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Conserved domains on  [gi|1387715659|gb|PWA14817|]
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hypothetical protein CCH79_00014482 [Gambusia affinis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 410-562 5.94e-46

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: 162.93  E-value: 5.94e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  410 CVVSGDPHYNTFDKKFYSFMGTCTYTLARTCKNNTGPWFSVEAKNEERGGPGlSYLRKLYITVNGITVTLMKSRRTLVNG 489
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  490 VRVALPHSPS-PLMSISLAGQ-YVTLETTFGLRVRWDGNHYAQISVPSSYYDQMCGLCGDYDGNPNNDFAKPDGS 562
Cdd:pfam00094   80 QKVSLPYKSDgGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1183-1335 1.00e-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: 147.90  E-value: 1.00e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659 1183 CHVAGDPHYYTFDGVMHTFMGTCTYTLVEVCNSSMVTPFKVVAKNEERGQPEAsYVRYVKIYLPhDTVVELQKGRRVLLN 1262
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVG-DLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387715659 1263 GRRVRTPLTVDAPGAKVITSG-SYLLLDTNFGLQVKFDGVHHLEITIPGEYFNKVCGMCGNYNHNSSDDNLMPD 1335
Cdd:pfam00094   79 GQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 796-950 1.20e-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: 147.90  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  796 CSVSGDPHYTTFDKKTHNYMGACSYTLTKPCNESSgLPYFTVDTMNEHRGSNKKvsYVRAVVINVNDVTFILGKGRKVQV 875
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP-DFSFSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659  876 NGTLVVPPVTS-ISGVQIYLSGK-FVVLETSFGLRVRFDGNHHADVSVPTSYNGLLCGMCGNFNGEPKDDNLKPDNT 950
Cdd:pfam00094   78 NGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 80-239 1.22e-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: 133.66  E-value: 1.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   80 CDFNrdsEPFCSFTQDASDNSDWTRHKGSTPTPGTGPPGDYPDGNGYYIYHECDNVANGQKARLLSPVISSPASKICVHF 159
Cdd:cd06263      1 CDFE---DGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  160 RYYMYGSDaNNVLKVLSKTSAGENE--VWKKTGIQSPSWLGDSITVSKASSESvTIVFEAQRGLTSFCDSALDNIVITEG 237
Cdd:cd06263     78 WYHMYGSG-VGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPF-QVVFEGVRGSGSRGDIALDDISLSPG 155


                   ..
gi 1387715659  238 GC 239
Cdd:cd06263    156 PC 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1571-1725 1.15e-29

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: 116.32  E-value: 1.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659 1571 CSITGDPHHKTFDGFNHHFQGAHTYILTRShnlLDSQVPLLVRGKNLRRGGNKKISFLDQMYVDVYGVNVRFLQKKVILV 1650
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD---CSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1651 NGERVTPPLSPVRGLTITMNS--KEVQLSTDFGLTVRFDGNIRGEIELPSTYRHSVRGLCGNYDGITRNEYMKPDGT 1725
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 604-676 3.03e-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: 112.05  E-value: 3.03e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387715659   604 KPDKCGKITDPAGPFRDCIAVVDPTSFFRSCVYDMCQFNGQQHVLCDQLQAYTDACQSAGATVHQWRTPDFCP 676
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 994-1061 7.80e-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: 108.20  E-value: 7.80e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659   994 CGMITDPNGIFKPCHSVVPPESFFENCVYDLCATGGQTVALCQAIESYADMCAAAGVPIH-WRDNTFCP 1061
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 246-399 7.21e-24

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: 99.76  E-value: 7.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  246 CDFDTPgnLCRWTvhNDNPLVYGFFQYSGPTETEGTGPDDDFSkPGLGEYMLLDSSEAIPGESSQLRSPVIPFTSG--Cl 323
Cdd:cd06263      1 CDFEDG--LCGWT--QDSTDDFDWTRVSGSTPSPGTPPDHTHG-TGSGHYLYVESSSGREGQKARLLSPLLPPPRSshC- 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659  324 eLSFHYYLYGtSTTMEIRVHAI-KGGNLGNPLFTVTGNQGQGWKPAEVRLKGTGN-IQFVIVGKYGETPQTDVAVDAV 399
Cdd:cd06263     75 -LSFWYHMYG-SGVGTLNVYVReEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDI 150
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1380-1449 2.90e-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: 95.10  E-value: 2.90e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387715659  1380 SSQCAAVIMSD-RFKPCHALVPPEVFLDNCIYDMCEYDGMQTTLCDNVEAYAQACQSAGVTIS-WRNNTFCP 1449
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1064-1119 8.56e-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: 70.42  E-value: 8.56e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1064 CPAGSHYEPCASACPqPSCQDPAGPGgSCSHPCVEGCVCNEGLVLS-GDKCVPLSEC 1119
Cdd:cd19941      1 CPPNEVYSECGSACP-PTCANPNAPP-PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1452-1507 3.02e-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: 68.88  E-value: 3.02e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659 1452 CPTNSHYSDCTPPCPPTCSDL-FPIFChlpPTTCVEGCQCNAGYVLS-DDKCVPLDKC 1507
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPnAPPPC---TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 679-732 4.96e-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: 68.18  E-value: 4.96e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  679 CPPNSSYSLCVSSCPETCLGAAGPPGCEDVCVEGCECNPGFILSDD-RCVALKDC 732
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1867-1921 1.95e-12

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 1.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1867 CGANSSYSQCMTACPSSCADLAAPSECdITSCVEGCQCASGFVMSE-GICVPYPKC 1921
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1121-1176 8.22e-12

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: 61.94  E-value: 8.22e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1121 CTDEDGKYRPVGDAWFTeTDCSERCKCNGNhNVTCEPWRCSPAQECKVVEGVLGCH 1176
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTCTGG-NIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 734-789 3.55e-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: 57.31  E-value: 3.55e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659  734 CLDASGTYYPVGEDWYLEGCEQKCECqEGGLLQCYNTSCRPGTEsCQLHDGRYECR 789
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTV-CKDNDGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1788-1833 1.92e-08

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: 53.11  E-value: 1.92e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  1788 KKCGALSDPEGPFEACHDTVEPRPYQD-------------------YEAYATACQEAGVKLGAWR 1833
Cdd:smart00832    6 SQCGILLSPRGPFAACHSVVDPEPFFEncvydtcacggdceclcdaLAAYAAACAEAGVCISPWR 70
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1509-1564 7.43e-07

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 47.68  E-value: 7.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1509 CVDSDGEYHDVGDSWLTDKCSESCTCnLGGGITCKSHSCNSNSVCaLDKNGDLYCQ 1564
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVC-KDNDGSSNCH 54
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1923-1975 9.78e-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: 41.91  E-value: 9.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387715659 1923 CTFLNRYYPLNEKFVTEDCSQSCDCTSRGAVCQPKSCQEGYLCTIFDLKRDCF 1975
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1980-2011 4.68e-04

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


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.29  E-value: 4.68e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1387715659 1980 CLSYPCLNGGTCVaANNNTYTCTCQEGFHGDN 2011
Cdd:pfam00008    1 CAPNPCSNGGTCV-DTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 410-562 5.94e-46

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: 162.93  E-value: 5.94e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  410 CVVSGDPHYNTFDKKFYSFMGTCTYTLARTCKNNTGPWFSVEAKNEERGGPGlSYLRKLYITVNGITVTLMKSRRTLVNG 489
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  490 VRVALPHSPS-PLMSISLAGQ-YVTLETTFGLRVRWDGNHYAQISVPSSYYDQMCGLCGDYDGNPNNDFAKPDGS 562
Cdd:pfam00094   80 QKVSLPYKSDgGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1183-1335 1.00e-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: 147.90  E-value: 1.00e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659 1183 CHVAGDPHYYTFDGVMHTFMGTCTYTLVEVCNSSMVTPFKVVAKNEERGQPEAsYVRYVKIYLPhDTVVELQKGRRVLLN 1262
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVG-DLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387715659 1263 GRRVRTPLTVDAPGAKVITSG-SYLLLDTNFGLQVKFDGVHHLEITIPGEYFNKVCGMCGNYNHNSSDDNLMPD 1335
Cdd:pfam00094   79 GQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 796-950 1.20e-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: 147.90  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  796 CSVSGDPHYTTFDKKTHNYMGACSYTLTKPCNESSgLPYFTVDTMNEHRGSNKKvsYVRAVVINVNDVTFILGKGRKVQV 875
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP-DFSFSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659  876 NGTLVVPPVTS-ISGVQIYLSGK-FVVLETSFGLRVRFDGNHHADVSVPTSYNGLLCGMCGNFNGEPKDDNLKPDNT 950
Cdd:pfam00094   78 NGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 400-561 9.32e-39

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: 142.93  E-value: 9.32e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   400 CIKSCTGSQdCVVSGDPHYNTFDKKFYSFMGTCTYTLARTCKNNtgPWFSVEAKNEERGGpGLSYLRKLYITVNGITVTL 479
Cdd:smart00216    3 CTQEECSPT-CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCGG-GATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   480 MKSRRT-LVNGVRVALPHSPS-PLMSISLAGQYVTLETTFGL-RVRWDGNHYAQISVPSSYYDQMCGLCGDYDGNPNNDF 556
Cdd:smart00216   79 KDDNGKvTVNGQQVSLPYKTSdGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1387715659   557 AKPDG 561
Cdd:smart00216  159 RTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1175-1335 4.22e-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: 135.22  E-value: 4.22e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  1175 CHSTGkGVCHVAGDPHYYTFDGVMHTFMGTCTYTLVEVCNSSMvtPFKVVAKNEERGQpEASYVRYVKIYLPHDTVVELQ 1254
Cdd:smart00216    5 QEECS-PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP--TFSVLLKNVPCGG-GATCLKSVKVELNGDEIELKD 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  1255 KGRRVLLNGRRVRTPLTVDAPGAKVITSGSYLLLDTNFGL-QVKFDGVHHLEITIPGEYFNKVCGMCGNYNHNSSDDNLM 1333
Cdd:smart00216   81 DNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRT 160


                    ..
gi 1387715659  1334 PD 1335
Cdd:smart00216  161 PD 162
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 80-239 1.22e-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: 133.66  E-value: 1.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   80 CDFNrdsEPFCSFTQDASDNSDWTRHKGSTPTPGTGPPGDYPDGNGYYIYHECDNVANGQKARLLSPVISSPASKICVHF 159
Cdd:cd06263      1 CDFE---DGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  160 RYYMYGSDaNNVLKVLSKTSAGENE--VWKKTGIQSPSWLGDSITVSKASSESvTIVFEAQRGLTSFCDSALDNIVITEG 237
Cdd:cd06263     78 WYHMYGSG-VGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPF-QVVFEGVRGSGSRGDIALDDISLSPG 155


                   ..
gi 1387715659  238 GC 239
Cdd:cd06263    156 PC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 794-949 4.75e-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: 132.14  E-value: 4.75e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   794 GICSVSGDPHYTTFDKKTHNYMGACSYTLTKPCNESsglPYFTVDTMNEHRGSNkkVSYVRAVVINVNDVT-FILGKGRK 872
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGG--ATCLKSVKVELNGDEiELKDDNGK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659   873 VQVNGTLV-VPPVTSISGVQIYLSGKFVVLETSFGL-RVRFDGNHHADVSVPTSYNGLLCGMCGNFNGEPKDDNLKPDN 949
Cdd:smart00216   85 VTVNGQQVsLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 80-239 1.05e-31

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: 122.47  E-value: 1.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   80 CDFnrDSEPFCSFTQDASDNSDWTRHKGSTPTPGTGPPGDYPDGNGYYIYHECDNVANGQKARLLSPVISSPASKICVHF 159
Cdd:pfam00629    1 CDF--EDGNLCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  160 RYYMYGSDANNvLKVLSKTSAGENE--VWKKTGIQSPSWLGDSITVSKaSSESVTIVFEAQRGLTSFCDSALDNIVITEG 237
Cdd:pfam00629   79 WYHMSGSGVGT-LRVYVRENGGTLDtlLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ..
gi 1387715659  238 GC 239
Cdd:pfam00629  157 PC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 79-239 8.25e-31

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: 119.76  E-value: 8.25e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659    79 SCDFnrDSEPFCSFTQDASDNSDWTRhkGSTPTPGTGPPGDYPDGNGYYIYHECDNVANGQKARLLSPVISSPASKICVH 158
Cdd:smart00137    5 NCDF--EEGSTCGWHQDSNDDGHWER--VSSATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   159 FRYYMYGSDANNvLKVLSKTSAGE--NEVWKKTGIQSPSWLGDSITVSKaSSESVTIVFEAQRGLTSFCDSALDNIVITE 236
Cdd:smart00137   81 FWYYMYGSGSGT-LNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1387715659   237 GGC 239
Cdd:smart00137  159 GPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1571-1725 1.15e-29

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: 116.32  E-value: 1.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659 1571 CSITGDPHHKTFDGFNHHFQGAHTYILTRShnlLDSQVPLLVRGKNLRRGGNKKISFLDQMYVDVYGVNVRFLQKKVILV 1650
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD---CSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1651 NGERVTPPLSPVRGLTITMNS--KEVQLSTDFGLTVRFDGNIRGEIELPSTYRHSVRGLCGNYDGITRNEYMKPDGT 1725
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 604-676 3.03e-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: 112.05  E-value: 3.03e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387715659   604 KPDKCGKITDPAGPFRDCIAVVDPTSFFRSCVYDMCQFNGQQHVLCDQLQAYTDACQSAGATVHQWRTPDFCP 676
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 994-1061 7.80e-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: 108.20  E-value: 7.80e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659   994 CGMITDPNGIFKPCHSVVPPESFFENCVYDLCATGGQTVALCQAIESYADMCAAAGVPIH-WRDNTFCP 1061
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1570-1724 2.66e-24

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: 101.32  E-value: 2.66e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  1570 RCSITGDPHHKTFDGFNHHFQGAHTYILTRSHnllDSQVPLLVRGKNLRRGGNkkISFLDQMYVDVYGVNVRFLQK-KVI 1648
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDDnGKV 85

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659  1649 LVNGERVTPPL-SPVRGLTITMNSKEVQLSTDFGL-TVRFDGNIRGEIELPSTYRHSVRGLCGNYDGITRNEYMKPDG 1724
Cdd:smart00216   86 TVNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 994-1060 5.97e-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: 96.68  E-value: 5.97e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659  994 CGMITDpNGIFKPCHSVVPPESFFENCVYDLCATGGQTVALCQAIESYADMCAAAGVPI-HWRDNTFC 1060
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 246-399 7.21e-24

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: 99.76  E-value: 7.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  246 CDFDTPgnLCRWTvhNDNPLVYGFFQYSGPTETEGTGPDDDFSkPGLGEYMLLDSSEAIPGESSQLRSPVIPFTSG--Cl 323
Cdd:cd06263      1 CDFEDG--LCGWT--QDSTDDFDWTRVSGSTPSPGTPPDHTHG-TGSGHYLYVESSSGREGQKARLLSPLLPPPRSshC- 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659  324 eLSFHYYLYGtSTTMEIRVHAI-KGGNLGNPLFTVTGNQGQGWKPAEVRLKGTGN-IQFVIVGKYGETPQTDVAVDAV 399
Cdd:cd06263     75 -LSFWYHMYG-SGVGTLNVYVReEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDI 150
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 607-675 1.45e-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: 95.91  E-value: 1.45e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659  607 KCGKITDpAGPFRDCIAVVDPTSFFRSCVYDMCQFNGQQHVLCDQLQAYTDACQSAGATVHQWRTPDFC 675
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1380-1449 2.90e-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: 95.10  E-value: 2.90e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387715659  1380 SSQCAAVIMSD-RFKPCHALVPPEVFLDNCIYDMCEYDGMQTTLCDNVEAYAQACQSAGVTIS-WRNNTFCP 1449
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1382-1448 7.24e-22

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 90.90  E-value: 7.24e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659 1382 QCAAVIMSDRFKPCHALVPPEVFLDNCIYDMCEYDGMQTTLCDNVEAYAQACQSAGVTI-SWRNNTFC 1448
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 246-399 2.76e-19

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: 86.65  E-value: 2.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  246 CDFDTpGNLCRWTvhNDNPLVYGFFQYSGPTEteGTGPDDDFSK-PGLGEYMLLDSSEAIPGESSQLRSPVIPFTSGCLE 324
Cdd:pfam00629    1 CDFED-GNLCGWT--QDSSDDFDWERVSGPSV--KTGPSSDHTQgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQC 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659  325 LSFHYYLYGTSTTmEIRVHA-IKGGNLGNPLFTVTGNQGQGWKPAEVRL-KGTGNIQFVIVGKYGETPQTDVAVDAV 399
Cdd:pfam00629   76 LRFWYHMSGSGVG-TLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDI 151
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 243-397 2.80e-18

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: 83.93  E-value: 2.80e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   243 DFECDFDTpGNLCRWtvHNDNPLVYGFFQYSGptETEGTGPDDDfSKPGLGEYMLLDSSEAIPGESSQLRSPVIPFTSGC 322
Cdd:smart00137    3 PGNCDFEE-GSTCGW--HQDSNDDGHWERVSS--ATGIPGPNRD-HTTGNGHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659   323 LELSFHYYLYG-TSTTMEIRVHAiKGGNLGNPLFTVTGNQGQGWKPAEVRL-KGTGNIQFVIVGKYGETPQTDVAVD 397
Cdd:smart00137   77 HCLTFWYYMYGsGSGTLNVYVRE-NNGSQDTLLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALD 152
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1064-1119 8.56e-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: 70.42  E-value: 8.56e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1064 CPAGSHYEPCASACPqPSCQDPAGPGgSCSHPCVEGCVCNEGLVLS-GDKCVPLSEC 1119
Cdd:cd19941      1 CPPNEVYSECGSACP-PTCANPNAPP-PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1064-1119 2.21e-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: 2.21e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1064 CPAGSHYEPCASACPqPSCQDPAGPGGsCSHPCVEGCVCNEGLVLS-GDKCVPLSEC 1119
Cdd:pfam01826    1 CPANEVYSECGSACP-PTCANLSPPDV-CPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1452-1507 3.02e-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: 68.88  E-value: 3.02e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659 1452 CPTNSHYSDCTPPCPPTCSDL-FPIFChlpPTTCVEGCQCNAGYVLS-DDKCVPLDKC 1507
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPnAPPPC---TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 679-732 4.96e-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: 68.18  E-value: 4.96e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  679 CPPNSSYSLCVSSCPETCLGAAGPPGCEDVCVEGCECNPGFILSDD-RCVALKDC 732
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 679-732 7.77e-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: 67.73  E-value: 7.77e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  679 CPPNSSYSLCVSSCPETCLGAAGPPGCEDVCVEGCECNPGFILS-DDRCVALKDC 732
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1452-1507 1.04e-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: 67.41  E-value: 1.04e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659 1452 CPTNSHYSDCTPPCPPTCSDLF-PIFCHLPpttCVEGCQCNAGYVLSDD-KCVPLDKC 1507
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSpPDVCPEP---CVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1867-1921 1.95e-12

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 1.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1867 CGANSSYSQCMTACPSSCADLAAPSECdITSCVEGCQCASGFVMSE-GICVPYPKC 1921
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1121-1176 8.22e-12

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: 61.94  E-value: 8.22e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1121 CTDEDGKYRPVGDAWFTeTDCSERCKCNGNhNVTCEPWRCSPAQECKVVEGVLGCH 1176
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTCTGG-NIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1867-1921 1.47e-10

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: 58.55  E-value: 1.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1867 CGANSSYSQCMTACPSSCADLAAPSECDiTSCVEGCQCASGFVMS-EGICVPYPKC 1921
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 734-789 3.55e-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: 57.31  E-value: 3.55e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659  734 CLDASGTYYPVGEDWYLEGCEQKCECqEGGLLQCYNTSCRPGTEsCQLHDGRYECR 789
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTV-CKDNDGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1788-1833 1.92e-08

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: 53.11  E-value: 1.92e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  1788 KKCGALSDPEGPFEACHDTVEPRPYQD-------------------YEAYATACQEAGVKLGAWR 1833
Cdd:smart00832    6 SQCGILLSPRGPFAACHSVVDPEPFFEncvydtcacggdceclcdaLAAYAAACAEAGVCISPWR 70
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1789-1838 2.15e-08

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: 52.77  E-value: 2.15e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659 1789 KCGALSDpEGPFEACHDTVEPRPYQD-------------------YEAYATACQEAGVKLGAWRQKLNC 1838
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEacvydmcscggddeclcaaLAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1509-1564 7.43e-07

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 47.68  E-value: 7.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1509 CVDSDGEYHDVGDSWLTDKCSESCTCnLGGGITCKSHSCNSNSVCaLDKNGDLYCQ 1564
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVC-KDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1923-1975 9.78e-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: 41.91  E-value: 9.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387715659 1923 CTFLNRYYPLNEKFVTEDCSQSCDCTSRGAVCQPKSCQEGYLCTIFDLKRDCF 1975
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1980-2011 4.68e-04

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.29  E-value: 4.68e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1387715659 1980 CLSYPCLNGGTCVaANNNTYTCTCQEGFHGDN 2011
Cdd:pfam00008    1 CAPNPCSNGGTCV-DTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1980-2013 6.99e-04

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 6.99e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1387715659 1980 CLSY-PCLNGGTCVaaN-NNTYTCTCQEGFHGDNCE 2013
Cdd:cd00054      5 CASGnPCQNGGTCV--NtVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 410-562 5.94e-46

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: 162.93  E-value: 5.94e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  410 CVVSGDPHYNTFDKKFYSFMGTCTYTLARTCKNNTGPWFSVEAKNEERGGPGlSYLRKLYITVNGITVTLMKSRRTLVNG 489
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASG-VCLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  490 VRVALPHSPS-PLMSISLAGQ-YVTLETTFGLRVRWDGNHYAQISVPSSYYDQMCGLCGDYDGNPNNDFAKPDGS 562
Cdd:pfam00094   80 QKVSLPYKSDgGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1183-1335 1.00e-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: 147.90  E-value: 1.00e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659 1183 CHVAGDPHYYTFDGVMHTFMGTCTYTLVEVCNSSMVTPFKVVAKNEERGQPEAsYVRYVKIYLPhDTVVELQKGRRVLLN 1262
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVG-DLEITLQKGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387715659 1263 GRRVRTPLTVDAPGAKVITSG-SYLLLDTNFGLQVKFDGVHHLEITIPGEYFNKVCGMCGNYNHNSSDDNLMPD 1335
Cdd:pfam00094   79 GQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 796-950 1.20e-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: 147.90  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  796 CSVSGDPHYTTFDKKTHNYMGACSYTLTKPCNESSgLPYFTVDTMNEHRGSNKKvsYVRAVVINVNDVTFILGKGRKVQV 875
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP-DFSFSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659  876 NGTLVVPPVTS-ISGVQIYLSGK-FVVLETSFGLRVRFDGNHHADVSVPTSYNGLLCGMCGNFNGEPKDDNLKPDNT 950
Cdd:pfam00094   78 NGQKVSLPYKSdGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 400-561 9.32e-39

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: 142.93  E-value: 9.32e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   400 CIKSCTGSQdCVVSGDPHYNTFDKKFYSFMGTCTYTLARTCKNNtgPWFSVEAKNEERGGpGLSYLRKLYITVNGITVTL 479
Cdd:smart00216    3 CTQEECSPT-CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCGG-GATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   480 MKSRRT-LVNGVRVALPHSPS-PLMSISLAGQYVTLETTFGL-RVRWDGNHYAQISVPSSYYDQMCGLCGDYDGNPNNDF 556
Cdd:smart00216   79 KDDNGKvTVNGQQVSLPYKTSdGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....*
gi 1387715659   557 AKPDG 561
Cdd:smart00216  159 RTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1175-1335 4.22e-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: 135.22  E-value: 4.22e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  1175 CHSTGkGVCHVAGDPHYYTFDGVMHTFMGTCTYTLVEVCNSSMvtPFKVVAKNEERGQpEASYVRYVKIYLPHDTVVELQ 1254
Cdd:smart00216    5 QEECS-PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEP--TFSVLLKNVPCGG-GATCLKSVKVELNGDEIELKD 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  1255 KGRRVLLNGRRVRTPLTVDAPGAKVITSGSYLLLDTNFGL-QVKFDGVHHLEITIPGEYFNKVCGMCGNYNHNSSDDNLM 1333
Cdd:smart00216   81 DNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRT 160


                    ..
gi 1387715659  1334 PD 1335
Cdd:smart00216  161 PD 162
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 80-239 1.22e-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: 133.66  E-value: 1.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   80 CDFNrdsEPFCSFTQDASDNSDWTRHKGSTPTPGTGPPGDYPDGNGYYIYHECDNVANGQKARLLSPVISSPASKICVHF 159
Cdd:cd06263      1 CDFE---DGLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPPRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  160 RYYMYGSDaNNVLKVLSKTSAGENE--VWKKTGIQSPSWLGDSITVSKASSESvTIVFEAQRGLTSFCDSALDNIVITEG 237
Cdd:cd06263     78 WYHMYGSG-VGTLNVYVREEGGGLGtlLWSASGGQGNQWQEAEVTLSASSKPF-QVVFEGVRGSGSRGDIALDDISLSPG 155


                   ..
gi 1387715659  238 GC 239
Cdd:cd06263    156 PC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 794-949 4.75e-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: 132.14  E-value: 4.75e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   794 GICSVSGDPHYTTFDKKTHNYMGACSYTLTKPCNESsglPYFTVDTMNEHRGSNkkVSYVRAVVINVNDVT-FILGKGRK 872
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGG--ATCLKSVKVELNGDEiELKDDNGK 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659   873 VQVNGTLV-VPPVTSISGVQIYLSGKFVVLETSFGL-RVRFDGNHHADVSVPTSYNGLLCGMCGNFNGEPKDDNLKPDN 949
Cdd:smart00216   85 VTVNGQQVsLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 80-239 1.05e-31

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: 122.47  E-value: 1.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   80 CDFnrDSEPFCSFTQDASDNSDWTRHKGSTPTPGTGPPGDYPDGNGYYIYHECDNVANGQKARLLSPVISSPASKICVHF 159
Cdd:pfam00629    1 CDF--EDGNLCGWTQDSSDDFDWERVSGPSVKTGPSSDHTQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQCLRF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  160 RYYMYGSDANNvLKVLSKTSAGENE--VWKKTGIQSPSWLGDSITVSKaSSESVTIVFEAQRGLTSFCDSALDNIVITEG 237
Cdd:pfam00629   79 WYHMSGSGVGT-LRVYVRENGGTLDtlLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISLSSG 156


                   ..
gi 1387715659  238 GC 239
Cdd:pfam00629  157 PC 158
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 79-239 8.25e-31

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: 119.76  E-value: 8.25e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659    79 SCDFnrDSEPFCSFTQDASDNSDWTRhkGSTPTPGTGPPGDYPDGNGYYIYHECDNVANGQKARLLSPVISSPASKICVH 158
Cdd:smart00137    5 NCDF--EEGSTCGWHQDSNDDGHWER--VSSATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   159 FRYYMYGSDANNvLKVLSKTSAGE--NEVWKKTGIQSPSWLGDSITVSKaSSESVTIVFEAQRGLTSFCDSALDNIVITE 236
Cdd:smart00137   81 FWYYMYGSGSGT-LNVYVRENNGSqdTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1387715659   237 GGC 239
Cdd:smart00137  159 GPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1571-1725 1.15e-29

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: 116.32  E-value: 1.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659 1571 CSITGDPHHKTFDGFNHHFQGAHTYILTRShnlLDSQVPLLVRGKNLRRGGNKKISFLDQMYVDVYGVNVRFLQKKVILV 1650
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKD---CSEEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1651 NGERVTPPLSPVRGLTITMNS--KEVQLSTDFGLTVRFDGNIRGEIELPSTYRHSVRGLCGNYDGITRNEYMKPDGT 1725
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSgfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 604-676 3.03e-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: 112.05  E-value: 3.03e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387715659   604 KPDKCGKITDPAGPFRDCIAVVDPTSFFRSCVYDMCQFNGQQHVLCDQLQAYTDACQSAGATVHQWRTPDFCP 676
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 994-1061 7.80e-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: 108.20  E-value: 7.80e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659   994 CGMITDPNGIFKPCHSVVPPESFFENCVYDLCATGGQTVALCQAIESYADMCAAAGVPIH-WRDNTFCP 1061
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1570-1724 2.66e-24

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: 101.32  E-value: 2.66e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  1570 RCSITGDPHHKTFDGFNHHFQGAHTYILTRSHnllDSQVPLLVRGKNLRRGGNkkISFLDQMYVDVYGVNVRFLQK-KVI 1648
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIELKDDnGKV 85

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659  1649 LVNGERVTPPL-SPVRGLTITMNSKEVQLSTDFGL-TVRFDGNIRGEIELPSTYRHSVRGLCGNYDGITRNEYMKPDG 1724
Cdd:smart00216   86 TVNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 994-1060 5.97e-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: 96.68  E-value: 5.97e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659  994 CGMITDpNGIFKPCHSVVPPESFFENCVYDLCATGGQTVALCQAIESYADMCAAAGVPI-HWRDNTFC 1060
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 246-399 7.21e-24

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: 99.76  E-value: 7.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  246 CDFDTPgnLCRWTvhNDNPLVYGFFQYSGPTETEGTGPDDDFSkPGLGEYMLLDSSEAIPGESSQLRSPVIPFTSG--Cl 323
Cdd:cd06263      1 CDFEDG--LCGWT--QDSTDDFDWTRVSGSTPSPGTPPDHTHG-TGSGHYLYVESSSGREGQKARLLSPLLPPPRSshC- 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659  324 eLSFHYYLYGtSTTMEIRVHAI-KGGNLGNPLFTVTGNQGQGWKPAEVRLKGTGN-IQFVIVGKYGETPQTDVAVDAV 399
Cdd:cd06263     75 -LSFWYHMYG-SGVGTLNVYVReEGGGLGTLLWSASGGQGNQWQEAEVTLSASSKpFQVVFEGVRGSGSRGDIALDDI 150
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 607-675 1.45e-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: 95.91  E-value: 1.45e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659  607 KCGKITDpAGPFRDCIAVVDPTSFFRSCVYDMCQFNGQQHVLCDQLQAYTDACQSAGATVHQWRTPDFC 675
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1380-1449 2.90e-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: 95.10  E-value: 2.90e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387715659  1380 SSQCAAVIMSD-RFKPCHALVPPEVFLDNCIYDMCEYDGMQTTLCDNVEAYAQACQSAGVTIS-WRNNTFCP 1449
Cdd:smart00832    5 CSQCGILLSPRgPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1382-1448 7.24e-22

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 90.90  E-value: 7.24e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659 1382 QCAAVIMSDRFKPCHALVPPEVFLDNCIYDMCEYDGMQTTLCDNVEAYAQACQSAGVTI-SWRNNTFC 1448
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 246-399 2.76e-19

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: 86.65  E-value: 2.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659  246 CDFDTpGNLCRWTvhNDNPLVYGFFQYSGPTEteGTGPDDDFSK-PGLGEYMLLDSSEAIPGESSQLRSPVIPFTSGCLE 324
Cdd:pfam00629    1 CDFED-GNLCGWT--QDSSDDFDWERVSGPSV--KTGPSSDHTQgTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSPQC 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659  325 LSFHYYLYGTSTTmEIRVHA-IKGGNLGNPLFTVTGNQGQGWKPAEVRL-KGTGNIQFVIVGKYGETPQTDVAVDAV 399
Cdd:pfam00629   76 LRFWYHMSGSGVG-TLRVYVrENGGTLDTLLWSISGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDI 151
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 243-397 2.80e-18

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: 83.93  E-value: 2.80e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387715659   243 DFECDFDTpGNLCRWtvHNDNPLVYGFFQYSGptETEGTGPDDDfSKPGLGEYMLLDSSEAIPGESSQLRSPVIPFTSGC 322
Cdd:smart00137    3 PGNCDFEE-GSTCGW--HQDSNDDGHWERVSS--ATGIPGPNRD-HTTGNGHFMFFETSSGAEGQTARLLSPPLYENRST 76

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659   323 LELSFHYYLYG-TSTTMEIRVHAiKGGNLGNPLFTVTGNQGQGWKPAEVRL-KGTGNIQFVIVGKYGETPQTDVAVD 397
Cdd:smart00137   77 HCLTFWYYMYGsGSGTLNVYVRE-NNGSQDTLLWSRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALD 152
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1064-1119 8.56e-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: 70.42  E-value: 8.56e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1064 CPAGSHYEPCASACPqPSCQDPAGPGgSCSHPCVEGCVCNEGLVLS-GDKCVPLSEC 1119
Cdd:cd19941      1 CPPNEVYSECGSACP-PTCANPNAPP-PCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1064-1119 2.21e-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: 2.21e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387715659 1064 CPAGSHYEPCASACPqPSCQDPAGPGGsCSHPCVEGCVCNEGLVLS-GDKCVPLSEC 1119
Cdd:pfam01826    1 CPANEVYSECGSACP-PTCANLSPPDV-CPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1452-1507 3.02e-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: 68.88  E-value: 3.02e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659 1452 CPTNSHYSDCTPPCPPTCSDL-FPIFChlpPTTCVEGCQCNAGYVLS-DDKCVPLDKC 1507
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPnAPPPC---TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 679-732 4.96e-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: 68.18  E-value: 4.96e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  679 CPPNSSYSLCVSSCPETCLGAAGPPGCEDVCVEGCECNPGFILSDD-RCVALKDC 732
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 679-732 7.77e-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: 67.73  E-value: 7.77e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  679 CPPNSSYSLCVSSCPETCLGAAGPPGCEDVCVEGCECNPGFILS-DDRCVALKDC 732
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1452-1507 1.04e-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: 67.41  E-value: 1.04e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387715659 1452 CPTNSHYSDCTPPCPPTCSDLF-PIFCHLPpttCVEGCQCNAGYVLSDD-KCVPLDKC 1507
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSpPDVCPEP---CVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1867-1921 1.95e-12

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 63.49  E-value: 1.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1867 CGANSSYSQCMTACPSSCADLAAPSECdITSCVEGCQCASGFVMSE-GICVPYPKC 1921
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1121-1176 8.22e-12

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: 61.94  E-value: 8.22e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1121 CTDEDGKYRPVGDAWFTeTDCSERCKCNGNhNVTCEPWRCSPAQECKVVEGVLGCH 1176
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTCTGG-NIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1867-1921 1.47e-10

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: 58.55  E-value: 1.47e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1867 CGANSSYSQCMTACPSSCADLAAPSECDiTSCVEGCQCASGFVMS-EGICVPYPKC 1921
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 734-789 3.55e-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: 57.31  E-value: 3.55e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659  734 CLDASGTYYPVGEDWYLEGCEQKCECqEGGLLQCYNTSCRPGTEsCQLHDGRYECR 789
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTV-CKDNDGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1788-1833 1.92e-08

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: 53.11  E-value: 1.92e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387715659  1788 KKCGALSDPEGPFEACHDTVEPRPYQD-------------------YEAYATACQEAGVKLGAWR 1833
Cdd:smart00832    6 SQCGILLSPRGPFAACHSVVDPEPFFEncvydtcacggdceclcdaLAAYAAACAEAGVCISPWR 70
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1789-1838 2.15e-08

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: 52.77  E-value: 2.15e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387715659 1789 KCGALSDpEGPFEACHDTVEPRPYQD-------------------YEAYATACQEAGVKLGAWRQKLNC 1838
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEacvydmcscggddeclcaaLAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1509-1564 7.43e-07

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 47.68  E-value: 7.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387715659 1509 CVDSDGEYHDVGDSWLTDKCSESCTCnLGGGITCKSHSCNSNSVCaLDKNGDLYCQ 1564
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVC-KDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1923-1975 9.78e-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: 41.91  E-value: 9.78e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1387715659 1923 CTFLNRYYPLNEKFVTEDCSQSCDCTSRGAVCQPKSCQEGYLCTIFDLKRDCF 1975
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1980-2011 4.68e-04

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.29  E-value: 4.68e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1387715659 1980 CLSYPCLNGGTCVaANNNTYTCTCQEGFHGDN 2011
Cdd:pfam00008    1 CAPNPCSNGGTCV-DTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1980-2013 6.99e-04

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 6.99e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1387715659 1980 CLSY-PCLNGGTCVaaN-NNTYTCTCQEGFHGDNCE 2013
Cdd:cd00054      5 CASGnPCQNGGTCV--NtVGSYRCSCPPGYTGRNCE 38
 
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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