdd:pfam00629  158 CP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
3833-3987 1.72e-47

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 169.08  E-value: 1.72e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3833 CDFDTD-FCEWEQSTTDSFDWQRNSGPTPslNTGPPYDHT--SADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 3908
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTqgTGSGHFMYVDTSSGAPGQTARLLSPLlPPSRSPQCLRF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3909 WYHMYGVAQNmALKVYLVEKGAAF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFSAGC 3985
Cdd:pfam00629   79 WYHMSGSGVG-TLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISLSSGP 157

                   ..
gi 2119003705 3986 CS 3987
Cdd:pfam00629  158 CP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
1340-1498 3.73e-47

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 168.31  E-value: 3.73e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1340 CDFDIDY-CGWAQSSSDSFDWLRYKGPTPslNTGPPYDHTSAEEEvdGYYVYIEGDFAKPGDVAHLLSPS-CPAYGPHCF 1417
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGS--GHFMYVDTSSGAPGQTARLLSPLlPPSRSPQCL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1418 RFWYHMYGVAQNmALKLYLVQKGVPV--LMWSQTGNQGNKWRLVEVELQ-LRGSFQIIIEGVRGSDYRSDVAVDDITFKA 1494
Cdd:pfam00629   77 RFWYHMSGSGVG-TLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSsSTQPFQVVFEGIRGGGSRGGIALDDISLSS 155

                   ....
gi 2119003705 1495 GCCA 1498
Cdd:pfam00629  156 GPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
2606-2761 4.49e-41

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 150.96  E-value: 4.49e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2606 LGCDFDTD-FCEWEQSTTDSFDWQRNRGPTPslNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 2683
Cdd:smart00137    4 GNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPlYENRSTHCLTF 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2684 WYHMYGVAQNmALKVYLVEKGSPF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFNAGC 2760
Cdd:smart00137   82 WYYMYGSGSG-TLNVYVRENNGSQdtLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILLSNGP 160

                    .
gi 2119003705  2761 C 2761
Cdd:smart00137  161 C 161
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
3831-3986 7.57e-41

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 150.19  E-value: 7.57e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3831 LGCDFDTD-FCEWEQSTTDSFDWQRNSGPTPslNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 3908
Cdd:smart00137    4 GNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPlYENRSTHCLTF 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3909 WYHMYGVAQNmALKVYLVEKGAAF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFSAGC 3985
Cdd:smart00137   82 WYYMYGSGSG-TLNVYVRENNGSQdtLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILLSNGP 160

                    .
gi 2119003705  3986 C 3986
Cdd:smart00137  161 C 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
5700-5854 7.66e-40

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: 147.13  E-value: 7.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5700 CTASGDPHYNTFDGRVHHFMGNCTYVLTKLCNESSgLPLFEVTTTNEHRGSNTKvsYVNSVHVNVYGNSISLLKNKKVNV 5779
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP-DFSFSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 5780 NGKRVNPPYSI-KDQIKVYFSGN-YLYLETDFRLVVRFDGNHYVDVSVSRNFNGLLCGMCGNSNGNPKDDIIKPDGT 5854
Cdd:pfam00094   78 NGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2790-2943 2.08e-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: 145.59  E-value: 2.08e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2790 CSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCDvNSSLPYFNVEAANENRGGNThvSYVKSVTVDVYSYRIILEKSKVVKV 2869
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 2870 NGQVQLFPLTlSPGVNIIISGQYVMLTS---DFGLRVKYDGNHRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 2943
Cdd:pfam00094   78 NGQKVSLPYK-SDGGEVEILGSGFVVVDlspGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4022-4175 2.91e-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: 145.21  E-value: 2.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4022 CSVHSDPHYHTFDGQPHTFMGTCTYTLSKLCDViSTLPYFNVEAANEHRGGNThvSYVKSVTVDVYSHRIILEKNKVVKI 4101
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 4102 NGQVQLLPLTlSPGVNIIISGQYVMLTS---DFGLRVKYDGNQRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 4175
Cdd:pfam00094   78 NGQKVSLPYK-SDGGEVEILGSGFVVVDlspGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4795-4945 2.53e-38

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: 2.53e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4795 CDIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSNY-FTITTRNEHRGNPSWtAINSVALNVNGVHIVLRKNKIVYVNG 4873
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4874 IPVTLPTSPMpGVAISLNGAY-VLVQTNFGLHLKFNGDQKLLVNVT--ERYKGQLCGLCGTYNGDQKDDFMRPDG 4945
Cdd:pfam00094   80 QKVSLPYKSD-GGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTlsPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
271-425 9.71e-38

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: 140.97  E-value: 9.71e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  271 CSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCDvNSTLPYFNVEAANENRGGNThvSYVKSVTVDVYSYRIILEKNKVVKV 350
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  351 NGiaQLIPLPLTPD---VTITQSGQ-YAMVMTSFGLRVKYDGNQRAEVTLPSTFQGKVCGMCGNYNSIRNDDFLNPDGK 425
Cdd:pfam00094   78 NG--QKVSLPYKSDggeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
6085-6238 4.94e-37

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: 139.04  E-value: 4.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 6085 CHVAGDPHYFTFDKVMHTFIGTCTYVLVQVCdkSNVIDLKVSG--KNEQRGLPfSSYLKEVYIDVYNTRITIQRSKALLL 6162
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDC--SEEPDFSFSVtnKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 6163 NGGRVHTPVENQIRGITINTNGI-YTIVETDFGMMVKFDGNHHLEISLPDSYFSKVCGLCGNYNMKKDDEFLMPSGQ 6238
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4408-4564 4.94e-37

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: 139.04  E-value: 4.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4408 CRVWGDPHYSTFDKETHHFMGNCTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKkeASRVL 4487
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 4488 IDDIWTNLPASLVKGAVTVDRSG-SYVLLETDFLLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNNLRADDFMKPDGS 4564
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3562-3713 8.83e-37

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: 138.27  E-value: 8.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3562 CHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSD-HFTVTTRNEHRGNPtWTAINSVALTVNGVHIALRKNRIVYVND 3640
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDfSFSVTNKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3641 ILVTLP-TSPIPDVTISLSG-AYVLVQTSFGLRLQFSGDHELLVNVTERYKGKLCGLCGTYTGKQQDDFMRPDGV 3713
Cdd:pfam00094   80 QKVSLPyKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3176-3332 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: 137.89  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3176 CRVWGDPHYSTFDKETHHFMGICTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKRETsrVL 3255
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGT--VL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 3256 VDNTWRTLPVTLVGGAVTVKRSGN-YVLLETDFLLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNKLRADDFMKPDGS 3332
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1060-1220 2.56e-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: 137.15  E-value: 2.56e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1060 WGC-HVANAAMCHIYGDPHYITFDGKLYHFQGACNYSVTQTCRNSAvNFSVTSRNEHRGSpKWSALNSVAFTISGLHIIL 1138
Cdd:smart00216    1 WCCtQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP-TFSVLLKNVPCGG-GATCLKSVKVELNGDEIEL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1139 KK-NNKVSVNGVNISLPYN-NGHGILVSKDGPYLVLQTHFGL-KLKYNGDHELFVHVNENFKGQLCGLCGTYNDDQLDDF 1215
Cdd:smart00216   79 KDdNGKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158

                    ....*
gi 2119003705  1216 TRPDG 1220
Cdd:smart00216  159 RTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2787-2943 2.63e-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: 137.15  E-value: 2.63e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2787 ASTCSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCdvnSSLPYFNVEAANENRGGNthVSYVKSVTVDVYSYRIILEKS-K 2865
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDDnG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2866 VVKVNGQVQLFPLTLSPG-VNIIISGQYVMLTSDFGL-RVKYDGNHRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 2943
Cdd:smart00216   84 KVTVNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
265-424 4.36e-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: 136.76  E-value: 4.36e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   265 GPCESTCSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCdvnSTLPYFNVEAANENRGGNthVSYVKSVTVDVYSYRIILEK 344
Cdd:smart00216    6 EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   345 -NKVVKVNGiaQLIPLPLTPD---VTITQSGQYAMVMTSFGL-RVKYDGNQRAEVTLPSTFQGKVCGMCGNYNSIRNDDF 419
Cdd:smart00216   81 dNGKVTVNG--QQVSLPYKTSdgsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158

                    ....*
gi 2119003705   420 LNPDG 424
Cdd:smart00216  159 RTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
684-840 1.03e-35

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 135.19  E-value: 1.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  684 CRVHNDPHYNTFDKETHHFMGTCTYTVAKVCANTTSlPYFNIETKNEHRGNPSVsYVQKVHVDVYGHRVSIIKkePSRVL 763
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  764 VDGvwQKLSVSLADGALLVRQSGRY---VQLETDFGLSVSYDTDHSVEVKVPSTYFNLTCGMCGNFNNLRKDDFMMPNGT 840
Cdd:pfam00094   77 VNG--QKVSLPYKSDGGEVEILGSGfvvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
4020-4175 1.04e-35

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 135.61  E-value: 1.04e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4020 SICSVHSDPHYHTFDGQPHTFMGTCTYTLSKLCdviSTLPYFNVEAANEHRGGNthVSYVKSVTVDVYSHRIILEK-NKV 4098
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDdNGK 84
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  4099 VKINGQVQLLPLTLSPG-VNIIISGQYVMLTSDFGL-RVKYDGNQRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 4175
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
1338-1497 1.40e-35

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 135.16  E-value: 1.40e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1338 LECDFDIDY-CGWAQSSSDSFDWLRYKGPTPslNTGPPYDHTSAeeevDGYYVYIEGDFAKPGDVAHLLSPS-CPAYGPH 1415
Cdd:smart00137    4 GNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTG----NGHFMFFETSSGAEGQTARLLSPPlYENRSTH 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1416 CFRFWYHMYGVAQNmALKLYLVQKGVPVLM--WSQTGNQGNKWRLVEVELQL-RGSFQIIIEGVRGSDYRSDVAVDDITF 1492
Cdd:smart00137   78 CLTFWYYMYGSGSG-TLNVYVRENNGSQDTllWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDILL 156

                    ....*
gi 2119003705  1493 KAGCC 1497
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
108-267 1.62e-35

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 134.81  E-value: 1.62e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  108 CDFNnnyQPFCDWVQpCDGDDGDWIRTKHATPTPETGPIGDYPGGNGYFIYQEASNFIPLGTNRLESPSL-GVLGDICIE 186
Cdd:cd06263      1 CDFE---DGLCGWTQ-DSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLpPPRSSHCLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  187 FWYHMLGSeNHNKLKVIIKDNA--TEAVIWSRTGNQSSFWLNASVPVTiSVEKHIKVIFEAVRGWTEYGDTAVDNVAVQK 264
Cdd:cd06263     77 FWYHMYGS-GVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLS-ASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154

                   ...
gi 2119003705  265 GPC 267
Cdd:cd06263    155 GPC 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1945-2106 2.20e-35

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: 134.42  E-value: 2.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1945 CRVWGDPHYSTFDKETHHFMGICTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKNQRTLlh 2024
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2025 lgsymVDNIWRTLPVTLVGGAVTVKRSG-SYVLLETDFLLSVYYDSDHTADVKVPSTYFNQTCGICGNYNNLRADDFMKP 2103
Cdd:pfam00094   77 -----VNGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151

                   ...
gi 2119003705 2104 DGS 2106
Cdd:pfam00094  152 DGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2337-2487 2.42e-35

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: 134.04  E-value: 2.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2337 CHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSD-HFTVTTRNEHRGNPtWTAINSVALTVNGVHIALRKNRIVYVND 2415
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDfSFSVTNKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 2416 ILVTLP-TSPIPDVTISLSGaYVLVQTSFGLHLRFSGDHELLVNVT--ERYKGELCGLCGTYTGKQQDDFMRPDG 2487
Cdd:pfam00094   80 QKVSLPyKSDGGEVEILGSG-FVVVDLSPGVGLQVDGDGRGQLFVTlsPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1070-1221 3.86e-35

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.65  E-value: 3.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1070 CHIYGDPHYITFDGKLYHFQGACNYSVTQTC-RNSAVNFSVTSRNEHRGSPKWSaLNSVAFTISGLHIILKKNNKVSVNG 1148
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 1149 VNISLPY--NNGHGILVSKDGPYLVLQTHFGLKLKYNGDHELFVHVNENFKGQLCGLCGTYNDDQLDDFTRPDGV 1221
Cdd:pfam00094   80 QKVSLPYksDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
4793-4945 1.06e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.53  E-value: 1.06e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4793 AVCDIYGDPHYITFDGKLYHFQGSCNYTVTETCGnTSNYFTITTRNEHRGnPSWTAINSVALNVNGVHIVL-RKNKIVYV 4871
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS-SEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELkDDNGKVTV 87
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  4872 NGIPVTLP-TSPMPGVAISLNGAYVLVQTNFGLH-LKFNGDQKLLVNVTERYKGQLCGLCGTYNGDQKDDFMRPDG 4945
Cdd:smart00216   88 NGQQVSLPyKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
6085-6237 1.43e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.14  E-value: 1.43e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  6085 CHVAGDPHYFTFDKVMHTFIGTCTYVLVQVCDKSNviDLKVSGKNEQRGlPFSSYLKEVYIDVYNTRITIQRS-KALLLN 6163
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP--TFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDnGKVTVN 88
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  6164 GGRVHTPVENQIRGITINTNGIYTIVETDFGMM-VKFDGNHHLEISLPDSYFSKVCGLCGNYNMKKDDEFLMPSG 6237
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3561-3712 1.81e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.14  E-value: 1.81e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3561 VCHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSDhFTVTTRNEHRGnPTWTAINSVALTVNGVHIAL-RKNRIVYVN 3639
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCG-GGATCLKSVKVELNGDEIELkDDNGKVTVN 88
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  3640 DILVTLP-TSPIPDVTISLSGAYVLVQTSFGL-RLQFSGDHELLVNVTERYKGKLCGLCGTYTGKQQDDFMRPDG 3712
Cdd:smart00216   89 GQQVSLPyKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
4404-4563 2.07e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.76  E-value: 2.07e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4404 TYGICRVWGDPHYSTFDKETHHFMGNCTYTwakLCTNATSLPYFNVEAKNEHRGnPSVSYIQKIHVDVYGHRVTMVKKEA 4483
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYV---LAQDCSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4484 SrVLIDDIWTNLPASLVKGAVTVDRSGSYVLLETDF-LLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNNLRADDFMKPD 4562
Cdd:smart00216   84 K-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLgLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162

                    .
gi 2119003705  4563 G 4563
Cdd:smart00216  163 G 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
674-839 2.96e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.37  E-value: 2.96e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   674 PGCYPHTY-GICRVHNDPHYNTFDKETHHFMGTCTYTVAKVCantTSLPYFNIETKNEHRGnPSVSYVQKVHVDVYGHRV 752
Cdd:smart00216    1 WCCTQEECsPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEI 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   753 SIIKKEPSrVLVDGVWQKLSVSLADGALLVRQSGRYVQLETDFGL-SVSYDTDHSVEVKVPSTYFNLTCGMCGNFNNLRK 831
Cdd:smart00216   77 ELKDDNGK-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155

                    ....*...
gi 2119003705   832 DDFMMPNG 839
Cdd:smart00216  156 DDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
5699-5853 3.08e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.37  E-value: 3.08e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  5699 VCTASGDPHYNTFDGRVHHFMGNCTYVLTKLCNESsglPLFEVTTTNEHRGSNtkVSYVNSVHVNVYGNSISLLK-NKKV 5777
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDdNGKV 85
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705  5778 NVNGKRVNPPYSIKD-QIKVYFSGNYLYLETDFRLV-VRFDGNHYVDVSVSRNFNGLLCGMCGNSNGNPKDDIIKPDG 5853
Cdd:smart00216   86 TVNGQQVSLPYKTSDgSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3172-3331 4.81e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 130.60  E-value: 4.81e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3172 TYGICRVWGDPHYSTFDKETHHFMGICTYTwakLCTNATSLPYFNVEAKNEHRGnPSVSYIQKIHVDVYGHRVTMVKRET 3251
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYV---LAQDCSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3252 SrVLVDNTWRTLPVTLVGGAVTVKRSGNYVLLETDF-LLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNKLRADDFMKPD 3330
Cdd:smart00216   84 K-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLgLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162

                    .
gi 2119003705  3331 G 3331
Cdd:smart00216  163 G 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1941-2105 6.75e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 130.21  E-value: 6.75e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1941 TYGICRVWGDPHYSTFDKETHHFMGICTYTwakLCTNATSLPYFNVEAKNEHRGnPSVSYIQKIHVDVYGHRVTMVKNQR 2020
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYV---LAQDCSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2021 TLLhlgsymVDNIWRTLPVTLVGGAVTVKRSGSYVLLETDF-LLSVYYDSDHTADVKVPSTYFNQTCGICGNYNNLRADD 2099
Cdd:smart00216   84 KVT------VNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLgLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157

                    ....*.
gi 2119003705  2100 FMKPDG 2105
Cdd:smart00216  158 FRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2336-2487 3.96e-33

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: 128.29  E-value: 3.96e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2336 VCHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSDhFTVTTRNEHRGnPTWTAINSVALTVNGVHIAL-RKNRIVYVN 2414
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCG-GGATCLKSVKVELNGDEIELkDDNGKVTVN 88
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2415 DILVTLP-TSPIPDVTISLSGAYVLVQTSFGLH-LRFSGDHELLVNVTERYKGELCGLCGTYTGKQQDDFMRPDG 2487
Cdd:smart00216   89 GQQVSLPyKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
6377-6532 1.99e-30

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 120.17  E-value: 1.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 6377 CAITGDPHYLTFDGLSHHFQGKYTYItaasLTDIPNTLQEFSIQGKNEPMQTNNKITYLKEISTHVYGHVVQFKQKKNVV 6456
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYV----LAKDCSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 6457 LDGEKIKPPAQPHDG-LRIFQKAT-RVYLETDFGLSVSFDGSENADITLPNTYKAKVGGLCGNFDGKYKNDFTKPDGT 6532
Cdd:pfam00094   77 VNGQKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
108-267 1.03e-29

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 118.23  E-value: 1.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  108 CDFNNNYqpFCDWVQPcDGDDGDWIRtkHATPTPETGPIGD--YPGGNGYFIYQEASNFIPLGTNRLESPSLGV-LGDIC 184
Cdd:pfam00629    1 CDFEDGN--LCGWTQD-SSDDFDWER--VSGPSVKTGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPsRSPQC 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  185 IEFWYHMLGSeNHNKLKVIIKDNATEA--VIWSRTGNQSSFWLNASVPVTISVEKHiKVIFEAVRGWTEYGDTAVDNVAV 262
Cdd:pfam00629   76 LRFWYHMSGS-GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPF-QVVFEGIRGGGSRGGIALDDISL 153

                   ....*
gi 2119003705  263 QKGPC 267
Cdd:pfam00629  154 SSGPC 158
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
877-952 1.22e-29

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: 1.22e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705   877 LYEGNDYCGIITKADGHFAVCHSVVNPSSFFDSCVFDLCALNGDRQRLCNALETYAHACQSAGVSIPPWRNETFCP 952
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
108-267 1.94e-29

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 117.44  E-value: 1.94e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   108 CDFNNNyqPFCDWVQPcDGDDGDWIRTKhaTPTPETGPIGDYPGGNGYFIYQEASNFIPLGTNRLESPSL-GVLGDICIE 186
Cdd:smart00137    6 CDFEEG--STCGWHQD-SNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLyENRSTHCLT 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   187 FWYHMLGSeNHNKLKVIIKDNATEA--VIWSRTGNQSSFWLNASVPVTISVEKHiKVIFEAVRGWTEYGDTAVDNVAVQK 264
Cdd:smart00137   81 FWYYMYGS-GSGTLNVYVRENNGSQdtLLWSRSGTQGGQWLQAEVALSSWPQPF-QVVFEGTRGKGHSGYIALDDILLSN 158

                    ...
gi 2119003705   265 GPC 267
Cdd:smart00137  159 GPC 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4601-4676 1.18e-28

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: 112.05  E-value: 1.18e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  4601 KYESSSYCGLITSKEGPFANCLHVVSPNSFFDSCVFDLCALNGSQDALCDSLQSYAVACQKAGVIIPPWRNSTFCP 4676
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1528-1713 1.82e-28

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: 114.39  E-value: 1.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1528 CSVHSDPHYHTFDGLAHTYMGNCSHLLSTICANSTLPyyEVAAANEFRGGNTHVSYVKSVSIDVNSYSIVLDKGKVVKda 1607
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF--SFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1608 rshmeiqnmpenhklkktkperrkcecsseVNGKVQQLPVTL-KSDINITFSGQ-YVMVSTDFGLRVKYDGNHRVEVTLP 1685
Cdd:pfam00094   77 ------------------------------VNGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLS 126
                          170       180
                   ....*....|....*....|....*...
gi 2119003705 1686 SKFKGNVFGMCGNYDGNKTDDLLNCEGK 1713
Cdd:pfam00094  127 PSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3369-3444 2.98e-28

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: 110.89  E-value: 2.98e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  3369 KYESSSYCGLITSKEGPFANCLHVVSPNSFFESCVFDLCALNGSQDTLCDSLQSYADACQKAGVIIPPWKNSTFCP 3444
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1522-1712 4.36e-28

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: 113.65  E-value: 4.36e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1522 GETEAICSVHSDPHYHTFDGLAHTYMGNCSHLLSTICanSTLPYYEVAAANEFRGGNthVSYVKSVSIDVNSYSIVLDKG 1601
Cdd:smart00216    6 EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC--SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDD 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1602 kvvkdarshmeiqnmpeNHKLKktkperrkcecsseVNGKVQQLPVTLKS-DINITFSGQYVMVSTDFGL-RVKYDGNHR 1679
Cdd:smart00216   82 -----------------NGKVT--------------VNGQQVSLPYKTSDgSIQIRSSGGYLVVITSLGLiQVTFDGLTL 130
                           170       180       190
                    ....*....|....*....|....*....|...
gi 2119003705  1680 VEVTLPSKFKGNVFGMCGNYDGNKTDDLLNCEG 1712
Cdd:smart00216  131 LSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2143-2217 2.36e-27

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: 108.20  E-value: 2.36e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2143 KYESSSYCGLITSKEGPFANCLHVVGPDSFFESCVFDLCALNGSQTALCDSLQSYADACQKAGVIVPPWRNSTFC 2217
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4215-4288 6.88e-27

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: 107.04  E-value: 6.88e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705  4215 ESNSYCGIITDTNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVTIETWRNQTFCP 4288
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2983-3056 1.59e-26

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: 105.89  E-value: 1.59e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705  2983 ESNSYCGIITDTNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVIIHPWRNQTFCP 3056
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
6375-6531 3.88e-26

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: 108.26  E-value: 3.88e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  6375 GKCAITGDPHYLTFDGLSHHFQGKYTYITAASLTDIPNtlqeFSIQGKNEPMQTNNkiTYLKEISTHVYGHVVQFKQKKN 6454
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGA--TCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  6455 -VVLDGEKIKPPAQPHDG-LRIFQKATRVYLETDFGL-SVSFDGSENADITLPNTYKAKVGGLCGNFDGKYKNDFTKPDG 6531
Cdd:smart00216   84 kVTVNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
464-537 5.90e-26

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: 104.34  E-value: 5.90e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705   464 ESNSYCGIITDTNGPFRQCHSVIDPKDYFDDCAYDLCELNMDTGALCSNLQAYADACQSEGVTIRPWRNETFCA 537
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1752-1824 1.53e-25

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: 103.19  E-value: 1.53e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119003705  1752 QSNSYCGIITDTNGPFKQCHSVIDPKDYFNDCAYDLCALNMDTGALCSNLQAYADACQSKGVTIEPWRNQTFC 1824
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
883-951 4.30e-25

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: 101.69  E-value: 4.30e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  883 YCGIITKaDGHFAVCHSVVNPSSFFDSCVFDLCALNGDRQRLCNALETYAHACQSAGVSIPPWRNETFC 951
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1756-1824 1.28e-24

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: 100.15  E-value: 1.28e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 1756 YCGIITDtNGPFKQCHSVIDPKDYFNDCAYDLCALNMDTGALCSNLQAYADACQSKGVTIEPWRNQTFC 1824
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2987-3055 1.45e-24

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: 100.15  E-value: 1.45e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 2987 YCGIITDtNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVIIHPWRNQTFC 3055
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
5898-5965 1.49e-24

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: 100.49  E-value: 1.49e-24
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  5898 CGMIKDPTGVFKDCHAVIPPENFFENCVIDFCASSGDSVSLCYALQSYASMCAEAGICV-AWRNSTFCP 5965
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
4219-4287 3.01e-24

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: 98.99  E-value: 3.01e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 4219 YCGIITDtNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVTIETWRNQTFC 4287
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
468-536 3.48e-24

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: 98.99  E-value: 3.48e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  468 YCGIITDtNGPFRQCHSVIDPKDYFDDCAYDLCELNMDTGALCSNLQAYADACQSEGVTIRPWRNETFC 536
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
4607-4675 1.46e-23

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: 97.07  E-value: 1.46e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 4607 YCGLITSKeGPFANCLHVVSPNSFFDSCVFDLCALNGSQDALCDSLQSYAVACQKAGVIIPPWRNSTFC 4675
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2149-2217 2.56e-23

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: 96.68  E-value: 2.56e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 2149 YCGLITSKeGPFANCLHVVGPDSFFESCVFDLCALNGSQTALCDSLQSYADACQKAGVIVPPWRNSTFC 2217
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
3375-3443 6.14e-23

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: 95.52  E-value: 6.14e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 3375 YCGLITSKeGPFANCLHVVSPNSFFESCVFDLCALNGSQDTLCDSLQSYADACQKAGVIIPPWKNSTFC 3443
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2525-2599 7.51e-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: 95.49  E-value: 7.51e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2525 EQAAAEHCKIVLDSNGPFAECHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYVAACEEAGVDLGDWRKDTVC 2599
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3750-3824 1.08e-22

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: 95.10  E-value: 1.08e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  3750 EQAAEEHCRIVLDSNGPFVNCHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYAAACEEAGVDLGDWRKDTVC 3824
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4983-5057 5.42e-22

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: 93.17  E-value: 5.42e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  4983 EQAATEHCRIVSDSNGPFAKCHGHISPELYFVSCVYDQCATNGSSEQLCNALESYAATCEEAGVDLGDWRKDTVC 5057
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2531-2599 2.76e-21

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: 90.90  E-value: 2.76e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 2531 HCKIVLDSnGPFAECHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYVAACEEAGVDLGDWRKDTVC 2599
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1263-1331 2.96e-21

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: 90.52  E-value: 2.96e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 1263 QCQIIMaSNGPFGSCHWYIPPQLYFESCVFDFCATNGSLEYFCSALESYATACAAAGVHVGDWKKETFC 1331
Cdd:pfam08742    1 KCGLLS-DSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1257-1331 1.57e-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: 88.94  E-value: 1.57e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  1257 EPEATLQCQIIMASNGPFGSCHWYIPPQLYFESCVFDFCATNGSLEYFCSALESYATACAAAGVHVGDWKKETFC 1331
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
4989-5057 1.59e-20

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: 88.59  E-value: 1.59e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 4989 HCRIVSDSnGPFAKCHGHISPELYFVSCVYDQCATNGSSEQLCNALESYAATCEEAGVDLGDWRKDTVC 5057
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
3756-3824 1.92e-20

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: 88.21  E-value: 1.92e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 3756 HCRIVLDSnGPFVNCHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYAAACEEAGVDLGDWRKDTVC 3824
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
6587-6658 2.32e-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: 88.55  E-value: 2.32e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119003705  6587 GTDYCGSLINPKGPFRACHNVFPPDAYLENCLYDLCAAFDNIALLCTNLEQYALTCQSEGVTLENWRKGTIC 6658
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
5898-5964 8.43e-20

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: 86.67  E-value: 8.43e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 5898 CGMIKDpTGVFKDCHAVIPPENFFENCVIDFCASSGDSVSLCYALQSYASMCAEAGICVA-WRNSTFC 5964
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
6283-6348 1.78e-19

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: 85.51  E-value: 1.78e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 6283 QCNVLLSN-AFVPCHSLVDPDLFIESCVYDMCKYDGKQSTLCDIVQAYVDICKNEGVTI-HWRNSTFC 6348
Cdd:pfam08742    1 KCGLLSDSgPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
6281-6348 9.66e-19

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: 83.93  E-value: 9.66e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119003705  6281 KAQCNVLLSN--AFVPCHSLVDPDLFIESCVYDMCKYDGKQSTLCDIVQAYVDICKNEGVTIH-WRNSTFC 6348
Cdd:smart00832    5 CSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
6590-6658 2.08e-18

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: 82.43  E-value: 2.08e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 6590 YCGsLINPKGPFRACHNVFPPDAYLENCLYDLCAAFDNIALLCTNLEQYALTCQSEGVTLENWRKGTIC 6658
Cdd:pfam08742    1 KCG-LLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
1828-1881 1.17e-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: 76.97  E-value: 1.17e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 1828 CKPKSHYKQCGPACPATCANPNAPSSCSLPCVEGCICDSGYML-YHDQCVPSTQC 1881
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
3059-3112 1.70e-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: 76.59  E-value: 1.70e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3059 CKPNSHYEHCGHACPATCANPNSPSSCSLPCVEGCICNSGYML-YHDQCVPSTQC 3112
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
4291-4344 3.56e-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: 75.82  E-value: 3.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4291 CKPNSHYEQCGSACPATCMNPNAPSTCSLPCVESCVCDSGYML-YHDRCVPNTQC 4344
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
567-620 5.26e-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: 75.43  E-value: 5.26e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  567 CKPNTHYQQCGPACPATCTNPNAPSSCSLPCVEDCVCDSGYLL-YHDRCVPSTQC 620
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
955-1008 1.41e-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: 73.89  E-value: 1.41e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  955 CPSNSHYNVCGSACPATCTDMSAPNNCSKPCVEGCHCDHEFVLS-GQTCVSVHDC 1008
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3059-3112 2.39e-15

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: 73.58  E-value: 2.39e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3059 CKPNSHYEHCGHACPATCANPNSPSSCSLPCVEGCICNSGYML-YHDQCVPSTQC 3112
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
567-620 1.06e-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: 71.65  E-value: 1.06e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  567 CKPNTHYQQCGPACPATCTNPNAPSSCSLPCVEDCVCDSGYLL-YHDRCVPSTQC 620
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
4291-4344 1.75e-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: 70.88  E-value: 1.75e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4291 CKPNSHYEQCGSACPATCMNPNAPSTCSLPCVESCVCDSGYML-YHDRCVPNTQC 4344
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
1828-1881 1.82e-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: 70.88  E-value: 1.82e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 1828 CKPKSHYKQCGPACPATCANPNAPSSCSLPCVEGCICDSGYML-YHDQCVPSTQC 1881
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
3447-3500 1.85e-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: 70.81  E-value: 1.85e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3447 CPDNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDTGFVLS-GSTCVNVADC 3500
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
5968-6021 3.89e-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: 70.04  E-value: 3.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 5968 CPAGSHYENCATGCPATCANTSPPSSCNASPAEGCICDDGYILS-GNKCVQQSDC 6021
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
6662-6715 5.86e-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: 69.27  E-value: 5.86e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 6662 CPLNSKYDMCTSACPATCGDLTAPSECDLPCLEGCECLPGYVMS-GFDCVPYKEC 6715
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
955-1008 6.52e-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: 69.34  E-value: 6.52e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  955 CPSNSHYNVCGSACPATCTDMSAPNNCSKPCVEGCHCDHEFVLS-GQTCVSVHDC 1008
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
2224-2275 2.74e-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: 67.34  E-value: 2.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 2224 PNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDSGFVLS-GNTCVNVADC 2275
Cdd:cd19941      3 PNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
4682-4733 4.25e-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: 66.96  E-value: 4.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4682 PNSHYEPCSSACPATCLDQFAPLNCSKPCVEACECDSGFVLS-GSTCVNVADC 4733
Cdd:cd19941      3 PNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3447-3500 7.20e-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: 66.26  E-value: 7.20e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3447 CPDNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDTGFVLS-GSTCVNVADC 3500
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
5968-6021 8.84e-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: 66.26  E-value: 8.84e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 5968 CPAGSHYENCATGCPATCANTSPPSSCNASPAEGCICDDGYILS-GNKCVQQSDC 6021
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
4682-4733 5.76e-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: 63.95  E-value: 5.76e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4682 PNSHYEPCSSACPATCLDQFAPLNCSKPCVEACECDSGFVLS-GSTCVNVADC 4733
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
6662-6715 6.67e-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: 63.56  E-value: 6.67e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 6662 CPLNSKYDMCTSACPATCGDLTAPSECDLPCLEGCECLPGYVMSGFD-CVPYKEC 6715
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
2224-2275 7.65e-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: 63.56  E-value: 7.65e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 2224 PNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDSGFVLS-GNTCVNVADC 2275
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
6023-6078 5.13e-10

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: 58.08  E-value: 5.13e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705 6023 CVDGDNNYYTVGESWYSyDNCTERCTCnSNNNITCQQWECGLLESCKIQDGVLGCY 6078
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
6717-6770 3.05e-05

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: 44.60  E-value: 3.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 6717 CMYENKYYEVGEHFITEDCSQSCVCTeSSSVSCEKNQCKLEELCATSNFVRGCY 6770
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
3114-3169 5.71e-05

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: 43.83  E-value: 5.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705 3114 CWQDGKHYPVGsEFWTDDSCSTKCRCPsaGSKLECFPASCPTGHYCGIKNGVPGCY 3169
Cdd:pfam12714    2 KDAQGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
5173-5374 1.14e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 47.59  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5173 TTSVDNVINTPHITSVTLQTSTHAASPSTSSPSGETKTTTKAPVTdiftsatsPSTSPSTSIPPVITSGigktTAKPDIE 5252
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT--------TTAILSTNTTTVTSTG----TTVTPVP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5253 TTSADNVINTphITSVTLQTSTHAaspstsspsgETKTTTKAPVTDiftsatspstspstsippiitsgiGKTTAKPdiE 5332
Cdd:PHA03255    93 TTSNASTINV--TTKVTAQNITAT----------EAGTGTSTGVTS------------------------NVTTRSS--S 134
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2119003705 5333 TTSAdniinTPHITLVTlqtsTHAPSPST-SPSGETKTTTKAP 5374
Cdd:PHA03255   135 TTSA-----TTRITNAT----TLAPTLSSkGTSNATKTTAELP 168
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
4735-4788 1.18e-04

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: 43.06  E-value: 1.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 4735 CWYQGKYYEKNEITMTENCEQQCKCLGNNdMHCTPTSCEPDKICKVKDGVLDCV 4788
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
2277-2330 6.41e-04

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: 41.14  E-value: 6.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 2277 CWYQGKYYEKHEDTMTENCEQQCQCSGNNdMNCTPTSCEPDKICKVEDGTLGCF 2330
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
3502-3555 6.41e-04

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: 41.14  E-value: 6.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 3502 CWYQGKYYEKHEDTMTENCEQQCQCSGNNdMNCTPTSCEPDKICKVEDGTLGCF 3555
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
4349-4401 1.06e-03

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: 40.36  E-value: 1.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4349 DGKHYPVGsEFWTDDSCSTKCSCPsrGGQLACVNASCPKDHYCGINNGVPGCY 4401
Cdd:pfam12714    5 QGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
622-677 1.46e-03

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: 39.98  E-value: 1.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  622 CWQDGKHYPVGsEFWTDDSCSTKCSCPsrGSQLVCVNASCPKDHYCGINNGVPGCY 677
Cdd:pfam12714    2 KDAQGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
5571-5706 2.11e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 43.74  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5571 TTSADNIINTPHITSVTLQTSTHAASPSASSQSGETKTTTKAPVTdifTSATSPSISPSTSIPPiitsgigktTAKPDIE 5650
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT---TTAILSTNTTTVTSTG---------TTVTPVP 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119003705 5651 TTSADNVINTphITSVTLQTSTHA------ASPSTSSQSGETKTTTKAPVTDHHVCTASGDP 5706
Cdd:PHA03255    93 TTSNASTINV--TTKVTAQNITATeagtgtSTGVTSNVTTRSSSTTSATTRITNATTLAPTL 152
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
1013-1063 9.79e-03

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: 37.67  E-value: 9.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2119003705 1013 NGKYHEKGHTFWEENCEHKCTCYGNNhLNCTAAKCESNEICKVQNGEWGCH 1063
Cdd:pfam12714    5 QGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
2608-2761 1.21e-54

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 189.51  E-value: 1.21e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2608 CDFDTDFCEWEQSTTDSFDWQRNRGPTPSLNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPSCPA-YGPHCFRFWYH 2686
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSFWYH 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 2687 MYGvAQNMALKVYLVEKGSPFLK--WVQTGNQGNKWRPVEVDLQ-LKGNFQIIIEGVRGSDYRSDVAVDDVTFNAGCC 2761
Cdd:cd06263     81 MYG-SGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
3833-3986 1.48e-54

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 189.13  E-value: 1.48e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3833 CDFDTDFCEWEQSTTDSFDWQRNSGPTPSLNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPSCPA-YGPHCFRFWYH 3911
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSFWYH 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 3912 MYGvAQNMALKVYLVEKGAAFLK--WVQTGNQGNKWRPVEVDLQ-LKGNFQIIIEGVRGSDYRSDVAVDDVTFSAGCC 3986
Cdd:cd06263     81 MYG-SGVGTLNVYVREEGGGLGTllWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
1340-1497 1.72e-51

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 180.27  E-value: 1.72e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1340 CDFDIDYCGWAQSSSDSFDWLRYKGPTPSLNTGPPYDHTSAEeevdGYYVYIEGDFAKPGDVAHLLSPSCPA-YGPHCFR 1418
Cdd:cd06263      1 CDFEDGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGS----GHYLYVESSSGREGQKARLLSPLLPPpRSSHCLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1419 FWYHMYGvAQNMALKLYLVQKGVPV--LMWSQTGNQGNKWRLVEVELQ-LRGSFQIIIEGVRGSDYRSDVAVDDITFKAG 1495
Cdd:cd06263     77 FWYHMYG-SGVGTLNVYVREEGGGLgtLLWSASGGQGNQWQEAEVTLSaSSKPFQVVFEGVRGSGSRGDIALDDISLSPG 155

                   ..
gi 2119003705 1496 CC 1497
Cdd:cd06263    156 PC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
2608-2762 5.48e-48

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 170.62  E-value: 5.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2608 CDFDTD-FCEWEQSTTDSFDWQRNRGPTPslNTGPPYDHT--SADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 2683
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTqgTGSGHFMYVDTSSGAPGQTARLLSPLlPPSRSPQCLRF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2684 WYHMYGVAQNmALKVYLVEKGSPF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFNAGC 2760
Cdd:pfam00629   79 WYHMSGSGVG-TLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISLSSGP 157

                   ..
gi 2119003705 2761 CS 2762
Cdd:pfam00629  158 CP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
3833-3987 1.72e-47

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 169.08  E-value: 1.72e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3833 CDFDTD-FCEWEQSTTDSFDWQRNSGPTPslNTGPPYDHT--SADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 3908
Cdd:pfam00629    1 CDFEDGnLCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTqgTGSGHFMYVDTSSGAPGQTARLLSPLlPPSRSPQCLRF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3909 WYHMYGVAQNmALKVYLVEKGAAF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFSAGC 3985
Cdd:pfam00629   79 WYHMSGSGVG-TLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQpFQVVFEGIRGGGSRGGIALDDISLSSGP 157

                   ..
gi 2119003705 3986 CS 3987
Cdd:pfam00629  158 CP 159
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
1340-1498 3.73e-47

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 168.31  E-value: 3.73e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1340 CDFDIDY-CGWAQSSSDSFDWLRYKGPTPslNTGPPYDHTSAEEEvdGYYVYIEGDFAKPGDVAHLLSPS-CPAYGPHCF 1417
Cdd:pfam00629    1 CDFEDGNlCGWTQDSSDDFDWERVSGPSV--KTGPSSDHTQGTGS--GHFMYVDTSSGAPGQTARLLSPLlPPSRSPQCL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1418 RFWYHMYGVAQNmALKLYLVQKGVPV--LMWSQTGNQGNKWRLVEVELQ-LRGSFQIIIEGVRGSDYRSDVAVDDITFKA 1494
Cdd:pfam00629   77 RFWYHMSGSGVG-TLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSsSTQPFQVVFEGIRGGGSRGGIALDDISLSS 155

                   ....
gi 2119003705 1495 GCCA 1498
Cdd:pfam00629  156 GPCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
2606-2761 4.49e-41

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 150.96  E-value: 4.49e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2606 LGCDFDTD-FCEWEQSTTDSFDWQRNRGPTPslNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 2683
Cdd:smart00137    4 GNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPlYENRSTHCLTF 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2684 WYHMYGVAQNmALKVYLVEKGSPF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFNAGC 2760
Cdd:smart00137   82 WYYMYGSGSG-TLNVYVRENNGSQdtLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILLSNGP 160

                    .
gi 2119003705  2761 C 2761
Cdd:smart00137  161 C 161
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
3831-3986 7.57e-41

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 150.19  E-value: 7.57e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3831 LGCDFDTD-FCEWEQSTTDSFDWQRNSGPTPslNTGPPYDHTSADGYYIYIEGDLAKPGDVAHLLSPS-CPAYGPHCFRF 3908
Cdd:smart00137    4 GNCDFEEGsTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPlYENRSTHCLTF 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3909 WYHMYGVAQNmALKVYLVEKGAAF--LKWVQTGNQGNKWRPVEVDLQLKGN-FQIIIEGVRGSDYRSDVAVDDVTFSAGC 3985
Cdd:smart00137   82 WYYMYGSGSG-TLNVYVRENNGSQdtLLWSRSGTQGGQWLQAEVALSSWPQpFQVVFEGTRGKGHSGYIALDDILLSNGP 160

                    .
gi 2119003705  3986 C 3986
Cdd:smart00137  161 C 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
5700-5854 7.66e-40

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: 147.13  E-value: 7.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5700 CTASGDPHYNTFDGRVHHFMGNCTYVLTKLCNESSgLPLFEVTTTNEHRGSNTKvsYVNSVHVNVYGNSISLLKNKKVNV 5779
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP-DFSFSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 5780 NGKRVNPPYSI-KDQIKVYFSGN-YLYLETDFRLVVRFDGNHYVDVSVSRNFNGLLCGMCGNSNGNPKDDIIKPDGT 5854
Cdd:pfam00094   78 NGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2790-2943 2.08e-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: 145.59  E-value: 2.08e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2790 CSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCDvNSSLPYFNVEAANENRGGNThvSYVKSVTVDVYSYRIILEKSKVVKV 2869
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 2870 NGQVQLFPLTlSPGVNIIISGQYVMLTS---DFGLRVKYDGNHRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 2943
Cdd:pfam00094   78 NGQKVSLPYK-SDGGEVEILGSGFVVVDlspGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4022-4175 2.91e-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: 145.21  E-value: 2.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4022 CSVHSDPHYHTFDGQPHTFMGTCTYTLSKLCDViSTLPYFNVEAANEHRGGNThvSYVKSVTVDVYSHRIILEKNKVVKI 4101
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 4102 NGQVQLLPLTlSPGVNIIISGQYVMLTS---DFGLRVKYDGNQRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 4175
Cdd:pfam00094   78 NGQKVSLPYK-SDGGEVEILGSGFVVVDlspGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4795-4945 2.53e-38

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: 2.53e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4795 CDIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSNY-FTITTRNEHRGNPSWtAINSVALNVNGVHIVLRKNKIVYVNG 4873
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFsFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4874 IPVTLPTSPMpGVAISLNGAY-VLVQTNFGLHLKFNGDQKLLVNVT--ERYKGQLCGLCGTYNGDQKDDFMRPDG 4945
Cdd:pfam00094   80 QKVSLPYKSD-GGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTlsPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
271-425 9.71e-38

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: 140.97  E-value: 9.71e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  271 CSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCDvNSTLPYFNVEAANENRGGNThvSYVKSVTVDVYSYRIILEKNKVVKV 350
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGASG--VCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  351 NGiaQLIPLPLTPD---VTITQSGQ-YAMVMTSFGLRVKYDGNQRAEVTLPSTFQGKVCGMCGNYNSIRNDDFLNPDGK 425
Cdd:pfam00094   78 NG--QKVSLPYKSDggeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
6085-6238 4.94e-37

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: 139.04  E-value: 4.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 6085 CHVAGDPHYFTFDKVMHTFIGTCTYVLVQVCdkSNVIDLKVSG--KNEQRGLPfSSYLKEVYIDVYNTRITIQRSKALLL 6162
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDC--SEEPDFSFSVtnKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119003705 6163 NGGRVHTPVENQIRGITINTNGI-YTIVETDFGMMVKFDGNHHLEISLPDSYFSKVCGLCGNYNMKKDDEFLMPSGQ 6238
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
4408-4564 4.94e-37

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: 139.04  E-value: 4.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 4408 CRVWGDPHYSTFDKETHHFMGNCTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKkeASRVL 4487
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 4488 IDDIWTNLPASLVKGAVTVDRSG-SYVLLETDFLLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNNLRADDFMKPDGS 4564
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3562-3713 8.83e-37

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: 138.27  E-value: 8.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3562 CHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSD-HFTVTTRNEHRGNPtWTAINSVALTVNGVHIALRKNRIVYVND 3640
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDfSFSVTNKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3641 ILVTLP-TSPIPDVTISLSG-AYVLVQTSFGLRLQFSGDHELLVNVTERYKGKLCGLCGTYTGKQQDDFMRPDGV 3713
Cdd:pfam00094   80 QKVSLPyKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
3176-3332 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: 137.89  E-value: 1.35e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 3176 CRVWGDPHYSTFDKETHHFMGICTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKRETsrVL 3255
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGT--VL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 3256 VDNTWRTLPVTLVGGAVTVKRSGN-YVLLETDFLLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNKLRADDFMKPDGS 3332
Cdd:pfam00094   77 VNGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1060-1220 2.56e-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: 137.15  E-value: 2.56e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1060 WGC-HVANAAMCHIYGDPHYITFDGKLYHFQGACNYSVTQTCRNSAvNFSVTSRNEHRGSpKWSALNSVAFTISGLHIIL 1138
Cdd:smart00216    1 WCCtQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP-TFSVLLKNVPCGG-GATCLKSVKVELNGDEIEL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1139 KK-NNKVSVNGVNISLPYN-NGHGILVSKDGPYLVLQTHFGL-KLKYNGDHELFVHVNENFKGQLCGLCGTYNDDQLDDF 1215
Cdd:smart00216   79 KDdNGKVTVNGQQVSLPYKtSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158

                    ....*
gi 2119003705  1216 TRPDG 1220
Cdd:smart00216  159 RTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2787-2943 2.63e-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: 137.15  E-value: 2.63e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2787 ASTCSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCdvnSSLPYFNVEAANENRGGNthVSYVKSVTVDVYSYRIILEKS-K 2865
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDDnG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2866 VVKVNGQVQLFPLTLSPG-VNIIISGQYVMLTSDFGL-RVKYDGNHRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 2943
Cdd:smart00216   84 KVTVNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
265-424 4.36e-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: 136.76  E-value: 4.36e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   265 GPCESTCSVHSDPHYRTFDGQPHTFMGTCTYTLSKLCdvnSTLPYFNVEAANENRGGNthVSYVKSVTVDVYSYRIILEK 344
Cdd:smart00216    6 EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   345 -NKVVKVNGiaQLIPLPLTPD---VTITQSGQYAMVMTSFGL-RVKYDGNQRAEVTLPSTFQGKVCGMCGNYNSIRNDDF 419
Cdd:smart00216   81 dNGKVTVNG--QQVSLPYKTSdgsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158

                    ....*
gi 2119003705   420 LNPDG 424
Cdd:smart00216  159 RTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
684-840 1.03e-35

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 135.19  E-value: 1.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  684 CRVHNDPHYNTFDKETHHFMGTCTYTVAKVCANTTSlPYFNIETKNEHRGNPSVsYVQKVHVDVYGHRVSIIKkePSRVL 763
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD-FSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQK--GGTVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  764 VDGvwQKLSVSLADGALLVRQSGRY---VQLETDFGLSVSYDTDHSVEVKVPSTYFNLTCGMCGNFNNLRKDDFMMPNGT 840
Cdd:pfam00094   77 VNG--QKVSLPYKSDGGEVEILGSGfvvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
4020-4175 1.04e-35

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 135.61  E-value: 1.04e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4020 SICSVHSDPHYHTFDGQPHTFMGTCTYTLSKLCdviSTLPYFNVEAANEHRGGNthVSYVKSVTVDVYSHRIILEK-NKV 4098
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDdNGK 84
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  4099 VKINGQVQLLPLTLSPG-VNIIISGQYVMLTSDFGL-RVKYDGNQRAEITLPSKFEGHVCGICGNYNGNKADDFLNPDG 4175
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
1338-1497 1.40e-35

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 135.16  E-value: 1.40e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1338 LECDFDIDY-CGWAQSSSDSFDWLRYKGPTPslNTGPPYDHTSAeeevDGYYVYIEGDFAKPGDVAHLLSPS-CPAYGPH 1415
Cdd:smart00137    4 GNCDFEEGStCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTG----NGHFMFFETSSGAEGQTARLLSPPlYENRSTH 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1416 CFRFWYHMYGVAQNmALKLYLVQKGVPVLM--WSQTGNQGNKWRLVEVELQL-RGSFQIIIEGVRGSDYRSDVAVDDITF 1492
Cdd:smart00137   78 CLTFWYYMYGSGSG-TLNVYVRENNGSQDTllWSRSGTQGGQWLQAEVALSSwPQPFQVVFEGTRGKGHSGYIALDDILL 156

                    ....*
gi 2119003705  1493 KAGCC 1497
Cdd:smart00137  157 SNGPC 161
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
108-267 1.62e-35

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 134.81  E-value: 1.62e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  108 CDFNnnyQPFCDWVQpCDGDDGDWIRTKHATPTPETGPIGDYPGGNGYFIYQEASNFIPLGTNRLESPSL-GVLGDICIE 186
Cdd:cd06263      1 CDFE---DGLCGWTQ-DSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLpPPRSSHCLS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  187 FWYHMLGSeNHNKLKVIIKDNA--TEAVIWSRTGNQSSFWLNASVPVTiSVEKHIKVIFEAVRGWTEYGDTAVDNVAVQK 264
Cdd:cd06263     77 FWYHMYGS-GVGTLNVYVREEGggLGTLLWSASGGQGNQWQEAEVTLS-ASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154

                   ...
gi 2119003705  265 GPC 267
Cdd:cd06263    155 GPC 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1945-2106 2.20e-35

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: 134.42  E-value: 2.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1945 CRVWGDPHYSTFDKETHHFMGICTYTWAKLCTNaTSLPYFNVEAKNEHRGNPSVsYIQKIHVDVYGHRVTMVKNQRTLlh 2024
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2025 lgsymVDNIWRTLPVTLVGGAVTVKRSG-SYVLLETDFLLSVYYDSDHTADVKVPSTYFNQTCGICGNYNNLRADDFMKP 2103
Cdd:pfam00094   77 -----VNGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151

                   ...
gi 2119003705 2104 DGS 2106
Cdd:pfam00094  152 DGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
2337-2487 2.42e-35

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: 134.04  E-value: 2.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 2337 CHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSD-HFTVTTRNEHRGNPtWTAINSVALTVNGVHIALRKNRIVYVND 2415
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDfSFSVTNKNCNGGAS-GVCLKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 2416 ILVTLP-TSPIPDVTISLSGaYVLVQTSFGLHLRFSGDHELLVNVT--ERYKGELCGLCGTYTGKQQDDFMRPDG 2487
Cdd:pfam00094   80 QKVSLPyKSDGGEVEILGSG-FVVVDLSPGVGLQVDGDGRGQLFVTlsPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1070-1221 3.86e-35

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 133.65  E-value: 3.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1070 CHIYGDPHYITFDGKLYHFQGACNYSVTQTC-RNSAVNFSVTSRNEHRGSPKWSaLNSVAFTISGLHIILKKNNKVSVNG 1148
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCsEEPDFSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVLVNG 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 1149 VNISLPY--NNGHGILVSKDGPYLVLQTHFGLKLKYNGDHELFVHVNENFKGQLCGLCGTYNDDQLDDFTRPDGV 1221
Cdd:pfam00094   80 QKVSLPYksDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
4793-4945 1.06e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.53  E-value: 1.06e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4793 AVCDIYGDPHYITFDGKLYHFQGSCNYTVTETCGnTSNYFTITTRNEHRGnPSWTAINSVALNVNGVHIVL-RKNKIVYV 4871
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS-SEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELkDDNGKVTV 87
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  4872 NGIPVTLP-TSPMPGVAISLNGAYVLVQTNFGLH-LKFNGDQKLLVNVTERYKGQLCGLCGTYNGDQKDDFMRPDG 4945
Cdd:smart00216   88 NGQQVSLPyKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
6085-6237 1.43e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.14  E-value: 1.43e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  6085 CHVAGDPHYFTFDKVMHTFIGTCTYVLVQVCDKSNviDLKVSGKNEQRGlPFSSYLKEVYIDVYNTRITIQRS-KALLLN 6163
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP--TFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDnGKVTVN 88
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  6164 GGRVHTPVENQIRGITINTNGIYTIVETDFGMM-VKFDGNHHLEISLPDSYFSKVCGLCGNYNMKKDDEFLMPSG 6237
Cdd:smart00216   89 GQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3561-3712 1.81e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 132.14  E-value: 1.81e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3561 VCHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSDhFTVTTRNEHRGnPTWTAINSVALTVNGVHIAL-RKNRIVYVN 3639
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCG-GGATCLKSVKVELNGDEIELkDDNGKVTVN 88
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  3640 DILVTLP-TSPIPDVTISLSGAYVLVQTSFGL-RLQFSGDHELLVNVTERYKGKLCGLCGTYTGKQQDDFMRPDG 3712
Cdd:smart00216   89 GQQVSLPyKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
4404-4563 2.07e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.76  E-value: 2.07e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4404 TYGICRVWGDPHYSTFDKETHHFMGNCTYTwakLCTNATSLPYFNVEAKNEHRGnPSVSYIQKIHVDVYGHRVTMVKKEA 4483
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYV---LAQDCSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  4484 SrVLIDDIWTNLPASLVKGAVTVDRSGSYVLLETDF-LLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNNLRADDFMKPD 4562
Cdd:smart00216   84 K-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLgLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162

                    .
gi 2119003705  4563 G 4563
Cdd:smart00216  163 G 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
674-839 2.96e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.37  E-value: 2.96e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   674 PGCYPHTY-GICRVHNDPHYNTFDKETHHFMGTCTYTVAKVCantTSLPYFNIETKNEHRGnPSVSYVQKVHVDVYGHRV 752
Cdd:smart00216    1 WCCTQEECsPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEI 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   753 SIIKKEPSrVLVDGVWQKLSVSLADGALLVRQSGRYVQLETDFGL-SVSYDTDHSVEVKVPSTYFNLTCGMCGNFNNLRK 831
Cdd:smart00216   77 ELKDDNGK-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPE 155

                    ....*...
gi 2119003705   832 DDFMMPNG 839
Cdd:smart00216  156 DDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
5699-5853 3.08e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 131.37  E-value: 3.08e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  5699 VCTASGDPHYNTFDGRVHHFMGNCTYVLTKLCNESsglPLFEVTTTNEHRGSNtkVSYVNSVHVNVYGNSISLLK-NKKV 5777
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDdNGKV 85
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705  5778 NVNGKRVNPPYSIKD-QIKVYFSGNYLYLETDFRLV-VRFDGNHYVDVSVSRNFNGLLCGMCGNSNGNPKDDIIKPDG 5853
Cdd:smart00216   86 TVNGQQVSLPYKTSDgSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
3172-3331 4.81e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 130.60  E-value: 4.81e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3172 TYGICRVWGDPHYSTFDKETHHFMGICTYTwakLCTNATSLPYFNVEAKNEHRGnPSVSYIQKIHVDVYGHRVTMVKRET 3251
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYV---LAQDCSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  3252 SrVLVDNTWRTLPVTLVGGAVTVKRSGNYVLLETDF-LLSVYYDSDHTAEVKVPSTYFNQTCGICGNYNKLRADDFMKPD 3330
Cdd:smart00216   84 K-VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLgLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162

                    .
gi 2119003705  3331 G 3331
Cdd:smart00216  163 G 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1941-2105 6.75e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 130.21  E-value: 6.75e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1941 TYGICRVWGDPHYSTFDKETHHFMGICTYTwakLCTNATSLPYFNVEAKNEHRGnPSVSYIQKIHVDVYGHRVTMVKNQR 2020
Cdd:smart00216    8 CSPTCSVSGDPHYTTFDGVAYTFPGNCYYV---LAQDCSSEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2021 TLLhlgsymVDNIWRTLPVTLVGGAVTVKRSGSYVLLETDF-LLSVYYDSDHTADVKVPSTYFNQTCGICGNYNNLRADD 2099
Cdd:smart00216   84 KVT------VNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLgLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157

                    ....*.
gi 2119003705  2100 FMKPDG 2105
Cdd:smart00216  158 FRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
2336-2487 3.96e-33

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: 128.29  E-value: 3.96e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  2336 VCHIYGDPHYITFDGKLYHFQGSCNYTVTETCGNTSDhFTVTTRNEHRGnPTWTAINSVALTVNGVHIAL-RKNRIVYVN 2414
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT-FSVLLKNVPCG-GGATCLKSVKVELNGDEIELkDDNGKVTVN 88
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2415 DILVTLP-TSPIPDVTISLSGAYVLVQTSFGLH-LRFSGDHELLVNVTERYKGELCGLCGTYTGKQQDDFMRPDG 2487
Cdd:smart00216   89 GQQVSLPyKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
6377-6532 1.99e-30

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 120.17  E-value: 1.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 6377 CAITGDPHYLTFDGLSHHFQGKYTYItaasLTDIPNTLQEFSIQGKNEPMQTNNKITYLKEISTHVYGHVVQFKQKKNVV 6456
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYV----LAKDCSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 6457 LDGEKIKPPAQPHDG-LRIFQKAT-RVYLETDFGLSVSFDGSENADITLPNTYKAKVGGLCGNFDGKYKNDFTKPDGT 6532
Cdd:pfam00094   77 VNGQKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
108-267 1.03e-29

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 118.23  E-value: 1.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  108 CDFNNNYqpFCDWVQPcDGDDGDWIRtkHATPTPETGPIGD--YPGGNGYFIYQEASNFIPLGTNRLESPSLGV-LGDIC 184
Cdd:pfam00629    1 CDFEDGN--LCGWTQD-SSDDFDWER--VSGPSVKTGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPsRSPQC 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  185 IEFWYHMLGSeNHNKLKVIIKDNATEA--VIWSRTGNQSSFWLNASVPVTISVEKHiKVIFEAVRGWTEYGDTAVDNVAV 262
Cdd:pfam00629   76 LRFWYHMSGS-GVGTLRVYVRENGGTLdtLLWSISGDQGPSWKEARVTLSSSTQPF-QVVFEGIRGGGSRGGIALDDISL 153

                   ....*
gi 2119003705  263 QKGPC 267
Cdd:pfam00629  154 SSGPC 158
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
877-952 1.22e-29

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: 1.22e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705   877 LYEGNDYCGIITKADGHFAVCHSVVNPSSFFDSCVFDLCALNGDRQRLCNALETYAHACQSAGVSIPPWRNETFCP 952
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
108-267 1.94e-29

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 117.44  E-value: 1.94e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   108 CDFNNNyqPFCDWVQPcDGDDGDWIRTKhaTPTPETGPIGDYPGGNGYFIYQEASNFIPLGTNRLESPSL-GVLGDICIE 186
Cdd:smart00137    6 CDFEEG--STCGWHQD-SNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLyENRSTHCLT 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705   187 FWYHMLGSeNHNKLKVIIKDNATEA--VIWSRTGNQSSFWLNASVPVTISVEKHiKVIFEAVRGWTEYGDTAVDNVAVQK 264
Cdd:smart00137   81 FWYYMYGS-GSGTLNVYVRENNGSQdtLLWSRSGTQGGQWLQAEVALSSWPQPF-QVVFEGTRGKGHSGYIALDDILLSN 158

                    ...
gi 2119003705   265 GPC 267
Cdd:smart00137  159 GPC 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4601-4676 1.18e-28

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: 112.05  E-value: 1.18e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  4601 KYESSSYCGLITSKEGPFANCLHVVSPNSFFDSCVFDLCALNGSQDALCDSLQSYAVACQKAGVIIPPWRNSTFCP 4676
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
1528-1713 1.82e-28

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: 114.39  E-value: 1.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1528 CSVHSDPHYHTFDGLAHTYMGNCSHLLSTICANSTLPyyEVAAANEFRGGNTHVSYVKSVSIDVNSYSIVLDKGKVVKda 1607
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDF--SFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVL-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 1608 rshmeiqnmpenhklkktkperrkcecsseVNGKVQQLPVTL-KSDINITFSGQ-YVMVSTDFGLRVKYDGNHRVEVTLP 1685
Cdd:pfam00094   77 ------------------------------VNGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLS 126
                          170       180
                   ....*....|....*....|....*...
gi 2119003705 1686 SKFKGNVFGMCGNYDGNKTDDLLNCEGK 1713
Cdd:pfam00094  127 PSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3369-3444 2.98e-28

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: 110.89  E-value: 2.98e-28
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  3369 KYESSSYCGLITSKEGPFANCLHVVSPNSFFESCVFDLCALNGSQDTLCDSLQSYADACQKAGVIIPPWKNSTFCP 3444
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
1522-1712 4.36e-28

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: 113.65  E-value: 4.36e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1522 GETEAICSVHSDPHYHTFDGLAHTYMGNCSHLLSTICanSTLPYYEVAAANEFRGGNthVSYVKSVSIDVNSYSIVLDKG 1601
Cdd:smart00216    6 EECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC--SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDD 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  1602 kvvkdarshmeiqnmpeNHKLKktkperrkcecsseVNGKVQQLPVTLKS-DINITFSGQYVMVSTDFGL-RVKYDGNHR 1679
Cdd:smart00216   82 -----------------NGKVT--------------VNGQQVSLPYKTSDgSIQIRSSGGYLVVITSLGLiQVTFDGLTL 130
                           170       180       190
                    ....*....|....*....|....*....|...
gi 2119003705  1680 VEVTLPSKFKGNVFGMCGNYDGNKTDDLLNCEG 1712
Cdd:smart00216  131 LSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2143-2217 2.36e-27

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: 108.20  E-value: 2.36e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2143 KYESSSYCGLITSKEGPFANCLHVVGPDSFFESCVFDLCALNGSQTALCDSLQSYADACQKAGVIVPPWRNSTFC 2217
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4215-4288 6.88e-27

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: 107.04  E-value: 6.88e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705  4215 ESNSYCGIITDTNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVTIETWRNQTFCP 4288
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2983-3056 1.59e-26

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: 105.89  E-value: 1.59e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705  2983 ESNSYCGIITDTNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVIIHPWRNQTFCP 3056
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
6375-6531 3.88e-26

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: 108.26  E-value: 3.88e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  6375 GKCAITGDPHYLTFDGLSHHFQGKYTYITAASLTDIPNtlqeFSIQGKNEPMQTNNkiTYLKEISTHVYGHVVQFKQKKN 6454
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGA--TCLKSVKVELNGDEIELKDDNG 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705  6455 -VVLDGEKIKPPAQPHDG-LRIFQKATRVYLETDFGL-SVSFDGSENADITLPNTYKAKVGGLCGNFDGKYKNDFTKPDG 6531
Cdd:smart00216   84 kVTVNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
464-537 5.90e-26

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: 104.34  E-value: 5.90e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119003705   464 ESNSYCGIITDTNGPFRQCHSVIDPKDYFDDCAYDLCELNMDTGALCSNLQAYADACQSEGVTIRPWRNETFCA 537
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1752-1824 1.53e-25

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: 103.19  E-value: 1.53e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119003705  1752 QSNSYCGIITDTNGPFKQCHSVIDPKDYFNDCAYDLCALNMDTGALCSNLQAYADACQSKGVTIEPWRNQTFC 1824
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
883-951 4.30e-25

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: 101.69  E-value: 4.30e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  883 YCGIITKaDGHFAVCHSVVNPSSFFDSCVFDLCALNGDRQRLCNALETYAHACQSAGVSIPPWRNETFC 951
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1756-1824 1.28e-24

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: 100.15  E-value: 1.28e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 1756 YCGIITDtNGPFKQCHSVIDPKDYFNDCAYDLCALNMDTGALCSNLQAYADACQSKGVTIEPWRNQTFC 1824
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2987-3055 1.45e-24

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: 100.15  E-value: 1.45e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 2987 YCGIITDtNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVIIHPWRNQTFC 3055
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
5898-5965 1.49e-24

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: 100.49  E-value: 1.49e-24
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  5898 CGMIKDPTGVFKDCHAVIPPENFFENCVIDFCASSGDSVSLCYALQSYASMCAEAGICV-AWRNSTFCP 5965
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
4219-4287 3.01e-24

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: 98.99  E-value: 3.01e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 4219 YCGIITDtNGPFKQCHSVIDPKDYFDDCAYDLCELNMDSGALCSNLQAYADACQSKGVTIETWRNQTFC 4287
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
468-536 3.48e-24

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: 98.99  E-value: 3.48e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705  468 YCGIITDtNGPFRQCHSVIDPKDYFDDCAYDLCELNMDTGALCSNLQAYADACQSEGVTIRPWRNETFC 536
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
4607-4675 1.46e-23

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: 97.07  E-value: 1.46e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 4607 YCGLITSKeGPFANCLHVVSPNSFFDSCVFDLCALNGSQDALCDSLQSYAVACQKAGVIIPPWRNSTFC 4675
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2149-2217 2.56e-23

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: 96.68  E-value: 2.56e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 2149 YCGLITSKeGPFANCLHVVGPDSFFESCVFDLCALNGSQTALCDSLQSYADACQKAGVIVPPWRNSTFC 2217
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
3375-3443 6.14e-23

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: 95.52  E-value: 6.14e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 3375 YCGLITSKeGPFANCLHVVSPNSFFESCVFDLCALNGSQDTLCDSLQSYADACQKAGVIIPPWKNSTFC 3443
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
2525-2599 7.51e-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: 95.49  E-value: 7.51e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  2525 EQAAAEHCKIVLDSNGPFAECHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYVAACEEAGVDLGDWRKDTVC 2599
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
3750-3824 1.08e-22

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: 95.10  E-value: 1.08e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  3750 EQAAEEHCRIVLDSNGPFVNCHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYAAACEEAGVDLGDWRKDTVC 3824
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
4983-5057 5.42e-22

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: 93.17  E-value: 5.42e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  4983 EQAATEHCRIVSDSNGPFAKCHGHISPELYFVSCVYDQCATNGSSEQLCNALESYAATCEEAGVDLGDWRKDTVC 5057
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
2531-2599 2.76e-21

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: 90.90  E-value: 2.76e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 2531 HCKIVLDSnGPFAECHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYVAACEEAGVDLGDWRKDTVC 2599
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
1263-1331 2.96e-21

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: 90.52  E-value: 2.96e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 1263 QCQIIMaSNGPFGSCHWYIPPQLYFESCVFDFCATNGSLEYFCSALESYATACAAAGVHVGDWKKETFC 1331
Cdd:pfam08742    1 KCGLLS-DSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
1257-1331 1.57e-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: 88.94  E-value: 1.57e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  1257 EPEATLQCQIIMASNGPFGSCHWYIPPQLYFESCVFDFCATNGSLEYFCSALESYATACAAAGVHVGDWKKETFC 1331
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
4989-5057 1.59e-20

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: 88.59  E-value: 1.59e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 4989 HCRIVSDSnGPFAKCHGHISPELYFVSCVYDQCATNGSSEQLCNALESYAATCEEAGVDLGDWRKDTVC 5057
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
3756-3824 1.92e-20

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: 88.21  E-value: 1.92e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 3756 HCRIVLDSnGPFVNCHWHIPPQLYFDSCVYDQCATNGSSEQLCNALESYAAACEEAGVDLGDWRKDTVC 3824
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
6587-6658 2.32e-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: 88.55  E-value: 2.32e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119003705  6587 GTDYCGSLINPKGPFRACHNVFPPDAYLENCLYDLCAAFDNIALLCTNLEQYALTCQSEGVTLENWRKGTIC 6658
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
5898-5964 8.43e-20

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: 86.67  E-value: 8.43e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 5898 CGMIKDpTGVFKDCHAVIPPENFFENCVIDFCASSGDSVSLCYALQSYASMCAEAGICVA-WRNSTFC 5964
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
6283-6348 1.78e-19

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: 85.51  E-value: 1.78e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119003705 6283 QCNVLLSN-AFVPCHSLVDPDLFIESCVYDMCKYDGKQSTLCDIVQAYVDICKNEGVTI-HWRNSTFC 6348
Cdd:pfam08742    1 KCGLLSDSgPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
6281-6348 9.66e-19

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: 83.93  E-value: 9.66e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119003705  6281 KAQCNVLLSN--AFVPCHSLVDPDLFIESCVYDMCKYDGKQSTLCDIVQAYVDICKNEGVTIH-WRNSTFC 6348
Cdd:smart00832    5 CSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
6590-6658 2.08e-18

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: 82.43  E-value: 2.08e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119003705 6590 YCGsLINPKGPFRACHNVFPPDAYLENCLYDLCAAFDNIALLCTNLEQYALTCQSEGVTLENWRKGTIC 6658
Cdd:pfam08742    1 KCG-LLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
1828-1881 1.17e-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: 76.97  E-value: 1.17e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 1828 CKPKSHYKQCGPACPATCANPNAPSSCSLPCVEGCICDSGYML-YHDQCVPSTQC 1881
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
3059-3112 1.70e-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: 76.59  E-value: 1.70e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3059 CKPNSHYEHCGHACPATCANPNSPSSCSLPCVEGCICNSGYML-YHDQCVPSTQC 3112
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
4291-4344 3.56e-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: 75.82  E-value: 3.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4291 CKPNSHYEQCGSACPATCMNPNAPSTCSLPCVESCVCDSGYML-YHDRCVPNTQC 4344
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
567-620 5.26e-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: 75.43  E-value: 5.26e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  567 CKPNTHYQQCGPACPATCTNPNAPSSCSLPCVEDCVCDSGYLL-YHDRCVPSTQC 620
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
955-1008 1.41e-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: 73.89  E-value: 1.41e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  955 CPSNSHYNVCGSACPATCTDMSAPNNCSKPCVEGCHCDHEFVLS-GQTCVSVHDC 1008
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3059-3112 2.39e-15

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: 73.58  E-value: 2.39e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3059 CKPNSHYEHCGHACPATCANPNSPSSCSLPCVEGCICNSGYML-YHDQCVPSTQC 3112
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
567-620 1.06e-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: 71.65  E-value: 1.06e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  567 CKPNTHYQQCGPACPATCTNPNAPSSCSLPCVEDCVCDSGYLL-YHDRCVPSTQC 620
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
4291-4344 1.75e-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: 70.88  E-value: 1.75e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 4291 CKPNSHYEQCGSACPATCMNPNAPSTCSLPCVESCVCDSGYML-YHDRCVPNTQC 4344
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
1828-1881 1.82e-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: 70.88  E-value: 1.82e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 1828 CKPKSHYKQCGPACPATCANPNAPSSCSLPCVEGCICDSGYML-YHDQCVPSTQC 1881
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRnSGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
3447-3500 1.85e-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: 70.81  E-value: 1.85e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3447 CPDNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDTGFVLS-GSTCVNVADC 3500
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
5968-6021 3.89e-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: 70.04  E-value: 3.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 5968 CPAGSHYENCATGCPATCANTSPPSSCNASPAEGCICDDGYILS-GNKCVQQSDC 6021
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
6662-6715 5.86e-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: 69.27  E-value: 5.86e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 6662 CPLNSKYDMCTSACPATCGDLTAPSECDLPCLEGCECLPGYVMS-GFDCVPYKEC 6715
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
955-1008 6.52e-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: 69.34  E-value: 6.52e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705  955 CPSNSHYNVCGSACPATCTDMSAPNNCSKPCVEGCHCDHEFVLS-GQTCVSVHDC 1008
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
2224-2275 2.74e-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: 67.34  E-value: 2.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 2224 PNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDSGFVLS-GNTCVNVADC 2275
Cdd:cd19941      3 PNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
4682-4733 4.25e-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: 66.96  E-value: 4.25e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4682 PNSHYEPCSSACPATCLDQFAPLNCSKPCVEACECDSGFVLS-GSTCVNVADC 4733
Cdd:cd19941      3 PNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
3447-3500 7.20e-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: 66.26  E-value: 7.20e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 3447 CPDNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDTGFVLS-GSTCVNVADC 3500
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
5968-6021 8.84e-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: 66.26  E-value: 8.84e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 5968 CPAGSHYENCATGCPATCANTSPPSSCNASPAEGCICDDGYILS-GNKCVQQSDC 6021
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
4682-4733 5.76e-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: 63.95  E-value: 5.76e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4682 PNSHYEPCSSACPATCLDQFAPLNCSKPCVEACECDSGFVLS-GSTCVNVADC 4733
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
6662-6715 6.67e-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: 63.56  E-value: 6.67e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2119003705 6662 CPLNSKYDMCTSACPATCGDLTAPSECDLPCLEGCECLPGYVMSGFD-CVPYKEC 6715
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
2224-2275 7.65e-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: 63.56  E-value: 7.65e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 2224 PNSHYEPCSSACPATCLDQFAPHNCSKPCVEACECDSGFVLS-GNTCVNVADC 2275
Cdd:pfam01826    3 ANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
6023-6078 5.13e-10

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: 58.08  E-value: 5.13e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705 6023 CVDGDNNYYTVGESWYSyDNCTERCTCnSNNNITCQQWECGLLESCKIQDGVLGCY 6078
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
6717-6770 3.05e-05

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: 44.60  E-value: 3.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 6717 CMYENKYYEVGEHFITEDCSQSCVCTeSSSVSCEKNQCKLEELCATSNFVRGCY 6770
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
3114-3169 5.71e-05

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: 43.83  E-value: 5.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705 3114 CWQDGKHYPVGsEFWTDDSCSTKCRCPsaGSKLECFPASCPTGHYCGIKNGVPGCY 3169
Cdd:pfam12714    2 KDAQGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
5173-5374 1.14e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 47.59  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5173 TTSVDNVINTPHITSVTLQTSTHAASPSTSSPSGETKTTTKAPVTdiftsatsPSTSPSTSIPPVITSGigktTAKPDIE 5252
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT--------TTAILSTNTTTVTSTG----TTVTPVP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5253 TTSADNVINTphITSVTLQTSTHAaspstsspsgETKTTTKAPVTDiftsatspstspstsippiitsgiGKTTAKPdiE 5332
Cdd:PHA03255    93 TTSNASTINV--TTKVTAQNITAT----------EAGTGTSTGVTS------------------------NVTTRSS--S 134
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2119003705 5333 TTSAdniinTPHITLVTlqtsTHAPSPST-SPSGETKTTTKAP 5374
Cdd:PHA03255   135 TTSA-----TTRITNAT----TLAPTLSSkGTSNATKTTAELP 168
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
4735-4788 1.18e-04

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: 43.06  E-value: 1.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 4735 CWYQGKYYEKNEITMTENCEQQCKCLGNNdMHCTPTSCEPDKICKVKDGVLDCV 4788
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
5253-5453 1.63e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 47.21  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5253 TTSADNVINTPHITSVTLQTSTHAASPSTSSPSGETKTTTKAPVTdiftsatspstspstsippiitsgigkTTAkpdie 5332
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT---------------------------TTA----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5333 ttsadniINTPHITLVTLQTSTHAPSPSTSPSGETKTTTKAPVTDIftsatspstssstsipPIITSGIGKTTAKPDIET 5412
Cdd:PHA03255    73 -------ILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTAQNI----------------TATEAGTGTSTGVTSNVT 129
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2119003705 5413 TSADNIIN-TPHITLVTlqtsTHAPSPST-SPSGETKTTTKAP 5453
Cdd:PHA03255   130 TRSSSTTSaTTRITNAT----TLAPTLSSkGTSNATKTTAELP 168
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
2277-2330 6.41e-04

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: 41.14  E-value: 6.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 2277 CWYQGKYYEKHEDTMTENCEQQCQCSGNNdMNCTPTSCEPDKICKVEDGTLGCF 2330
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
3502-3555 6.41e-04

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: 41.14  E-value: 6.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2119003705 3502 CWYQGKYYEKHEDTMTENCEQQCQCSGNNdMNCTPTSCEPDKICKVEDGTLGCF 3555
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
4349-4401 1.06e-03

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: 40.36  E-value: 1.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119003705 4349 DGKHYPVGsEFWTDDSCSTKCSCPsrGGQLACVNASCPKDHYCGINNGVPGCY 4401
Cdd:pfam12714    5 QGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
622-677 1.46e-03

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: 39.98  E-value: 1.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119003705  622 CWQDGKHYPVGsEFWTDDSCSTKCSCPsrGSQLVCVNASCPKDHYCGINNGVPGCY 677
Cdd:pfam12714    2 KDAQGNYIPAG-KTWFSSGCTQSCTCT--GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
5571-5706 2.11e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 43.74  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5571 TTSADNIINTPHITSVTLQTSTHAASPSASSQSGETKTTTKAPVTdifTSATSPSISPSTSIPPiitsgigktTAKPDIE 5650
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT---TTAILSTNTTTVTSTG---------TTVTPVP 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119003705 5651 TTSADNVINTphITSVTLQTSTHA------ASPSTSSQSGETKTTTKAPVTDHHVCTASGDP 5706
Cdd:PHA03255    93 TTSNASTINV--TTKVTAQNITATeagtgtSTGVTSNVTTRSSSTTSATTRITNATTLAPTL 152
PHA03255 PHA03255
BDLF3; Provisional
5491-5693 3.41e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.97  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5491 TTSADNIINTPHITSVTLQTSTHAASPSTSSPSGETKTTTKEPVTdiftsatsPSTSPSTSIPPIITSGigktTAMPDIE 5570
Cdd:PHA03255    25 TSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPIT--------TTAILSTNTTTVTSTG----TTVTPVP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119003705 5571 TTSADNIINTphITSVTLQTSTHAaspsassqsgETKTTTKAPVTDIFTSatspsispstsippiitsgigKTTAkpdie 5650
Cdd:PHA03255    93 TTSNASTINV--TTKVTAQNITAT----------EAGTGTSTGVTSNVTT---------------------RSSS----- 134
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2119003705 5651 TTSAdnvinTPHITSVTlqtsTHAASPSTSSQSGETKTTTKAP 5693
Cdd:PHA03255   135 TTSA-----TTRITNAT----TLAPTLSSKGTSNATKTTAELP 168
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
1013-1063 9.79e-03

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: 37.67  E-value: 9.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2119003705 1013 NGKYHEKGHTFWEENCEHKCTCYGNNhLNCTAAKCESNEICKVQNGEWGCH 1063
Cdd:pfam12714    5 QGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
 
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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