NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1149817606|ref|XP_020137269|]
View 

zonadhesin isoform X2 [Microcebus murinus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1333-1486 1.86e-47

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: 167.55  E-value: 1.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1333 CTASGDPHYLTFDGALHHFMGTCTYVLTKPCWtKLPQNYFVVSTSNENRGGilEASFVKAVHVQIFGLKISLLKGRKVML 1412
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGA--SGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1413 NGHRVALPVWPLKGLVTLRLSGI-FVVLYTTIGLLVRYDGVHLVEVTVPSSYAGQLCGLCGNYNNNSLDDNLRPD 1486
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 948-1100 1.17e-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: 165.24  E-value: 1.17e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  948 CLVYGDPHYVTFDGRHFGFMGRCTYILTQPCGNSTDPFFRVTAVKDGWEQQGMsYLNKVYVTLPETTVTLLKGRRTLVGS 1027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1028 QQVTLPAIPSKG-VFLAASGR-FVELHTEFGLWVRWDGDQQLFVSVARTYSSKLCGLCGNYDGDMSNDHLKPDGQ 1100
Cdd:pfam00094   80 QKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 389-546 4.09e-41

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: 149.43  E-value: 4.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  389 CDFEDDDhpFCDWTQKSQDGGHWIRGHRNVPLQ--STDFPRGS---HYIYLQSDKFsQAGQSVILVSRPFCAPG-DICVE 462
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVKTgpSSDHTQGTgsgHFMYVDTSSG-APGQTARLLSPLLPPSRsPQCLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  463 FAYHMYGLGEGTtLKFLLGSPAGSTPITLWSRVGSQSPDWQNASITISSGhQQPMQLIFKATRGSSTAFVVAIDFILVSH 542
Cdd:pfam00629   78 FWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ....
gi 1149817606  543 GICR 546
Cdd:pfam00629  156 GPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 57-218 1.10e-39

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: 145.60  E-value: 1.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   57 CDFEDeskPFCDWTQVSADDGDWIRASGPSKTGTTGPLGGYPSGEGNYLHMVSKAFRRGGVARLRSPYLWV-QGPLCVRF 135
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  136 VYHMFGLSwGAQLRLLLLSSTQGQRpSVLWKHRNTQSPSWMPTAVTVPAGFAlPTQLMFEGMRGNTAYLDIALDAISIHR 215
Cdd:cd06263     78 WYHMYGSG-VGTLNVYVREEGGGLG-TLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1149817606  216 GSC 218
Cdd:cd06263    155 GPC 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1722-1875 1.74e-38

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 141.74  E-value: 1.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1722 CRVSGDARYVSFDGSEHFIRGTCAHVLMKVCHPNMNmpfFKISAKNKKLVGRPKSFHLHQVYIDIYNSQIILQNNHHVLI 1801
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1802 NGKQVTLPESSQIPGVSILSRGIH-TIVKFKLGARVTFDGRHLLEIELPTGYYGKVCGVCGNFNGEEDDELMMPS 1875
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2113-2267 1.06e-36

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 136.73  E-value: 1.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 2113 CSVFGDPHYHTFDHLSYHFMGRMTYILIKTVDVLPEGVERLLVKGRNKMHEPWspiILNEVIIIVYGYKVQLQTGLGLVV 2192
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV---CLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 2193 NDQKMAIPY-RPNEHLWVTLRGQ-RLYLVTDFELVVSFDGRRNAVISLPSTYQGLVRGLCGNYDKNHKNELMLPSGV 2267
Cdd:pfam00094   78 NGQKVSLPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 227-381 2.04e-30

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: 119.02  E-value: 2.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  227 CSFDTpnDLCGWSWIPTaTGAKWIQKKGQSGKPGMGPDDDFSsPGNGYYMLLDPRNARPRQKSVFLSPLSH---SSGCls 303
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPDHTHG-TGSGHYLYVESSSGREGQKARLLSPLLPpprSSHC-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  304 LSFHYTLWGQSPGaALHVYASVLGSIRRHTLF--SGQPKPNWQPVSVNY-TGQGQIQFTVVGVFGKIPEPAVAVDDISIA 380
Cdd:cd06263     75 LSFWYHMYGSGVG-TLNVYVREEGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                   .
gi 1149817606  381 P 381
Cdd:cd06263    154 P 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2323-2398 1.76e-22

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 93.17  E-value: 1.76e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606  2323 STQACRVLVDPLGPFAACHQTVAPEPFQEHCVLDLCSAGDpreQEEMRCQVLSAYAILCQEAGVALASWRNHTRCA 2398
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGG---DCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1529-1600 2.30e-21

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: 90.09  E-value: 2.30e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149817606  1529 WNKNCAILTDPQGPFSQCHEVVPPQASLASCVRGQCGTKGDTTALCHSLQAYASLCTQAGQAP-VWRNSTFCP 1600
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1140-1214 1.02e-20

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 88.17  E-value: 1.02e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  1140 MSGPGFCGRLVDSRGPFEACLFHLKATSFFDNCMFDMCNFQGLQQMLCAHMSAMTTSCQDAGYPMKPWREPHFCP 1214
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2051-2106 6.89e-17

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: 76.57  E-value: 6.89e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606 2051 CEDAQGGLIPPGKTWISSGCTDSCVCMGGTIQCRAFRCPSGSHCQPSSDhsNSNCA 2106
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDG--SSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1217-1270 6.54e-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: 70.81  E-value: 6.54e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1217 CPPNSKYSLCARPCPDTCHSAFSGMFCPDRCVEGCECNPGFVLSGLN-CVPQSQC 1270
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2401-2454 1.61e-12

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 64.33  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 2401 CPANTVYQSCMTPCPASCADLADPRDCEGPCVEGCASIPGYIYS-GTQSLPLAHC 2454
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 888-941 1.63e-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: 64.25  E-value: 1.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149817606  888 CFYNNYNYKTGAEWFSPNCTEYCHCwPGNQIECQSSQCGARTMCQLKNGQYGCY 941
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1603-1658 1.94e-11

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: 61.18  E-value: 1.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 1603 CPPGSSYSPCVRPCPATCLSLVAPRDCPAslPCAEGCECQKGHILS-GTSCVPFSQC 1658
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1272-1326 4.89e-11

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 60.01  E-value: 4.89e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1272 CLDSNGSYFKVGEKWHKPGCRQLCFCKDNNrIRCYSWKCKAQEICDYQDGIYGCH 1326
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1993-2049 1.17e-10

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: 58.87  E-value: 1.17e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1993 CPPHSSYTNCLPPCSPSCWDLD--GRCegvkvPSTCAEGCICQPGYVLNED-KCVPRSQC 2049
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-----TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1922-1989 3.42e-10

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: 58.16  E-value: 3.42e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606 1922 KCEAALEAPAWSQCASHLVLKPFLVSCANTLCEFGGLNHALCQALQAFGSTCESQGLKPPLWRNSSFC 1989
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2456-2509 4.68e-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: 4.68e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149817606 2456 CTSNGIYYQRGDSFVTEDCSQRCTCAHaGILLCKPFSCSVGETCTLGNLTRGCF 2509
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 837-886 1.08e-09

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 56.17  E-value: 1.08e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  837 CPLNAHYESC--ACPASCKNPR--PSCGLLCQAGCVCNPGFLFSDNG-CINASSC 886
Cdd:cd19941      1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1660-1715 7.75e-08

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: 50.77  E-value: 7.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606 1660 CIDPKGFYHLVGESWYTeSTCSWLCTCSiHNNITCFQTTCKPNQMCWSLDGVLRCR 1715
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 469-836 1.26e-07

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 56.89  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  469 GLGEGTTLKfLLGSPAGSTPITlwsrVGSQSPdwqnasiTISSGhqqPMQLIFKATRGSstafvvaidfilvshgICRA- 547
Cdd:pfam17823  105 GAADGAASR-ALAAAASSSPSS----AAQSLP-------AAIAA---LPSEAFSAPRAA----------------ACRAn 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  548 -QVPPVPPDKSPVSPTGPSETTGLAEKPTIPTETTTVPTEAPAFSTETTmVPTEQPTistetttvptetttvpteQPTIP 626
Cdd:pfam17823  154 aSAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSA-PATLTPA------------------RGIST 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  627 TEVPTEEPAISTETTTVPTeqpTIPTETTTIPTEIPTVPTETTTVPTETTTVPTEQPTVPTETTTIPTEKPTVHTETTAv 706
Cdd:pfam17823  215 AATATGHPAAGTALAAVGN---SSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDT- 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  707 pTEITTVPTEKPTVDTETTTVPIEKPaVHTETTVPTEKPTVHTEKP----------TALTEETTIPTKEPT---VPTeKP 773
Cdd:pfam17823  291 -MARNPAAPMGAQAQGPIIQVSTDQP-VHNTAGEPTPSPSNTTLEPntpksvastnLAVVTTTKAQAKEPSaspVPV-LH 367

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  774 TT--PIKESTSvtrePTTTVTPHPSTVLVHTvPALLgMVPQHVPntsmTSATLGiTTTPGPATES 836
Cdd:pfam17823  368 TSmiPEVEATS----PTTQPSPLLPTQGAAG-PGIL-LAPEQVA----TEATAG-TASAGPTPRS 421
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2514-2543 5.12e-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: 5.12e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1149817606 2514 CLRNPCQNDGRCQEQGASFTCQCELGYGGD 2543
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1333-1486 1.86e-47

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: 167.55  E-value: 1.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1333 CTASGDPHYLTFDGALHHFMGTCTYVLTKPCWtKLPQNYFVVSTSNENRGGilEASFVKAVHVQIFGLKISLLKGRKVML 1412
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGA--SGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1413 NGHRVALPVWPLKGLVTLRLSGI-FVVLYTTIGLLVRYDGVHLVEVTVPSSYAGQLCGLCGNYNNNSLDDNLRPD 1486
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 948-1100 1.17e-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: 165.24  E-value: 1.17e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  948 CLVYGDPHYVTFDGRHFGFMGRCTYILTQPCGNSTDPFFRVTAVKDGWEQQGMsYLNKVYVTLPETTVTLLKGRRTLVGS 1027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1028 QQVTLPAIPSKG-VFLAASGR-FVELHTEFGLWVRWDGDQQLFVSVARTYSSKLCGLCGNYDGDMSNDHLKPDGQ 1100
Cdd:pfam00094   80 QKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 389-546 4.09e-41

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: 149.43  E-value: 4.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  389 CDFEDDDhpFCDWTQKSQDGGHWIRGHRNVPLQ--STDFPRGS---HYIYLQSDKFsQAGQSVILVSRPFCAPG-DICVE 462
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVKTgpSSDHTQGTgsgHFMYVDTSSG-APGQTARLLSPLLPPSRsPQCLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  463 FAYHMYGLGEGTtLKFLLGSPAGSTPITLWSRVGSQSPDWQNASITISSGhQQPMQLIFKATRGSSTAFVVAIDFILVSH 542
Cdd:pfam00629   78 FWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ....
gi 1149817606  543 GICR 546
Cdd:pfam00629  156 GPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 57-218 1.10e-39

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: 145.60  E-value: 1.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   57 CDFEDeskPFCDWTQVSADDGDWIRASGPSKTGTTGPLGGYPSGEGNYLHMVSKAFRRGGVARLRSPYLWV-QGPLCVRF 135
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  136 VYHMFGLSwGAQLRLLLLSSTQGQRpSVLWKHRNTQSPSWMPTAVTVPAGFAlPTQLMFEGMRGNTAYLDIALDAISIHR 215
Cdd:cd06263     78 WYHMYGSG-VGTLNVYVREEGGGLG-TLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1149817606  216 GSC 218
Cdd:cd06263    155 GPC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1330-1486 1.81e-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: 145.24  E-value: 1.81e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  1330 AATCTASGDPHYLTFDGALHHFMGTCTYVLTKPCwtkLPQNYFVVSTSNENRGGilEASFVKAVHVQIFGLKISLLK-GR 1408
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGG--GATCLKSVKVELNGDEIELKDdNG 83

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149817606  1409 KVMLNGHRVALPVWPLKGLVTLRLSGIFVVLYTTIGLL-VRYDGVHLVEVTVPSSYAGQLCGLCGNYNNNSLDDNLRPD 1486
Cdd:smart00216   84 KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 385-545 2.34e-39

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: 144.79  E-value: 2.34e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   385 SFPQCDFEDDDhpFCDWTQKSQDGGHW--IRGHRNVPLQSTDFPRGS-HYIYLQSDKFSQaGQSVILVSRPFCAPGD-IC 460
Cdd:smart00137    2 SPGNCDFEEGS--TCGWHQDSNDDGHWerVSSATGIPGPNRDHTTGNgHFMFFETSSGAE-GQTARLLSPPLYENRStHC 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   461 VEFAYHMYGLGEGTtLKFLLGSPAGSTPITLWSRVGSQSPDWQNASITISSgHQQPMQLIFKATRGSSTAFVVAIDFILV 540
Cdd:smart00137   79 LTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 1149817606   541 SHGIC 545
Cdd:smart00137  157 SNGPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1722-1875 1.74e-38

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 141.74  E-value: 1.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1722 CRVSGDARYVSFDGSEHFIRGTCAHVLMKVCHPNMNmpfFKISAKNKKLVGRPKSFHLHQVYIDIYNSQIILQNNHHVLI 1801
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1802 NGKQVTLPESSQIPGVSILSRGIH-TIVKFKLGARVTFDGRHLLEIELPTGYYGKVCGVCGNFNGEEDDELMMPS 1875
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2113-2267 1.06e-36

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 136.73  E-value: 1.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 2113 CSVFGDPHYHTFDHLSYHFMGRMTYILIKTVDVLPEGVERLLVKGRNKMHEPWspiILNEVIIIVYGYKVQLQTGLGLVV 2192
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV---CLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 2193 NDQKMAIPY-RPNEHLWVTLRGQ-RLYLVTDFELVVSFDGRRNAVISLPSTYQGLVRGLCGNYDKNHKNELMLPSGV 2267
Cdd:pfam00094   78 NGQKVSLPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 946-1099 2.09e-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: 133.30  E-value: 2.09e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   946 GTCLVYGDPHYVTFDGRHFGFMGRCTYILTQPCgnSTDPFFRVTaVKDGWEQQGMSYLNKVYVTLPETTVTLLKGRRT-L 1024
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC--SSEPTFSVL-LKNVPCGGGATCLKSVKVELNGDEIELKDDNGKvT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606  1025 VGSQQVTLPAIPS-KGVFLAASGRFVELHTEFGLW-VRWDGDQQLFVSVARTYSSKLCGLCGNYDGDMSNDHLKPDG 1099
Cdd:smart00216   87 VNGQQVSLPYKTSdGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 389-545 2.87e-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: 132.89  E-value: 2.87e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  389 CDFEDDdhpFCDWTQKSQDGGHWIRGHRNVPLQST----DFPRGS-HYIYLQSDkFSQAGQSVILVSRPFCAP-GDICVE 462
Cdd:cd06263      1 CDFEDG---LCGWTQDSTDDFDWTRVSGSTPSPGTppdhTHGTGSgHYLYVESS-SGREGQKARLLSPLLPPPrSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  463 FAYHMYGLGEGTtLKFLLGSPAGSTPITLWSRVGSQSPDWQNASITISSGHQqPMQLIFKATRGSSTAFVVAIDFILVSH 542
Cdd:cd06263     77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1149817606  543 GIC 545
Cdd:cd06263    155 GPC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1719-1875 3.67e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 129.83  E-value: 3.67e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  1719 RGVCRVSGDARYVSFDGSEHFIRGTCAHVLMKVCHPNmnmPFFKISAKNKKLVGRPksFHLHQVYIDIYNSQIIL-QNNH 1797
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIELkDDNG 83

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149817606  1798 HVLINGKQVTLPESSQIPGVSILSRGIHTIVKFKLG-ARVTFDGRHLLEIELPTGYYGKVCGVCGNFNGEEDDELMMPS 1875
Cdd:smart00216   84 KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 57-219 2.81e-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: 121.32  E-value: 2.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   57 CDFEDESkpFCDWTQVSADDGDWIRASGPSKTgtTGPLGG--YPSGEGNYLHMVSKAFRRGGVARLRSPYLWVQG-PLCV 133
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  134 RFVYHMFGLSWGaQLRLLLLSStQGQRPSVLWKHRNTQSPSWMPTAVTVPAgFALPTQLMFEGMRGNTAYLDIALDAISI 213
Cdd:pfam00629   77 RFWYHMSGSGVG-TLRVYVREN-GGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1149817606  214 HRGSCS 219
Cdd:pfam00629  154 SSGPCP 159
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2113-2266 4.96e-31

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 120.97  E-value: 4.96e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  2113 CSVFGDPHYHTFDHLSYHFMGRMTYILIKTVDVLPEgverLLVKGRNKmHEPWSPIILNEVIIIVYGYKVQL-QTGLGLV 2191
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNV-PCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606  2192 VNDQKMAIPY-RPNEHLWVTLRGQRLYLVTDFELV-VSFDGRRNAVISLPSTYQGLVRGLCGNYDKNHKNELMLPSG 2266
Cdd:smart00216   87 VNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 227-381 2.04e-30

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: 119.02  E-value: 2.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  227 CSFDTpnDLCGWSWIPTaTGAKWIQKKGQSGKPGMGPDDDFSsPGNGYYMLLDPRNARPRQKSVFLSPLSH---SSGCls 303
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPDHTHG-TGSGHYLYVESSSGREGQKARLLSPLLPpprSSHC-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  304 LSFHYTLWGQSPGaALHVYASVLGSIRRHTLF--SGQPKPNWQPVSVNY-TGQGQIQFTVVGVFGKIPEPAVAVDDISIA 380
Cdd:cd06263     75 LSFWYHMYGSGVG-TLNVYVREEGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                   .
gi 1149817606  381 P 381
Cdd:cd06263    154 P 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 57-218 7.14e-25

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: 103.19  E-value: 7.14e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606    57 CDFEDEskPFCDWTQVSADDGDWIRASgpSKTGTTGPLGGYPSGEGNYLHMVSKAFRRGGVARLRSPYLW-VQGPLCVRF 135
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYeNRSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   136 VYHMFGLSWGaQLRLLLLSStQGQRPSVLWKHRNTQSPSWMPTAVTVPAgFALPTQLMFEGMRGNTAYLDIALDAISIHR 215
Cdd:smart00137   82 WYYMYGSGSG-TLNVYVREN-NGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1149817606   216 GSC 218
Cdd:smart00137  159 GPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 227-383 3.75e-24

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: 100.90  E-value: 3.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  227 CSFDTPNdLCGWsWIPTATGAKWIQKKGQSgkPGMGPDDDFS-SPGNGYYMLLDPRNARPRQKSVFLSPLSH---SSGCl 302
Cdd:pfam00629    1 CDFEDGN-LCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  303 sLSFHYTLWGQSPGaALHVYASVLGSIRRHTLFS--GQPKPNWQPVSVNY-TGQGQIQFTVVGVFGKIPEPAVAVDDISI 379
Cdd:pfam00629   76 -LRFWYHMSGSGVG-TLRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1149817606  380 A--PCG 383
Cdd:pfam00629  154 SsgPCP 159
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2323-2398 1.76e-22

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 93.17  E-value: 1.76e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606  2323 STQACRVLVDPLGPFAACHQTVAPEPFQEHCVLDLCSAGDpreQEEMRCQVLSAYAILCQEAGVALASWRNHTRCA 2398
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGG---DCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1529-1600 2.30e-21

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: 90.09  E-value: 2.30e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149817606  1529 WNKNCAILTDPQGPFSQCHEVVPPQASLASCVRGQCGTKGDTTALCHSLQAYASLCTQAGQAP-VWRNSTFCP 1600
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1140-1214 1.02e-20

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 88.17  E-value: 1.02e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  1140 MSGPGFCGRLVDSRGPFEACLFHLKATSFFDNCMFDMCNFQGLQQMLCAHMSAMTTSCQDAGYPMKPWREPHFCP 1214
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2327-2397 2.98e-18

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 80.89  E-value: 2.98e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149817606 2327 CRVLVDPlGPFAACHQTVAPEPFQEHCVLDLCSAGDpreQEEMRCQVLSAYAILCQEAGVALASWRNHTRC 2397
Cdd:pfam08742    2 CGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGG---DDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2051-2106 6.89e-17

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: 76.57  E-value: 6.89e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606 2051 CEDAQGGLIPPGKTWISSGCTDSCVCMGGTIQCRAFRCPSGSHCQPSSDhsNSNCA 2106
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDG--SSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1533-1599 2.96e-16

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 75.11  E-value: 2.96e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606 1533 CAILTDpQGPFSQCHEVVPPQASLASCVRGQCGTKGDTTALCHSLQAYASLCTQAGQAPV-WRNSTFC 1599
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1145-1213 4.38e-16

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 74.72  E-value: 4.38e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149817606 1145 FCGRLVDSrGPFEACLFHLKATSFFDNCMFDMCNFQGLQQMLCAHMSAMTTSCQDAGYPMKPWREPHFC 1213
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1217-1270 6.54e-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: 70.81  E-value: 6.54e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1217 CPPNSKYSLCARPCPDTCHSAFSGMFCPDRCVEGCECNPGFVLSGLN-CVPQSQC 1270
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1217-1270 4.30e-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: 68.57  E-value: 4.30e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1217 CPPNSKYSLCARPCPDTCHSAFSGMFCPDRCVEGCECNPGFVLSGLN-CVPQSQC 1270
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2401-2454 1.61e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 64.33  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 2401 CPANTVYQSCMTPCPASCADLADPRDCEGPCVEGCASIPGYIYS-GTQSLPLAHC 2454
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 888-941 1.63e-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: 64.25  E-value: 1.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149817606  888 CFYNNYNYKTGAEWFSPNCTEYCHCwPGNQIECQSSQCGARTMCQLKNGQYGCY 941
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1603-1658 1.94e-11

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: 61.18  E-value: 1.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 1603 CPPGSSYSPCVRPCPATCLSLVAPRDCPAslPCAEGCECQKGHILS-GTSCVPFSQC 1658
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1603-1658 2.51e-11

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: 60.86  E-value: 2.51e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 1603 CPPGSSYSPCVRPCPATCLSLVAPRDCPAslPCAEGCECQKGHILS-GTSCVPFSQC 1658
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPE--PCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1272-1326 4.89e-11

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 60.01  E-value: 4.89e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1272 CLDSNGSYFKVGEKWHKPGCRQLCFCKDNNrIRCYSWKCKAQEICDYQDGIYGCH 1326
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1993-2049 1.17e-10

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: 58.87  E-value: 1.17e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1993 CPPHSSYTNCLPPCSPSCWDLD--GRCegvkvPSTCAEGCICQPGYVLNED-KCVPRSQC 2049
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-----TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2401-2444 1.40e-10

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: 58.48  E-value: 1.40e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1149817606 2401 CPANTVYQSCMTPCPASCADLADPRDCEGPCVEGCASIPGYIYS 2444
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRN 44
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1922-1989 3.42e-10

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: 58.16  E-value: 3.42e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606 1922 KCEAALEAPAWSQCASHLVLKPFLVSCANTLCEFGGLNHALCQALQAFGSTCESQGLKPPLWRNSSFC 1989
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2456-2509 4.68e-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: 4.68e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149817606 2456 CTSNGIYYQRGDSFVTEDCSQRCTCAHaGILLCKPFSCSVGETCTLGNLTRGCF 2509
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1993-2049 8.31e-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: 56.63  E-value: 8.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606 1993 CPPHSSYTNCLPPCSPSCWDLDGRcegVKVPSTCAEGCICQPGYVLNED-KCVPRSQC 2049
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPP---DVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 837-886 1.08e-09

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 56.17  E-value: 1.08e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  837 CPLNAHYESC--ACPASCKNPR--PSCGLLCQAGCVCNPGFLFSDNG-CINASSC 886
Cdd:cd19941      1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 837-886 2.61e-09

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 55.09  E-value: 2.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  837 CPLNAHYESC--ACPASCKNPRPS--CGLLCQAGCVCNPGFLFSDNG-CINASSC 886
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPPdvCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1933-1990 2.66e-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: 52.73  E-value: 2.66e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606  1933 SQCASHLVLKPFLVSCANTLCEFGGLNHALCQALQAFGSTCESQGLKPPLWRNSSFCP 1990
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1660-1715 7.75e-08

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: 50.77  E-value: 7.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606 1660 CIDPKGFYHLVGESWYTeSTCSWLCTCSiHNNITCFQTTCKPNQMCWSLDGVLRCR 1715
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 469-836 1.26e-07

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 56.89  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  469 GLGEGTTLKfLLGSPAGSTPITlwsrVGSQSPdwqnasiTISSGhqqPMQLIFKATRGSstafvvaidfilvshgICRA- 547
Cdd:pfam17823  105 GAADGAASR-ALAAAASSSPSS----AAQSLP-------AAIAA---LPSEAFSAPRAA----------------ACRAn 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  548 -QVPPVPPDKSPVSPTGPSETTGLAEKPTIPTETTTVPTEAPAFSTETTmVPTEQPTistetttvptetttvpteQPTIP 626
Cdd:pfam17823  154 aSAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSA-PATLTPA------------------RGIST 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  627 TEVPTEEPAISTETTTVPTeqpTIPTETTTIPTEIPTVPTETTTVPTETTTVPTEQPTVPTETTTIPTEKPTVHTETTAv 706
Cdd:pfam17823  215 AATATGHPAAGTALAAVGN---SSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDT- 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  707 pTEITTVPTEKPTVDTETTTVPIEKPaVHTETTVPTEKPTVHTEKP----------TALTEETTIPTKEPT---VPTeKP 773
Cdd:pfam17823  291 -MARNPAAPMGAQAQGPIIQVSTDQP-VHNTAGEPTPSPSNTTLEPntpksvastnLAVVTTTKAQAKEPSaspVPV-LH 367

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  774 TT--PIKESTSvtrePTTTVTPHPSTVLVHTvPALLgMVPQHVPntsmTSATLGiTTTPGPATES 836
Cdd:pfam17823  368 TSmiPEVEATS----PTTQPSPLLPTQGAAG-PGIL-LAPEQVA----TEATAG-TASAGPTPRS 421
rne PRK10811
ribonuclease E; Reviewed
 697-833 5.26e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.88  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  697 PTVHTETTAVPTEITTVPTEKPTVDTETTTVPIEKPAVHTETTVP-------TEKPTVhTEKPTALTEETTIPTKEPTVP 769
Cdd:PRK10811   873 VPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPeviaapvTEQPQV-ITESDVAVAQEVAEHAEPVVE 951

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606  770 TEKPTTPIKESTSVTREPTTTVTPHPSTVLVHTVPALLGMVPQHVPNTSMTS------------ATLGITTTPGPA 833
Cdd:PRK10811   952 PQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPaqvpeatvehnhATAPMTRAPAPE 1027
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2456-2519 1.04e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 42.55  E-value: 1.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149817606  2456 CTSNGIYYQRGDSFVtEDCsQRCTCAHaGILLCKPFSCSVGEtCTLGNLTRGCFRESP-------CLRNPC 2519
Cdd:smart00215    1 CWNNGSYYPPGAKWD-DDC-NRCTCLN-GRVSCTKVWCGPKP-CLLHNLSGECPLGQGcvpslsdCLSSPC 67
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2514-2543 5.12e-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: 5.12e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1149817606 2514 CLRNPCQNDGRCQEQGASFTCQCELGYGGD 2543
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 696-797 8.89e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 44.76  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  696 KPTVHTETTAVPTEITTVP-TEKPTVDTETTTvpiEKPAV--HTETTVPTEKPTVHTEKPTALTE-ETTIPTKEPTVPTE 771
Cdd:NF033839   362 KPEVKPQPEKPKPEVKPQPeTPKPEVKPQPEK---PKPEVkpQPEKPKPEVKPQPEKPKPEVKPQpEKPKPEVKPQPEKP 438

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1149817606  772 KPTT---PIKESTSVTREPTT---TVTPHPST 797
Cdd:NF033839   439 KPEVkpqPEKPKPEVKPQPETpkpEVKPQPEK 470
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2517-2546 1.14e-03

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 1.14e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1149817606 2517 NPCQNDGRCQEQGASFTCQCELGYGGDLCT 2546
Cdd:cd00054      9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1333-1486 1.86e-47

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: 167.55  E-value: 1.86e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1333 CTASGDPHYLTFDGALHHFMGTCTYVLTKPCWtKLPQNYFVVSTSNENRGGilEASFVKAVHVQIFGLKISLLKGRKVML 1412
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS-EEPDFSFSVTNKNCNGGA--SGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1413 NGHRVALPVWPLKGLVTLRLSGI-FVVLYTTIGLLVRYDGVHLVEVTVPSSYAGQLCGLCGNYNNNSLDDNLRPD 1486
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 948-1100 1.17e-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: 165.24  E-value: 1.17e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  948 CLVYGDPHYVTFDGRHFGFMGRCTYILTQPCGNSTDPFFRVTAVKDGWEQQGMsYLNKVYVTLPETTVTLLKGRRTLVGS 1027
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1028 QQVTLPAIPSKG-VFLAASGR-FVELHTEFGLWVRWDGDQQLFVSVARTYSSKLCGLCGNYDGDMSNDHLKPDGQ 1100
Cdd:pfam00094   80 QKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 389-546 4.09e-41

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: 149.43  E-value: 4.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  389 CDFEDDDhpFCDWTQKSQDGGHWIRGHRNVPLQ--STDFPRGS---HYIYLQSDKFsQAGQSVILVSRPFCAPG-DICVE 462
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVKTgpSSDHTQGTgsgHFMYVDTSSG-APGQTARLLSPLLPPSRsPQCLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  463 FAYHMYGLGEGTtLKFLLGSPAGSTPITLWSRVGSQSPDWQNASITISSGhQQPMQLIFKATRGSSTAFVVAIDFILVSH 542
Cdd:pfam00629   78 FWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISLSS 155


                   ....
gi 1149817606  543 GICR 546
Cdd:pfam00629  156 GPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 57-218 1.10e-39

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: 145.60  E-value: 1.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   57 CDFEDeskPFCDWTQVSADDGDWIRASGPSKTGTTGPLGGYPSGEGNYLHMVSKAFRRGGVARLRSPYLWV-QGPLCVRF 135
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  136 VYHMFGLSwGAQLRLLLLSSTQGQRpSVLWKHRNTQSPSWMPTAVTVPAGFAlPTQLMFEGMRGNTAYLDIALDAISIHR 215
Cdd:cd06263     78 WYHMYGSG-VGTLNVYVREEGGGLG-TLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1149817606  216 GSC 218
Cdd:cd06263    155 GPC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1330-1486 1.81e-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: 145.24  E-value: 1.81e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  1330 AATCTASGDPHYLTFDGALHHFMGTCTYVLTKPCwtkLPQNYFVVSTSNENRGGilEASFVKAVHVQIFGLKISLLK-GR 1408
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGG--GATCLKSVKVELNGDEIELKDdNG 83

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149817606  1409 KVMLNGHRVALPVWPLKGLVTLRLSGIFVVLYTTIGLL-VRYDGVHLVEVTVPSSYAGQLCGLCGNYNNNSLDDNLRPD 1486
Cdd:smart00216   84 KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 385-545 2.34e-39

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: 144.79  E-value: 2.34e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   385 SFPQCDFEDDDhpFCDWTQKSQDGGHW--IRGHRNVPLQSTDFPRGS-HYIYLQSDKFSQaGQSVILVSRPFCAPGD-IC 460
Cdd:smart00137    2 SPGNCDFEEGS--TCGWHQDSNDDGHWerVSSATGIPGPNRDHTTGNgHFMFFETSSGAE-GQTARLLSPPLYENRStHC 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   461 VEFAYHMYGLGEGTtLKFLLGSPAGSTPITLWSRVGSQSPDWQNASITISSgHQQPMQLIFKATRGSSTAFVVAIDFILV 540
Cdd:smart00137   79 LTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILL 156


                    ....*
gi 1149817606   541 SHGIC 545
Cdd:smart00137  157 SNGPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1722-1875 1.74e-38

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 141.74  E-value: 1.74e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1722 CRVSGDARYVSFDGSEHFIRGTCAHVLMKVCHPNMNmpfFKISAKNKKLVGRPKSFHLHQVYIDIYNSQIILQNNHHVLI 1801
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1802 NGKQVTLPESSQIPGVSILSRGIH-TIVKFKLGARVTFDGRHLLEIELPTGYYGKVCGVCGNFNGEEDDELMMPS 1875
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVvVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2113-2267 1.06e-36

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 136.73  E-value: 1.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 2113 CSVFGDPHYHTFDHLSYHFMGRMTYILIKTVDVLPEGVERLLVKGRNKMHEPWspiILNEVIIIVYGYKVQLQTGLGLVV 2192
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV---CLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 2193 NDQKMAIPY-RPNEHLWVTLRGQ-RLYLVTDFELVVSFDGRRNAVISLPSTYQGLVRGLCGNYDKNHKNELMLPSGV 2267
Cdd:pfam00094   78 NGQKVSLPYkSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 946-1099 2.09e-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: 133.30  E-value: 2.09e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   946 GTCLVYGDPHYVTFDGRHFGFMGRCTYILTQPCgnSTDPFFRVTaVKDGWEQQGMSYLNKVYVTLPETTVTLLKGRRT-L 1024
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC--SSEPTFSVL-LKNVPCGGGATCLKSVKVELNGDEIELKDDNGKvT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606  1025 VGSQQVTLPAIPS-KGVFLAASGRFVELHTEFGLW-VRWDGDQQLFVSVARTYSSKLCGLCGNYDGDMSNDHLKPDG 1099
Cdd:smart00216   87 VNGQQVSLPYKTSdGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 389-545 2.87e-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: 132.89  E-value: 2.87e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  389 CDFEDDdhpFCDWTQKSQDGGHWIRGHRNVPLQST----DFPRGS-HYIYLQSDkFSQAGQSVILVSRPFCAP-GDICVE 462
Cdd:cd06263      1 CDFEDG---LCGWTQDSTDDFDWTRVSGSTPSPGTppdhTHGTGSgHYLYVESS-SGREGQKARLLSPLLPPPrSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  463 FAYHMYGLGEGTtLKFLLGSPAGSTPITLWSRVGSQSPDWQNASITISSGHQqPMQLIFKATRGSSTAFVVAIDFILVSH 542
Cdd:cd06263     77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1149817606  543 GIC 545
Cdd:cd06263    155 GPC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1719-1875 3.67e-34

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 129.83  E-value: 3.67e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  1719 RGVCRVSGDARYVSFDGSEHFIRGTCAHVLMKVCHPNmnmPFFKISAKNKKLVGRPksFHLHQVYIDIYNSQIIL-QNNH 1797
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIELkDDNG 83

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149817606  1798 HVLINGKQVTLPESSQIPGVSILSRGIHTIVKFKLG-ARVTFDGRHLLEIELPTGYYGKVCGVCGNFNGEEDDELMMPS 1875
Cdd:smart00216   84 KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 57-219 2.81e-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: 121.32  E-value: 2.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   57 CDFEDESkpFCDWTQVSADDGDWIRASGPSKTgtTGPLGG--YPSGEGNYLHMVSKAFRRGGVARLRSPYLWVQG-PLCV 133
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  134 RFVYHMFGLSWGaQLRLLLLSStQGQRPSVLWKHRNTQSPSWMPTAVTVPAgFALPTQLMFEGMRGNTAYLDIALDAISI 213
Cdd:pfam00629   77 RFWYHMSGSGVG-TLRVYVREN-GGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1149817606  214 HRGSCS 219
Cdd:pfam00629  154 SSGPCP 159
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2113-2266 4.96e-31

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 120.97  E-value: 4.96e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  2113 CSVFGDPHYHTFDHLSYHFMGRMTYILIKTVDVLPEgverLLVKGRNKmHEPWSPIILNEVIIIVYGYKVQL-QTGLGLV 2191
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNV-PCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606  2192 VNDQKMAIPY-RPNEHLWVTLRGQRLYLVTDFELV-VSFDGRRNAVISLPSTYQGLVRGLCGNYDKNHKNELMLPSG 2266
Cdd:smart00216   87 VNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 227-381 2.04e-30

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: 119.02  E-value: 2.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  227 CSFDTpnDLCGWSWIPTaTGAKWIQKKGQSGKPGMGPDDDFSsPGNGYYMLLDPRNARPRQKSVFLSPLSH---SSGCls 303
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPDHTHG-TGSGHYLYVESSSGREGQKARLLSPLLPpprSSHC-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  304 LSFHYTLWGQSPGaALHVYASVLGSIRRHTLF--SGQPKPNWQPVSVNY-TGQGQIQFTVVGVFGKIPEPAVAVDDISIA 380
Cdd:cd06263     75 LSFWYHMYGSGVG-TLNVYVREEGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                   .
gi 1149817606  381 P 381
Cdd:cd06263    154 P 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 57-218 7.14e-25

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: 103.19  E-value: 7.14e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606    57 CDFEDEskPFCDWTQVSADDGDWIRASgpSKTGTTGPLGGYPSGEGNYLHMVSKAFRRGGVARLRSPYLW-VQGPLCVRF 135
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYeNRSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606   136 VYHMFGLSWGaQLRLLLLSStQGQRPSVLWKHRNTQSPSWMPTAVTVPAgFALPTQLMFEGMRGNTAYLDIALDAISIHR 215
Cdd:smart00137   82 WYYMYGSGSG-TLNVYVREN-NGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1149817606   216 GSC 218
Cdd:smart00137  159 GPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 227-383 3.75e-24

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: 100.90  E-value: 3.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  227 CSFDTPNdLCGWsWIPTATGAKWIQKKGQSgkPGMGPDDDFS-SPGNGYYMLLDPRNARPRQKSVFLSPLSH---SSGCl 302
Cdd:pfam00629    1 CDFEDGN-LCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  303 sLSFHYTLWGQSPGaALHVYASVLGSIRRHTLFS--GQPKPNWQPVSVNY-TGQGQIQFTVVGVFGKIPEPAVAVDDISI 379
Cdd:pfam00629   76 -LRFWYHMSGSGVG-TLRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1149817606  380 A--PCG 383
Cdd:pfam00629  154 SsgPCP 159
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2323-2398 1.76e-22

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 93.17  E-value: 1.76e-22
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606  2323 STQACRVLVDPLGPFAACHQTVAPEPFQEHCVLDLCSAGDpreQEEMRCQVLSAYAILCQEAGVALASWRNHTRCA 2398
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGG---DCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1529-1600 2.30e-21

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: 90.09  E-value: 2.30e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149817606  1529 WNKNCAILTDPQGPFSQCHEVVPPQASLASCVRGQCGTKGDTTALCHSLQAYASLCTQAGQAP-VWRNSTFCP 1600
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1140-1214 1.02e-20

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 88.17  E-value: 1.02e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  1140 MSGPGFCGRLVDSRGPFEACLFHLKATSFFDNCMFDMCNFQGLQQMLCAHMSAMTTSCQDAGYPMKPWREPHFCP 1214
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2327-2397 2.98e-18

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 80.89  E-value: 2.98e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149817606 2327 CRVLVDPlGPFAACHQTVAPEPFQEHCVLDLCSAGDpreQEEMRCQVLSAYAILCQEAGVALASWRNHTRC 2397
Cdd:pfam08742    2 CGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGG---DDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2051-2106 6.89e-17

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: 76.57  E-value: 6.89e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606 2051 CEDAQGGLIPPGKTWISSGCTDSCVCMGGTIQCRAFRCPSGSHCQPSSDhsNSNCA 2106
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDG--SSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1533-1599 2.96e-16

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 75.11  E-value: 2.96e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606 1533 CAILTDpQGPFSQCHEVVPPQASLASCVRGQCGTKGDTTALCHSLQAYASLCTQAGQAPV-WRNSTFC 1599
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1145-1213 4.38e-16

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 74.72  E-value: 4.38e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149817606 1145 FCGRLVDSrGPFEACLFHLKATSFFDNCMFDMCNFQGLQQMLCAHMSAMTTSCQDAGYPMKPWREPHFC 1213
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1217-1270 6.54e-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: 70.81  E-value: 6.54e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1217 CPPNSKYSLCARPCPDTCHSAFSGMFCPDRCVEGCECNPGFVLSGLN-CVPQSQC 1270
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1217-1270 4.30e-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: 68.57  E-value: 4.30e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1217 CPPNSKYSLCARPCPDTCHSAFSGMFCPDRCVEGCECNPGFVLSGLN-CVPQSQC 1270
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2401-2454 1.61e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 64.33  E-value: 1.61e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 2401 CPANTVYQSCMTPCPASCADLADPRDCEGPCVEGCASIPGYIYS-GTQSLPLAHC 2454
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 888-941 1.63e-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: 64.25  E-value: 1.63e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149817606  888 CFYNNYNYKTGAEWFSPNCTEYCHCwPGNQIECQSSQCGARTMCQLKNGQYGCY 941
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1603-1658 1.94e-11

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: 61.18  E-value: 1.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 1603 CPPGSSYSPCVRPCPATCLSLVAPRDCPAslPCAEGCECQKGHILS-GTSCVPFSQC 1658
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTK--QCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1603-1658 2.51e-11

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: 60.86  E-value: 2.51e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606 1603 CPPGSSYSPCVRPCPATCLSLVAPRDCPAslPCAEGCECQKGHILS-GTSCVPFSQC 1658
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPE--PCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1272-1326 4.89e-11

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 60.01  E-value: 4.89e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606 1272 CLDSNGSYFKVGEKWHKPGCRQLCFCKDNNrIRCYSWKCKAQEICDYQDGIYGCH 1326
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1993-2049 1.17e-10

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: 58.87  E-value: 1.17e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606 1993 CPPHSSYTNCLPPCSPSCWDLD--GRCegvkvPSTCAEGCICQPGYVLNED-KCVPRSQC 2049
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-----TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2401-2444 1.40e-10

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: 58.48  E-value: 1.40e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1149817606 2401 CPANTVYQSCMTPCPASCADLADPRDCEGPCVEGCASIPGYIYS 2444
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRN 44
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1922-1989 3.42e-10

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: 58.16  E-value: 3.42e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606 1922 KCEAALEAPAWSQCASHLVLKPFLVSCANTLCEFGGLNHALCQALQAFGSTCESQGLKPPLWRNSSFC 1989
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2456-2509 4.68e-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: 4.68e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149817606 2456 CTSNGIYYQRGDSFVTEDCSQRCTCAHaGILLCKPFSCSVGETCTLGNLTRGCF 2509
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTCTG-GNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1993-2049 8.31e-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: 56.63  E-value: 8.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606 1993 CPPHSSYTNCLPPCSPSCWDLDGRcegVKVPSTCAEGCICQPGYVLNED-KCVPRSQC 2049
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPP---DVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 837-886 1.08e-09

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 56.17  E-value: 1.08e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  837 CPLNAHYESC--ACPASCKNPR--PSCGLLCQAGCVCNPGFLFSDNG-CINASSC 886
Cdd:cd19941      1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 837-886 2.61e-09

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 55.09  E-value: 2.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  837 CPLNAHYESC--ACPASCKNPRPS--CGLLCQAGCVCNPGFLFSDNG-CINASSC 886
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPPdvCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1933-1990 2.66e-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: 52.73  E-value: 2.66e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149817606  1933 SQCASHLVLKPFLVSCANTLCEFGGLNHALCQALQAFGSTCESQGLKPPLWRNSSFCP 1990
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1660-1715 7.75e-08

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: 50.77  E-value: 7.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606 1660 CIDPKGFYHLVGESWYTeSTCSWLCTCSiHNNITCFQTTCKPNQMCWSLDGVLRCR 1715
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFS-SGCTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 469-836 1.26e-07

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 56.89  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  469 GLGEGTTLKfLLGSPAGSTPITlwsrVGSQSPdwqnasiTISSGhqqPMQLIFKATRGSstafvvaidfilvshgICRA- 547
Cdd:pfam17823  105 GAADGAASR-ALAAAASSSPSS----AAQSLP-------AAIAA---LPSEAFSAPRAA----------------ACRAn 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  548 -QVPPVPPDKSPVSPTGPSETTGLAEKPTIPTETTTVPTEAPAFSTETTmVPTEQPTistetttvptetttvpteQPTIP 626
Cdd:pfam17823  154 aSAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSA-PATLTPA------------------RGIST 214

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  627 TEVPTEEPAISTETTTVPTeqpTIPTETTTIPTEIPTVPTETTTVPTETTTVPTEQPTVPTETTTIPTEKPTVHTETTAv 706
Cdd:pfam17823  215 AATATGHPAAGTALAAVGN---SSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDT- 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  707 pTEITTVPTEKPTVDTETTTVPIEKPaVHTETTVPTEKPTVHTEKP----------TALTEETTIPTKEPT---VPTeKP 773
Cdd:pfam17823  291 -MARNPAAPMGAQAQGPIIQVSTDQP-VHNTAGEPTPSPSNTTLEPntpksvastnLAVVTTTKAQAKEPSaspVPV-LH 367

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149817606  774 TT--PIKESTSvtrePTTTVTPHPSTVLVHTvPALLgMVPQHVPntsmTSATLGiTTTPGPATES 836
Cdd:pfam17823  368 TSmiPEVEATS----PTTQPSPLLPTQGAAG-PGIL-LAPEQVA----TEATAG-TASAGPTPRS 421
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 481-857 6.54e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 6.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  481 GSPAGSTPITlwsrvGSQSPDwQNASITISSGHQQPMQLIFKATRGSSTAfvvaidfilVSHGICRAQVPPVPPDKSPVS 560
Cdd:pfam05109  371 GTPSGCENIS-----GAFASN-RTFDITVSGLGTAPKTLIITRTATNATT---------TTHKVIFSKAPESTTTSPTLN 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  561 PTG---PSETTGLAEKPTIPTETTTVPTEAPAFSTETTMVPTEQPTISTEtttvptetttvpteQPTIPTEVP------T 631
Cdd:pfam05109  436 TTGfaaPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGA--------------SPVTPSPSPrdngteS 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  632 EEPAISTETT--TVPTEQPTIPTETTTIPTEIPTVPTETTTVPTETTtvpteqptvptetttiptekpTVHTETTAVPTE 709
Cdd:pfam05109  502 KAPDMTSPTSavTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAV---------------------TTPTPNATSPTP 560

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  710 ITTVPTEKPTVDTETTTVPIEkpAVHTETTVPTEkPTVHTEKPTAlteETTIPTKEPTVPTEKPTTPIKESTS------- 782
Cdd:pfam05109  561 AVTTPTPNATIPTLGKTSPTS--AVTTPTPNATS-PTVGETSPQA---NTTNHTLGGTSSTPVVTSPPKNATSavttgqh 634

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149817606  783 -VTREPTTTVTPHPSTVLVHTVPALLGMVPQHVPNTSMTSATLGITTTP-GPATEScplnAHYESCACPAscknPRP 857
Cdd:pfam05109  635 nITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQvTPASTS----THHVSTSSPA----PRP 703
rne PRK10811
ribonuclease E; Reviewed
 697-833 5.26e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.88  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  697 PTVHTETTAVPTEITTVPTEKPTVDTETTTVPIEKPAVHTETTVP-------TEKPTVhTEKPTALTEETTIPTKEPTVP 769
Cdd:PRK10811   873 VPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPeviaapvTEQPQV-ITESDVAVAQEVAEHAEPVVE 951

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149817606  770 TEKPTTPIKESTSVTREPTTTVTPHPSTVLVHTVPALLGMVPQHVPNTSMTS------------ATLGITTTPGPA 833
Cdd:PRK10811   952 PQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPaqvpeatvehnhATAPMTRAPAPE 1027
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 699-836 8.20e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 48.03  E-value: 8.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  699 VHTETTAVPTEITTVPTEKPTVDTETTTVPiekpavhtETTVPTEKPTVHTEKPTALTEETTIPTKEPTvpTEKPTTPIK 778
Cdd:pfam17823   86 VTAEHTPHGTDLSEPATREGAADGAASRAL--------AAAASSSPSSAAQSLPAAIAALPSEAFSAPR--AAACRANAS 155

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149817606  779 ESTS---VTREPTTTVTPHPSTVLVHTVPALLGMVPQHVPNTSMTSATLGITTTPGPATES 836
Cdd:pfam17823  156 AAPRaaiAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAA 216
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2456-2519 1.04e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 42.55  E-value: 1.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149817606  2456 CTSNGIYYQRGDSFVtEDCsQRCTCAHaGILLCKPFSCSVGEtCTLGNLTRGCFRESP-------CLRNPC 2519
Cdd:smart00215    1 CWNNGSYYPPGAKWD-DDC-NRCTCLN-GRVSCTKVWCGPKP-CLLHNLSGECPLGQGcvpslsdCLSSPC 67
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2514-2543 5.12e-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: 5.12e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1149817606 2514 CLRNPCQNDGRCQEQGASFTCQCELGYGGD 2543
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 696-797 8.89e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 44.76  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  696 KPTVHTETTAVPTEITTVP-TEKPTVDTETTTvpiEKPAV--HTETTVPTEKPTVHTEKPTALTE-ETTIPTKEPTVPTE 771
Cdd:NF033839   362 KPEVKPQPEKPKPEVKPQPeTPKPEVKPQPEK---PKPEVkpQPEKPKPEVKPQPEKPKPEVKPQpEKPKPEVKPQPEKP 438

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1149817606  772 KPTT---PIKESTSVTREPTT---TVTPHPST 797
Cdd:NF033839   439 KPEVkpqPEKPKPEVKPQPETpkpEVKPQPEK 470
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2517-2546 1.14e-03

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 1.14e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1149817606 2517 NPCQNDGRCQEQGASFTCQCELGYGGDLCT 2546
Cdd:cd00054      9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PHA03255 PHA03255
BDLF3; Provisional
 698-826 3.33e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 41.81  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  698 TVHTETTAVPTEITTVPTEKPTVDTETTTVpiekPAVHTETTVPTEKPTVHTEKPTALTEETTIPTKEPTvpTEKPTTPI 777
Cdd:PHA03255    59 TTLTTTSAPITTTAILSTNTTTVTSTGTTV----TPVPTTSNASTINVTTKVTAQNITATEAGTGTSTGV--TSNVTTRS 132

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149817606  778 KESTSVTREPT--TTVTPHPSTVLVHTVPALLGMVPQhVPNTSMTSATLGI 826
Cdd:PHA03255   133 SSTTSATTRITnaTTLAPTLSSKGTSNATKTTAELPT-VPDERQPSLSYGL 182
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
701-790 3.56e-03

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 42.92  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  701 TETTAVPTEiTTVPTEKPTVDT-ETTTVPiekPAVHTETTVPTEKPTVHTEKPTA-LTEETTIPTKEPTVPTEKPTTPIK 778
Cdd:PRK11907    35 TPATSTEAE-QTTPVESDATEEaDNTETP---VAATTAAEAPSSSETAETSDPTSeATDTTTSEARTVTPAATETSKPVE 110

                           90
                   ....*....|..
gi 1149817606  779 ESTSVTREPTTT 790
Cdd:PRK11907   111 GQTVDVRILSTT 122
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
 697-797 4.13e-03

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 40.71  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  697 PTVHTETTAVPTEITTVPT-----EKPTVDTeTTTVPIE-----KPAVHTETTVPTEKPTVHT-EKPTALTEETTIPTKe 765
Cdd:pfam09595   68 PPLNEAAKEAPSESEDAPDidpnnQHPSQDR-SEAPPLEpaaktKPSEHEPANPPDASNRLSPpDASTAAIREARTFRK- 145

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1149817606  766 PTVPTEKPTTPIKESTSVTR---EPTTTVTPHPST 797
Cdd:pfam09595  146 PSTGKRNNPSSAQSDQSPPRanhEAIGRANPFAMS 180
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 701-858 4.30e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 4.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  701 TETTAVPTEITTVPTEKPTvdtetTTVPIEKPAvhtettvPTEKPTVHTEKPTALTEETTIPTKEPTVPTEKPTTPIKES 780
Cdd:PLN03209   401 VDAVAKPAEPDVVPSPGSA-----SNVPEVEPA-------QVEAKKTRPLSPYARYEDLKPPTSPSPTAPTGVSPSVSST 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  781 TSVTREPTTTVTPHPSTVLVHTVPALLGMVPQHV-----PNTSMTSATLGITTTPGPATESCPL--NAHYESCACPASCK 853
Cdd:PLN03209   469 SSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVyddlkPPTSPSPAAPVGKVAPSSTNEVVKVgnSAPPTALADEQHHA 548


                   ....*
gi 1149817606  854 NPRPS 858
Cdd:PLN03209   549 QPKPR 553
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 623-864 5.13e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 42.25  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  623 PTIPTEVPTEEPAISTETTTVPTEQPtiptettTIPTEIPTVPTE-----TTTVPTETTTVPTEQPTVPTETTTIPTEKP 697
Cdd:pfam17823   66 APAPVTLTKGTSAAHLNSTEVTAEHT-------PHGTDLSEPATRegaadGAASRALAAAASSSPSSAAQSLPAAIAALP 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  698 TVH--TETTAVPTEITTVPTEKPTVDTETTTVPIEKPAVHTETTVPTEKPTVHTEKPT--ALTEETTIPTKEPTVPTEKP 773
Cdd:pfam17823  139 SEAfsAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTtaASSAPATLTPARGISTAATA 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  774 TTPIKESTSVTREPTTTVTPHPSTVLVHTV-PALLGMVPQHVPNTSMTSATLG----ITTTPGPAtESCPLNahyescac 848
Cdd:pfam17823  219 TGHPAAGTALAAVGNSSPAAGTVTAAVGTVtPAALATLAAAAGTVASAAGTINmgdpHARRLSPA-KHMPSD-------- 289

                          250
                   ....*....|....*.
gi 1149817606  849 pASCKNPRPSCGLLCQ 864
Cdd:pfam17823  290 -TMARNPAAPMGAQAQ 304
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 545-858 5.35e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.87  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  545 CRAQVPPVPP-----------DKSPVSPTGPSETTGLAEKPTIPTETTTVPTEAPAFSTETTMVPTEQPTISTEtttvPT 613
Cdd:pfam17823   61 CAATAAPAPVtltkgtsaahlNSTEVTAEHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAI----AA 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  614 EtttvpteqPTIPTEVPTEEpAISTETTTVPTEQPTIPTETTTIPTEIPTVPTETTTVPTETTTVPTEQPTVPTETTTIP 693
Cdd:pfam17823  137 L--------PSEAFSAPRAA-ACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLT 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  694 TEKPT----VHTETTAVPTEITTVPTEKPTVDTETTTVPIEKPA-VHTET----TVPTEKPTVHTEKP--TALTEETTIP 762
Cdd:pfam17823  208 PARGIstaaTATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAaLATLAaaagTVASAAGTINMGDPhaRRLSPAKHMP 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149817606  763 T----KEPtVPTEKPTTPIKESTSVTREPTTTVTPHPSTVLVHTvpALLGMVPQHVPNTSMTSATLGITTTPGPATESCP 838
Cdd:pfam17823  288 SdtmaRNP-AAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNT--TLEPNTPKSVASTNLAVVTTTKAQAKEPSASPVP 364

                          330       340
                   ....*....|....*....|
gi 1149817606  839 LNAHYESCACPASCKNPRPS 858
Cdd:pfam17823  365 VLHTSMIPEVEATSPTTQPS 384
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH