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Conserved domains on  [gi|1039771140|ref|XP_017176299|]
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zonadhesin isoform X7 [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 3.03e-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: 3.03e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 1715 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1794
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 6.18e-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: 6.18e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 1326 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1405
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 1406 QEVTLPAILSD-DTYVGLSGR-FVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGM 1478
Cdd:pfam00094   80 QKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 375-540 1.81e-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: 1.81e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   375 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 453
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   454 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 533
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1039771140   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 2.50e-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: 2.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2102 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2181
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 5.34e-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: 5.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  217 CTFDTlNDLCGWsWVPTATGAKWTQKKGPTgkQGVGPAEDFS-NPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCm 292
Cdd:pfam00629    1 CDFED-GNLCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  293 tLSFHYIMHGQGHEEgLFVYATFLGNIRKYTLFS--GHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISI 369
Cdd:pfam00629   76 -LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1039771140  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 2.67e-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: 122.10  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263     78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1039771140  206 GTC 208
Cdd:cd06263    155 GPC 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4909-5029 9.94e-22

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: 94.74  E-value: 9.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4909 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4987
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039771140 4988 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSA 5029
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQL 121
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1911-1982 1.03e-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: 1.03e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039771140  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 3.80e-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: 3.80e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140  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 1.78e-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: 1.78e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.49e-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: 3.49e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.78e-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: 1.78e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.86e-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: 1.86e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.10e-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: 2.10e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.31e-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: 2.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.58e-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: 3.58e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 7.82e-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: 7.82e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 1.08e-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: 1.08e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.64e-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: 2.64e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.61e-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: 3.61e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.72e-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: 3.72e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 4488 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4542
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3284-3338 1.28e-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: 1.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.05e-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: 2.05e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.13e-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: 2.13e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.21e-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: 3.21e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 5.18e-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: 5.18e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 5.77e-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: 5.77e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039771140 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 8.27e-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: 8.27e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039771140 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 1.18e-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: 1.18e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.80e-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: 2.80e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.26e-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: 76.54  E-value: 2.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  486 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 565
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  566 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 644
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  645 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 724
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  725 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 798
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  799 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 877
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1039771140  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 7.99e-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: 7.99e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.18e-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: 2.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.56e-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: 1.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039771140 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 1.42e-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: 1.42e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 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 ...
 4548-4606 3.20e-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: 55.47  E-value: 3.20e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4548 CPAHSHYSKCLPPCQPSCSDPdghceGTSPEAPSTCEEGCVCEPDYVLSND-KCVPSSEC 4606
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3937-3995 2.52e-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: 2.52e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.47e-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: 50.85  E-value: 1.47e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4073 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4131
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2314-2380 2.11e-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: 2.11e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 2314 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2380
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3104-3162 2.20e-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: 2.20e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 3104 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3162
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2384-2442 3.92e-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: 3.92e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 5.85e-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: 5.85e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 6.09e-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: 6.09e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2864 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2922
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4308-4366 8.01e-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: 48.85  E-value: 8.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4366
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4788-4846 8.17e-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: 8.17e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 4788 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2504-2562 9.37e-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: 48.54  E-value: 9.37e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 1.15e-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: 1.15e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1039771140 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 1.25e-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: 1.25e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.56e-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: 1.56e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 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 2.65e-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: 2.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 3.39e-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: 3.39e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 8.19e-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: 8.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 9.87e-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: 9.87e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 4.26e-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: 4.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 4.75e-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: 4.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 5.85e-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: 5.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 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 1.79e-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: 1.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 3.03e-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: 3.03e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 1715 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1794
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 6.18e-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: 6.18e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 1326 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1405
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.16e-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: 1.16e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  1707 CHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCwskSQENNFVVSATNEIHDGNLEVsyVKAVHVQVFDLKISM 1786
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGATC--LKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771140  1787 FKGQ-KVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGL-QVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDD 1863
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 375-540 1.81e-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: 1.81e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   375 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 453
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   454 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 533
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1039771140   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 2.64e-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: 2.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  379 CDFEDrvHPFCDWNQVYGDMGHWSWGSksVPTLIAGSPREFPYGGE--HYIFFDSVKlSQEGQSARLVSPPFCAPG-DIC 455
Cdd:pfam00629    1 CDFED--GNLCGWTQDSSDDFDWERVS--GPSVKTGPSSDHTQGTGsgHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  456 VEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILI 535
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1039771140  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 2.50e-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: 2.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2102 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2181
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.85e-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: 1.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  379 CDFEDrvhPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKlSQEGQSARLVSPPFCAP-GDICVE 457
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  458 FAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILISH 537
Cdd:cd06263     77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSA-SSKPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1039771140  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 5.34e-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: 5.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  217 CTFDTlNDLCGWsWVPTATGAKWTQKKGPTgkQGVGPAEDFS-NPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCm 292
Cdd:pfam00629    1 CDFED-GNLCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  293 tLSFHYIMHGQGHEEgLFVYATFLGNIRKYTLFS--GHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISI 369
Cdd:pfam00629   76 -LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1039771140  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 2.67e-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: 122.10  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263     78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1039771140  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 6.85e-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: 6.85e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  217 CTFDTlnDLCGWSWVPTaTGAKWTQKKGPTGKQGVGPAeDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCmt 293
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPD-HTHGTGSGHYLYVESSSGREGQKARLLSPLLPpprSSHC-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  294 LSFHYIMHGQGHEEgLFVYATFLGNIRKYTLF--SGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA 370
Cdd:cd06263     75 LSFWYHMYGSGVGT-LNVYVREEGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                   .
gi 1039771140  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 5.32e-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: 5.32e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  1324 ATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNStdHFFRITANTEERGvEGVSCLDKVVISLPETTVTMISGRHTLI 1403
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140  1404 GD-QEVTLPAILSDDT-YVGLSGRFVELRTTFGL-RVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDG 1477
Cdd:smart00216   87 VNgQQVSLPYKTSDGSiQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-209 8.25e-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: 8.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   47 CDFEDNSrpFCDWSQMSADDGDWIRTTGPSLTgtSGPPGG--YPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQG-PLCV 123
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  124 HFAFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSI 203
Cdd:pfam00629   77 RFWYHMSGSGVGT--LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ-PFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1039771140  204 QRGTCN 209
Cdd:pfam00629  154 SSGPCP 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4909-5029 9.94e-22

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: 94.74  E-value: 9.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4909 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4987
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039771140 4988 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSA 5029
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQL 121
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1911-1982 1.03e-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: 1.03e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039771140  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: 94.78  E-value: 1.11e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  2100 GECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNtnmPFFMISAKtdiNTNGKNKTFGVYQLYIDIFNFHITLQKDHL 2179
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLK---NVPCGGGATCLKSVKVELNGDEIELKDDNG 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  2180 VLIslINDSIVTLPTTTHIPGVSV-MTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTP 2258
Cdd:smart00216   84 KVT--VNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 1039771140  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 6.54e-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: 6.54e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140    47 CDFEDNsrPFCDWSQMSADDGDWIRTTgpSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQ-GPLCVHF 125
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   126 AFHMFGLswGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPAdHDIPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:smart00137   82 WYYMYGS--GSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1039771140   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 3.80e-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: 3.80e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140  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 1.78e-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: 1.78e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.49e-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: 3.49e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.78e-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: 1.78e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.86e-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: 1.86e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.10e-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: 2.10e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.31e-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: 2.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.58e-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: 3.58e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 7.82e-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: 7.82e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 1.08e-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: 1.08e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.64e-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: 2.64e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.61e-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: 3.61e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.72e-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: 3.72e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 4488 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4542
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3284-3338 1.28e-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: 1.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.05e-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: 2.05e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.13e-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: 2.13e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.21e-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: 3.21e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 5.18e-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: 5.18e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 5.77e-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: 5.77e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039771140 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 8.27e-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: 8.27e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039771140 3881 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3931
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 217-372 1.10e-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: 1.10e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   217 CTFDTlNDLCGWSwVPTATGAKWTQKKGPTGkqGVGPAEDfSNPGNGYYMLLDSTNARPGQKAVLLSPLSH-SRGCMTLS 295
Cdd:smart00137    6 CDFEE-GSTCGWH-QDSNDDGHWERVSSATG--IPGPNRD-HTTGNGHFMFFETSSGAEGQTARLLSPPLYeNRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   296 FHYIMHGQGHeeGLFVYATFLGNIRKYTL---FSGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA- 370
Cdd:smart00137   81 FWYYMYGSGS--GTLNVYVRENNGSQDTLlwsRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDILLSn 158


                    ...
gi 1039771140   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 1.13e-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: 1.13e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771140 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 ...
 4728-4782 1.18e-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: 1.18e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.80e-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: 2.80e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.26e-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: 76.54  E-value: 2.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  486 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 565
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  566 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 644
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  645 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 724
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  725 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 798
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  799 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 877
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1039771140  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 6.73e-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: 6.73e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771140 1527 LCGQLvNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFC 1595
Cdd:pfam08742    1 KCGLL-SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1654-1708 7.99e-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: 7.99e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.18e-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: 2.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 6.09e-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: 6.09e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.56e-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: 1.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039771140 1266 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1319
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
 702-857 2.19e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 64.15  E-value: 2.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  702 ETTL-YTEVPTVPTEVTGVH--TEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPee 778
Cdd:PHA03255    19 ETSLiWTSSGSSTASAGNVTgtTAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTP-- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  779 tILTTLYTEVPTVPTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 853
Cdd:PHA03255    91 -VPTTSNASTINVTTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169


                   ....
gi 1039771140  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 1.42e-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: 1.42e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 1985 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 4908-5028 1.84e-09

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: 59.72  E-value: 1.84e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  4908 RCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRgiepLIMEGRNKISPKGSSTLHEVTTIVYGYKIQL-QEELVVL 4986
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1039771140  4987 VNDEKVAVPYNPNEHLRVMLRAQRLLLV-TDFE-MVLDFDGKHS 5028
Cdd:smart00216   87 VNGQQVSLPYKTSDGSIQIRSSGGYLVViTSLGlIQVTFDGLTL 130
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4548-4606 3.20e-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: 55.47  E-value: 3.20e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 4.96e-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: 4.96e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 1985 CPPRSSYNPCANSCPATCLTLSTPRDCpTLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4548-4606 1.14e-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: 1.14e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.52e-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: 2.52e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 8.66e-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: 8.66e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.47e-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: 50.85  E-value: 1.47e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4073 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4131
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2314-2380 2.11e-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: 2.11e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 2314 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2380
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3104-3162 2.20e-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: 2.20e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 3104 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3162
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4073-4131 2.33e-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: 2.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 3.31e-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: 3.31e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 3.92e-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: 3.92e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 5.85e-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: 5.85e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 6.09e-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: 6.09e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 7.26e-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: 7.26e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2384 CPAHSHYTNCLPSCPPSCLDPDSRCegsghKVPATCREGCICQPDYVLLND-KCVLRSHC 2442
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4308-4366 8.01e-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: 48.85  E-value: 8.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4366
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4788-4846 8.17e-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: 8.17e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 4788 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2864-2922 8.25e-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: 8.25e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 8.33e-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: 8.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 9.37e-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: 48.54  E-value: 9.37e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 1.15e-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: 1.15e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1039771140 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 1.25e-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: 1.25e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.31e-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: 1.31e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.36e-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: 1.36e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.56e-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: 1.56e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 3344 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3399
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3344-3399 1.94e-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: 1.94e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 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 2.20e-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: 2.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.60e-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: 2.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.65e-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: 2.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 3.39e-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: 3.39e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 5.64e-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: 5.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 6.16e-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: 6.16e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2744 CPDHSLYTHCLPSCLPSCSDPdglcrGTSPEAPSTCKEGCVCEPDYVLSND-KCVLRIEC 2802
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
636-928 8.18e-06

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 51.59  E-value: 8.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  636 SPTEVTPVPT-------DVTaayVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTE 708
Cdd:COG3291     36 TSTEANPSHTyttpgtyTVT---LTVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  709 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEV 788
Cdd:COG3291    113 GVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTG 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  789 PTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSP 868
Cdd:COG3291    193 TIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVV 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  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 8.19e-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: 8.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 9.87e-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: 9.87e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.27e-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: 1.27e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039771140  2324 AHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCP 2381
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2624-2682 1.56e-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: 1.56e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.00e-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: 2.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.21e-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: 2.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.71e-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: 2.71e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 4.26e-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: 4.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 4.75e-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: 4.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 5.85e-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: 5.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 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 9.17e-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: 9.17e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 1.40e-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: 1.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.79e-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: 1.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1039771140 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 3.03e-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: 3.03e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 1715 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1794
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 6.18e-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: 6.18e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 1326 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1405
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.16e-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: 1.16e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  1707 CHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCwskSQENNFVVSATNEIHDGNLEVsyVKAVHVQVFDLKISM 1786
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGATC--LKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771140  1787 FKGQ-KVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGL-QVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDD 1863
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 375-540 1.81e-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: 1.81e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   375 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 453
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   454 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 533
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1039771140   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 2.64e-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: 2.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  379 CDFEDrvHPFCDWNQVYGDMGHWSWGSksVPTLIAGSPREFPYGGE--HYIFFDSVKlSQEGQSARLVSPPFCAPG-DIC 455
Cdd:pfam00629    1 CDFED--GNLCGWTQDSSDDFDWERVS--GPSVKTGPSSDHTQGTGsgHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  456 VEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILI 535
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1039771140  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 2.50e-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: 2.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2102 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2181
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.85e-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: 1.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  379 CDFEDrvhPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKlSQEGQSARLVSPPFCAP-GDICVE 457
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  458 FAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILISH 537
Cdd:cd06263     77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSA-SSKPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1039771140  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 5.34e-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: 5.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  217 CTFDTlNDLCGWsWVPTATGAKWTQKKGPTgkQGVGPAEDFS-NPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCm 292
Cdd:pfam00629    1 CDFED-GNLCGW-TQDSSDDFDWERVSGPS--VKTGPSSDHTqGTGSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  293 tLSFHYIMHGQGHEEgLFVYATFLGNIRKYTLFS--GHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISI 369
Cdd:pfam00629   76 -LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSisGDQGPSWKEARVTLsSSTQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1039771140  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 2.67e-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: 122.10  E-value: 2.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263     78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1039771140  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 6.85e-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: 6.85e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  217 CTFDTlnDLCGWSWVPTaTGAKWTQKKGPTGKQGVGPAeDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGCmt 293
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPD-HTHGTGSGHYLYVESSSGREGQKARLLSPLLPpprSSHC-- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  294 LSFHYIMHGQGHEEgLFVYATFLGNIRKYTLF--SGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA 370
Cdd:cd06263     75 LSFWYHMYGSGVGT-LNVYVREEGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLS 153


                   .
gi 1039771140  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 5.32e-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: 5.32e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  1324 ATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNStdHFFRITANTEERGvEGVSCLDKVVISLPETTVTMISGRHTLI 1403
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140  1404 GD-QEVTLPAILSDDT-YVGLSGRFVELRTTFGL-RVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDG 1477
Cdd:smart00216   87 VNgQQVSLPYKTSDGSiQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-209 8.25e-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: 8.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   47 CDFEDNSrpFCDWSQMSADDGDWIRTTGPSLTgtSGPPGG--YPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQG-PLCV 123
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  124 HFAFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSI 203
Cdd:pfam00629   77 RFWYHMSGSGVGT--LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ-PFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1039771140  204 QRGTCN 209
Cdd:pfam00629  154 SSGPCP 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4909-5029 9.94e-22

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: 94.74  E-value: 9.94e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4909 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4987
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039771140 4988 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSA 5029
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQL 121
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1911-1982 1.03e-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: 1.03e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039771140  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: 94.78  E-value: 1.11e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  2100 GECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNtnmPFFMISAKtdiNTNGKNKTFGVYQLYIDIFNFHITLQKDHL 2179
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLK---NVPCGGGATCLKSVKVELNGDEIELKDDNG 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  2180 VLIslINDSIVTLPTTTHIPGVSV-MTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTP 2258
Cdd:smart00216   84 KVT--VNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 1039771140  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 6.54e-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: 6.54e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140    47 CDFEDNsrPFCDWSQMSADDGDWIRTTgpSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQ-GPLCVHF 125
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   126 AFHMFGLswGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPAdHDIPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:smart00137   82 WYYMYGS--GSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1039771140   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 3.80e-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: 3.80e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140  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 1.78e-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: 1.78e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.49e-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: 3.49e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.78e-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: 1.78e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.86e-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: 1.86e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.10e-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: 2.10e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.31e-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: 2.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.58e-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: 3.58e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 7.82e-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: 7.82e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 1.08e-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: 1.08e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.64e-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: 2.64e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.61e-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: 3.61e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.72e-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: 3.72e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 4488 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4542
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3284-3338 1.28e-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: 1.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.05e-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: 2.05e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.13e-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: 2.13e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 3.21e-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: 3.21e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 5.18e-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: 5.18e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 5.77e-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: 5.77e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039771140 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 8.27e-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: 8.27e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039771140 3881 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3931
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 217-372 1.10e-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: 1.10e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   217 CTFDTlNDLCGWSwVPTATGAKWTQKKGPTGkqGVGPAEDfSNPGNGYYMLLDSTNARPGQKAVLLSPLSH-SRGCMTLS 295
Cdd:smart00137    6 CDFEE-GSTCGWH-QDSNDDGHWERVSSATG--IPGPNRD-HTTGNGHFMFFETSSGAEGQTARLLSPPLYeNRSTHCLT 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140   296 FHYIMHGQGHeeGLFVYATFLGNIRKYTL---FSGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIA- 370
Cdd:smart00137   81 FWYYMYGSGS--GTLNVYVRENNGSQDTLlwsRSGTQGGQWLQAEVALsSWPQPFQVVFEGTRGKGHSGYIALDDILLSn 158


                    ...
gi 1039771140   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 1.13e-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: 1.13e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771140 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 ...
 4728-4782 1.18e-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: 1.18e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.80e-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: 2.80e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 2.26e-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: 76.54  E-value: 2.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  486 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 565
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  566 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 644
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  645 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 724
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  725 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 798
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  799 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 877
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1039771140  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 6.73e-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: 6.73e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771140 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 5.24e-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: 72.64  E-value: 5.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  546 TEIPSSPLLPP--TGPSeSTVPTLPMEQPTSPTKATTVTIEIPTTPTEeatiptetttvptevinvSPKET---SIPPEV 620
Cdd:pfam05109  446 TGLPSSTHVPTnlTAPA-STGPTVSTADVTSPTPAGTTSGASPVTPSP------------------SPRDNgteSKAPDM 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  621 TIPTEVITVSPEEIISPTEVTPVPT-DVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFP 699
Cdd:pfam05109  507 TSPTSAVTTPTPNATSPTPAVTTPTpNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTP 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  700 TGETTLYTEVPTVPTEVTGVHT-EVTNVSPEETSVPTEETISTevttvspeeTTLPTEVPTVSTEVTNVSPEETSVPPEE 778
Cdd:pfam05109  587 TPNATSPTVGETSPQANTTNHTlGGTSSTPVVTSPPKNATSAV---------TTGQHNITSSSTSSMSLRPSSISETLSP 657

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  779 TILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSvpteetiSTEVTTVSPEETtlptevPTVSTEVTNVSPEETSVPPEET 858
Cdd:pfam05109  658 STSDNSTSHMPLLTSAHPTGGENITQVTPASTS-------THHVSTSSPAPR------PGTTSQASGPGNSSTSTKPGEV 724

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  859 ILTEITtvSPEETVFPIEGTTLPTEVLTVpievtTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPT---EVAT 935
Cdd:pfam05109  725 NVTKGT--PPKNATSPQAPSGQKTAVPTV-----TSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRtryNATT 797


                   ....*
gi 1039771140  936 VLPAS 940
Cdd:pfam05109  798 YLPPS 802
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1654-1708 7.99e-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: 7.99e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.61e-11

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: 70.37  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  621 TIPTEVITVSPEEIISPTEVTPVPTDVT----AAYVEATNASPEETsvpPEVTILTEVTT-------------VSPEETT 683
Cdd:pfam17823   46 AVPRADNKSSEQ*NFCAATAAPAPVTLTkgtsAAHLNSTEVTAEHT---PHGTDLSEPATregaadgaasralAAAASSS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  684 vPTEVPIVLIEATAFPTGE--TTLYTEVPTVPTEVTGVHTEVTNVSPEE-TSVPTEETISTEVTTVSPEETTLPTE--VP 758
Cdd:pfam17823  123 -PSSAAQSLPAAIAALPSEafSAPRAAACRANASAAPRAAIAAASAPHAaSPAPRTAASSTTAASSTTAASSAPTTaaSS 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  759 TVSTeVTNVSPEETSVPPEET-ILTTLYTEVPTVPTEVTGVHTEVTNVSPE-----ETSVPTEETISTEVTTVSPEETTl 832
Cdd:pfam17823  202 APAT-LTPARGISTAATATGHpAAGTALAAVGNSSPAAGTVTAAVGTVTPAalatlAAAAGTVASAAGTINMGDPHARR- 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  833 PTEVPTVSTEVTNVSPEETSVPPEETILTEITT------VSPEETVFPIEGTTLPTEVLTVPIEVTTFPTgETTVPTEVP 906
Cdd:pfam17823  280 LSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTdqpvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVT-TTKAQAKEP 358

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1039771140  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 2.18e-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: 2.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 6.09e-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: 6.09e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 1.56e-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: 1.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039771140 1266 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1319
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
 702-857 2.19e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 64.15  E-value: 2.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  702 ETTL-YTEVPTVPTEVTGVH--TEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPee 778
Cdd:PHA03255    19 ETSLiWTSSGSSTASAGNVTgtTAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTP-- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  779 tILTTLYTEVPTVPTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 853
Cdd:PHA03255    91 -VPTTSNASTINVTTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169


                   ....
gi 1039771140  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 1.42e-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: 1.42e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 1985 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2039
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 4908-5028 1.84e-09

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: 59.72  E-value: 1.84e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  4908 RCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRgiepLIMEGRNKISPKGSSTLHEVTTIVYGYKIQL-QEELVVL 4986
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1039771140  4987 VNDEKVAVPYNPNEHLRVMLRAQRLLLV-TDFE-MVLDFDGKHS 5028
Cdd:smart00216   87 VNGQQVSLPYKTSDGSIQIRSSGGYLVViTSLGlIQVTFDGLTL 130
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4548-4606 3.20e-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: 55.47  E-value: 3.20e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 4.96e-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: 4.96e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 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 1.00e-08

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: 61.51  E-value: 1.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  725 NVSPEetSVPTEETISTE-----VTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTT-------LYTEVPTVP 792
Cdd:pfam17823   41 NASGD--AVPRADNKSSEq*nfcAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDLSEPATregaadgAASRALAAA 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  793 TEVTGvhTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSpeeTSVPPEETILTEITTVSPEETV 872
Cdd:pfam17823  119 ASSSP--SSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAA---SPAPRTAASSTTAASSTTAASS 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  873 FPIEGTTlpTEVLTVpieVTTFPTGETTVPTEVPTVSTemtgVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTPTEV 952
Cdd:pfam17823  194 APTTAAS--SAPATL---TPARGISTAATATGHPAAGT----ALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVA 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  953 TTTPPEETTIPAEVTTIPPVSIPSEETTTPTEVTTTPPEETTIpAEVTTVPPV------SIPSEETTTPTEVTTTPPEET 1026
Cdd:pfam17823  265 SAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPI-IQVSTDQPVhntagePTPSPSNTTLEPNTPKSVAST 343

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1039771140 1027 TIPAEVTTVPPVSIPSeETTIPTEVTTVPPE-ETTIP 1062
Cdd:pfam17823  344 NLAVVTTTKAQAKEPS-ASPVPVLHTSMIPEvEATSP 379
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4548-4606 1.14e-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: 1.14e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4548 CPAHSHYSKCLPPCQPSCSDPDghcegTSPEAPSTCEEGCVCEPDYVLS-NDKCVPSSEC 4606
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 652-832 1.22e-08

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 61.98  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  652 VEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPtgettlytEVPTV---PTEVTGVHTEVTNVSP 728
Cdd:PRK10811   848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVV--------EEPVVvaePQPEEVVVVETTHPEV 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  729 EETSVPTEETISTEVTTVSPEETTLPTEvptvstEVTNVSPEETSVPPEETIlttlyTEVPTVPTEVTgVHTEVTNVSPE 808
Cdd:PRK10811   920 IAAPVTEQPQVITESDVAVAQEVAEHAE------PVVEPQDETADIEEAAET-----AEVVVAEPEVV-AQPAAPVVAEV 987

                          170       180
                   ....*....|....*....|....
gi 1039771140  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 2.52e-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: 2.52e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 6.18e-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: 59.54  E-value: 6.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  560 SESTVPTLPMEQPTSPTKATTV--TIEIPTTPTEEAtiptetttvptevinvSPKETSIPPEVTIPTEVITVSPEEIISP 637
Cdd:pfam05109  427 STTTSPTLNTTGFAAPNTTTGLpsSTHVPTNLTAPA----------------STGPTVSTADVTSPTPAGTTSGASPVTP 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  638 tevTPVP---------TDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTevpivliEATAFPTGETTLYTE 708
Cdd:pfam05109  491 ---SPSPrdngteskaPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPT-------SAVTTPTPNATSPTP 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  709 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTevtnvSPEETSVPPEETilttlyTEV 788
Cdd:pfam05109  561 AVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS-----TPVVTSPPKNAT------SAV 629

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  789 PTVPTEVTGVHTEVTNVSPEETSvpteETISTEVTTVSPEETTLPTEV-PTVSTEVTNVSPEETSVppeetilTEITTVS 867
Cdd:pfam05109  630 TTGQHNITSSSTSSMSLRPSSIS----ETLSPSTSDNSTSHMPLLTSAhPTGGENITQVTPASTST-------HHVSTSS 698

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  868 PEetvfPIEGTTL-------------PTEVLT---VPIEVTTFPTGETTVPTEVPTVSTemTGVHTEVTT 921
Cdd:pfam05109  699 PA----PRPGTTSqasgpgnsststkPGEVNVtkgTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTT 762
PHA03255 PHA03255
BDLF3; Provisional
 638-794 7.23e-08

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 56.84  E-value: 7.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  638 TEVTPVP---TDVTAAyVEATNASPEeTSVPPEVTILTEVTTVSPEETTV--PTEVPIVLIEATAFPTGETTLYTEVPTV 712
Cdd:PHA03255    25 TSSGSSTasaGNVTGT-TAVTTPSPS-ASGPSTNQSTTLTTTSAPITTTAilSTNTTTVTSTGTTVTPVPTTSNASTINV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  713 PTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLpteVPTVSTEVTNVSPEETSvppeetilttlytE 787
Cdd:PHA03255   103 TTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTL---APTLSSKGTSNATKTTA-------------E 166


                   ....*..
gi 1039771140  788 VPTVPTE 794
Cdd:PHA03255   167 LPTVPDE 173
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3937-3995 8.66e-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: 8.66e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.47e-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: 50.85  E-value: 1.47e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4073 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4131
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2314-2380 2.11e-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: 2.11e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 2314 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2380
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3104-3162 2.20e-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: 2.20e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 3104 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3162
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4073-4131 2.33e-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: 2.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 4073 CPAHSHFTSCLPSCPPSCSNLD--GSCvesnfkaPSVCKKGCICQPGYLLN-NDKCVLRIQC 4131
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 629-910 2.66e-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: 57.23  E-value: 2.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  629 VSPEEIISPTEVTPVPTDVTAAYVEATNASP---EETSVPPEVTIltEVTTVSPEETTVPTEVPIVLIEATafPTGETTL 705
Cdd:pfam05109  304 VFSDEIPASQDMPTNTTDITYVGDNATYSVPmvtSEDANSPNVTV--TAFWAWPNNTETDFKCKWTLTSGT--PSGCENI 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  706 ---YTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVS---PEETSVPpeeT 779
Cdd:pfam05109  380 sgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTtglPSSTHVP---T 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  780 ILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETI 859
Cdd:pfam05109  457 NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATS 536

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039771140  860 LTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVST 910
Cdd:pfam05109  537 PTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPT 587
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3104-3162 3.31e-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: 3.31e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 3.92e-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: 3.92e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 2384 CPAHSHYTNCLPSCPPSCLDPD--SRCegsghkvPATCREGCICQPDYVL-LNDKCVLRSHC 2442
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 559-792 5.11e-07

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 56.59  E-value: 5.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  559 PSESTVPtLPMEQpTSPTKAT-TVTIEIPTTPTEEATIPTETTtvpteviNVSPKETSIPPEVTIPTEVITVSPEEIISP 637
Cdd:PRK10811   820 PTQSPMP-LTVAC-ASPEMASgKVWIRYPVVRPQDVQVEEQRE-------AEEVQVQPVVAEVPVAAAVEPVVSAPVVEA 890

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  638 TEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVptevpivlieatafptgettlytevptVPTEVT 717
Cdd:PRK10811   891 VAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVA---------------------------VAQEVA 943

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140  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 5.85e-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: 5.85e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 6.09e-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: 6.09e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2864 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2922
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 624-878 6.80e-07

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 56.20  E-value: 6.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  624 TEVITVSPEE-IISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTV--------SPEETTV---------- 684
Cdd:PRK10811   737 EEAVAPVVEEtVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENRDNNgmprrsrrSPRHLRVsgqrrrryrd 816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  685 ---PTEVPIVLIEATAFP---TGEttLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 758
Cdd:PRK10811   817 eryPTQSPMPLTVACASPemaSGK--VWIRYPVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEV 894

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  759 TVSTEVTNVSPEETSVPPEETilttlYTEVPTVP-TEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 837
Cdd:PRK10811   895 VEEPVVVAEPQPEEVVVVETT-----HPEVIAAPvTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVV 969

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1039771140  838 TVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGT 878
Cdd:PRK10811   970 VAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEAT 1010
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2384-2442 7.26e-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: 7.26e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2384 CPAHSHYTNCLPSCPPSCLDPDSRCegsghKVPATCREGCICQPDYVLLND-KCVLRSHC 2442
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4308-4366 8.01e-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: 48.85  E-value: 8.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4308 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4366
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4788-4846 8.17e-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: 8.17e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 4788 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4846
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2864-2922 8.25e-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: 8.25e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 8.33e-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: 8.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 9.37e-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: 48.54  E-value: 9.37e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 2504 CPAHSKFTDCLPPCHPSCSDP--DGHCEGIstnahsnCKEGCVCQPGYVLRND-KCVLRIEC 2562
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLspPDVCPEP-------CVEGCVCPPGFVRNSGgKCVPPSDC 55
rne PRK10811
ribonuclease E; Reviewed
 668-939 1.01e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 55.43  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  668 VTILTEVTTvsPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSP-EETSVPTEETISTEVTTV 746
Cdd:PRK10811   729 VRIEQSVAE--EAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENrDNNGMPRRSRRSPRHLRV 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  747 S------------PEETTLPTEVPTVSTE-----------VTNVSPEET--SVPPEETILTTLYTEVPTVPTEVTGVHTE 801
Cdd:PRK10811   807 SgqrrrryrderyPTQSPMPLTVACASPEmasgkvwirypVVRPQDVQVeeQREAEEVQVQPVVAEVPVAAAVEPVVSAP 886

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  802 VTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEET-ILTEITTVSPEETVFPIEGTTl 880
Cdd:PRK10811   887 VVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAeHAEPVVEPQDETADIEEAAET- 965

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039771140  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 1.15e-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: 1.15e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1039771140 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 1.25e-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: 1.25e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2624 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 2682
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
rne PRK10811
ribonuclease E; Reviewed
 620-794 1.29e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 55.05  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  620 VTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASP-----EETSVPPEVTILTEVTTVSPEETTVPtevpivliE 694
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPvveavAEVVEEPVVVAEPQPEEVVVVETTHP--------E 918

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  695 ATAFPTGETTLYTEVPTVPtevtgVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVptVSTEVTNVSPEETSV 774
Cdd:PRK10811   919 VIAAPVTEQPQVITESDVA-----VAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVV--AQPAAPVVAEVAAEV 991

                          170       180
                   ....*....|....*....|
gi 1039771140  775 PPEETILTTLYTEVPTVPTE 794
Cdd:PRK10811   992 ETVTAVEPEVAPAQVPEATV 1011
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3224-3282 1.31e-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: 1.31e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.36e-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: 1.36e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.56e-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: 1.56e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 3344 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3399
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3344-3399 1.94e-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: 1.94e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039771140 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 2.20e-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: 2.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.60e-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: 2.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.65e-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: 2.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 3.39e-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: 3.39e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 4193 CPAHSHYTNCLPACSRSCTDLdghceGTSPKVPSPCKEGCLCQPGYVVHNH-KCVLQIHC 4251
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 552-906 5.50e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 5.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  552 PLLPPTGPSEST---VPTlPMEQPTSPTKATTVTIEIPTTPTEEAT----IPTETTTVPTEVINVSPKETSIP-PEVTIP 623
Cdd:PHA03247  2553 PPLPPAAPPAAPdrsVPP-PRPAPRPSEPAVTSRARRPDAPPQSARprapVDDRGDPRGPAPPSPLPPDTHAPdPPPPSP 2631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  624 TEVITVSPEEIISPTEVTPVPTDVTA-----------AYVEATNAS-----PEETSVPPEVTILTEVTTVSPEETTvPTE 687
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarRLGRAAQASsppqrPRRRAARPTVGSLTSLADPPPPPPT-PEP 2710

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  688 VPIVLIEATAFPTG---------ETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 758
Cdd:PHA03247  2711 APHALVSATPLPPGpaaarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  759 TVSTEVTNVSPEETS-----VPPEETILTTLYTEVPTVPTEvtgvhTEVTNVSPEETSVPTEETISTE------------ 821
Cdd:PHA03247  2791 LSESRESLPSPWDPAdppaaVLAPAAALPPAASPAGPLPPP-----TSAQPTAPPPPPGPPPPSLPLGgsvapggdvrrr 2865

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  822 ----------VTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTvSPEETVFPIEGTTLPTEVLT-VPIE 890
Cdd:PHA03247  2866 ppsrspaakpAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPqPPLA 2944

                          410
                   ....*....|....*.
gi 1039771140  891 VTTFPTGETTVPTEVP 906
Cdd:PHA03247  2945 PTTDPAGAGEPSGAVP 2960
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1215-1264 5.64e-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: 5.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140 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 6.16e-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: 6.16e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 2744 CPDHSLYTHCLPSCLPSCSDPdglcrGTSPEAPSTCKEGCVCEPDYVLSND-KCVLRIEC 2802
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
636-928 8.18e-06

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 51.59  E-value: 8.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  636 SPTEVTPVPT-------DVTaayVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTE 708
Cdd:COG3291     36 TSTEANPSHTyttpgtyTVT---LTVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  709 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEV 788
Cdd:COG3291    113 GVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTG 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  789 PTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSP 868
Cdd:COG3291    193 TIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVV 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  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 8.19e-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: 8.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 9.87e-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: 9.87e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.27e-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: 1.27e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039771140  2324 AHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCP 2381
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2624-2682 1.56e-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: 1.56e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.62e-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: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  573 TSPTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYV 652
Cdd:COG5492    195 VVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGSG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  653 EATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETS 732
Cdd:COG5492    275 STTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTS 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  733 V--PTEETISTEVtTVSPEETTLPTEVPTVS-TEVTNVSPEE--TSVPPEETILTtlYTevpTVPTEVTGVHT-EVTNVS 806
Cdd:COG5492    355 VtlAVGQTLTLTA-TVTPANATNKNVTWSSSdPSVATVDSNGlvTAVAAGTATIT--AT---TKDGGKTATCTvTVTAAG 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  807 PEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLT 886
Cdd:COG5492    429 STGTVVVVSLAATSAVSASVVLTPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTVTASVAEVATSVGGGATVTVT 508

                          330       340
                   ....*....|....*....|....
gi 1039771140  887 VPIEVTTFPTGETTVPTEVPTVST 910
Cdd:COG5492    509 VSTAATVTVTVGVKSTGIAVAGST 532
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4193-4251 2.00e-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: 2.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.21e-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: 2.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 2.71e-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: 2.71e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 2984 CPAHSHFTNCLPPCQPSC--LDSEGHCegsttkaPSACQEGCVCEPDYVV-LNNKCVPRIEC 3042
Cdd:cd19941      1 CPPNEVYSECGSACPPTCanPNAPPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
PHA03255 PHA03255
BDLF3; Provisional
 777-932 3.20e-05

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 48.75  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  777 EETILTTLYTEVPTVPTEVTGVhTEVTNVSPEETSVPTEETiSTEVTTVSPEETT--LPTEVPTVSTEVTNVSPEET--- 851
Cdd:PHA03255    19 ETSLIWTSSGSSTASAGNVTGT-TAVTTPSPSASGPSTNQS-TTLTTTSAPITTTaiLSTNTTTVTSTGTTVTPVPTtsn 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  852 -SVPPEETILTEITTVSPEETVFPIEGTTlpTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPeetSIP 930
Cdd:PHA03255    97 aSTINVTTKVTAQNITATEAGTGTSTGVT--SNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELP---TVP 171


                   ..
gi 1039771140  931 TE 932
Cdd:PHA03255   172 DE 173
YbbR COG4856
Cyclic di-AMP synthase regulator CdaR, YbbR domain [Signal transduction mechanisms];
636-905 3.49e-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: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  636 SPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILT----EVTTVSPEETTV----------PTEVPIVLIEATAFPTG 701
Cdd:COG4856     71 PRSVLLSLSASDIKAYVDLSGLKPGTHTVPVKVEGNLpsgvEVVEVSPSTITVtlekkvtkevPVEVEVKGKPAEGYEVG 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  702 ETTLytEVPTVptEVTGVHTEVTNVSPEETSVPTE---ETISTEVT-------------TVSPEETTLptEVPTVSTEVT 765
Cdd:COG4856    151 EVSV--SPSTV--TVSGPESVVNQIDSVKATVDVSgatEDFTKSVPvkaydangneldvTISPSTVEV--TVPVLPSKTV 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  766 NVSPEETSVPPEETILTTLYTEVPTVptEVTGVHTEVTNVSpeetSVPTE--------ETISTEVTTVSPEETTLPTEVP 837
Cdd:COG4856    225 PVKVNTTGEPAEGYSVTSITVSPSTV--TIYGPEEVLDSIS----SIETEpidlsgltESTTVEVKLKLPEGVTLVDPPS 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  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 4.26e-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: 4.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 4.75e-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: 4.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 3821 CPTHSNYTDCLPFCLPSCLDPSalcggTSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3879
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 534-871 5.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 5.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  534 LISHGPCRVLLQTEIPSSPLLP--PTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTPTEEATIPTEtttvptevinvsp 611
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPaaPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR------------- 2781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  612 keTSIPPEVTIPTEVITVSPeeiiSPTEVTPVPTDVTA-AYVEATNASPEETSVPPevtilTEVTTVSPEETTVPTEVPI 690
Cdd:PHA03247  2782 --RLTRPAVASLSESRESLP----SPWDPADPPAAVLApAAALPPAASPAGPLPPP-----TSAQPTAPPPPPGPPPPSL 2850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  691 VLIEATAfPTGETTLY-TEVPTVPTEVTGVHTEVTNVSPEETSVPTEetiSTEVTTVSPEETTLPtEVPTVSTEVTNVSP 769
Cdd:PHA03247  2851 PLGGSVA-PGGDVRRRpPSRSPAAKPAAPARPPVRRLARPAVSRSTE---SFALPPDQPERPPQP-QAPPPPQPQPQPPP 2925

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  770 EETSVPPEEtilTTLYTEVPTVPTEVTGVHTEVTNVSPE---------ETSVPTEETISTEVTTVSPEETTLP---TEVP 837
Cdd:PHA03247  2926 PPQPQPPPP---PPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgalvpgRVAVPRFRVPQPAPSREAPASSTPPltgHSLS 3002

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1039771140  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 5.85e-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: 5.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 2041 CSDQDGSYHLLGESWYTEKtCTTLCTCSaHSNITCSPTACKANHVCLRQEGLLRCA 2096
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 614-941 6.82e-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: 6.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  614 TSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLI 693
Cdd:COG5492    116 TATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNTVV 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  694 EATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETS 773
Cdd:COG5492    196 VTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGSGS 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  774 VPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 853
Cdd:COG5492    276 TTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTSV 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  854 ppeetILTEITTVSPEETVFPIEGTTLP-------TEVLTVPIE--VTTFPTGETTVptevpTVSTEMTGVHTEVT-TVF 923
Cdd:COG5492    356 -----TLAVGQTLTLTATVTPANATNKNvtwsssdPSVATVDSNglVTAVAAGTATI-----TATTKDGGKTATCTvTVT 425

                          330
                   ....*....|....*...
gi 1039771140  924 PEETSIPTEVATVLPASI 941
Cdd:COG5492    426 AAGSTGTVVVVSLAATSA 443
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 545-750 8.07e-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: 47.77  E-value: 8.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  545 QTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTKATTVT-----------------------IEIPTTPTEEATIPTEttt 601
Cdd:pfam11596   12 ETDIPTTTTATTTPTGSGTITLISTGNSSVSTKAGSSItvagtsstgsdnddddddetdceTEIPTVPTGTTTIDPT--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  602 vptevinVSPKETSIPPEVTIPTEviTVSPEEIIsptevTPVPTDVTAAYVEATNaspeeTSVPPEVTILTEVTTVSPEE 681
Cdd:pfam11596   89 -------GNGTITGIPTASDTDDE--TDCETETD-----TVEPSIGTATTGVTTT-----TVISDGVTTTQTVTTVAPVP 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039771140  682 TTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVhtEVTNVSPEETSVPTEETISTEVT-----TVSPEE 750
Cdd:pfam11596  150 TQTHTETETVTITYTGAGQTFTTYLTQSGEICDETVTY--TVTTTCPTTTVAQGGGVYTTTVTvitthTVYPED 221
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4428-4486 9.17e-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: 9.17e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140 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 1.18e-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: 1.18e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039771140 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 1.40e-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: 1.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 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 1.79e-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: 1.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140 3581 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLSNN-KCLLRNRC 3639
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 519-775 1.84e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  519 TRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTkatTVTIEIPTTPTEEATipte 598
Cdd:PTZ00449   686 SKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQ---PDDIEFFTPPEEERT---- 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  599 tttvpteVINVSPKETSIPPEVT--IPTEVITV---SPEEII----SPTEVTPVPTdvtaayveATNAS-PEETSVPPEV 668
Cdd:PTZ00449   759 -------FFHETPADTPLPDILAeeFKEEDIHAetgEPDEAMkrpdSPSEHEDKPP--------GDHPSlPKKRHRLDGL 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  669 TI-LTEVTTVSPEETTVPTEVPIVLIEATAFptGETTLYTEVPTVPTEVTG--VHTEVTNVSPEETSvPTEETISTEVTT 745
Cdd:PTZ00449   824 ALsTTDLESDAGRIAKDASGKIVKLKRSKSF--DDLTTVEEAEEMGAEARKivVDDDGTEADDEDTH-PPEEKHKSEVRR 900

                          250       260       270
                   ....*....|....*....|....*....|
gi 1039771140  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 1039771140 3581 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLS-NNKCLLRNRC 3639
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 613-829 2.19e-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: 46.22  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  613 ETSIPP---EVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNAS-----PEETSVPPEV-TILTEVTTVSPEETT 683
Cdd:pfam11596   12 ETDIPTtttATTTPTGSGTITLISTGNSSVSTKAGSSITVAGTSSTGSDnddddDDETDCETEIpTVPTGTTTIDPTGNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  684 VPTEVPIVlIEATAFPTGETTLYTEVPTVPTEVTGVHTEvtnvspeeTSVPTEETISTEVTTVSPEETTLPTEVPTVSTE 763
Cdd:pfam11596   92 TITGIPTA-SDTDDETDCETETDTVEPSIGTATTGVTTT--------TVISDGVTTTQTVTTVAPVPTQTHTETETVTIT 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039771140  764 VTNVSpeetsvppeeTILTTLYTEVPTVPTEVTGVhtEVTNVSPEETSVPTEETISTEVT-----TVSPEE 829
Cdd:pfam11596  163 YTGAG----------QTFTTYLTQSGEICDETVTY--TVTTTCPTTTVAQGGGVYTTTVTvitthTVYPED 221
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 549-895 2.59e-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: 47.60  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  549 PSSPLLPPTGPSESTVPTLPMEQP---------TSPTKATTVTIEIPTTPTEEATIPTETttvptevinvspkeTSIPP- 618
Cdd:pfam05109  509 PTSAVTTPTPNATSPTPAVTTPTPnatsptlgkTSPTSAVTTPTPNATSPTPAVTTPTPN--------------ATIPTl 574

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  619 EVTIPTEVITVSPEEIISPT--EVTPvPTDVTAAYVEATNASPEETSVPPEVT--ILTEVTTVSPEETTVPTEVPIVLIE 694
Cdd:pfam05109  575 GKTSPTSAVTTPTPNATSPTvgETSP-QANTTNHTLGGTSSTPVVTSPPKNATsaVTTGQHNITSSSTSSMSLRPSSISE 653

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  695 aTAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSvpteetiSTEVTTVSPEETtlptevPTVSTEVTNVSPEETSV 774
Cdd:pfam05109  654 -TLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTS-------THHVSTSSPAPR------PGTTSQASGPGNSSTST 719

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  775 PPEETILTTlytevPTVPTEVTGVHTEvtnvSPEETSVPTEETISTEVTTVSPEETTLPTEVPTvSTEVTNVSPEETSVP 854
Cdd:pfam05109  720 KPGEVNVTK-----GTPPKNATSPQAP----SGQKTAVPTVTSTGGKANSTTGGKHTTGHGART-STEPTTDYGGDSTTP 789

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1039771140  855 PEETILTEITTVSPEETVFPIEGTTLP---TEVLTVPIEVTTFP 895
Cdd:pfam05109  790 RTRYNATTYLPPSTSSKLRPRWTFTSPpvtTAQATVPVPPTSQP 833
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 576-936 2.79e-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: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  576 TKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEAT 655
Cdd:COG5492    114 TGTATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNT 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  656 NASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPT 735
Cdd:COG5492    194 VVVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGS 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  736 EETISTEVTTVSPEETTLPTEV-----PTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEET 810
Cdd:COG5492    274 GSTTSTNTVTAGVGDTGVSVAVasssaATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPT 353

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  811 SV--PTEETISTEVtTVSPEETTLPT--------EVPTVSTE--VTNVSPEETSVppeeTILTE------ITTVspeeTV 872
Cdd:COG5492    354 SVtlAVGQTLTLTA-TVTPANATNKNvtwsssdpSVATVDSNglVTAVAAGTATI----TATTKdggktaTCTV----TV 424

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039771140  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 6.21e-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: 45.07  E-value: 6.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  707 TEVPTVPTEVTgvhtevtnVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYT 786
Cdd:pfam11596   13 TDIPTTTTATT--------TPTGSGTITLISTGNSSVSTKAGSSITVAGTSSTGSDNDDDDDDETDCETEIPTVPTGTTT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  787 EVPTVPTEVTGVHT--EVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEIT 864
Cdd:pfam11596   85 IDPTGNGTITGIPTasDTDDETDCETETDTVEPSIGTATTGVTTTTVISDGVTTTQTVTTVAPVPTQTHTETETVTITYT 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039771140  865 TVSPEETVFPIEGTTLPTEVLTVPIeVTTFPTgeTTVPTEVPTVSTEMTGVHTEvtTVFPEE 926
Cdd:pfam11596  165 GAGQTFTTYLTQSGEICDETVTYTV-TTTCPT--TTVAQGGGVYTTTVTVITTH--TVYPED 221
rne PRK10811
ribonuclease E; Reviewed
 800-949 6.75e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 46.19  E-value: 6.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  800 TEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEV-PTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGT 878
Cdd:PRK10811   848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSaPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQ 927

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039771140  879 TLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTP 949
Cdd:PRK10811   928 PQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
777-886 9.06e-04

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 45.61  E-value: 9.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  777 EETILTTlyteVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVspEETSVPPE 856
Cdd:PRK11907    28 AEEIVTT----TPATSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETSDPTSEATDTTTS--EARTVTPA 101

                           90       100       110
                   ....*....|....*....|....*....|
gi 1039771140  857 ETilteittvspeETVFPIEGTTLPTEVLT 886
Cdd:PRK11907   102 AT-----------ETSKPVEGQTVDVRILS 120
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 626-936 1.14e-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: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  626 VITVSPE-EIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTIltEVTTVSPEETTVPTEVPIVLIEATafptGETT 704
Cdd:COG4932    219 TETKAPEgYVLDTKDPTGATITVTVNAGGTVTVTLKNTPKYTKGSV--TVTKTDADTGEPLAGATFTLTDAD----GNTV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  705 LYTEVptVPTEVTGvHTEVTNVSP-----EETSVPT-----EETISTEVTTVSPEETTLPTE---VPTVSTEVTNVSPEE 771
Cdd:COG4932    293 VTTTV--TVTDADG-SYTFTDLPPgtytvTETKAPAgydldGEAVKVTITAGQTTTVTVTNGnneVKTGSVTLTKVDADD 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  772 TSVPPEE---TILTTLYTEVPTVPTEVTGVHTeVTNVSP-----EETSVPTEETISTEVT--TVSPEETTLPTEV----P 837
Cdd:COG4932    370 GEAPLAGaefTLTDADGTVVATITTDADGTAS-FKGLAPgtytlTETKAPEGYTLDSTPItvTVTDGGTGAIDTItnerK 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  838 TVSTEVTNVSP-----EETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEM 912
Cdd:COG4932    449 KGSVQVTKVDAplagaTFTLTDADGTVVTLTTDADLAGATFEADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITDD 528

                          330       340
                   ....*....|....*....|....
gi 1039771140  913 TGVHTEVTTVFPEETSIPTEVATV 936
Cdd:COG4932    529 TDGTVGDEATGTDPEVTVTGKSTT 552
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 575-936 1.28e-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: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  575 PTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEA 654
Cdd:COG5492     27 STAGVTSSSVTANLSVLASNDTSTTSSVASVVSTAGSGGTANTSSTVAVSGAALAAGAVSTVGVDATTVAQTVATASLEA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  655 TNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVP 734
Cdd:COG5492    107 GGVSSTGTGTATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTT 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  735 TEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPT 814
Cdd:COG5492    187 ASGSLNTVVVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATS 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  815 EETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTlptevltvpiEVTTF 894
Cdd:COG5492    267 SASTLGSGSTTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVV----------TASSV 336

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039771140  895 PTGETTVP-TEV---PTVSTEMTGVHTEVT-TVFPEE--------TSIPTEVATV 936
Cdd:COG5492    337 ATTVDVVPvTGVtlnPTSVTLAVGQTLTLTaTVTPANatnknvtwSSSDPSVATV 391
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 755-936 1.42e-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: 43.91  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  755 TEVPTVSTEVTNVSPEETSvppeeTILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVsPEETTlpT 834
Cdd:pfam11596   13 TDIPTTTTATTTPTGSGTI-----TLISTGNSSVSTKAGSSITVAGTSSTGSDNDDDDDDETDCETEIPTV-PTGTT--T 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  835 EVPTVSTEVTNVsPEETSVPPEETILTEITTV--SPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEM 912
Cdd:pfam11596   85 IDPTGNGTITGI-PTASDTDDETDCETETDTVepSIGTATTGVTTTTVISDGVTTTQTVTTVAPVPTQTHTETETVTITY 163

                          170       180
                   ....*....|....*....|....
gi 1039771140  913 TGVHTEVTTVFPEETSIPTEVATV 936
Cdd:pfam11596  164 TGAGQTFTTYLTQSGEICDETVTY 187
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
691-804 1.92e-03

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 44.84  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  691 VLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVspE 770
Cdd:PRK11907    17 LLTASNPKLAQAEEIVTTTPATSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETSDPTSEATDTTTS--E 94

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1039771140  771 ETSVPPEETIlTTLYTEVPTVPTEV---TGVHTEVTN 804
Cdd:PRK11907    95 ARTVTPAATE-TSKPVEGQTVDVRIlstTDLHTNLVN 130
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
580-848 2.30e-03

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 43.89  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  580 TVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASP 659
Cdd:COG3291     57 TVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTT 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  660 EETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETI 739
Cdd:COG3291    137 GTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  740 STEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPeETSVPTEETIS 819
Cdd:COG3291    217 GTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNG-TGGLGTTTAIT 295

                          250       260
                   ....*....|....*....|....*....
gi 1039771140  820 TEVTTVSPEETTLPTEVPTVSTEVTNVSP 848
Cdd:COG3291    296 PGNVSTTADVTGGTATLAVSSTLTTNDTT 324
PHA03255 PHA03255
BDLF3; Provisional
 519-715 5.04e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.20  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  519 TRGTSTAfVVALnfILIshgpCRV-LLQTEIPSSPLlPPTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTP-TEEATIP 596
Cdd:PHA03255     4 ARDKAGA-VLAM--ILI----CETsLIWTSSGSSTA-SAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPiTTTAILS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  597 TETTTVPTEVINVSPKETSipPEVTIPTEVITVSPEEIISPTEVTPVPTDVTaayveaTNASPEETSVPPEVTILTEVTT 676
Cdd:PHA03255    76 TNTTTVTSTGTTVTPVPTT--SNASTINVTTKVTAQNITATEAGTGTSTGVT------SNVTTRSSSTTSATTRITNATT 147

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039771140  677 VSPEETTVptevpivlieaTAFPTGETTlyTEVPTVPTE 715
Cdd:PHA03255   148 LAPTLSSK-----------GTSNATKTT--AELPTVPDE 173
COG1470 COG1470
Uncharacterized membrane protein [Function unknown];
731-940 5.41e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 441079 [Multi-domain]  Cd Length: 475  Bit Score: 42.92  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  731 TSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEE--TILTTLYTEVPTVPTEVTgVHTEVTNVSPE 808
Cdd:COG1470      4 AGLVASSTVAAGALAALLDLTTPLVGSTVALTSTASALSGERTTLAALaaTGGLVTATPVSPTSATLT-LSVEVPSNATV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039771140  809 ETSVPTEETISTEVTTVSPEETTL---PTEVPTVSTEVTNVSPEETSVPPE-ETILTEITTVSPEETVFPIEgttlPTEV 884
Cdd:COG1470     83 GTYLPITVTVAPYGLTLSVESPSLevaPGETVTYTVTLTNTGDEPDTVSLSaEGLPEGWTVTFTPDTSVSLA----PGES 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039771140  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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