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Conserved domains on  [gi|256665241|ref|NP_035871|]
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zonadhesin precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1715-1865 3.21e-49

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: 173.71  E-value: 3.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  1715 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1794
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241  1795 NNQRVVLPVWPSQGRVTIRLSGI-FVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNL 1865
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1326-1478 6.66e-43

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: 155.61  E-value: 6.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  1326 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1405
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1406 QEVTLPAILSD-DTYVGLSGR-FVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGM 1478
Cdd:pfam00094   80 QKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4909-5062 3.19e-39

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 144.82  E-value: 3.19e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4909 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4987
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  4988 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGV 5062
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 375-540 1.89e-37

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: 140.17  E-value: 1.89e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    375 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 453
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    454 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 533
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 256665241    534 LISHGPC 540
Cdd:smart00137  155 LLSNGPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2102-2260 2.62e-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: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2102 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2181
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2182 IsliNDSIVTLPTTTHIPGVSVMTED-VYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSG 2260
Cdd:pfam00094   77 V---NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 217-373 5.70e-32

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: 124.40  E-value: 5.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   217 CTFDTlNDLCGWsWVPTATGAKWTQKKGPTgkQGVGPAEDFS-NPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCm 292
Cdd:pfam00629    1 CDFED-GNLCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   293 tLSFHYIMHGQGHEEgLFVYATFLGNIRKYTLFS--GHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISI 369
Cdd:pfam00629   76 -LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 256665241   370 A--PCG 373
Cdd:pfam00629  154 SsgPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 47-208 2.64e-31

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: 122.49  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263     1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263    78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                  ...
gi 256665241  206 GTC 208
Cdd:cd06263   155 GPC 157
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1911-1982 1.10e-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: 92.02  E-value: 1.10e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256665241   1911 WTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFCP 1982
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1521-1596 4.09e-19

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 84.70  E-value: 4.09e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241   1521 TMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFCP 1596
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3521-3575 1.69e-18

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: 81.97  E-value: 1.69e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3521 CKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNeDGNSNCA 3575
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3761-3815 3.31e-18

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: 81.20  E-value: 3.31e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3761 CKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNeDGNSNCA 3815
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3164-3218 1.67e-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: 79.27  E-value: 1.67e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3164 CKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDlKDGSSNCT 3218
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3044-3098 1.79e-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: 79.27  E-value: 1.79e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3044 CKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIeDGNSNCT 3098
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2804-2858 2.03e-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: 78.88  E-value: 2.03e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2804 CKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDlEDGNSNCT 2858
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2444-2498 2.22e-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: 78.88  E-value: 2.22e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2444 CKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNsNDGSSNCV 2498
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3997-4051 3.44e-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: 78.11  E-value: 3.44e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3997 CKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSgDGSSNCT 4051
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4133-4184 7.49e-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: 77.34  E-value: 7.49e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 256665241  4133 CKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSR 4184
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3401-3455 1.06e-16

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 76.96  E-value: 1.06e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3401 CKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSeGSSTCT 3455
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2564-2618 2.56e-16

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.80  E-value: 2.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2564 CQHTQGGFIPAGKSWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIeDGTSNCA 2618
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3641-3695 3.46e-16

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.42  E-value: 3.46e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3641 CKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSFQCPPGAYCKDNeDGSSNCA 3695
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4488-4542 3.60e-16

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.42  E-value: 3.60e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4488 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4542
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 5115-5191 7.27e-16

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: 75.45  E-value: 7.27e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241   5115 SSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTgwkTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCA 5191
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCA---CGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3284-3338 1.24e-15

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.88  E-value: 1.24e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3284 CKNTQGAFISADKTWISRGCTQSCTCSAGAIHCRNFKCPSGTYCKNGDnGSSNCT 3338
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4368-4422 1.95e-15

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.49  E-value: 1.95e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4368 CKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDsVDGGSNCT 4422
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2924-2978 2.06e-15

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 2.06e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2924 CKDTQGVLIPADKTWINRGCTQSCTCKGGAIQCQKYHCSSGTYCKDMeDDSSSCA 2978
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4848-4902 3.17e-15

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: 72.72  E-value: 3.17e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4848 CKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNeDGSSDCA 4902
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2684-2738 4.97e-15

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: 72.34  E-value: 4.97e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2684 CKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDiKDDTSNCT 2738
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4253-4300 5.64e-15

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: 71.95  E-value: 5.64e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 256665241  4253 CKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSS 4300
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND 48
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3881-3931 8.09e-15

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: 71.57  E-value: 8.09e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  3881 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3931
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4728-4782 1.14e-14

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: 71.18  E-value: 1.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4728 CKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESeDGSSNCV 4782
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4608-4662 2.74e-14

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: 70.03  E-value: 2.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4608 CKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNeGNSNCV 4662
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 486-913 1.03e-13

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: 77.69  E-value: 1.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   486 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 565
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   566 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 644
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   645 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 724
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   725 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 798
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   799 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 877
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 256665241   878 TTLPTEVLtvPIEVTTFPtGETTVPTEVPTVSTEMT 913
Cdd:pfam17823  380 TTQPSPLL--PTQGAAGP-GILLAPEQVATEATAGT 412
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1654-1708 7.97e-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: 63.09  E-value: 7.97e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1654 CTSFQGRYFKLQEQWFNPDCKEICTCeSHNHILCKPWKCKAQEACSYKNGVLGCH 1708
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1599-1652 2.17e-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: 61.95  E-value: 2.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241 1599 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1652
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1266-1319 1.62e-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: 59.24  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  1266 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1319
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1985-2039 1.43e-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: 56.63  E-value: 1.43e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241  1985 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 5194-5247 1.46e-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: 56.63  E-value: 1.46e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  5194 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDT-QSLPVTHC 5247
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4548-4606 3.15e-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: 55.86  E-value: 3.15e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4548 CPAHSHYSKCLPPCQPSCSDPdghceGTSPEAPSTCEEGCVCEPDYVLSND-KCVPSSEC 4606
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 5249-5302 6.72e-09

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: 54.62  E-value: 6.72e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  5249 CTADGIYYKLGDSFVTNDCSQHCTCaSQGILLCEPYGCRAGESCMVANFTRGCF 5302
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3937-3995 2.42e-08

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: 53.16  E-value: 2.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3937 CPAHSHFTSCLPSCPPSCANLDGSCEQTSPkvpstCKEGCLCQPGYFLNN-GKCVLQTHC 3995
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP-----CVEGCVCPPGFVRNSgGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4073-4131 1.42e-07

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: 51.23  E-value: 1.42e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4073 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4131
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3104-3162 2.13e-07

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: 50.46  E-value: 2.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3104 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3162
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2314-2380 2.30e-07

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: 50.84  E-value: 2.30e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  2314 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2380
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2384-2442 3.90e-07

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: 49.62  E-value: 3.90e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 2384 CPAHSHYTNCLPSCPPSCLDPD--SRCegsghkvPATCREGCICQPDYVL-LNDKCVLRSHC 2442
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3461-3519 5.89e-07

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: 49.31  E-value: 5.89e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3461 CPAHTQYTSCLPSCLPSCLDPEGlckdiSPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3519
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2864-2922 6.01e-07

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: 49.24  E-value: 6.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2864 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2922
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4788-4846 7.98e-07

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: 48.85  E-value: 7.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 4788 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4308-4366 7.98e-07

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: 48.85  E-value: 7.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4366
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2504-2562 9.16e-07

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: 48.92  E-value: 9.16e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241  2504 CPAHSKFTDCLPPCHPSCSDP--DGHCEGIstnahsnCKEGCVCQPGYVLRND-KCVLRIEC 2562
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLspPDVCPEP-------CVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3224-3282 1.12e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.54  E-value: 1.12e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3224 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3282
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1215-1264 1.17e-06

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: 48.47  E-value: 1.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241 1215 CPPNAHIELC--ACPASCESPK--PSCQPPCIPGCVCNPGFLFS-NNQCINESSC 1264
Cdd:cd19941     1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2624-2682 1.23e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.54  E-value: 1.23e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2624 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 2682
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3344-3399 1.54e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  3344 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3399
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2744-2802 2.61e-06

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: 47.31  E-value: 2.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2744 CPDHSLYTHCLPSCLPSCSDPDglcrgTSPEAPSTCKEGCVCEPDYVLS-NDKCVLRIEC 2802
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4193-4251 3.37e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.00  E-value: 3.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4193 CPAHSHYTNCLPACSRSCTDLdghceGTSPKVPSPCKEGCLCQPGYVVHNH-KCVLQIHC 4251
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2984-3042 8.08e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.23  E-value: 8.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2984 CPAHSHFTNCLPPCQPSCLDseghcEGSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 3042
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4668-4726 9.83e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 45.84  E-value: 9.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4668 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4726
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4428-4486 4.16e-05

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: 43.92  E-value: 4.16e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4428 CPAHSHHTYCLPSCIPSCSNvndrcESTSLQRPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4486
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3821-3879 4.78e-05

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: 43.92  E-value: 4.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3821 CPTHSNYTDCLPFCLPSCLDPSalcggTSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3879
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 2041-2096 6.06e-05

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 43.45  E-value: 6.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241  2041 CSDQDGSYHLLGESWYTEKtCTTLCTCSaHSNITCSPTACKANHVCLRQEGLLRCA 2096
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3581-3639 1.80e-04

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: 42.37  E-value: 1.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3581 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLSNN-KCLLRNRC 3639
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1715-1865 3.21e-49

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: 173.71  E-value: 3.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  1715 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1794
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241  1795 NNQRVVLPVWPSQGRVTIRLSGI-FVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNL 1865
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1326-1478 6.66e-43

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: 155.61  E-value: 6.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  1326 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1405
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1406 QEVTLPAILSD-DTYVGLSGR-FVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGM 1478
Cdd:pfam00094   80 QKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1707-1863 1.14e-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: 146.39  E-value: 1.14e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   1707 CHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCwskSQENNFVVSATNEIHDGNLEVsyVKAVHVQVFDLKISM 1786
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGATC--LKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256665241   1787 FKGQ-KVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGL-QVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDD 1863
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4909-5062 3.19e-39

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 144.82  E-value: 3.19e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4909 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4987
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  4988 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGV 5062
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 375-540 1.89e-37

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: 140.17  E-value: 1.89e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    375 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 453
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    454 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 533
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 256665241    534 LISHGPC 540
Cdd:smart00137  155 LLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 379-541 2.82e-37

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: 139.42  E-value: 2.82e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   379 CDFEDrvHPFCDWNQVYGDMGHWSWGSksVPTLIAGSPREFPYGGE--HYIFFDSVKlSQEGQSARLVSPPFCAPG-DIC 455
Cdd:pfam00629    1 CDFED--GNLCGWTQDSSDDFDWERVS--GPSVKTGPSSDHTQGTGsgHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   456 VEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILI 535
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 256665241   536 SHGPCR 541
Cdd:pfam00629  154 SSGPCP 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2102-2260 2.62e-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: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2102 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2181
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2182 IsliNDSIVTLPTTTHIPGVSVMTED-VYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSG 2260
Cdd:pfam00094   77 V---NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 379-540 1.84e-33

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: 128.65  E-value: 1.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  379 CDFEDrvhPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKlSQEGQSARLVSPPFCAP-GDICVE 457
Cdd:cd06263     1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  458 FAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILISH 537
Cdd:cd06263    77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSA-SSKPFQVVFEGVRGSGSRGDIALDDISLSP 154


                  ...
gi 256665241  538 GPC 540
Cdd:cd06263   155 GPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 217-373 5.70e-32

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: 124.40  E-value: 5.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   217 CTFDTlNDLCGWsWVPTATGAKWTQKKGPTgkQGVGPAEDFS-NPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCm 292
Cdd:pfam00629    1 CDFED-GNLCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   293 tLSFHYIMHGQGHEEgLFVYATFLGNIRKYTLFS--GHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISI 369
Cdd:pfam00629   76 -LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 256665241   370 A--PCG 373
Cdd:pfam00629  154 SsgPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 47-208 2.64e-31

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: 122.49  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263     1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263    78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                  ...
gi 256665241  206 GTC 208
Cdd:cd06263   155 GPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 217-371 6.58e-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: 118.25  E-value: 6.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  217 CTFDTlnDLCGWSWVPTaTGAKWTQKKGPTGKQGVGPAeDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCmt 293
Cdd:cd06263     1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPD-HTHGTGSGHYLYVESSSGREGQKARLLSPLLPpprSSHC-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  294 LSFHYIMHGQGHEEgLFVYATFLGNIRKYTLF--SGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA 370
Cdd:cd06263    75 LSFWYHMYGSGVGT-LNVYVREEGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                  .
gi 256665241  371 P 371
Cdd:cd06263   154 P 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1324-1477 5.58e-29

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: 115.96  E-value: 5.58e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   1324 ATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNStdHFFRITANTEERGvEGVSCLDKVVISLPETTVTMISGRHTLI 1403
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241   1404 GD-QEVTLPAILSDDT-YVGLSGRFVELRTTFGL-RVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDG 1477
Cdd:smart00216   87 VNgQQVSLPYKTSDGSiQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 4908-5061 2.51e-25

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: 105.56  E-value: 2.51e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   4908 RCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRgiepLIMEGRNKISPKGSSTLHEVTTIVYGYKIQL-QEELVVL 4986
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241   4987 VNDEKVAVPYNPNEHLRVMLRAQRLLLV-TDFE-MVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSG 5061
Cdd:smart00216   87 VNGQQVSLPYKTSDGSIQIRSSGGYLVViTSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-209 8.73e-25

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: 103.60  E-value: 8.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    47 CDFEDNSrpFCDWSQMSADDGDWIRTTGPSLTgtSGPPGG--YPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQG-PLCV 123
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   124 HFAFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSI 203
Cdd:pfam00629   77 RFWYHMSGSGVGT--LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ-PFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 256665241   204 QRGTCN 209
Cdd:pfam00629  154 SSGPCP 159
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1911-1982 1.10e-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: 92.02  E-value: 1.10e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256665241   1911 WTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFCP 1982
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2100-2260 1.11e-21

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: 95.16  E-value: 1.11e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   2100 GECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNtnmPFFMISAKtdiNTNGKNKTFGVYQLYIDIFNFHITLQKDHL 2179
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLK---NVPCGGGATCLKSVKVELNGDEIELKDDNG 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   2180 VLIslINDSIVTLPTTTHIPGVSV-MTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTP 2258
Cdd:smart00216   84 KVT--VNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 256665241   2259 SG 2260
Cdd:smart00216  162 DG 163
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 47-208 6.72e-20

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: 89.71  E-value: 6.72e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241     47 CDFEDNsrPFCDWSQMSADDGDWIRTTgpSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQ-GPLCVHF 125
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    126 AFHMFGLswGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPAdHDIPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:smart00137   82 WYYMYGS--GSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 256665241    206 GTC 208
Cdd:smart00137  159 GPC 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1521-1596 4.09e-19

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 84.70  E-value: 4.09e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241   1521 TMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFCP 1596
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3521-3575 1.69e-18

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: 81.97  E-value: 1.69e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3521 CKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNeDGNSNCA 3575
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3761-3815 3.31e-18

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: 81.20  E-value: 3.31e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3761 CKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNeDGNSNCA 3815
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3164-3218 1.67e-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: 79.27  E-value: 1.67e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3164 CKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDlKDGSSNCT 3218
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3044-3098 1.79e-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: 79.27  E-value: 1.79e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3044 CKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIeDGNSNCT 3098
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2804-2858 2.03e-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: 78.88  E-value: 2.03e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2804 CKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDlEDGNSNCT 2858
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2444-2498 2.22e-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: 78.88  E-value: 2.22e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2444 CKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNsNDGSSNCV 2498
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3997-4051 3.44e-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: 78.11  E-value: 3.44e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3997 CKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSgDGSSNCT 4051
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4133-4184 7.49e-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: 77.34  E-value: 7.49e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 256665241  4133 CKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSR 4184
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3401-3455 1.06e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 76.96  E-value: 1.06e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3401 CKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSeGSSTCT 3455
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2564-2618 2.56e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.80  E-value: 2.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2564 CQHTQGGFIPAGKSWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIeDGTSNCA 2618
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3641-3695 3.46e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.42  E-value: 3.46e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3641 CKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSFQCPPGAYCKDNeDGSSNCA 3695
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4488-4542 3.60e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.42  E-value: 3.60e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4488 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4542
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 5115-5191 7.27e-16

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: 75.45  E-value: 7.27e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241   5115 SSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTgwkTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCA 5191
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCA---CGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3284-3338 1.24e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.88  E-value: 1.24e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3284 CKNTQGAFISADKTWISRGCTQSCTCSAGAIHCRNFKCPSGTYCKNGDnGSSNCT 3338
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4368-4422 1.95e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.49  E-value: 1.95e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4368 CKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDsVDGGSNCT 4422
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2924-2978 2.06e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 2.06e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2924 CKDTQGVLIPADKTWINRGCTQSCTCKGGAIQCQKYHCSSGTYCKDMeDDSSSCA 2978
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4848-4902 3.17e-15

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: 72.72  E-value: 3.17e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4848 CKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNeDGSSDCA 4902
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2684-2738 4.97e-15

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: 72.34  E-value: 4.97e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2684 CKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDiKDDTSNCT 2738
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4253-4300 5.64e-15

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: 71.95  E-value: 5.64e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 256665241  4253 CKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSS 4300
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND 48
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3881-3931 8.09e-15

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: 71.57  E-value: 8.09e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  3881 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3931
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4728-4782 1.14e-14

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: 71.18  E-value: 1.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4728 CKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESeDGSSNCV 4782
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 217-372 1.16e-14

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: 74.69  E-value: 1.16e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    217 CTFDTlNDLCGWSwVPTATGAKWTQKKGPTGkqGVGPAEDfSNPGNGYYMLLDSTNARPGQKAVLLSPLSH-SRGCMTLS 295
Cdd:smart00137    6 CDFEE-GSTCGWH-QDSNDDGHWERVSSATG--IPGPNRD-HTTGNGHFMFFETSSGAEGQTARLLSPPLYeNRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    296 FHYIMHGQGHeeGLFVYATFLGNIRKYTL---FSGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA- 370
Cdd:smart00137   81 FWYYMYGSGS--GTLNVYVRENNGSQDTLlwsRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDILLSn 158


                    ...
gi 256665241    371 -PC 372
Cdd:smart00137  159 gPC 161
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1914-1981 1.26e-14

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: 71.64  E-value: 1.26e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256665241  1914 KCAILMNPlGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFC 1981
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4608-4662 2.74e-14

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: 70.03  E-value: 2.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4608 CKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNeGNSNCV 4662
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 486-913 1.03e-13

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: 77.69  E-value: 1.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   486 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 565
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   566 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 644
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   645 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 724
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   725 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 798
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   799 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 877
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 256665241   878 TTLPTEVLtvPIEVTTFPtGETTVPTEVPTVSTEMT 913
Cdd:pfam17823  380 TTQPSPLL--PTQGAAGP-GILLAPEQVATEATAGT 412
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1527-1595 7.54e-13

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: 66.63  E-value: 7.54e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256665241  1527 LCGQLvNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFC 1595
Cdd:pfam08742    1 KCGLL-SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 5120-5190 5.36e-12

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: 63.94  E-value: 5.36e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256665241  5120 CRVLVDpQGPFAACHQIIAPEPFEQRCMLDMCtgwKTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHC 5190
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMC---SCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1654-1708 7.97e-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: 63.09  E-value: 7.97e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1654 CTSFQGRYFKLQEQWFNPDCKEICTCeSHNHILCKPWKCKAQEACSYKNGVLGCH 1708
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1599-1652 2.17e-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: 61.95  E-value: 2.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241 1599 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1652
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1599-1652 6.19e-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: 60.48  E-value: 6.19e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1599 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1652
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1266-1319 1.62e-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: 59.24  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  1266 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1319
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
 702-857 1.69e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 64.54  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  702 ETTL-YTEVPTVPTEVTGVH--TEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPee 778
Cdd:PHA03255   19 ETSLiWTSSGSSTASAGNVTgtTAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTP-- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  779 tILTTLYTEVPTVPTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 853
Cdd:PHA03255   91 -VPTTSNASTINVTTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169


                  ....
gi 256665241  854 PPEE 857
Cdd:PHA03255  170 VPDE 173
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1985-2039 1.43e-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: 56.63  E-value: 1.43e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241  1985 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 5194-5247 1.46e-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: 56.63  E-value: 1.46e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  5194 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDT-QSLPVTHC 5247
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4548-4606 3.15e-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: 55.86  E-value: 3.15e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4548 CPAHSHYSKCLPPCQPSCSDPdghceGTSPEAPSTCEEGCVCEPDYVLSND-KCVPSSEC 4606
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1985-2039 5.05e-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: 55.02  E-value: 5.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241 1985 CPPRSSYNPCANSCPATCLTLSTPRDCpTLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 5249-5302 6.72e-09

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: 54.62  E-value: 6.72e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  5249 CTADGIYYKLGDSFVTNDCSQHCTCaSQGILLCEPYGCRAGESCMVANFTRGCF 5302
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4548-4606 1.11e-08

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: 54.25  E-value: 1.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4548 CPAHSHYSKCLPPCQPSCSDPDghcegTSPEAPSTCEEGCVCEPDYVLS-NDKCVPSSEC 4606
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3937-3995 2.42e-08

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: 53.16  E-value: 2.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3937 CPAHSHFTSCLPSCPPSCANLDGSCEQTSPkvpstCKEGCLCQPGYFLNN-GKCVLQTHC 3995
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP-----CVEGCVCPPGFVRNSgGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3937-3995 8.55e-08

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: 51.55  E-value: 8.55e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3937 CPAHSHFTSCLPSCPPSCANLDgsceqTSPKVPSTCKEGCLCQPGYFLN-NGKCVLQTHC 3995
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4073-4131 1.42e-07

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: 51.23  E-value: 1.42e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4073 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4131
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3104-3162 2.13e-07

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: 50.46  E-value: 2.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3104 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3162
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2314-2380 2.30e-07

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: 50.84  E-value: 2.30e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  2314 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2380
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4073-4131 2.32e-07

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: 50.39  E-value: 2.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 4073 CPAHSHFTSCLPSCPPSCSNLD--GSCvesnfkaPSVCKKGCICQPGYLLN-NDKCVLRIQC 4131
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3104-3162 3.30e-07

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: 50.01  E-value: 3.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3104 CPANSNFTSCLPSCQPSCSNTDvhcegSSPNALSSCREGCVCQSGYVLH-NDKCILRNQC 3162
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2384-2442 3.90e-07

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: 49.62  E-value: 3.90e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 2384 CPAHSHYTNCLPSCPPSCLDPD--SRCegsghkvPATCREGCICQPDYVL-LNDKCVLRSHC 2442
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3461-3519 5.89e-07

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: 49.31  E-value: 5.89e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3461 CPAHTQYTSCLPSCLPSCLDPEGlckdiSPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3519
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2864-2922 6.01e-07

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: 49.24  E-value: 6.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2864 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2922
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2384-2442 7.10e-07

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: 48.92  E-value: 7.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2384 CPAHSHYTNCLPSCPPSCLDPDSRCegsghKVPATCREGCICQPDYVLLND-KCVLRSHC 2442
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4788-4846 7.98e-07

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: 48.85  E-value: 7.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 4788 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4308-4366 7.98e-07

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: 48.85  E-value: 7.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4366
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2864-2922 8.06e-07

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: 48.92  E-value: 8.06e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2864 CPAHSHYTNCLPTCQPSCSDPdghceGSSTKAPSACKEGCVCEPDYVMLNN-KCVPRIEC 2922
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4788-4846 8.14e-07

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: 48.92  E-value: 8.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4788 CPANSLYTHCLPTCLPSCSNPDGRCegtshKAPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2504-2562 9.16e-07

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: 48.92  E-value: 9.16e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241  2504 CPAHSKFTDCLPPCHPSCSDP--DGHCEGIstnahsnCKEGCVCQPGYVLRND-KCVLRIEC 2562
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLspPDVCPEP-------CVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3224-3282 1.12e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.54  E-value: 1.12e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3224 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3282
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1215-1264 1.17e-06

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: 48.47  E-value: 1.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241 1215 CPPNAHIELC--ACPASCESPK--PSCQPPCIPGCVCNPGFLFS-NNQCINESSC 1264
Cdd:cd19941     1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2624-2682 1.23e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.54  E-value: 1.23e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2624 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 2682
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3224-3282 1.30e-06

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: 48.47  E-value: 1.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3224 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3282
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4308-4366 1.30e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVLRED-KCVLRTQC 4366
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3344-3399 1.54e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  3344 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3399
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 5194-5238 1.84e-06

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: 48.08  E-value: 1.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 256665241 5194 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSD 5238
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNS 45
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3344-3399 1.93e-06

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: 47.70  E-value: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241 3344 CPTNSQFTDCLPSCVPSCSNRceVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3399
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANP--NAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3461-3519 2.17e-06

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: 47.70  E-value: 2.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3461 CPAHTQYTSCLPSCLPSCLDPEglckdISPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3519
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2504-2562 2.51e-06

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: 47.70  E-value: 2.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2504 CPAHSKFTDCLPPCHPSCSDPDghcegISTNAHSNCKEGCVCQPGYVL-RNDKCVLRIEC 2562
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2744-2802 2.61e-06

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: 47.31  E-value: 2.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2744 CPDHSLYTHCLPSCLPSCSDPDglcrgTSPEAPSTCKEGCVCEPDYVLS-NDKCVLRIEC 2802
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4193-4251 3.37e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.00  E-value: 3.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4193 CPAHSHYTNCLPACSRSCTDLdghceGTSPKVPSPCKEGCLCQPGYVVHNH-KCVLQIHC 4251
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1215-1264 5.62e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 5.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1215 CPPNAHIELC--ACPASCESPKPS--CQPPCIPGCVCNPGFLFSNN-QCINESSC 1264
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPPdvCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2744-2802 6.08e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 6.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2744 CPDHSLYTHCLPSCLPSCSDPdglcrGTSPEAPSTCKEGCVCEPDYVLSND-KCVLRIEC 2802
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
636-928 7.08e-06

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 51.98  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  636 SPTEVTPVPT-------DVTaayVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTE 708
Cdd:COG3291    36 TSTEANPSHTyttpgtyTVT---LTVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  709 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEV 788
Cdd:COG3291   113 GVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTG 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  789 PTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSP 868
Cdd:COG3291   193 TIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVV 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  869 EETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETS 928
Cdd:COG3291   273 TTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTV 332
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2984-3042 8.08e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.23  E-value: 8.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2984 CPAHSHFTNCLPPCQPSCLDseghcEGSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 3042
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4668-4726 9.83e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 45.84  E-value: 9.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4668 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4726
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2324-2381 1.35e-05

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: 46.18  E-value: 1.35e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 256665241   2324 AHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCP 2381
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2624-2682 1.53e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.39  E-value: 1.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2624 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVV-LNNKCVPRIEC 2682
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4193-4251 1.93e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 1.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4193 CPAHSHYTNCLPACSRSCTDLDghcegTSPKVPSPCKEGCLCQPGYVVH-NHKCVLQIHC 4251
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4668-4726 2.18e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 2.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4668 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4726
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2984-3042 2.68e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 44.62  E-value: 2.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 2984 CPAHSHFTNCLPPCQPSC--LDSEGHCegsttkaPSACQEGCVCEPDYVV-LNNKCVPRIEC 3042
Cdd:cd19941     1 CPPNEVYSECGSACPPTCanPNAPPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4428-4486 4.16e-05

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: 43.92  E-value: 4.16e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4428 CPAHSHHTYCLPSCIPSCSNvndrcESTSLQRPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4486
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3821-3879 4.78e-05

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: 43.92  E-value: 4.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3821 CPTHSNYTDCLPFCLPSCLDPSalcggTSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3879
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2041-2096 6.06e-05

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 43.45  E-value: 6.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241  2041 CSDQDGSYHLLGESWYTEKtCTTLCTCSaHSNITCSPTACKANHVCLRQEGLLRCA 2096
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4428-4486 9.22e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.07  E-value: 9.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 4428 CPAHSHHTYCLPSCIPSCSNVND--RCestslqrPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4486
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAppPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3821-3879 1.39e-04

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: 42.69  E-value: 1.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3821 CPTHSNYTDCLPFCLPSCLDPSAlcggtSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3879
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNA-----PPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3581-3639 1.80e-04

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: 42.37  E-value: 1.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3581 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLSNN-KCLLRNRC 3639
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3581-3639 2.15e-04

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: 41.92  E-value: 2.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3581 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLS-NNKCLLRNRC 3639
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1715-1865 3.21e-49

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: 173.71  E-value: 3.21e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  1715 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1794
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241  1795 NNQRVVLPVWPSQGRVTIRLSGI-FVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNL 1865
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1326-1478 6.66e-43

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: 155.61  E-value: 6.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  1326 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1405
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1406 QEVTLPAILSD-DTYVGLSGR-FVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGM 1478
Cdd:pfam00094   80 QKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1707-1863 1.14e-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: 146.39  E-value: 1.14e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   1707 CHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCwskSQENNFVVSATNEIHDGNLEVsyVKAVHVQVFDLKISM 1786
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGATC--LKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256665241   1787 FKGQ-KVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGL-QVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDD 1863
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4909-5062 3.19e-39

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 144.82  E-value: 3.19e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4909 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4987
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  4988 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGV 5062
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 375-540 1.89e-37

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: 140.17  E-value: 1.89e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    375 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 453
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    454 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 533
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 256665241    534 LISHGPC 540
Cdd:smart00137  155 LLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 379-541 2.82e-37

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: 139.42  E-value: 2.82e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   379 CDFEDrvHPFCDWNQVYGDMGHWSWGSksVPTLIAGSPREFPYGGE--HYIFFDSVKlSQEGQSARLVSPPFCAPG-DIC 455
Cdd:pfam00629    1 CDFED--GNLCGWTQDSSDDFDWERVS--GPSVKTGPSSDHTQGTGsgHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   456 VEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILI 535
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 256665241   536 SHGPCR 541
Cdd:pfam00629  154 SSGPCP 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2102-2260 2.62e-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: 2.62e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2102 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2181
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2182 IsliNDSIVTLPTTTHIPGVSVMTED-VYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSG 2260
Cdd:pfam00094   77 V---NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 379-540 1.84e-33

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: 128.65  E-value: 1.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  379 CDFEDrvhPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKlSQEGQSARLVSPPFCAP-GDICVE 457
Cdd:cd06263     1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  458 FAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILISH 537
Cdd:cd06263    77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSA-SSKPFQVVFEGVRGSGSRGDIALDDISLSP 154


                  ...
gi 256665241  538 GPC 540
Cdd:cd06263   155 GPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 217-373 5.70e-32

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: 124.40  E-value: 5.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   217 CTFDTlNDLCGWsWVPTATGAKWTQKKGPTgkQGVGPAEDFS-NPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCm 292
Cdd:pfam00629    1 CDFED-GNLCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   293 tLSFHYIMHGQGHEEgLFVYATFLGNIRKYTLFS--GHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISI 369
Cdd:pfam00629   76 -LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 256665241   370 A--PCG 373
Cdd:pfam00629  154 SsgPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 47-208 2.64e-31

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: 122.49  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263     1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263    78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                  ...
gi 256665241  206 GTC 208
Cdd:cd06263   155 GPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 217-371 6.58e-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: 118.25  E-value: 6.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  217 CTFDTlnDLCGWSWVPTaTGAKWTQKKGPTGKQGVGPAeDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCmt 293
Cdd:cd06263     1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPD-HTHGTGSGHYLYVESSSGREGQKARLLSPLLPpprSSHC-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  294 LSFHYIMHGQGHEEgLFVYATFLGNIRKYTLF--SGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA 370
Cdd:cd06263    75 LSFWYHMYGSGVGT-LNVYVREEGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                  .
gi 256665241  371 P 371
Cdd:cd06263   154 P 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1324-1477 5.58e-29

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: 115.96  E-value: 5.58e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   1324 ATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNStdHFFRITANTEERGvEGVSCLDKVVISLPETTVTMISGRHTLI 1403
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241   1404 GD-QEVTLPAILSDDT-YVGLSGRFVELRTTFGL-RVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDG 1477
Cdd:smart00216   87 VNgQQVSLPYKTSDGSiQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 4908-5061 2.51e-25

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: 105.56  E-value: 2.51e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   4908 RCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRgiepLIMEGRNKISPKGSSTLHEVTTIVYGYKIQL-QEELVVL 4986
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241   4987 VNDEKVAVPYNPNEHLRVMLRAQRLLLV-TDFE-MVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSG 5061
Cdd:smart00216   87 VNGQQVSLPYKTSDGSIQIRSSGGYLVViTSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-209 8.73e-25

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: 103.60  E-value: 8.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    47 CDFEDNSrpFCDWSQMSADDGDWIRTTGPSLTgtSGPPGG--YPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQG-PLCV 123
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   124 HFAFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSI 203
Cdd:pfam00629   77 RFWYHMSGSGVGT--LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ-PFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 256665241   204 QRGTCN 209
Cdd:pfam00629  154 SSGPCP 159
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1911-1982 1.10e-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: 92.02  E-value: 1.10e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256665241   1911 WTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFCP 1982
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2100-2260 1.11e-21

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: 95.16  E-value: 1.11e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   2100 GECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNtnmPFFMISAKtdiNTNGKNKTFGVYQLYIDIFNFHITLQKDHL 2179
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLK---NVPCGGGATCLKSVKVELNGDEIELKDDNG 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   2180 VLIslINDSIVTLPTTTHIPGVSV-MTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTP 2258
Cdd:smart00216   84 KVT--VNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 256665241   2259 SG 2260
Cdd:smart00216  162 DG 163
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 47-208 6.72e-20

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: 89.71  E-value: 6.72e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241     47 CDFEDNsrPFCDWSQMSADDGDWIRTTgpSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQ-GPLCVHF 125
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    126 AFHMFGLswGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPAdHDIPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:smart00137   82 WYYMYGS--GSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 256665241    206 GTC 208
Cdd:smart00137  159 GPC 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1521-1596 4.09e-19

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 84.70  E-value: 4.09e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241   1521 TMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFCP 1596
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3521-3575 1.69e-18

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: 81.97  E-value: 1.69e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3521 CKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNeDGNSNCA 3575
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3761-3815 3.31e-18

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: 81.20  E-value: 3.31e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3761 CKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNeDGNSNCA 3815
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3164-3218 1.67e-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: 79.27  E-value: 1.67e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3164 CKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDlKDGSSNCT 3218
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3044-3098 1.79e-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: 79.27  E-value: 1.79e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3044 CKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIeDGNSNCT 3098
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2804-2858 2.03e-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: 78.88  E-value: 2.03e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2804 CKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDlEDGNSNCT 2858
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2444-2498 2.22e-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: 78.88  E-value: 2.22e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2444 CKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNsNDGSSNCV 2498
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3997-4051 3.44e-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: 78.11  E-value: 3.44e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3997 CKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSgDGSSNCT 4051
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4133-4184 7.49e-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: 77.34  E-value: 7.49e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 256665241  4133 CKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSR 4184
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3401-3455 1.06e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 76.96  E-value: 1.06e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3401 CKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSeGSSTCT 3455
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2564-2618 2.56e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.80  E-value: 2.56e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2564 CQHTQGGFIPAGKSWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIeDGTSNCA 2618
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3641-3695 3.46e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.42  E-value: 3.46e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3641 CKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSFQCPPGAYCKDNeDGSSNCA 3695
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4488-4542 3.60e-16

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 75.42  E-value: 3.60e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4488 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4542
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 5115-5191 7.27e-16

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: 75.45  E-value: 7.27e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241   5115 SSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTgwkTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCA 5191
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCA---CGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3284-3338 1.24e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.88  E-value: 1.24e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  3284 CKNTQGAFISADKTWISRGCTQSCTCSAGAIHCRNFKCPSGTYCKNGDnGSSNCT 3338
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4368-4422 1.95e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.49  E-value: 1.95e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4368 CKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDsVDGGSNCT 4422
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2924-2978 2.06e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 2.06e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2924 CKDTQGVLIPADKTWINRGCTQSCTCKGGAIQCQKYHCSSGTYCKDMeDDSSSCA 2978
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4848-4902 3.17e-15

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: 72.72  E-value: 3.17e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4848 CKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNeDGSSDCA 4902
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2684-2738 4.97e-15

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: 72.34  E-value: 4.97e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  2684 CKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDiKDDTSNCT 2738
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4253-4300 5.64e-15

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: 71.95  E-value: 5.64e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 256665241  4253 CKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSS 4300
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND 48
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3881-3931 8.09e-15

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: 71.57  E-value: 8.09e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  3881 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3931
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4728-4782 1.14e-14

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: 71.18  E-value: 1.14e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4728 CKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESeDGSSNCV 4782
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 217-372 1.16e-14

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: 74.69  E-value: 1.16e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    217 CTFDTlNDLCGWSwVPTATGAKWTQKKGPTGkqGVGPAEDfSNPGNGYYMLLDSTNARPGQKAVLLSPLSH-SRGCMTLS 295
Cdd:smart00137    6 CDFEE-GSTCGWH-QDSNDDGHWERVSSATG--IPGPNRD-HTTGNGHFMFFETSSGAEGQTARLLSPPLYeNRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241    296 FHYIMHGQGHeeGLFVYATFLGNIRKYTL---FSGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA- 370
Cdd:smart00137   81 FWYYMYGSGS--GTLNVYVRENNGSQDTLlwsRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDILLSn 158


                    ...
gi 256665241    371 -PC 372
Cdd:smart00137  159 gPC 161
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1914-1981 1.26e-14

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: 71.64  E-value: 1.26e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256665241  1914 KCAILMNPlGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFC 1981
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4608-4662 2.74e-14

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: 70.03  E-value: 2.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  4608 CKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNeGNSNCV 4662
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 486-913 1.03e-13

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: 77.69  E-value: 1.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   486 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 565
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   566 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 644
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   645 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 724
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   725 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 798
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   799 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 877
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 256665241   878 TTLPTEVLtvPIEVTTFPtGETTVPTEVPTVSTEMT 913
Cdd:pfam17823  380 TTQPSPLL--PTQGAAGP-GILLAPEQVATEATAGT 412
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1527-1595 7.54e-13

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: 66.63  E-value: 7.54e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256665241  1527 LCGQLvNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFC 1595
Cdd:pfam08742    1 KCGLL-SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 546-940 3.16e-12

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: 73.80  E-value: 3.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   546 TEIPSSPLLPP--TGPSeSTVPTLPMEQPTSPTKATTVTIEIPTTPTEeatiptetttvptevinvSPKET---SIPPEV 620
Cdd:pfam05109  446 TGLPSSTHVPTnlTAPA-STGPTVSTADVTSPTPAGTTSGASPVTPSP------------------SPRDNgteSKAPDM 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   621 TIPTEVITVSPEEIISPTEVTPVPT-DVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFP 699
Cdd:pfam05109  507 TSPTSAVTTPTPNATSPTPAVTTPTpNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTP 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   700 TGETTLYTEVPTVPTEVTGVHT-EVTNVSPEETSVPTEET--ISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVpp 776
Cdd:pfam05109  587 TPNATSPTVGETSPQANTTNHTlGGTSSTPVVTSPPKNATsaVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNST-- 664

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   777 eetilttlyTEVPTVPTEVTGVHTEVTNVSPEETSvpteetiSTEVTTVSPEETtlptevPTVSTEVTNVSPEETSVPPE 856
Cdd:pfam05109  665 ---------SHMPLLTSAHPTGGENITQVTPASTS-------THHVSTSSPAPR------PGTTSQASGPGNSSTSTKPG 722

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   857 ETILTEITtvSPEETVFPIEGTTLPTEVLTVpievtTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPT---EV 933
Cdd:pfam05109  723 EVNVTKGT--PPKNATSPQAPSGQKTAVPTV-----TSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRtryNA 795


                   ....*..
gi 256665241   934 ATVLPAS 940
Cdd:pfam05109  796 TTYLPPS 802
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 5120-5190 5.36e-12

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: 63.94  E-value: 5.36e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256665241  5120 CRVLVDpQGPFAACHQIIAPEPFEQRCMLDMCtgwKTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHC 5190
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMC---SCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1654-1708 7.97e-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: 63.09  E-value: 7.97e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1654 CTSFQGRYFKLQEQWFNPDCKEICTCeSHNHILCKPWKCKAQEACSYKNGVLGCH 1708
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 621-938 8.37e-12

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: 71.53  E-value: 8.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   621 TIPTEVITVSPEEIISPTEVTPVPTDVT----AAYVEATNASPEETsvpPEVTILTEVTT-------------VSPEETT 683
Cdd:pfam17823   46 AVPRADNKSSEQ*NFCAATAAPAPVTLTkgtsAAHLNSTEVTAEHT---PHGTDLSEPATregaadgaasralAAAASSS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   684 vPTEVPIVLIEATAFPTGE--TTLYTEVPTVPTEVTGVHTEVTNVSPEE-TSVPTEETISTEVTTVSPEETTLPTE--VP 758
Cdd:pfam17823  123 -PSSAAQSLPAAIAALPSEafSAPRAAACRANASAAPRAAIAAASAPHAaSPAPRTAASSTTAASSTTAASSAPTTaaSS 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   759 TVSTeVTNVSPEETSVPPEET-ILTTLYTEVPTVPTEVTGVHTEVTNVSPE-----ETSVPTEETISTEVTTVSPEETTl 832
Cdd:pfam17823  202 APAT-LTPARGISTAATATGHpAAGTALAAVGNSSPAAGTVTAAVGTVTPAalatlAAAAGTVASAAGTINMGDPHARR- 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   833 PTEVPTVSTEVTNVSPEETSVPPEETILTEITT------VSPEETVFPIEGTTLPTEVLTVPIEVTTFPTgETTVPTEVP 906
Cdd:pfam17823  280 LSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTdqpvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVT-TTKAQAKEP 358

                          330       340       350
                   ....*....|....*....|....*....|...
gi 256665241   907 TVSTemtgVHTEVTTVFPE-ETSIPTEVATVLP 938
Cdd:pfam17823  359 SASP----VPVLHTSMIPEvEATSPTTQPSPLL 387
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1599-1652 2.17e-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: 61.95  E-value: 2.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241 1599 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1652
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1599-1652 6.19e-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: 60.48  E-value: 6.19e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1599 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1652
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1266-1319 1.62e-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: 59.24  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  1266 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1319
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
 702-857 1.69e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 64.54  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  702 ETTL-YTEVPTVPTEVTGVH--TEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPee 778
Cdd:PHA03255   19 ETSLiWTSSGSSTASAGNVTgtTAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTP-- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  779 tILTTLYTEVPTVPTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 853
Cdd:PHA03255   91 -VPTTSNASTINVTTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169


                  ....
gi 256665241  854 PPEE 857
Cdd:PHA03255  170 VPDE 173
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1985-2039 1.43e-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: 56.63  E-value: 1.43e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241  1985 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 5194-5247 1.46e-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: 56.63  E-value: 1.46e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  5194 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDT-QSLPVTHC 5247
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4548-4606 3.15e-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: 55.86  E-value: 3.15e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4548 CPAHSHYSKCLPPCQPSCSDPdghceGTSPEAPSTCEEGCVCEPDYVLSND-KCVPSSEC 4606
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1985-2039 5.05e-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: 55.02  E-value: 5.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241 1985 CPPRSSYNPCANSCPATCLTLSTPRDCpTLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 725-1062 6.26e-09

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: 62.28  E-value: 6.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   725 NVSPEetSVPTEETISTE-----VTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTT-------LYTEVPTVP 792
Cdd:pfam17823   41 NASGD--AVPRADNKSSEq*nfcAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDLSEPATregaadgAASRALAAA 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   793 TEVTGvhTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSpeeTSVPPEETILTEITTVSPEETV 872
Cdd:pfam17823  119 ASSSP--SSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAA---SPAPRTAASSTTAASSTTAASS 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   873 FPIEGTTlpTEVLTVpieVTTFPTGETTVPTEVPTVSTemtgVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTPTEV 952
Cdd:pfam17823  194 APTTAAS--SAPATL---TPARGISTAATATGHPAAGT----ALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVA 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   953 TTTPPEETTIPAEVTTIPPVSIPSEETTTPTEVTTTPPEETTIpAEVTTVPPV------SIPSEETTTPTEVTTTPPEET 1026
Cdd:pfam17823  265 SAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPI-IQVSTDQPVhntagePTPSPSNTTLEPNTPKSVAST 343

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 256665241  1027 TIPAEVTTVPPVSIPSeETTIPTEVTTVPPE-ETTIP 1062
Cdd:pfam17823  344 NLAVVTTTKAQAKEPS-ASPVPVLHTSMIPEvEATSP 379
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 5249-5302 6.72e-09

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: 54.62  E-value: 6.72e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 256665241  5249 CTADGIYYKLGDSFVTNDCSQHCTCaSQGILLCEPYGCRAGESCMVANFTRGCF 5302
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4548-4606 1.11e-08

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: 54.25  E-value: 1.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4548 CPAHSHYSKCLPPCQPSCSDPDghcegTSPEAPSTCEEGCVCEPDYVLS-NDKCVPSSEC 4606
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 652-832 1.31e-08

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 61.98  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  652 VEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPtgettlytEVPTV---PTEVTGVHTEVTNVSP 728
Cdd:PRK10811  848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVV--------EEPVVvaePQPEEVVVVETTHPEV 919

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  729 EETSVPTEETISTEVTTVSPEETTLPTEvptvstEVTNVSPEETSVPPEETIlttlyTEVPTVPTEVTgVHTEVTNVSPE 808
Cdd:PRK10811  920 IAAPVTEQPQVITESDVAVAQEVAEHAE------PVVEPQDETADIEEAAET-----AEVVVAEPEVV-AQPAAPVVAEV 987

                         170       180
                  ....*....|....*....|....
gi 256665241  809 ETSVPTEETISTEVTTVSPEETTL 832
Cdd:PRK10811  988 AAEVETVTAVEPEVAPAQVPEATV 1011
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3937-3995 2.42e-08

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: 53.16  E-value: 2.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3937 CPAHSHFTSCLPSCPPSCANLDGSCEQTSPkvpstCKEGCLCQPGYFLNN-GKCVLQTHC 3995
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP-----CVEGCVCPPGFVRNSgGKCVPPSDC 55
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 560-921 3.69e-08

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: 60.32  E-value: 3.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   560 SESTVPTLPMEQPTSPTKATTV--TIEIPTTPTEEAtiptetttvptevinvSPKETSIPPEVTIPTEVITVSPEEIISP 637
Cdd:pfam05109  427 STTTSPTLNTTGFAAPNTTTGLpsSTHVPTNLTAPA----------------STGPTVSTADVTSPTPAGTTSGASPVTP 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   638 tevTPVP---------TDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTevpivliEATAFPTGETTLYTE 708
Cdd:pfam05109  491 ---SPSPrdngteskaPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPT-------SAVTTPTPNATSPTP 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   709 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTevtnvSPEETSVPPEETilttlyTEV 788
Cdd:pfam05109  561 AVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS-----TPVVTSPPKNAT------SAV 629

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   789 PTVPTEVTGVHTEVTNVSPEETSvpteETISTEVTTVSPEETTLPTEV-PTVSTEVTNVSPEETSVppeetilTEITTVS 867
Cdd:pfam05109  630 TTGQHNITSSSTSSMSLRPSSIS----ETLSPSTSDNSTSHMPLLTSAhPTGGENITQVTPASTST-------HHVSTSS 698

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   868 PEetvfPIEGT-------------TLPTEVLT---VPIEVTTFPTGETTVPTEVPTVSTemTGVHTEVTT 921
Cdd:pfam05109  699 PA----PRPGTtsqasgpgnsstsTKPGEVNVtkgTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTT 762
PHA03255 PHA03255
BDLF3; Provisional
 638-794 5.64e-08

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 57.22  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  638 TEVTPVP---TDVTAAyVEATNASPEeTSVPPEVTILTEVTTVSPEETTV--PTEVPIVLIEATAFPTGETTLYTEVPTV 712
Cdd:PHA03255   25 TSSGSSTasaGNVTGT-TAVTTPSPS-ASGPSTNQSTTLTTTSAPITTTAilSTNTTTVTSTGTTVTPVPTTSNASTINV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  713 PTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLpteVPTVSTEVTNVSPEETSvppeetilttlytE 787
Cdd:PHA03255  103 TTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTL---APTLSSKGTSNATKTTA-------------E 166


                  ....*..
gi 256665241  788 VPTVPTE 794
Cdd:PHA03255  167 LPTVPDE 173
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3937-3995 8.55e-08

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: 51.55  E-value: 8.55e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3937 CPAHSHFTSCLPSCPPSCANLDgsceqTSPKVPSTCKEGCLCQPGYFLN-NGKCVLQTHC 3995
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4073-4131 1.42e-07

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: 51.23  E-value: 1.42e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4073 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4131
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 629-910 2.02e-07

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: 58.00  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   629 VSPEEIISPTEVTPVPTDVTAAYVEATNASP---EETSVPPEVTIltEVTTVSPEETTVPTEVPIVLIEATafPTGETTL 705
Cdd:pfam05109  304 VFSDEIPASQDMPTNTTDITYVGDNATYSVPmvtSEDANSPNVTV--TAFWAWPNNTETDFKCKWTLTSGT--PSGCENI 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   706 ---YTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVS---PEETSVPpeeT 779
Cdd:pfam05109  380 sgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTtglPSSTHVP---T 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   780 ILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETI 859
Cdd:pfam05109  457 NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATS 536

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 256665241   860 LTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVST 910
Cdd:pfam05109  537 PTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPT 587
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3104-3162 2.13e-07

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: 50.46  E-value: 2.13e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3104 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3162
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2314-2380 2.30e-07

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: 50.84  E-value: 2.30e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  2314 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2380
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4073-4131 2.32e-07

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: 50.39  E-value: 2.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 4073 CPAHSHFTSCLPSCPPSCSNLD--GSCvesnfkaPSVCKKGCICQPGYLLN-NDKCVLRIQC 4131
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3104-3162 3.30e-07

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: 50.01  E-value: 3.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3104 CPANSNFTSCLPSCQPSCSNTDvhcegSSPNALSSCREGCVCQSGYVLH-NDKCILRNQC 3162
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2384-2442 3.90e-07

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: 49.62  E-value: 3.90e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 2384 CPAHSHYTNCLPSCPPSCLDPD--SRCegsghkvPATCREGCICQPDYVL-LNDKCVLRSHC 2442
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 559-792 5.47e-07

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 56.59  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  559 PSESTVPtLPMEQpTSPTKAT-TVTIEIPTTPTEEATIPTETTtvpteviNVSPKETSIPPEVTIPTEVITVSPEEIISP 637
Cdd:PRK10811  820 PTQSPMP-LTVAC-ASPEMASgKVWIRYPVVRPQDVQVEEQRE-------AEEVQVQPVVAEVPVAAAVEPVVSAPVVEA 890

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  638 TEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVptevpivlieatafptgettlytevptVPTEVT 717
Cdd:PRK10811  891 VAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVA---------------------------VAQEVA 943

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  718 GVHTEVTNVSPEETSVPTEETIsTEVTTVSPEETTLPTEVPTVSTEVTNVSP--EETSVPPEETILTTLYTEVPTVP 792
Cdd:PRK10811  944 EHAEPVVEPQDETADIEEAAET-AEVVVAEPEVVAQPAAPVVAEVAAEVETVtaVEPEVAPAQVPEATVEHNHATAP 1019
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3461-3519 5.89e-07

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: 49.31  E-value: 5.89e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3461 CPAHTQYTSCLPSCLPSCLDPEGlckdiSPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3519
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2864-2922 6.01e-07

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: 49.24  E-value: 6.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2864 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2922
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2384-2442 7.10e-07

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: 48.92  E-value: 7.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2384 CPAHSHYTNCLPSCPPSCLDPDSRCegsghKVPATCREGCICQPDYVLLND-KCVLRSHC 2442
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
rne PRK10811
ribonuclease E; Reviewed
 624-878 7.28e-07

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 56.20  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  624 TEVITVSPEE-IISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTV--------SPEETTV---------- 684
Cdd:PRK10811  737 EEAVAPVVEEtVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENRDNNgmprrsrrSPRHLRVsgqrrrryrd 816

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  685 ---PTEVPIVLIEATAFP---TGEttLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 758
Cdd:PRK10811  817 eryPTQSPMPLTVACASPemaSGK--VWIRYPVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEV 894

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  759 TVSTEVTNVSPEETSVPPEETilttlYTEVPTVP-TEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 837
Cdd:PRK10811  895 VEEPVVVAEPQPEEVVVVETT-----HPEVIAAPvTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVV 969

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 256665241  838 TVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGT 878
Cdd:PRK10811  970 VAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEAT 1010
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4788-4846 7.98e-07

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: 48.85  E-value: 7.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 4788 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4308-4366 7.98e-07

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: 48.85  E-value: 7.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4366
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2864-2922 8.06e-07

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: 48.92  E-value: 8.06e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2864 CPAHSHYTNCLPTCQPSCSDPdghceGSSTKAPSACKEGCVCEPDYVMLNN-KCVPRIEC 2922
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4788-4846 8.14e-07

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: 48.92  E-value: 8.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4788 CPANSLYTHCLPTCLPSCSNPDGRCegtshKAPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2504-2562 9.16e-07

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: 48.92  E-value: 9.16e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241  2504 CPAHSKFTDCLPPCHPSCSDP--DGHCEGIstnahsnCKEGCVCQPGYVLRND-KCVLRIEC 2562
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLspPDVCPEP-------CVEGCVCPPGFVRNSGgKCVPPSDC 55
rne PRK10811
ribonuclease E; Reviewed
 668-939 1.08e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 55.43  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  668 VTILTEVTTvsPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSP-EETSVPTEETISTEVTTV 746
Cdd:PRK10811  729 VRIEQSVAE--EAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENrDNNGMPRRSRRSPRHLRV 806

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  747 S------------PEETTLPTEVPTVSTE-----------VTNVSPEET--SVPPEETILTTLYTEVPTVPTEVTGVHTE 801
Cdd:PRK10811  807 SgqrrrryrderyPTQSPMPLTVACASPEmasgkvwirypVVRPQDVQVeeQREAEEVQVQPVVAEVPVAAAVEPVVSAP 886

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  802 VTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEET-ILTEITTVSPEETVFPIEGTTl 880
Cdd:PRK10811  887 VVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAeHAEPVVEPQDETADIEEAAET- 965

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256665241  881 pTEVLTVPIEVTTFPTGETTVPTEVPTV--STEMTGVHTEVTTVFPEETSIPTEVATVLPA 939
Cdd:PRK10811  966 -AEVVVAEPEVVAQPAAPVVAEVAAEVEtvTAVEPEVAPAQVPEATVEHNHATAPMTRAPA 1025
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3224-3282 1.12e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.54  E-value: 1.12e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3224 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3282
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1215-1264 1.17e-06

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: 48.47  E-value: 1.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241 1215 CPPNAHIELC--ACPASCESPK--PSCQPPCIPGCVCNPGFLFS-NNQCINESSC 1264
Cdd:cd19941     1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2624-2682 1.23e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.54  E-value: 1.23e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2624 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 2682
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3224-3282 1.30e-06

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: 48.47  E-value: 1.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3224 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3282
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4308-4366 1.30e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVLRED-KCVLRTQC 4366
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
rne PRK10811
ribonuclease E; Reviewed
 620-794 1.38e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 55.05  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  620 VTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASP-----EETSVPPEVTILTEVTTVSPEETTVPtevpivliE 694
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPvveavAEVVEEPVVVAEPQPEEVVVVETTHP--------E 918

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  695 ATAFPTGETTLYTEVPTVPtevtgVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVptVSTEVTNVSPEETSV 774
Cdd:PRK10811  919 VIAAPVTEQPQVITESDVA-----VAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVV--AQPAAPVVAEVAAEV 991

                         170       180
                  ....*....|....*....|
gi 256665241  775 PPEETILTTLYTEVPTVPTE 794
Cdd:PRK10811  992 ETVTAVEPEVAPAQVPEATV 1011
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3344-3399 1.54e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241  3344 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3399
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 5194-5238 1.84e-06

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: 48.08  E-value: 1.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 256665241 5194 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSD 5238
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNS 45
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3344-3399 1.93e-06

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: 47.70  E-value: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 256665241 3344 CPTNSQFTDCLPSCVPSCSNRceVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3399
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANP--NAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3461-3519 2.17e-06

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: 47.70  E-value: 2.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3461 CPAHTQYTSCLPSCLPSCLDPEglckdISPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3519
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2504-2562 2.51e-06

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: 47.70  E-value: 2.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2504 CPAHSKFTDCLPPCHPSCSDPDghcegISTNAHSNCKEGCVCQPGYVL-RNDKCVLRIEC 2562
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2744-2802 2.61e-06

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: 47.31  E-value: 2.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2744 CPDHSLYTHCLPSCLPSCSDPDglcrgTSPEAPSTCKEGCVCEPDYVLS-NDKCVLRIEC 2802
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4193-4251 3.37e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 47.00  E-value: 3.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4193 CPAHSHYTNCLPACSRSCTDLdghceGTSPKVPSPCKEGCLCQPGYVVHNH-KCVLQIHC 4251
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1215-1264 5.62e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 5.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  1215 CPPNAHIELC--ACPASCESPKPS--CQPPCIPGCVCNPGFLFSNN-QCINESSC 1264
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPPdvCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2744-2802 6.08e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 6.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2744 CPDHSLYTHCLPSCLPSCSDPdglcrGTSPEAPSTCKEGCVCEPDYVLSND-KCVLRIEC 2802
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 552-906 6.19e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  552 PLLPPTGPSEST---VPTlPMEQPTSPTKATTVTIEIPTTPTEEAT----IPTETTTVPTEVINVSPKETSIP-PEVTIP 623
Cdd:PHA03247 2553 PPLPPAAPPAAPdrsVPP-PRPAPRPSEPAVTSRARRPDAPPQSARprapVDDRGDPRGPAPPSPLPPDTHAPdPPPPSP 2631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  624 TEVITVSPEEIISPTEVTPVPTDVTA-----------AYVEATNAS-----PEETSVPPEVTILTEVTTVSPEETTvPTE 687
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarRLGRAAQASsppqrPRRRAARPTVGSLTSLADPPPPPPT-PEP 2710

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  688 VPIVLIEATAFPTG---------ETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 758
Cdd:PHA03247 2711 APHALVSATPLPPGpaaarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  759 TVSTEVTNVSPEETS-----VPPEETILTTLYTEVPTVPTEvtgvhTEVTNVSPEETSVPTEETISTE------------ 821
Cdd:PHA03247 2791 LSESRESLPSPWDPAdppaaVLAPAAALPPAASPAGPLPPP-----TSAQPTAPPPPPGPPPPSLPLGgsvapggdvrrr 2865

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  822 ----------VTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTvSPEETVFPIEGTTLPTEVLT-VPIE 890
Cdd:PHA03247 2866 ppsrspaakpAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPqPPLA 2944

                         410
                  ....*....|....*.
gi 256665241  891 VTTFPTGETTVPTEVP 906
Cdd:PHA03247 2945 PTTDPAGAGEPSGAVP 2960
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
636-928 7.08e-06

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 51.98  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  636 SPTEVTPVPT-------DVTaayVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTE 708
Cdd:COG3291    36 TSTEANPSHTyttpgtyTVT---LTVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  709 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEV 788
Cdd:COG3291   113 GVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTG 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  789 PTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSP 868
Cdd:COG3291   193 TIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVV 272

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  869 EETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETS 928
Cdd:COG3291   273 TTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTV 332
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2984-3042 8.08e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.23  E-value: 8.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  2984 CPAHSHFTNCLPPCQPSCLDseghcEGSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 3042
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4668-4726 9.83e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 45.84  E-value: 9.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4668 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4726
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2324-2381 1.35e-05

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: 46.18  E-value: 1.35e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 256665241   2324 AHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCP 2381
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2624-2682 1.53e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.39  E-value: 1.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 2624 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVV-LNNKCVPRIEC 2682
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 573-910 1.75e-05

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


Pssm-ID: 444243 [Multi-domain]  Cd Length: 613  Bit Score: 51.23  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  573 TSPTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYV 652
Cdd:COG5492   195 VVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGSG 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  653 EATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETS 732
Cdd:COG5492   275 STTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTS 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  733 V--PTEETISTEVtTVSPEETTLPTEVPTVS-TEVTNVSPEE--TSVPPEETILTtlYTevpTVPTEVTGVHT-EVTNVS 806
Cdd:COG5492   355 VtlAVGQTLTLTA-TVTPANATNKNVTWSSSdPSVATVDSNGlvTAVAAGTATIT--AT---TKDGGKTATCTvTVTAAG 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  807 PEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLT 886
Cdd:COG5492   429 STGTVVVVSLAATSAVSASVVLTPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTVTASVAEVATSVGGGATVTVT 508

                         330       340
                  ....*....|....*....|....
gi 256665241  887 VPIEVTTFPTGETTVPTEVPTVST 910
Cdd:COG5492   509 VSTAATVTVTVGVKSTGIAVAGST 532
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4193-4251 1.93e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 1.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4193 CPAHSHYTNCLPACSRSCTDLDghcegTSPKVPSPCKEGCLCQPGYVVH-NHKCVLQIHC 4251
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4668-4726 2.18e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 2.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 4668 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4726
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
PHA03255 PHA03255
BDLF3; Provisional
 777-932 2.65e-05

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 49.13  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  777 EETILTTLYTEVPTVPTEVTGVhTEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPE 856
Cdd:PHA03255   19 ETSLIWTSSGSSTASAGNVTGT-TAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTPV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  857 ETI----LTEITTVSPEETVFPIE---GTTLPT--EVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPeet 927
Cdd:PHA03255   92 PTTsnasTINVTTKVTAQNITATEagtGTSTGVtsNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELP--- 168


                  ....*
gi 256665241  928 SIPTE 932
Cdd:PHA03255  169 TVPDE 173
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2984-3042 2.68e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 44.62  E-value: 2.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 2984 CPAHSHFTNCLPPCQPSC--LDSEGHCegsttkaPSACQEGCVCEPDYVV-LNNKCVPRIEC 3042
Cdd:cd19941     1 CPPNEVYSECGSACPPTCanPNAPPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
YbbR COG4856
Cyclic di-AMP synthase regulator CdaR, YbbR domain [Signal transduction mechanisms];
636-905 3.73e-05

Cyclic di-AMP synthase regulator CdaR, YbbR domain [Signal transduction mechanisms];


Pssm-ID: 443884 [Multi-domain]  Cd Length: 392  Bit Score: 49.67  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  636 SPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILT----EVTTVSPEETTV----------PTEVPIVLIEATAFPTG 701
Cdd:COG4856    71 PRSVLLSLSASDIKAYVDLSGLKPGTHTVPVKVEGNLpsgvEVVEVSPSTITVtlekkvtkevPVEVEVKGKPAEGYEVG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  702 ETTLytEVPTVptEVTGVHTEVTNVSPEETSVPTE---ETISTEVT-------------TVSPEETTLptEVPTVSTEVT 765
Cdd:COG4856   151 EVSV--SPSTV--TVSGPESVVNQIDSVKATVDVSgatEDFTKSVPvkaydangneldvTISPSTVEV--TVPVLPSKTV 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  766 NVSPEETSVPPEETILTTLYTEVPTVptEVTGVHTEVTNVSpeetSVPTE--------ETISTEVTTVSPEETTLPTEVP 837
Cdd:COG4856   225 PVKVNTTGEPAEGYSVTSITVSPSTV--TIYGPEEVLDSIS----SIETEpidlsgltESTTVEVKLKLPEGVTLVDPPS 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  838 TVstEVT-NVSPEETSVPPEETILTE------ITTVSPEETVFPIEGT-----TLPTEVLTVPIEVTTFPTGETTVPTEV 905
Cdd:COG4856   299 TV--TVTvEVEKKTTKTFENIPITVEnlpdglTASISPGTVDVTVSGPksvldSLTASDIKAYVDLSGLGPGEYTVPVQV 376
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4428-4486 4.16e-05

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: 43.92  E-value: 4.16e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  4428 CPAHSHHTYCLPSCIPSCSNvndrcESTSLQRPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4486
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3821-3879 4.78e-05

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: 43.92  E-value: 4.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3821 CPTHSNYTDCLPFCLPSCLDPSalcggTSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3879
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 534-871 5.79e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  534 LISHGPCRVLLQTEIPSSPLLP--PTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTPTEEATIPTEtttvptevinvsp 611
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPaaPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR------------- 2781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  612 keTSIPPEVTIPTEVITVSPeeiiSPTEVTPVPTDVTA-AYVEATNASPEETSVPPevtilTEVTTVSPEETTVPTEVPI 690
Cdd:PHA03247 2782 --RLTRPAVASLSESRESLP----SPWDPADPPAAVLApAAALPPAASPAGPLPPP-----TSAQPTAPPPPPGPPPPSL 2850

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  691 VLIEATAfPTGETTLY-TEVPTVPTEVTGVHTEVTNVSPEETSVPTEetiSTEVTTVSPEETTLPtEVPTVSTEVTNVSP 769
Cdd:PHA03247 2851 PLGGSVA-PGGDVRRRpPSRSPAAKPAAPARPPVRRLARPAVSRSTE---SFALPPDQPERPPQP-QAPPPPQPQPQPPP 2925

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  770 EETSVPPEEtilTTLYTEVPTVPTEVTGVHTEVTNVSPE---------ETSVPTEETISTEVTTVSPEETTLP---TEVP 837
Cdd:PHA03247 2926 PPQPQPPPP---PPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgalvpgRVAVPRFRVPQPAPSREAPASSTPPltgHSLS 3002

                         330       340       350
                  ....*....|....*....|....*....|....
gi 256665241  838 TVSTEVTNVSPEETSVPPEETILTeiTTVSPEET 871
Cdd:PHA03247 3003 RVSSWASSLALHEETDPPPVSLKQ--TLWPPDDT 3034
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2041-2096 6.06e-05

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 43.45  E-value: 6.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241  2041 CSDQDGSYHLLGESWYTEKtCTTLCTCSaHSNITCSPTACKANHVCLRQEGLLRCA 2096
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 545-750 6.39e-05

Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein.


Pssm-ID: 371619 [Multi-domain]  Cd Length: 241  Bit Score: 48.15  E-value: 6.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   545 QTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTKATTVT-----------------------IEIPTTPTEEATIPTEttt 601
Cdd:pfam11596   12 ETDIPTTTTATTTPTGSGTITLISTGNSSVSTKAGSSItvagtsstgsdnddddddetdceTEIPTVPTGTTTIDPT--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   602 vptevinVSPKETSIPPEVTIPTEviTVSPEEIIsptevTPVPTDVTAAYVEATNaspeeTSVPPEVTILTEVTTVSPEE 681
Cdd:pfam11596   89 -------GNGTITGIPTASDTDDE--TDCETETD-----TVEPSIGTATTGVTTT-----TVISDGVTTTQTVTTVAPVP 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256665241   682 TTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVhtEVTNVSPEETSVPTEETISTEVT-----TVSPEE 750
Cdd:pfam11596  150 TQTHTETETVTITYTGAGQTFTTYLTQSGEICDETVTY--TVTTTCPTTTVAQGGGVYTTTVTvitthTVYPED 221
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 614-941 7.30e-05

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


Pssm-ID: 444243 [Multi-domain]  Cd Length: 613  Bit Score: 49.30  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  614 TSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLI 693
Cdd:COG5492   116 TATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNTVV 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  694 EATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETS 773
Cdd:COG5492   196 VTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGSGS 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  774 VPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 853
Cdd:COG5492   276 TTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTSV 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  854 ppeetILTEITTVSPEETVFPIEGTTLP-------TEVLTVPIE--VTTFPTGETTVptevpTVSTEMTGVHTEVT-TVF 923
Cdd:COG5492   356 -----TLAVGQTLTLTATVTPANATNKNvtwsssdPSVATVDSNglVTAVAAGTATI-----TATTKDGGKTATCTvTVT 425

                         330
                  ....*....|....*...
gi 256665241  924 PEETSIPTEVATVLPASI 941
Cdd:COG5492   426 AAGSTGTVVVVSLAATSA 443
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4428-4486 9.22e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.07  E-value: 9.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241 4428 CPAHSHHTYCLPSCIPSCSNVND--RCestslqrPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4486
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAppPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 1383-1444 1.26e-04

Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.


Pssm-ID: 400265 [Multi-domain]  Cd Length: 93  Bit Score: 43.75  E-value: 1.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256665241  1383 KVVISLPETTVTMISGRHTL-IGDQEVTL---PAILSDDTYVGLsgRFVElrTTFGLRVRWDGDQQ 1444
Cdd:pfam07833   28 TVTITKGGTTIKLTIGSNTAtVNGQEITLdvpPVLINGRTYVPL--RFVA--EALGAKVDWDEATR 89
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3821-3879 1.39e-04

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: 42.69  E-value: 1.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3821 CPTHSNYTDCLPFCLPSCLDPSAlcggtSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3879
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNA-----PPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 613-829 1.63e-04

Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein.


Pssm-ID: 371619 [Multi-domain]  Cd Length: 241  Bit Score: 46.61  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   613 ETSIPP---EVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNAS-----PEETSVPPEV-TILTEVTTVSPEETT 683
Cdd:pfam11596   12 ETDIPTtttATTTPTGSGTITLISTGNSSVSTKAGSSITVAGTSSTGSDnddddDDETDCETEIpTVPTGTTTIDPTGNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   684 VPTEVPIVlIEATAFPTGETTLYTEVPTVPTEVTGVHTEvtnvspeeTSVPTEETISTEVTTVSPEETTLPTEVPTVSTE 763
Cdd:pfam11596   92 TITGIPTA-SDTDDETDCETETDTVEPSIGTATTGVTTT--------TVISDGVTTTQTVTTVAPVPTQTHTETETVTIT 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256665241   764 VTNVSpeetsvppeeTILTTLYTEVPTVPTEVTGVhtEVTNVSPEETSVPTEETISTEVT-----TVSPEE 829
Cdd:pfam11596  163 YTGAG----------QTFTTYLTQSGEICDETVTY--TVTTTCPTTTVAQGGGVYTTTVTvitthTVYPED 221
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3581-3639 1.80e-04

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: 42.37  E-value: 1.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  3581 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLSNN-KCLLRNRC 3639
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 549-895 1.91e-04

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: 47.99  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   549 PSSPLLPPTGPSESTVPTLPMEQP---------TSPTKATTVTIEIPTTPTEEATIPTETttvptevinvspkeTSIPP- 618
Cdd:pfam05109  509 PTSAVTTPTPNATSPTPAVTTPTPnatsptlgkTSPTSAVTTPTPNATSPTPAVTTPTPN--------------ATIPTl 574

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   619 EVTIPTEVITVSPEEIISPT--EVTPvPTDVTAAYVEATNASPEETSVPPEVT--ILTEVTTVSPEETTVPTEVPIVLIE 694
Cdd:pfam05109  575 GKTSPTSAVTTPTPNATSPTvgETSP-QANTTNHTLGGTSSTPVVTSPPKNATsaVTTGQHNITSSSTSSMSLRPSSISE 653

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   695 aTAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSvpteetiSTEVTTVSPEETtlptevPTVSTEVTNVSPEETSV 774
Cdd:pfam05109  654 -TLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTS-------THHVSTSSPAPR------PGTTSQASGPGNSSTST 719

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   775 PPEETILTTlytevPTVPTEVTGVHTEvtnvSPEETSVPTEETISTEVTTVSPEETTLPTEVPTvSTEVTNVSPEETSVP 854
Cdd:pfam05109  720 KPGEVNVTK-----GTPPKNATSPQAP----SGQKTAVPTVTSTGGKANSTTGGKHTTGHGART-STEPTTDYGGDSTTP 789

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 256665241   855 PEETILTEITTVSPEETVFPIEGTTLP---TEVLTVPIEVTTFP 895
Cdd:pfam05109  790 RTRYNATTYLPPSTSSKLRPRWTFTSPpvtTAQATVPVPPTSQP 833
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 519-775 1.96e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  519 TRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTkatTVTIEIPTTPTEEATipte 598
Cdd:PTZ00449  686 SKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQ---PDDIEFFTPPEEERT---- 758

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  599 tttvpteVINVSPKETSIPPEVT--IPTEVITV---SPEEII----SPTEVTPVPTdvtaayveATNAS-PEETSVPPEV 668
Cdd:PTZ00449  759 -------FFHETPADTPLPDILAeeFKEEDIHAetgEPDEAMkrpdSPSEHEDKPP--------GDHPSlPKKRHRLDGL 823

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  669 TI-LTEVTTVSPEETTVPTEVPIVLIEATAFptGETTLYTEVPTVPTEVTG--VHTEVTNVSPEETSvPTEETISTEVTT 745
Cdd:PTZ00449  824 ALsTTDLESDAGRIAKDASGKIVKLKRSKSF--DDLTTVEEAEEMGAEARKivVDDDGTEADDEDTH-PPEEKHKSEVRR 900

                         250       260       270
                  ....*....|....*....|....*....|
gi 256665241  746 VSPEETtlPTEVPTVSTEVTNVSPEETSVP 775
Cdd:PTZ00449  901 RRPPKK--PSKPKKPSKPKKPKKPDSAFIP 928
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3581-3639 2.15e-04

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: 41.92  E-value: 2.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241 3581 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLS-NNKCLLRNRC 3639
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 576-936 3.04e-04

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


Pssm-ID: 444243 [Multi-domain]  Cd Length: 613  Bit Score: 47.38  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  576 TKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEAT 655
Cdd:COG5492   114 TGTATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  656 NASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPT 735
Cdd:COG5492   194 VVVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGS 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  736 EETISTEVTTVSPEETTLPTEV-----PTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEET 810
Cdd:COG5492   274 GSTTSTNTVTAGVGDTGVSVAVasssaATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPT 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  811 SV--PTEETISTEVtTVSPEETTLPT--------EVPTVSTE--VTNVSPEETSVppeeTILTE------ITTVspeeTV 872
Cdd:COG5492   354 SVtlAVGQTLTLTA-TVTPANATNKNvtwsssdpSVATVDSNglVTAVAAGTATI----TATTKdggktaTCTV----TV 424

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256665241  873 FPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPTEVATV 936
Cdd:COG5492   425 TAAGSTGTVVVVSLAATSAVSASVVLTPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTV 488
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 707-926 5.06e-04

Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein.


Pssm-ID: 371619 [Multi-domain]  Cd Length: 241  Bit Score: 45.45  E-value: 5.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   707 TEVPTVPTEVTgvhtevtnVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYT 786
Cdd:pfam11596   13 TDIPTTTTATT--------TPTGSGTITLISTGNSSVSTKAGSSITVAGTSSTGSDNDDDDDDETDCETEIPTVPTGTTT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   787 EVPTVPTEVTGVHT--EVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEIT 864
Cdd:pfam11596   85 IDPTGNGTITGIPTasDTDDETDCETETDTVEPSIGTATTGVTTTTVISDGVTTTQTVTTVAPVPTQTHTETETVTITYT 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256665241   865 TVSPEETVFPIEGTTLPTEVLTVPIeVTTFPTgeTTVPTEVPTVSTEMTGVHTEvtTVFPEE 926
Cdd:pfam11596  165 GAGQTFTTYLTQSGEICDETVTYTV-TTTCPT--TTVAQGGGVYTTTVTVITTH--TVYPED 221
rne PRK10811
ribonuclease E; Reviewed
 800-949 7.28e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 46.19  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  800 TEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEV-PTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGT 878
Cdd:PRK10811  848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSaPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQ 927

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256665241  879 TLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTP 949
Cdd:PRK10811  928 PQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
777-886 9.69e-04

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 45.61  E-value: 9.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  777 EETILTTlyteVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVspEETSVPPE 856
Cdd:PRK11907   28 AEEIVTT----TPATSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETSDPTSEATDTTTS--EARTVTPA 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 256665241  857 ETilteittvspeETVFPIEGTTLPTEVLT 886
Cdd:PRK11907  102 AT-----------ETSKPVEGQTVDVRILS 120
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 755-936 1.15e-03

Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose members, Swiss:A3LUS4 from Pichia stipitis is described as being an extremely serine rich protein-mucin-like protein.


Pssm-ID: 371619 [Multi-domain]  Cd Length: 241  Bit Score: 44.30  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   755 TEVPTVSTEVTNVSPEETSvppeeTILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVsPEETTlpT 834
Cdd:pfam11596   13 TDIPTTTTATTTPTGSGTI-----TLISTGNSSVSTKAGSSITVAGTSSTGSDNDDDDDDETDCETEIPTV-PTGTT--T 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241   835 EVPTVSTEVTNVsPEETSVPPEETILTEITTV--SPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEM 912
Cdd:pfam11596   85 IDPTGNGTITGI-PTASDTDDETDCETETDTVepSIGTATTGVTTTTVISDGVTTTQTVTTVAPVPTQTHTETETVTITY 163

                          170       180
                   ....*....|....*....|....
gi 256665241   913 TGVHTEVTTVFPEETSIPTEVATV 936
Cdd:pfam11596  164 TGAGQTFTTYLTQSGEICDETVTY 187
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 626-936 1.22e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 45.35  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  626 VITVSPE-EIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTIltEVTTVSPEETTVPTEVPIVLIEATafptGETT 704
Cdd:COG4932   219 TETKAPEgYVLDTKDPTGATITVTVNAGGTVTVTLKNTPKYTKGSV--TVTKTDADTGEPLAGATFTLTDAD----GNTV 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  705 LYTEVptVPTEVTGvHTEVTNVSP-----EETSVPT-----EETISTEVTTVSPEETTLPTE---VPTVSTEVTNVSPEE 771
Cdd:COG4932   293 VTTTV--TVTDADG-SYTFTDLPPgtytvTETKAPAgydldGEAVKVTITAGQTTTVTVTNGnneVKTGSVTLTKVDADD 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  772 TSVPPEE---TILTTLYTEVPTVPTEVTGVHTeVTNVSP-----EETSVPTEETISTEVT--TVSPEETTLPTEV----P 837
Cdd:COG4932   370 GEAPLAGaefTLTDADGTVVATITTDADGTAS-FKGLAPgtytlTETKAPEGYTLDSTPItvTVTDGGTGAIDTItnerK 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  838 TVSTEVTNVSP-----EETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEM 912
Cdd:COG4932   449 KGSVQVTKVDAplagaTFTLTDADGTVVTLTTDADLAGATFEADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITDD 528

                         330       340
                  ....*....|....*....|....
gi 256665241  913 TGVHTEVTTVFPEETSIPTEVATV 936
Cdd:COG4932   529 TDGTVGDEATGTDPEVTVTGKSTT 552
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 575-936 1.37e-03

Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only];


Pssm-ID: 444243 [Multi-domain]  Cd Length: 613  Bit Score: 45.07  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  575 PTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEA 654
Cdd:COG5492    27 STAGVTSSSVTANLSVLASNDTSTTSSVASVVSTAGSGGTANTSSTVAVSGAALAAGAVSTVGVDATTVAQTVATASLEA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  655 TNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVP 734
Cdd:COG5492   107 GGVSSTGTGTATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTT 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  735 TEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPT 814
Cdd:COG5492   187 ASGSLNTVVVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATS 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  815 EETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTlptevltvpiEVTTF 894
Cdd:COG5492   267 SASTLGSGSTTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVV----------TASSV 336

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 256665241  895 PTGETTVP-TEV---PTVSTEMTGVHTEVT-TVFPEE--------TSIPTEVATV 936
Cdd:COG5492   337 ATTVDVVPvTGVtlnPTSVTLAVGQTLTLTaTVTPANatnknvtwSSSDPSVATV 391
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
691-804 2.06e-03

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 44.84  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  691 VLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVspE 770
Cdd:PRK11907   17 LLTASNPKLAQAEEIVTTTPATSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETSDPTSEATDTTTS--E 94

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 256665241  771 ETSVPPEETIlTTLYTEVPTVPTEV---TGVHTEVTN 804
Cdd:PRK11907   95 ARTVTPAATE-TSKPVEGQTVDVRIlstTDLHTNLVN 130
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
580-848 2.18e-03

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 43.89  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  580 TVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASP 659
Cdd:COG3291    57 TVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTT 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  660 EETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETI 739
Cdd:COG3291   137 GTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  740 STEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPeETSVPTEETIS 819
Cdd:COG3291   217 GTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNG-TGGLGTTTAIT 295

                         250       260
                  ....*....|....*....|....*....
gi 256665241  820 TEVTTVSPEETTLPTEVPTVSTEVTNVSP 848
Cdd:COG3291   296 PGNVSTTADVTGGTATLAVSSTLTTNDTT 324
PHA03255 PHA03255
BDLF3; Provisional
 519-715 4.14e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.58  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  519 TRGTSTAfVVALnfILIshgpCRV-LLQTEIPSSPLlPPTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTP-TEEATIP 596
Cdd:PHA03255    4 ARDKAGA-VLAM--ILI----CETsLIWTSSGSSTA-SAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPiTTTAILS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  597 TETTTVPTEVINVSPKETSipPEVTIPTEVITVSPEEIISPTEVTPVPTDVTaayveaTNASPEETSVPPEVTILTEVTT 676
Cdd:PHA03255   76 TNTTTVTSTGTTVTPVPTT--SNASTINVTTKVTAQNITATEAGTGTSTGVT------SNVTTRSSSTTSATTRITNATT 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 256665241  677 VSPEETTVptevpivlieaTAFPTGETTlyTEVPTVPTE 715
Cdd:PHA03255  148 LAPTLSSK-----------GTSNATKTT--AELPTVPDE 173
COG1470 COG1470
Uncharacterized membrane protein [Function unknown];
731-940 5.79e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 441079 [Multi-domain]  Cd Length: 475  Bit Score: 42.92  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  731 TSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEE--TILTTLYTEVPTVPTEVTgVHTEVTNVSPE 808
Cdd:COG1470     4 AGLVASSTVAAGALAALLDLTTPLVGSTVALTSTASALSGERTTLAALaaTGGLVTATPVSPTSATLT-LSVEVPSNATV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256665241  809 ETSVPTEETISTEVTTVSPEETTL---PTEVPTVSTEVTNVSPEETSVPPE-ETILTEITTVSPEETVFPIEgttlPTEV 884
Cdd:COG1470    83 GTYLPITVTVAPYGLTLSVESPSLevaPGETVTYTVTLTNTGDEPDTVSLSaEGLPEGWTVTFTPDTSVSLA----PGES 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256665241  885 LTVPIEVT---TFPTGETTVPTEVPTVSTEMTGVhTEVTTVFPEETSIpteVATVLPAS 940
Cdd:COG1470   159 KTVTLEVTppaNAEPGTYPVTVTATSGEDSSSAS-LTLTLTVTGSYEL---ELSSTPTG 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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