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Conserved domains on  [gi|1907162178|ref|XP_036020895|]
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zonadhesin isoform X3 [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 ...
 1689-1839 3.07e-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: 3.07e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 1689 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1768
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 1769 NNQRVVLPVWPSQGRVTIRLSGI-FVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNL 1839
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1300-1452 6.50e-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: 6.50e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 1300 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1379
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1380 QEVTLPAILSD-DTYVGLSGR-FVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGM 1452
Cdd:pfam00094   80 QKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4883-5036 3.12e-39

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


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 144.82  E-value: 3.12e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4883 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4961
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 4962 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGV 5036
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 349-514 1.89e-37

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


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 140.17  E-value: 1.89e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   349 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 427
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   428 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 507
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1907162178   508 LISHGPC 514
Cdd:smart00137  155 LLSNGPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2076-2234 2.56e-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: 2.56e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2076 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2155
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2156 IsliNDSIVTLPTTTHIPGVSVMTED-VYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSG 2234
Cdd:pfam00094   77 V---NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 47-208 2.51e-31

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


:

Pssm-ID: 99706  Cd Length: 157  Bit Score: 122.49  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263     78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1907162178  206 GTC 208
Cdd:cd06263    155 GPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 217-345 2.74e-22

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: 96.68  E-value: 2.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  217 CTFDTlnDLCGWSWVPTaTGAKWTQKKGPTGKQGVGPAeDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGC-- 291
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPD-HTHGTGSGHYLYVESSSGREGQKARLLSPLLPpprSSHCls 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162178  292 ---------------------NIRKYTLF--SGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIAP 345
Cdd:cd06263     77 fwyhmygsgvgtlnvyvreegGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1885-1956 1.17e-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: 91.63  E-value: 1.17e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162178  1885 WTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFCP 1956
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1495-1570 4.32e-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: 84.31  E-value: 4.32e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178  1495 TMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFCP 1570
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3495-3549 1.84e-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: 1.84e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3495 CKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNeDGNSNCA 3549
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3735-3789 3.60e-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: 3.60e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3735 CKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNeDGNSNCA 3789
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3138-3192 1.81e-17

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 79.27  E-value: 1.81e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3138 CKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDlKDGSSNCT 3192
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3018-3072 1.92e-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: 1.92e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3018 CKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIeDGNSNCT 3072
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2778-2832 2.16e-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: 2.16e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2778 CKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDlEDGNSNCT 2832
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2418-2472 2.38e-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: 2.38e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2418 CKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNsNDGSSNCV 2472
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3971-4025 3.70e-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: 3.70e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3971 CKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSgDGSSNCT 4025
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4107-4158 8.14e-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: 8.14e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4107 CKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSR 4158
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3375-3429 1.12e-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: 1.12e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3375 CKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSeGSSTCT 3429
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2538-2592 2.73e-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: 2.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2538 CQHTQGGFIPAGKSWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIeDGTSNCA 2592
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3615-3669 3.73e-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: 3.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3615 CKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSFQCPPGAYCKDNeDGSSNCA 3669
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4462-4516 3.88e-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: 3.88e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4462 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4516
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 5089-5165 7.90e-16

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.07  E-value: 7.90e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  5089 SSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTgwkTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCA 5165
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCA---CGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3258-3312 1.34e-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: 1.34e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3258 CKNTQGAFISADKTWISRGCTQSCTCSAGAIHCRNFKCPSGTYCKNGDnGSSNCT 3312
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4342-4396 2.11e-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: 2.11e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4342 CKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDsVDGGSNCT 4396
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2898-2952 2.24e-15

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


:

Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 2.24e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2898 CKDTQGVLIPADKTWINRGCTQSCTCKGGAIQCQKYHCSSGTYCKDMeDDSSSCA 2952
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4822-4876 3.35e-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: 3.35e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4822 CKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNeDGSSDCA 4876
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2658-2712 5.34e-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: 5.34e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2658 CKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDiKDDTSNCT 2712
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4227-4274 6.01e-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: 6.01e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907162178 4227 CKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSS 4274
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND 48
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3855-3905 8.62e-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: 8.62e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 3855 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3905
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4702-4756 1.20e-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: 1.20e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4702 CKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESeDGSSNCV 4756
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4582-4636 2.89e-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: 2.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4582 CKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNeGNSNCV 4636
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.
 460-887 1.31e-13

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


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 77.31  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  460 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 539
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  540 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 618
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  619 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 698
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  699 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 772
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  773 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 851
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1907162178  852 TTLPTEVLtvPIEVTTFPtGETTVPTEVPTVSTEMT 887
Cdd:pfam17823  380 TTQPSPLL--PTQGAAGP-GILLAPEQVATEATAGT 412
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1628-1682 8.33e-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: 8.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1628 CTSFQGRYFKLQEQWFNPDCKEICTCeSHNHILCKPWKCKAQEACSYKNGVLGCH 1682
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1573-1626 2.34e-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: 2.34e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1573 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1626
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1240-1293 1.64e-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: 1.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 1240 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1293
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1959-2013 1.49e-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: 1.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 1959 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2013
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 5168-5221 1.55e-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: 1.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 5168 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDT-QSLPVTHC 5221
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4522-4580 3.33e-09

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 55.86  E-value: 3.33e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4522 CPAHSHYSKCLPPCQPSCSDPdghceGTSPEAPSTCEEGCVCEPDYVLSND-KCVPSSEC 4580
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 5223-5276 7.02e-09

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 54.62  E-value: 7.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 5223 CTADGIYYKLGDSFVTNDCSQHCTCaSQGILLCEPYGCRAGESCMVANFTRGCF 5276
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3911-3969 2.63e-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: 2.63e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3911 CPAHSHFTSCLPSCPPSCANLDGSCEQTSPkvpstCKEGCLCQPGYFLNN-GKCVLQTHC 3969
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP-----CVEGCVCPPGFVRNSgGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4047-4105 1.53e-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: 1.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4047 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4105
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3078-3136 2.29e-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: 2.29e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3078 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3136
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2288-2354 2.34e-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: 2.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 2288 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2354
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2358-2416 4.20e-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: 4.20e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2358 CPAHSHYTNCLPSCPPSCLDPD--SRCegsghkvPATCREGCICQPDYVL-LNDKCVLRSHC 2416
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3435-3493 6.10e-07

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 49.31  E-value: 6.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3435 CPAHTQYTSCLPSCLPSCLDPEGlckdiSPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3493
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2838-2896 6.53e-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: 6.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2838 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2896
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4282-4340 8.59e-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: 8.59e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4282 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4340
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4762-4820 8.68e-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: 8.68e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4762 CPANSLYTHCLPTCLPSCSNPDGRCegtshKAPSTCREGCVCQPGYLLNKD-TCVHKNQC 4820
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2478-2536 9.76e-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: 9.76e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2478 CPAHSKFTDCLPPCHPSCSDP--DGHCEGIstnahsnCKEGCVCQPGYVLRND-KCVLRIEC 2536
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLspPDVCPEP-------CVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3198-3256 1.20e-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: 1.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3198 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3256
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1189-1238 1.26e-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: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1189 CPPNAHIELC--ACPASCESPK--PSCQPPCIPGCVCNPGFLFS-NNQCINESSC 1238
Cdd:cd19941      1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2598-2656 1.30e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2598 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 2656
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3318-3373 1.62e-06

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 3318 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3373
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2718-2776 2.84e-06

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 2.84e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2718 CPDHSLYTHCLPSCLPSCSDPDglcrgTSPEAPSTCKEGCVCEPDYVLS-NDKCVLRIEC 2776
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4167-4225 3.53e-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: 3.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4167 CPAHSHYTNCLPACSRSCTDLdghceGTSPKVPSPCKEGCLCQPGYVVHNH-KCVLQIHC 4225
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2958-3016 8.53e-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: 8.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2958 CPAHSHFTNCLPPCQPSCLDseghcEGSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 3016
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4642-4700 1.03e-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: 45.84  E-value: 1.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4642 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4700
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4402-4460 4.44e-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: 4.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4402 CPAHSHHTYCLPSCIPSCSNvndrcESTSLQRPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4460
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3795-3853 4.94e-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: 4.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3795 CPTHSNYTDCLPFCLPSCLDPSalcggTSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3853
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 ...
 2015-2070 6.15e-05

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 43.45  E-value: 6.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 2015 CSDQDGSYHLLGESWYTEKtCTTLCTCSaHSNITCSPTACKANHVCLRQEGLLRCA 2070
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3555-3613 1.86e-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: 1.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3555 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLSNN-KCLLRNRC 3613
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 ...
 1689-1839 3.07e-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: 3.07e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 1689 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1768
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 1769 NNQRVVLPVWPSQGRVTIRLSGI-FVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNL 1839
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1300-1452 6.50e-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: 6.50e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 1300 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1379
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1380 QEVTLPAILSD-DTYVGLSGR-FVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGM 1452
Cdd:pfam00094   80 QKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1681-1837 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 1907162178  1681 CHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCwskSQENNFVVSATNEIHDGNLEVsyVKAVHVQVFDLKISM 1760
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGATC--LKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162178  1761 FKGQ-KVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGL-QVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDD 1837
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4883-5036 3.12e-39

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 144.82  E-value: 3.12e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4883 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4961
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 4962 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGV 5036
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 349-514 1.89e-37

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


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 140.17  E-value: 1.89e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   349 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 427
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   428 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 507
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1907162178   508 LISHGPC 514
Cdd:smart00137  155 LLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 353-515 2.75e-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: 2.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  353 CDFEDrvHPFCDWNQVYGDMGHWSWGSksVPTLIAGSPREFPYGGE--HYIFFDSVKlSQEGQSARLVSPPFCAPG-DIC 429
Cdd:pfam00629    1 CDFED--GNLCGWTQDSSDDFDWERVS--GPSVKTGPSSDHTQGTGsgHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  430 VEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILI 509
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1907162178  510 SHGPCR 515
Cdd:pfam00629  154 SSGPCP 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2076-2234 2.56e-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: 2.56e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2076 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2155
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2156 IsliNDSIVTLPTTTHIPGVSVMTED-VYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSG 2234
Cdd:pfam00094   77 V---NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 353-514 1.80e-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: 1.80e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  353 CDFEDrvhPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKlSQEGQSARLVSPPFCAP-GDICVE 431
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  432 FAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILISH 511
Cdd:cd06263     77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSA-SSKPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1907162178  512 GPC 514
Cdd:cd06263    155 GPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 47-208 2.51e-31

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


Pssm-ID: 99706  Cd Length: 157  Bit Score: 122.49  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263     78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1907162178  206 GTC 208
Cdd:cd06263    155 GPC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1298-1451 5.66e-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: 5.66e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  1298 ATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNStdHFFRITANTEERGvEGVSCLDKVVISLPETTVTMISGRHTLI 1377
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  1378 GD-QEVTLPAILSDDT-YVGLSGRFVELRTTFGL-RVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDG 1451
Cdd:smart00216   87 VNgQQVSLPYKTSDGSiQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 4882-5035 2.57e-25

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 105.56  E-value: 2.57e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  4882 RCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRgiepLIMEGRNKISPKGSSTLHEVTTIVYGYKIQL-QEELVVL 4960
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  4961 VNDEKVAVPYNPNEHLRVMLRAQRLLLV-TDFE-MVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSG 5035
Cdd:smart00216   87 VNGQQVSLPYKTSDGSIQIRSSGGYLVViTSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-209 8.69e-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: 8.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   47 CDFEDNSrpFCDWSQMSADDGDWIRTTGPSLTgtSGPPGG--YPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQG-PLCV 123
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  124 HFAFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSI 203
Cdd:pfam00629   77 RFWYHMSGSGVGT--LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ-PFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1907162178  204 QRGTCN 209
Cdd:pfam00629  154 SSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 217-345 2.74e-22

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: 96.68  E-value: 2.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  217 CTFDTlnDLCGWSWVPTaTGAKWTQKKGPTGKQGVGPAeDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGC-- 291
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPD-HTHGTGSGHYLYVESSSGREGQKARLLSPLLPpprSSHCls 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162178  292 ---------------------NIRKYTLF--SGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIAP 345
Cdd:cd06263     77 fwyhmygsgvgtlnvyvreegGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2074-2234 1.13e-21

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 95.16  E-value: 1.13e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  2074 GECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNtnmPFFMISAKtdiNTNGKNKTFGVYQLYIDIFNFHITLQKDHL 2153
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLK---NVPCGGGATCLKSVKVELNGDEIELKDDNG 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  2154 VLIslINDSIVTLPTTTHIPGVSV-MTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTP 2232
Cdd:smart00216   84 KVT--VNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 1907162178  2233 SG 2234
Cdd:smart00216  162 DG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1885-1956 1.17e-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: 91.63  E-value: 1.17e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162178  1885 WTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFCP 1956
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 47-208 6.69e-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: 6.69e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178    47 CDFEDNsrPFCDWSQMSADDGDWIRTTgpSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQ-GPLCVHF 125
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   126 AFHMFGLswGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPAdHDIPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:smart00137   82 WYYMYGS--GSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1907162178   206 GTC 208
Cdd:smart00137  159 GPC 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1495-1570 4.32e-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: 84.31  E-value: 4.32e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178  1495 TMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFCP 1570
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3495-3549 1.84e-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: 1.84e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3495 CKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNeDGNSNCA 3549
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3735-3789 3.60e-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: 3.60e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3735 CKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNeDGNSNCA 3789
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3138-3192 1.81e-17

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 79.27  E-value: 1.81e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3138 CKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDlKDGSSNCT 3192
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3018-3072 1.92e-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: 1.92e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3018 CKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIeDGNSNCT 3072
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2778-2832 2.16e-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: 2.16e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2778 CKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDlEDGNSNCT 2832
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2418-2472 2.38e-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: 2.38e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2418 CKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNsNDGSSNCV 2472
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3971-4025 3.70e-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: 3.70e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3971 CKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSgDGSSNCT 4025
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4107-4158 8.14e-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: 8.14e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4107 CKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSR 4158
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3375-3429 1.12e-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: 1.12e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3375 CKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSeGSSTCT 3429
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2538-2592 2.73e-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: 2.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2538 CQHTQGGFIPAGKSWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIeDGTSNCA 2592
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3615-3669 3.73e-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: 3.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3615 CKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSFQCPPGAYCKDNeDGSSNCA 3669
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4462-4516 3.88e-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: 3.88e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4462 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4516
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 5089-5165 7.90e-16

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.07  E-value: 7.90e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  5089 SSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTgwkTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCA 5165
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCA---CGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3258-3312 1.34e-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: 1.34e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3258 CKNTQGAFISADKTWISRGCTQSCTCSAGAIHCRNFKCPSGTYCKNGDnGSSNCT 3312
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4342-4396 2.11e-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: 2.11e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4342 CKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDsVDGGSNCT 4396
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2898-2952 2.24e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 2.24e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2898 CKDTQGVLIPADKTWINRGCTQSCTCKGGAIQCQKYHCSSGTYCKDMeDDSSSCA 2952
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4822-4876 3.35e-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: 3.35e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4822 CKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNeDGSSDCA 4876
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2658-2712 5.34e-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: 5.34e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2658 CKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDiKDDTSNCT 2712
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4227-4274 6.01e-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: 6.01e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907162178 4227 CKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSS 4274
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND 48
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3855-3905 8.62e-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: 8.62e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 3855 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3905
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4702-4756 1.20e-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: 1.20e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4702 CKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESeDGSSNCV 4756
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1888-1955 1.28e-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: 1.28e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162178 1888 KCAILMNPlGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFC 1955
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4582-4636 2.89e-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: 2.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4582 CKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNeGNSNCV 4636
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 460-887 1.31e-13

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 77.31  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  460 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 539
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  540 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 618
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  619 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 698
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  699 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 772
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  773 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 851
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1907162178  852 TTLPTEVLtvPIEVTTFPtGETTVPTEVPTVSTEMT 887
Cdd:pfam17823  380 TTQPSPLL--PTQGAAGP-GILLAPEQVATEATAGT 412
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1501-1569 7.80e-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: 66.25  E-value: 7.80e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162178 1501 LCGQLvNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFC 1569
Cdd:pfam08742    1 KCGLL-SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 5094-5164 5.55e-12

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 63.94  E-value: 5.55e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162178 5094 CRVLVDpQGPFAACHQIIAPEPFEQRCMLDMCtgwKTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHC 5164
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMC---SCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1628-1682 8.33e-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: 8.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1628 CTSFQGRYFKLQEQWFNPDCKEICTCeSHNHILCKPWKCKAQEACSYKNGVLGCH 1682
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1573-1626 2.34e-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: 2.34e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1573 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1626
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1573-1626 6.40e-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: 6.40e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1573 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1626
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1240-1293 1.64e-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: 1.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 1240 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1293
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
 676-831 1.68e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 64.54  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  676 ETTL-YTEVPTVPTEVTGVH--TEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPee 752
Cdd:PHA03255    19 ETSLiWTSSGSSTASAGNVTgtTAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTP-- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  753 tILTTLYTEVPTVPTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 827
Cdd:PHA03255    91 -VPTTSNASTINVTTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169


                   ....
gi 1907162178  828 PPEE 831
Cdd:PHA03255   170 VPDE 173
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1959-2013 1.49e-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: 1.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 1959 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2013
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 5168-5221 1.55e-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: 1.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 5168 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDT-QSLPVTHC 5221
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4522-4580 3.33e-09

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 55.86  E-value: 3.33e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4522 CPAHSHYSKCLPPCQPSCSDPdghceGTSPEAPSTCEEGCVCEPDYVLSND-KCVPSSEC 4580
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1959-2013 5.32e-09

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 55.02  E-value: 5.32e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 1959 CPPRSSYNPCANSCPATCLTLSTPRDCpTLPCVEGCECQSGHILS-GTTCVPLRQC 2013
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 5223-5276 7.02e-09

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 54.62  E-value: 7.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 5223 CTADGIYYKLGDSFVTNDCSQHCTCaSQGILLCEPYGCRAGESCMVANFTRGCF 5276
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4522-4580 1.22e-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: 1.22e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4522 CPAHSHYSKCLPPCQPSCSDPDghcegTSPEAPSTCEEGCVCEPDYVLS-NDKCVPSSEC 4580
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3911-3969 2.63e-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: 2.63e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3911 CPAHSHFTSCLPSCPPSCANLDGSCEQTSPkvpstCKEGCLCQPGYFLNN-GKCVLQTHC 3969
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP-----CVEGCVCPPGFVRNSgGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3911-3969 9.29e-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: 9.29e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3911 CPAHSHFTSCLPSCPPSCANLDgsceqTSPKVPSTCKEGCLCQPGYFLN-NGKCVLQTHC 3969
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4047-4105 1.53e-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: 1.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4047 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4105
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3078-3136 2.29e-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: 2.29e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3078 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3136
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2288-2354 2.34e-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: 2.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 2288 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2354
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4047-4105 2.50e-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: 2.50e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4047 CPAHSHFTSCLPSCPPSCSNLD--GSCvesnfkaPSVCKKGCICQPGYLLN-NDKCVLRIQC 4105
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3078-3136 3.56e-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: 3.56e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3078 CPANSNFTSCLPSCQPSCSNTDvhcegSSPNALSSCREGCVCQSGYVLH-NDKCILRNQC 3136
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2358-2416 4.20e-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: 4.20e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2358 CPAHSHYTNCLPSCPPSCLDPD--SRCegsghkvPATCREGCICQPDYVL-LNDKCVLRSHC 2416
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3435-3493 6.10e-07

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 49.31  E-value: 6.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3435 CPAHTQYTSCLPSCLPSCLDPEGlckdiSPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3493
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2838-2896 6.53e-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: 6.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2838 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2896
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2358-2416 7.56e-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: 7.56e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2358 CPAHSHYTNCLPSCPPSCLDPDSRCegsghKVPATCREGCICQPDYVLLND-KCVLRSHC 2416
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4282-4340 8.59e-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: 8.59e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4282 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4340
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2838-2896 8.59e-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: 8.59e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2838 CPAHSHYTNCLPTCQPSCSDPdghceGSSTKAPSACKEGCVCEPDYVMLNN-KCVPRIEC 2896
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4762-4820 8.68e-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: 8.68e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4762 CPANSLYTHCLPTCLPSCSNPDGRCegtshKAPSTCREGCVCQPGYLLNKD-TCVHKNQC 4820
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4762-4820 8.76e-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: 8.76e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4762 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4820
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2478-2536 9.76e-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: 9.76e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2478 CPAHSKFTDCLPPCHPSCSDP--DGHCEGIstnahsnCKEGCVCQPGYVLRND-KCVLRIEC 2536
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLspPDVCPEP-------CVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3198-3256 1.20e-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: 1.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3198 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3256
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1189-1238 1.26e-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: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1189 CPPNAHIELC--ACPASCESPK--PSCQPPCIPGCVCNPGFLFS-NNQCINESSC 1238
Cdd:cd19941      1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2598-2656 1.30e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2598 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 2656
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3198-3256 1.40e-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: 1.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3198 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3256
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4282-4340 1.42e-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: 1.42e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4282 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVLRED-KCVLRTQC 4340
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3318-3373 1.62e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 3318 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3373
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 5168-5212 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
                   ....*....|....*....|....*....|....*....|....*
gi 1907162178 5168 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSD 5212
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNS 45
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3318-3373 2.08e-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: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 3318 CPTNSQFTDCLPSCVPSCSNRceVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3373
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANP--NAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3435-3493 2.36e-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: 2.36e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3435 CPAHTQYTSCLPSCLPSCLDPEglckdISPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3493
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2478-2536 2.79e-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: 2.79e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2478 CPAHSKFTDCLPPCHPSCSDPDghcegISTNAHSNCKEGCVCQPGYVL-RNDKCVLRIEC 2536
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2718-2776 2.84e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 2.84e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2718 CPDHSLYTHCLPSCLPSCSDPDglcrgTSPEAPSTCKEGCVCEPDYVLS-NDKCVLRIEC 2776
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4167-4225 3.53e-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: 3.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4167 CPAHSHYTNCLPACSRSCTDLdghceGTSPKVPSPCKEGCLCQPGYVVHNH-KCVLQIHC 4225
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1189-1238 5.93e-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: 5.93e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1189 CPPNAHIELC--ACPASCESPKPS--CQPPCIPGCVCNPGFLFSNN-QCINESSC 1238
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPPdvCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2718-2776 6.42e-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: 6.42e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2718 CPDHSLYTHCLPSCLPSCSDPdglcrGTSPEAPSTCKEGCVCEPDYVLSND-KCVLRIEC 2776
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
610-902 7.36e-06

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 51.98  E-value: 7.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  610 SPTEVTPVPT-------DVTaayVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTE 682
Cdd:COG3291     36 TSTEANPSHTyttpgtyTVT---LTVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  683 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEV 762
Cdd:COG3291    113 GVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTG 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  763 PTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSP 842
Cdd:COG3291    193 TIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVV 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  843 EETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETS 902
Cdd:COG3291    273 TTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTV 332
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2958-3016 8.53e-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: 8.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2958 CPAHSHFTNCLPPCQPSCLDseghcEGSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 3016
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4642-4700 1.03e-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: 45.84  E-value: 1.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4642 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4700
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2298-2355 1.41e-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: 1.41e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162178  2298 AHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCP 2355
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2598-2656 1.68e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 1.68e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2598 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVV-LNNKCVPRIEC 2656
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4167-4225 2.15e-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: 2.15e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4167 CPAHSHYTNCLPACSRSCTDLDghcegTSPKVPSPCKEGCLCQPGYVVH-NHKCVLQIHC 4225
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4642-4700 2.37e-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: 2.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4642 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4700
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2958-3016 2.91e-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: 2.91e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2958 CPAHSHFTNCLPPCQPSC--LDSEGHCegsttkaPSACQEGCVCEPDYVV-LNNKCVPRIEC 3016
Cdd:cd19941      1 CPPNEVYSECGSACPPTCanPNAPPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4402-4460 4.44e-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: 4.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4402 CPAHSHHTYCLPSCIPSCSNvndrcESTSLQRPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4460
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3795-3853 4.94e-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: 4.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3795 CPTHSNYTDCLPFCLPSCLDPSalcggTSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3853
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2015-2070 6.15e-05

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 43.45  E-value: 6.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 2015 CSDQDGSYHLLGESWYTEKtCTTLCTCSaHSNITCSPTACKANHVCLRQEGLLRCA 2070
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4402-4460 9.83e-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: 9.83e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4402 CPAHSHHTYCLPSCIPSCSNVND--RCestslqrPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4460
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAppPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3795-3853 1.50e-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: 1.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3795 CPTHSNYTDCLPFCLPSCLDPSAlcggtSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3853
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNA-----PPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3555-3613 1.86e-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: 1.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3555 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLSNN-KCLLRNRC 3613
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3555-3613 2.31e-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: 2.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3555 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLS-NNKCLLRNRC 3613
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 ...
 1689-1839 3.07e-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: 3.07e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 1689 CMVSGDPHYLTFDGALHHFMGTCTYVLTQPCWSKSqenNFVVSATNEIHDGNLEVSYVKAVHVQVFDLKISMFKGQKVVL 1768
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 1769 NNQRVVLPVWPSQGRVTIRLSGI-FVLLYTNFGLQVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDDNL 1839
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFM 149
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1300-1452 6.50e-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: 6.50e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 1300 CLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNSTDHFFRITANTEERGVEGVsCLDKVVISLPETTVTMISGRHTLIGD 1379
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1380 QEVTLPAILSD-DTYVGLSGR-FVELRTTFGLRVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDGM 1452
Cdd:pfam00094   80 QKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1681-1837 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 1907162178  1681 CHAQGAATCMVSGDPHYLTFDGALHHFMGTCTYVLTQPCwskSQENNFVVSATNEIHDGNLEVsyVKAVHVQVFDLKISM 1760
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGGATC--LKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162178  1761 FKGQ-KVVLNNQRVVLPVWPSQGRVTIRLSGIFVLLYTNFGL-QVRYDGRHLVEVTVPSSYTGSLCGLCGNYNNNSMDD 1837
Cdd:smart00216   79 KDDNgKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDD 157
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 4883-5036 3.12e-39

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


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 144.82  E-value: 3.12e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4883 CTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPrgiEPLIMEGRNKISPKGSST-LHEVTTIVYGYKIQLQEELVVLV 4961
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVcLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 4962 NDEKVAVPYNPNE-HLRVMLRAQ-RLLLVTDFEMVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSGV 5036
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 349-514 1.89e-37

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


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 140.17  E-value: 1.89e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   349 SFPQCDFEDrvHPFCDWNQVYGDMGHWSWGSKSVPtlIAGSPREFPYGGEHYIFFDSVKLSqEGQSARLVSPPFCAPGD- 427
Cdd:smart00137    2 SPGNCDFEE--GSTCGWHQDSNDDGHWERVSSATG--IPGPNRDHTTGNGHFMFFETSSGA-EGQTARLLSPPLYENRSt 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   428 ICVEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFI 507
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 1907162178   508 LISHGPC 514
Cdd:smart00137  155 LLSNGPC 161
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 353-515 2.75e-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: 2.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  353 CDFEDrvHPFCDWNQVYGDMGHWSWGSksVPTLIAGSPREFPYGGE--HYIFFDSVKlSQEGQSARLVSPPFCAPG-DIC 429
Cdd:pfam00629    1 CDFED--GNLCGWTQDSSDDFDWERVS--GPSVKTGPSSDHTQGTGsgHFMYVDTSS-GAPGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  430 VEFAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILI 509
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSS-STQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1907162178  510 SHGPCR 515
Cdd:pfam00629  154 SSGPCP 159
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 2076-2234 2.56e-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: 2.56e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2076 CRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNTNmpfFMISAKTDINTNGKNKTFgVYQLYIDIFNFHITLQKDHLVL 2155
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVC-LKSVTVIVGDLEITLQKGGTVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2156 IsliNDSIVTLPTTTHIPGVSVMTED-VYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTPSG 2234
Cdd:pfam00094   77 V---NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDG 153
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 353-514 1.80e-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: 1.80e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  353 CDFEDrvhPFCDWNQVYGDMGHWSWGSKSVPTLIAGSPREFPYGGEHYIFFDSVKlSQEGQSARLVSPPFCAP-GDICVE 431
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSS-GREGQKARLLSPLLPPPrSSHCLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  432 FAYHMYGLGKGTtLKLLLGSPAGSFPIPLWNRVGSQSSGWMNSSVTIPKgYQQPMQLFIEATRGTSTAFVVALNFILISH 511
Cdd:cd06263     77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSA-SSKPFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1907162178  512 GPC 514
Cdd:cd06263    155 GPC 157
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 47-208 2.51e-31

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


Pssm-ID: 99706  Cd Length: 157  Bit Score: 122.49  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   47 CDFEDnsrPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWE-QGPLCVHF 125
Cdd:cd06263      1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESSSGREGQKARLLSPLLPPpRSSHCLSF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  126 AFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:cd06263     78 WYHMYGSGVGT--LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASSK-PFQVVFEGVRGSGSRGDIALDDISLSP 154


                   ...
gi 1907162178  206 GTC 208
Cdd:cd06263    155 GPC 157
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1298-1451 5.66e-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: 5.66e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  1298 ATCLVYGDLHFVTFDERHIGFTGTCTYILTQTCSNStdHFFRITANTEERGvEGVSCLDKVVISLPETTVTMISGRHTLI 1377
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE--PTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  1378 GD-QEVTLPAILSDDT-YVGLSGRFVELRTTFGL-RVRWDGDQQLFVTVSSTFSGKLCGFCGNYDGDSSNDNLKSDG 1451
Cdd:smart00216   87 VNgQQVSLPYKTSDGSiQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 4882-5035 2.57e-25

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 105.56  E-value: 2.57e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  4882 RCTIFGDPYYLTFDGFTYHFLGRMNYYLIKTVDKLPRgiepLIMEGRNKISPKGSSTLHEVTTIVYGYKIQL-QEELVVL 4960
Cdd:smart00216   11 TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGGGATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  4961 VNDEKVAVPYNPNEHLRVMLRAQRLLLV-TDFE-MVLDFDGKHSAVISLPTTYRGLTRGLCGNYDRDQSNELMLPSG 5035
Cdd:smart00216   87 VNGQQVSLPYKTSDGSIQIRSSGGYLVViTSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 47-209 8.69e-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: 8.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   47 CDFEDNSrpFCDWSQMSADDGDWIRTTGPSLTgtSGPPGG--YPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQG-PLCV 123
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSGPSVK--TGPSSDhtQGTGSGHFMYVDTSSGAPGQTARLLSPLLPPSRsPQCL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  124 HFAFHMFGLSWGAqlRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDiPSWLMFEGMRGNTAYLDISLDGLSI 203
Cdd:pfam00629   77 RFWYHMSGSGVGT--LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSSTQ-PFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 1907162178  204 QRGTCN 209
Cdd:pfam00629  154 SSGPCP 159
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 217-345 2.74e-22

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: 96.68  E-value: 2.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  217 CTFDTlnDLCGWSWVPTaTGAKWTQKKGPTGKQGVGPAeDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSH---SRGC-- 291
Cdd:cd06263      1 CDFED--GLCGWTQDST-DDFDWTRVSGSTPSPGTPPD-HTHGTGSGHYLYVESSSGREGQKARLLSPLLPpprSSHCls 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162178  292 ---------------------NIRKYTLF--SGHPGPDWQAVSVNY-TGQGQIQFMVVGMFGNIPEPAIAVDAISIAP 345
Cdd:cd06263     77 fwyhmygsgvgtlnvyvreegGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 2074-2234 1.13e-21

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 95.16  E-value: 1.13e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  2074 GECRISEDSQIVSFDDHSHPIQDTCTYILVKVCHPNtnmPFFMISAKtdiNTNGKNKTFGVYQLYIDIFNFHITLQKDHL 2153
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLK---NVPCGGGATCLKSVKVELNGDEIELKDDNG 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  2154 VLIslINDSIVTLPTTTHIPGVSV-MTEDVYTIVTIKDEIQVKFESNNFLDVKIPASSNGKVCGVCGNFNGEEEDELMTP 2232
Cdd:smart00216   84 KVT--VNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 1907162178  2233 SG 2234
Cdd:smart00216  162 DG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1885-1956 1.17e-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: 91.63  E-value: 1.17e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162178  1885 WTKKCAILMNPLGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFCP 1956
Cdd:smart00832    4 ACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGvCISPWRTPTFCP 76
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 47-208 6.69e-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: 6.69e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178    47 CDFEDNsrPFCDWSQMSADDGDWIRTTgpSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQ-GPLCVHF 125
Cdd:smart00137    6 CDFEEG--STCGWHQDSNDDGHWERVS--SATGIPGPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCLTF 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178   126 AFHMFGLswGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPAdHDIPSWLMFEGMRGNTAYLDISLDGLSIQR 205
Cdd:smart00137   82 WYYMYGS--GSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDILLSN 158


                    ...
gi 1907162178   206 GTC 208
Cdd:smart00137  159 GPC 161
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1495-1570 4.32e-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: 84.31  E-value: 4.32e-19
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178  1495 TMSGPKLCGQLVNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFCP 1570
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3495-3549 1.84e-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: 1.84e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3495 CKDAQGALIPAGKTWTSPGCTQSCACMGGAVQCQSSQCPPGTYCKDNeDGNSNCA 3549
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3735-3789 3.60e-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: 3.60e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3735 CKDAQGALIPSGKTWTSPGCTQSCACMGGVVQCQSSQCPPGTYCKDNeDGNSNCA 3789
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3138-3192 1.81e-17

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 79.27  E-value: 1.81e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3138 CKDAQGALIPEGKTWITSGCTQSCNCTGGAIQCQNFQCPLKTYCKDlKDGSSNCT 3192
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3018-3072 1.92e-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: 1.92e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3018 CKDAQGVLIPADKTWINRGCTQSCTCKGGAIQCQKFQCPSETYCKDIeDGNSNCT 3072
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2778-2832 2.16e-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: 2.16e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2778 CKDAQGVLIPAGKTWINRGCTQSCSCMGGAIQCQNFKCPSEAYCQDlEDGNSNCT 2832
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2418-2472 2.38e-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: 2.38e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2418 CKDAQGVFIPAGKTWISEDCTQSCTCMKGSMRCWDFQCPPGTYCKNsNDGSSNCV 2472
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3971-4025 3.70e-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: 3.70e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3971 CKDAEGGLVPAGKTWTSKDCTQSCACTGGAVQCQNFQCPLGTYCKDSgDGSSNCT 4025
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4107-4158 8.14e-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: 8.14e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4107 CKDTQGGLIPAGRTWISSDCTKSCSCMGGIIQCRDFQCPPGTYCKESNDSSR 4158
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSN 52
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3375-3429 1.12e-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: 1.12e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3375 CKDARGAIIPAGKTWTSKGCTQSCACVEGNIQCQNFQCPPETYCKDNSeGSSTCT 3429
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2538-2592 2.73e-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: 2.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2538 CQHTQGGFIPAGKSWTSRGCSQSCDCMEGVIRCQNFQCPSGTYCQDIeDGTSNCA 2592
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3615-3669 3.73e-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: 3.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3615 CKDAHGALIPEDKTWVSRGCTQSCVCTGGSIQCLSFQCPPGAYCKDNeDGSSNCA 3669
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4462-4516 3.88e-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: 3.88e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4462 CKDSQGTLIPAGKNWITTGCSQRCTCTGGLVQCHDFQCPSGAECQDIeDGNSNCV 4516
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 5089-5165 7.90e-16

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.07  E-value: 7.90e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  5089 SSTQACRVLVDPQGPFAACHQIIAPEPFEQRCMLDMCTgwkTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHCA 5165
Cdd:smart00832    3 YACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCA---CGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3258-3312 1.34e-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: 1.34e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 3258 CKNTQGAFISADKTWISRGCTQSCTCSAGAIHCRNFKCPSGTYCKNGDnGSSNCT 3312
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4342-4396 2.11e-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: 2.11e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4342 CKDAQGDLIPANKTWLTRGCAQKCTCKGGNIHCWNFKCPLGTECKDsVDGGSNCT 4396
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2898-2952 2.24e-15

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 73.11  E-value: 2.24e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2898 CKDTQGVLIPADKTWINRGCTQSCTCKGGAIQCQKYHCSSGTYCKDMeDDSSSCA 2952
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4822-4876 3.35e-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: 3.35e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4822 CKDIRGNIIPAGNTWISSDCTQSCACTDGVIQCQNFVCPSGSHCQYNeDGSSDCA 4876
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2658-2712 5.34e-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: 5.34e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 2658 CKDAQGVLIPADKIWINKGCTQTCACVTGTIHCRDFQCPSGTYCKDiKDDTSNCT 2712
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKD-NDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4227-4274 6.01e-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: 6.01e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907162178 4227 CKDAQGGFVPAGKTWISRGCTQSCACVGGAVQCHNFTCPTGTQCQNSS 4274
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND 48
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 3855-3905 8.62e-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: 8.62e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 3855 CRDTQGAVIPAGKTWLSTGCIQSCACVEGTIQCQNFQCPPGTYC---NHNNNCA 3905
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCkdnDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4702-4756 1.20e-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: 1.20e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4702 CKDFQGSLIKTGQTWISSGCSKICTCKGGFFQCQSYKCPSGTQCEESeDGSSNCV 4756
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1888-1955 1.28e-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: 1.28e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162178 1888 KCAILMNPlGPFSNCHEAVPPQASFSSCVYGQCETNGDNLTLCHSLQAYASLCAQAG-QVTTWRNSTFC 1955
Cdd:pfam08742    1 KCGLLSDS-GPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGvCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 4582-4636 2.89e-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: 2.89e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 4582 CKDAHGVLIPESKTWVSRGCTKNCTCKGGTVQCHDFSCPTGSRCLDNNeGNSNCV 4636
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDND-GSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 460-887 1.31e-13

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 77.31  E-value: 1.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  460 LWNRVGSQssgwmNSSVtipkgyqqpmqlfiEATRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVP 539
Cdd:pfam17823   33 MWNGAGKQ-----NASG--------------DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPH 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  540 TLPMEQP-TSPTKATTVTIEIPTTPTeeATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEeiiSPTEVTPVP 618
Cdd:pfam17823   94 GTDLSEPaTREGAADGAASRALAAAA--SSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPR---AAIAAASAP 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  619 TDVTAAYVEATNASPEETSVPPEVTILTEVTTvspeeTTVPTEVPIVLIEATAFPTGETTLYTEVPTVPtevtgvhtevt 698
Cdd:pfam17823  169 HAASPAPRTAASSTTAASSTTAASSAPTTAAS-----SAPATLTPARGISTAATATGHPAAGTALAAVG----------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  699 nvspeeTSVPTEETISTEVTTVSPEET-TLPTEVPTVSTEVTNV---SPEETSVPPEETILTTLYTEVPTVPT--EVTGV 772
Cdd:pfam17823  233 ------NSSPAAGTVTAAVGTVTPAALaTLAAAAGTVASAAGTInmgDPHARRLSPAKHMPSDTMARNPAAPMgaQAQGP 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  773 HTEVTNVSPEETSVPtEETISTEVTTVSPEEttlPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPE-ETVFPieg 851
Cdd:pfam17823  307 IIQVSTDQPVHNTAG-EPTPSPSNTTLEPNT---PKSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEvEATSP--- 379

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1907162178  852 TTLPTEVLtvPIEVTTFPtGETTVPTEVPTVSTEMT 887
Cdd:pfam17823  380 TTQPSPLL--PTQGAAGP-GILLAPEQVATEATAGT 412
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1501-1569 7.80e-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: 66.25  E-value: 7.80e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162178 1501 LCGQLvNPSGPFEACLLHLKASSFLDNCVTDMCSFQGLQQKLCAHMSAMTATCQDAGYPVKPWREPQFC 1569
Cdd:pfam08742    1 KCGLL-SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 520-914 3.42e-12

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 73.41  E-value: 3.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  520 TEIPSSPLLPP--TGPSeSTVPTLPMEQPTSPTKATTVTIEIPTTPTEeatiptetttvptevinvSPKET---SIPPEV 594
Cdd:pfam05109  446 TGLPSSTHVPTnlTAPA-STGPTVSTADVTSPTPAGTTSGASPVTPSP------------------SPRDNgteSKAPDM 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  595 TIPTEVITVSPEEIISPTEVTPVPT-DVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFP 673
Cdd:pfam05109  507 TSPTSAVTTPTPNATSPTPAVTTPTpNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTP 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  674 TGETTLYTEVPTVPTEVTGVHT-EVTNVSPEETSVPTEETISTevttvspeeTTLPTEVPTVSTEVTNVSPEETSVPPEE 752
Cdd:pfam05109  587 TPNATSPTVGETSPQANTTNHTlGGTSSTPVVTSPPKNATSAV---------TTGQHNITSSSTSSMSLRPSSISETLSP 657

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  753 TILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSvpteetiSTEVTTVSPEETtlptevPTVSTEVTNVSPEETSVPPEET 832
Cdd:pfam05109  658 STSDNSTSHMPLLTSAHPTGGENITQVTPASTS-------THHVSTSSPAPR------PGTTSQASGPGNSSTSTKPGEV 724

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  833 ILTEITtvSPEETVFPIEGTTLPTEVLTVpievtTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPT---EVAT 909
Cdd:pfam05109  725 NVTKGT--PPKNATSPQAPSGQKTAVPTV-----TSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRtryNATT 797


                   ....*
gi 1907162178  910 VLPAS 914
Cdd:pfam05109  798 YLPPS 802
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 5094-5164 5.55e-12

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 63.94  E-value: 5.55e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162178 5094 CRVLVDpQGPFAACHQIIAPEPFEQRCMLDMCtgwKTKEEEELRCRVLSGYAIICQEAGANMTGWRDHTHC 5164
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMC---SCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1628-1682 8.33e-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: 8.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1628 CTSFQGRYFKLQEQWFNPDCKEICTCeSHNHILCKPWKCKAQEACSYKNGVLGCH 1682
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 595-912 1.07e-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: 71.14  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  595 TIPTEVITVSPEEIISPTEVTPVPTDVT----AAYVEATNASPEETsvpPEVTILTEVTT-------------VSPEETT 657
Cdd:pfam17823   46 AVPRADNKSSEQ*NFCAATAAPAPVTLTkgtsAAHLNSTEVTAEHT---PHGTDLSEPATregaadgaasralAAAASSS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  658 vPTEVPIVLIEATAFPTGE--TTLYTEVPTVPTEVTGVHTEVTNVSPEE-TSVPTEETISTEVTTVSPEETTLPTE--VP 732
Cdd:pfam17823  123 -PSSAAQSLPAAIAALPSEafSAPRAAACRANASAAPRAAIAAASAPHAaSPAPRTAASSTTAASSTTAASSAPTTaaSS 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  733 TVSTeVTNVSPEETSVPPEET-ILTTLYTEVPTVPTEVTGVHTEVTNVSPE-----ETSVPTEETISTEVTTVSPEETTl 806
Cdd:pfam17823  202 APAT-LTPARGISTAATATGHpAAGTALAAVGNSSPAAGTVTAAVGTVTPAalatlAAAAGTVASAAGTINMGDPHARR- 279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  807 PTEVPTVSTEVTNVSPEETSVPPEETILTEITT------VSPEETVFPIEGTTLPTEVLTVPIEVTTFPTgETTVPTEVP 880
Cdd:pfam17823  280 LSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTdqpvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVT-TTKAQAKEP 358

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1907162178  881 TVSTemtgVHTEVTTVFPE-ETSIPTEVATVLP 912
Cdd:pfam17823  359 SASP----VPVLHTSMIPEvEATSPTTQPSPLL 387
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1573-1626 2.34e-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: 2.34e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1573 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1626
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1573-1626 6.40e-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: 6.40e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1573 CPKNSRYSLCAKPCPETCHPISTTQHCSDKCVEGCECDPGFILS-GSECVPSSQC 1626
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1240-1293 1.64e-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: 1.64e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 1240 CPYNNKYYKPGEEWFTPNCTERCRClPGSLMECQISQCGTHTVCQLKSDQYQCE 1293
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
PHA03255 PHA03255
BDLF3; Provisional
 676-831 1.68e-10

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 64.54  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  676 ETTL-YTEVPTVPTEVTGVH--TEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPee 752
Cdd:PHA03255    19 ETSLiWTSSGSSTASAGNVTgtTAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTP-- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  753 tILTTLYTEVPTVPTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 827
Cdd:PHA03255    91 -VPTTSNASTINVTTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELPT 169


                   ....
gi 1907162178  828 PPEE 831
Cdd:PHA03255   170 VPDE 173
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1959-2013 1.49e-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: 1.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 1959 CPPRSSYNPCANSCPATCLTLSTPRDCPtLPCVEGCECQSGHILS-GTTCVPLRQC 2013
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP-EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 5168-5221 1.55e-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: 1.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 5168 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSDT-QSLPVTHC 5221
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4522-4580 3.33e-09

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 55.86  E-value: 3.33e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4522 CPAHSHYSKCLPPCQPSCSDPdghceGTSPEAPSTCEEGCVCEPDYVLSND-KCVPSSEC 4580
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1959-2013 5.32e-09

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 55.02  E-value: 5.32e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 1959 CPPRSSYNPCANSCPATCLTLSTPRDCpTLPCVEGCECQSGHILS-GTTCVPLRQC 2013
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPC-TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 5223-5276 7.02e-09

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 54.62  E-value: 7.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907162178 5223 CTADGIYYKLGDSFVTNDCSQHCTCaSQGILLCEPYGCRAGESCMVANFTRGCF 5276
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 699-1036 7.72e-09

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 61.90  E-value: 7.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  699 NVSPEetSVPTEETISTE-----VTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTT-------LYTEVPTVP 766
Cdd:pfam17823   41 NASGD--AVPRADNKSSEq*nfcAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDLSEPATregaadgAASRALAAA 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  767 TEVTGvhTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSpeeTSVPPEETILTEITTVSPEETV 846
Cdd:pfam17823  119 ASSSP--SSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAA---SPAPRTAASSTTAASSTTAASS 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  847 FPIEGTTlpTEVLTVpieVTTFPTGETTVPTEVPTVSTemtgVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTPTEV 926
Cdd:pfam17823  194 APTTAAS--SAPATL---TPARGISTAATATGHPAAGT----ALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVA 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  927 TTTPPEETTIPAEVTTIPPVSIPSEETTTPTEVTTTPPEETTIpAEVTTVPPV------SIPSEETTTPTEVTTTPPEET 1000
Cdd:pfam17823  265 SAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPI-IQVSTDQPVhntagePTPSPSNTTLEPNTPKSVAST 343

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1907162178 1001 TIPAEVTTVPPVSIPSeETTIPTEVTTVPPE-ETTIP 1036
Cdd:pfam17823  344 NLAVVTTTKAQAKEPS-ASPVPVLHTSMIPEvEATSP 379
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4522-4580 1.22e-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: 1.22e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4522 CPAHSHYSKCLPPCQPSCSDPDghcegTSPEAPSTCEEGCVCEPDYVLS-NDKCVPSSEC 4580
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 626-806 1.30e-08

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 61.98  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  626 VEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPtgettlytEVPTV---PTEVTGVHTEVTNVSP 702
Cdd:PRK10811   848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVV--------EEPVVvaePQPEEVVVVETTHPEV 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  703 EETSVPTEETISTEVTTVSPEETTLPTEvptvstEVTNVSPEETSVPPEETIlttlyTEVPTVPTEVTgVHTEVTNVSPE 782
Cdd:PRK10811   920 IAAPVTEQPQVITESDVAVAQEVAEHAE------PVVEPQDETADIEEAAET-----AEVVVAEPEVV-AQPAAPVVAEV 987

                          170       180
                   ....*....|....*....|....
gi 1907162178  783 ETSVPTEETISTEVTTVSPEETTL 806
Cdd:PRK10811   988 AAEVETVTAVEPEVAPAQVPEATV 1011
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3911-3969 2.63e-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: 2.63e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3911 CPAHSHFTSCLPSCPPSCANLDGSCEQTSPkvpstCKEGCLCQPGYFLNN-GKCVLQTHC 3969
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEP-----CVEGCVCPPGFVRNSgGKCVPPSDC 55
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 534-895 3.86e-08

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 60.32  E-value: 3.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  534 SESTVPTLPMEQPTSPTKATTV--TIEIPTTPTEEAtiptetttvptevinvSPKETSIPPEVTIPTEVITVSPEEIISP 611
Cdd:pfam05109  427 STTTSPTLNTTGFAAPNTTTGLpsSTHVPTNLTAPA----------------STGPTVSTADVTSPTPAGTTSGASPVTP 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  612 tevTPVP---------TDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTevpivliEATAFPTGETTLYTE 682
Cdd:pfam05109  491 ---SPSPrdngteskaPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPT-------SAVTTPTPNATSPTP 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  683 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTevtnvSPEETSVPPEETilttlyTEV 762
Cdd:pfam05109  561 AVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS-----TPVVTSPPKNAT------SAV 629

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  763 PTVPTEVTGVHTEVTNVSPEETSvpteETISTEVTTVSPEETTLPTEV-PTVSTEVTNVSPEETSVppeetilTEITTVS 841
Cdd:pfam05109  630 TTGQHNITSSSTSSMSLRPSSIS----ETLSPSTSDNSTSHMPLLTSAhPTGGENITQVTPASTST-------HHVSTSS 698

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  842 PEetvfPIEGT-------------TLPTEVLT---VPIEVTTFPTGETTVPTEVPTVSTemTGVHTEVTT 895
Cdd:pfam05109  699 PA----PRPGTtsqasgpgnsstsTKPGEVNVtkgTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTT 762
PHA03255 PHA03255
BDLF3; Provisional
 612-768 5.51e-08

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 57.22  E-value: 5.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  612 TEVTPVP---TDVTAAyVEATNASPEeTSVPPEVTILTEVTTVSPEETTV--PTEVPIVLIEATAFPTGETTLYTEVPTV 686
Cdd:PHA03255    25 TSSGSSTasaGNVTGT-TAVTTPSPS-ASGPSTNQSTTLTTTSAPITTTAilSTNTTTVTSTGTTVTPVPTTSNASTINV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  687 PTEVTG---VHTEV-TNVSPEETS-VPTEETISTEVTTVSPEETTLpteVPTVSTEVTNVSPEETSvppeetilttlytE 761
Cdd:PHA03255   103 TTKVTAqniTATEAgTGTSTGVTSnVTTRSSSTTSATTRITNATTL---APTLSSKGTSNATKTTA-------------E 166


                   ....*..
gi 1907162178  762 VPTVPTE 768
Cdd:PHA03255   167 LPTVPDE 173
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3911-3969 9.29e-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: 9.29e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3911 CPAHSHFTSCLPSCPPSCANLDgsceqTSPKVPSTCKEGCLCQPGYFLN-NGKCVLQTHC 3969
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4047-4105 1.53e-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: 1.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4047 CPAHSHFTSCLPSCPPSCSNLDGSCVEsnfkaPSVCKKGCICQPGYLLNND-KCVLRIQC 4105
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVC-----PEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 603-884 2.09e-07

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 58.00  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  603 VSPEEIISPTEVTPVPTDVTAAYVEATNASP---EETSVPPEVTIltEVTTVSPEETTVPTEVPIVLIEATafPTGETTL 679
Cdd:pfam05109  304 VFSDEIPASQDMPTNTTDITYVGDNATYSVPmvtSEDANSPNVTV--TAFWAWPNNTETDFKCKWTLTSGT--PSGCENI 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  680 ---YTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVS---PEETSVPpeeT 753
Cdd:pfam05109  380 sgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTtglPSSTHVP---T 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  754 ILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETI 833
Cdd:pfam05109  457 NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATS 536

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907162178  834 LTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVST 884
Cdd:pfam05109  537 PTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPT 587
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3078-3136 2.29e-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: 2.29e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3078 CPANSNFTSCLPSCQPSCSNTDVhcegsSPNALSSCREGCVCQSGYVLHND-KCILRNQC 3136
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2288-2354 2.34e-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: 2.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 2288 CQTALQGPAWAHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFC 2354
Cdd:pfam08742    2 CGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4047-4105 2.50e-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: 2.50e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4047 CPAHSHFTSCLPSCPPSCSNLD--GSCvesnfkaPSVCKKGCICQPGYLLN-NDKCVLRIQC 4105
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3078-3136 3.56e-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: 3.56e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3078 CPANSNFTSCLPSCQPSCSNTDvhcegSSPNALSSCREGCVCQSGYVLH-NDKCILRNQC 3136
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2358-2416 4.20e-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: 4.20e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2358 CPAHSHYTNCLPSCPPSCLDPD--SRCegsghkvPATCREGCICQPDYVL-LNDKCVLRSHC 2416
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 533-766 5.39e-07

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 56.59  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  533 PSESTVPtLPMEQpTSPTKAT-TVTIEIPTTPTEEATIPTETTtvpteviNVSPKETSIPPEVTIPTEVITVSPEEIISP 611
Cdd:PRK10811   820 PTQSPMP-LTVAC-ASPEMASgKVWIRYPVVRPQDVQVEEQRE-------AEEVQVQPVVAEVPVAAAVEPVVSAPVVEA 890

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  612 TEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVptevpivlieatafptgettlytevptVPTEVT 691
Cdd:PRK10811   891 VAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVA---------------------------VAQEVA 943

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178  692 GVHTEVTNVSPEETSVPTEETIsTEVTTVSPEETTLPTEVPTVSTEVTNVSP--EETSVPPEETILTTLYTEVPTVP 766
Cdd:PRK10811   944 EHAEPVVEPQDETADIEEAAET-AEVVVAEPEVVAQPAAPVVAEVAAEVETVtaVEPEVAPAQVPEATVEHNHATAP 1019
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3435-3493 6.10e-07

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 49.31  E-value: 6.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3435 CPAHTQYTSCLPSCLPSCLDPEGlckdiSPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3493
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSP-----PDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2838-2896 6.53e-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: 6.53e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2838 CPAHSHYTNCLPTCQPSCSDPDghcegSSTKAPSACKEGCVCEPDYVM-LNNKCVPRIEC 2896
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
rne PRK10811
ribonuclease E; Reviewed
 598-852 7.24e-07

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 56.20  E-value: 7.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  598 TEVITVSPEE-IISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTV--------SPEETTV---------- 658
Cdd:PRK10811   737 EEAVAPVVEEtVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENRDNNgmprrsrrSPRHLRVsgqrrrryrd 816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  659 ---PTEVPIVLIEATAFP---TGEttLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 732
Cdd:PRK10811   817 eryPTQSPMPLTVACASPemaSGK--VWIRYPVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEV 894

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  733 TVSTEVTNVSPEETSVPPEETilttlYTEVPTVP-TEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 811
Cdd:PRK10811   895 VEEPVVVAEPQPEEVVVVETT-----HPEVIAAPvTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVV 969

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907162178  812 TVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGT 852
Cdd:PRK10811   970 VAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEAT 1010
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2358-2416 7.56e-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: 7.56e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2358 CPAHSHYTNCLPSCPPSCLDPDSRCegsghKVPATCREGCICQPDYVLLND-KCVLRSHC 2416
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4282-4340 8.59e-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: 8.59e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4282 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVL-REDKCVLRTQC 4340
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2838-2896 8.59e-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: 8.59e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2838 CPAHSHYTNCLPTCQPSCSDPdghceGSSTKAPSACKEGCVCEPDYVMLNN-KCVPRIEC 2896
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4762-4820 8.68e-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: 8.68e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4762 CPANSLYTHCLPTCLPSCSNPDGRCegtshKAPSTCREGCVCQPGYLLNKD-TCVHKNQC 4820
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPD-----VCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4762-4820 8.76e-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: 8.76e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4762 CPANSLYTHCLPTCLPSCSNPD--GRCegtshkaPSTCREGCVCQPGYLLNKD-TCVHKNQC 4820
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNapPPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2478-2536 9.76e-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: 9.76e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2478 CPAHSKFTDCLPPCHPSCSDP--DGHCEGIstnahsnCKEGCVCQPGYVLRND-KCVLRIEC 2536
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLspPDVCPEP-------CVEGCVCPPGFVRNSGgKCVPPSDC 55
rne PRK10811
ribonuclease E; Reviewed
 642-913 1.08e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 55.43  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  642 VTILTEVTTvsPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSP-EETSVPTEETISTEVTTV 720
Cdd:PRK10811   729 VRIEQSVAE--EAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENrDNNGMPRRSRRSPRHLRV 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  721 S------------PEETTLPTEVPTVSTE-----------VTNVSPEET--SVPPEETILTTLYTEVPTVPTEVTGVHTE 775
Cdd:PRK10811   807 SgqrrrryrderyPTQSPMPLTVACASPEmasgkvwirypVVRPQDVQVeeQREAEEVQVQPVVAEVPVAAAVEPVVSAP 886

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  776 VTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEET-ILTEITTVSPEETVFPIEGTTl 854
Cdd:PRK10811   887 VVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAeHAEPVVEPQDETADIEEAAET- 965

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162178  855 pTEVLTVPIEVTTFPTGETTVPTEVPTV--STEMTGVHTEVTTVFPEETSIPTEVATVLPA 913
Cdd:PRK10811   966 -AEVVVAEPEVVAQPAAPVVAEVAAEVEtvTAVEPEVAPAQVPEATVEHNHATAPMTRAPA 1025
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3198-3256 1.20e-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: 1.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3198 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3256
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1189-1238 1.26e-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: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1189 CPPNAHIELC--ACPASCESPK--PSCQPPCIPGCVCNPGFLFS-NNQCINESSC 1238
Cdd:cd19941      1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2598-2656 1.30e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2598 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 2656
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
rne PRK10811
ribonuclease E; Reviewed
 594-768 1.37e-06

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 55.05  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  594 VTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASP-----EETSVPPEVTILTEVTTVSPEETTVPtevpivliE 668
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPvveavAEVVEEPVVVAEPQPEEVVVVETTHP--------E 918

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  669 ATAFPTGETTLYTEVPTVPtevtgVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVptVSTEVTNVSPEETSV 748
Cdd:PRK10811   919 VIAAPVTEQPQVITESDVA-----VAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVV--AQPAAPVVAEVAAEV 991

                          170       180
                   ....*....|....*....|
gi 1907162178  749 PPEETILTTLYTEVPTVPTE 768
Cdd:PRK10811   992 ETVTAVEPEVAPAQVPEATV 1011
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3198-3256 1.40e-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: 1.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3198 CPAHSHYTNCLPSCPPSCLDPEglcegTSPKVPSTCREGCICQPGYLMHKN-KCVLRIFC 3256
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4282-4340 1.42e-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: 1.42e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4282 CPAHSHYTTCLPSCLPSCFDPEglcgdASPRAPPTCREGCVCEADYVLRED-KCVLRTQC 4340
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3318-3373 1.62e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 48.15  E-value: 1.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 3318 CPTNSQFTDCLPSCVPSCSNrcEVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3373
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN--LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 5168-5212 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
                   ....*....|....*....|....*....|....*....|....*
gi 1907162178 5168 CPANTVYQRCMTPCPASCAKFVTPKVCEGPCVEGCASLPGYIYSD 5212
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNS 45
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3318-3373 2.08e-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: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907162178 3318 CPTNSQFTDCLPSCVPSCSNRceVTSPSVPSSCREGCLCNHGFVFSED-KCVPRTQC 3373
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANP--NAPPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3435-3493 2.36e-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: 2.36e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3435 CPAHTQYTSCLPSCLPSCLDPEglckdISPKVPSTCKEGCVCQSGYVLNSD-KCVLRAEC 3493
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2478-2536 2.79e-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: 2.79e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2478 CPAHSKFTDCLPPCHPSCSDPDghcegISTNAHSNCKEGCVCQPGYVL-RNDKCVLRIEC 2536
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2718-2776 2.84e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 2.84e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2718 CPDHSLYTHCLPSCLPSCSDPDglcrgTSPEAPSTCKEGCVCEPDYVLS-NDKCVLRIEC 2776
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4167-4225 3.53e-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: 3.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4167 CPAHSHYTNCLPACSRSCTDLdghceGTSPKVPSPCKEGCLCQPGYVVHNH-KCVLQIHC 4225
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1189-1238 5.93e-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: 5.93e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178 1189 CPPNAHIELC--ACPASCESPKPS--CQPPCIPGCVCNPGFLFSNN-QCINESSC 1238
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPPdvCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 526-880 6.05e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  526 PLLPPTGPSEST---VPTlPMEQPTSPTKATTVTIEIPTTPTEEAT----IPTETTTVPTEVINVSPKETSIP-PEVTIP 597
Cdd:PHA03247  2553 PPLPPAAPPAAPdrsVPP-PRPAPRPSEPAVTSRARRPDAPPQSARprapVDDRGDPRGPAPPSPLPPDTHAPdPPPPSP 2631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  598 TEVITVSPEEIISPTEVTPVPTDVTA-----------AYVEATNAS-----PEETSVPPEVTILTEVTTVSPEETTvPTE 661
Cdd:PHA03247  2632 SPAANEPDPHPPPTVPPPERPRDDPApgrvsrprrarRLGRAAQASsppqrPRRRAARPTVGSLTSLADPPPPPPT-PEP 2710

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  662 VPIVLIEATAFPTG---------ETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVP 732
Cdd:PHA03247  2711 APHALVSATPLPPGpaaarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  733 TVSTEVTNVSPEETS-----VPPEETILTTLYTEVPTVPTEvtgvhTEVTNVSPEETSVPTEETISTE------------ 795
Cdd:PHA03247  2791 LSESRESLPSPWDPAdppaaVLAPAAALPPAASPAGPLPPP-----TSAQPTAPPPPPGPPPPSLPLGgsvapggdvrrr 2865

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  796 ----------VTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTvSPEETVFPIEGTTLPTEVLT-VPIE 864
Cdd:PHA03247  2866 ppsrspaakpAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPqPPLA 2944

                          410
                   ....*....|....*.
gi 1907162178  865 VTTFPTGETTVPTEVP 880
Cdd:PHA03247  2945 PTTDPAGAGEPSGAVP 2960
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2718-2776 6.42e-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: 6.42e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2718 CPDHSLYTHCLPSCLPSCSDPdglcrGTSPEAPSTCKEGCVCEPDYVLSND-KCVLRIEC 2776
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANL-----SPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
610-902 7.36e-06

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 51.98  E-value: 7.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  610 SPTEVTPVPT-------DVTaayVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTE 682
Cdd:COG3291     36 TSTEANPSHTyttpgtyTVT---LTVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  683 VPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEV 762
Cdd:COG3291    113 GVATSTTTAAAPGGGGGTGTTTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTG 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  763 PTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSP 842
Cdd:COG3291    193 TIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVV 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  843 EETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETS 902
Cdd:COG3291    273 TTSAATGTSTNGTGGLGTTTAITPGNVSTTADVTGGTATLAVSSTLTTNDTTGSSSTGTV 332
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2958-3016 8.53e-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: 8.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2958 CPAHSHFTNCLPPCQPSCLDseghcEGSTTKAPSACQEGCVCEPDYVVLNN-KCVPRIEC 3016
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4642-4700 1.03e-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: 45.84  E-value: 1.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4642 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4700
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2298-2355 1.41e-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: 1.41e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162178  2298 AHCSSRVPIKPFLLKCMNSFCEFRELFRALCDSLQSFEDACQNQGLKPPIWRNSSFCP 2355
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2598-2656 1.68e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 45.00  E-value: 1.68e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 2598 CPAHSSFTNCLPPCQPSCSDPEghcggSTTKAPSACQEGCVCEPDYVV-LNNKCVPRIEC 2656
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 547-884 1.74e-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: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  547 TSPTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYV 626
Cdd:COG5492    195 VVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGSG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  627 EATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETS 706
Cdd:COG5492    275 STTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTS 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  707 V--PTEETISTEVtTVSPEETTLPTEVPTVS-TEVTNVSPEE--TSVPPEETILTtlYTevpTVPTEVTGVHT-EVTNVS 780
Cdd:COG5492    355 VtlAVGQTLTLTA-TVTPANATNKNVTWSSSdPSVATVDSNGlvTAVAAGTATIT--AT---TKDGGKTATCTvTVTAAG 428

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  781 PEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLT 860
Cdd:COG5492    429 STGTVVVVSLAATSAVSASVVLTPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTVTASVAEVATSVGGGATVTVT 508

                          330       340
                   ....*....|....*....|....
gi 1907162178  861 VPIEVTTFPTGETTVPTEVPTVST 884
Cdd:COG5492    509 VSTAATVTVTVGVKSTGIAVAGST 532
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4167-4225 2.15e-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: 2.15e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4167 CPAHSHYTNCLPACSRSCTDLDghcegTSPKVPSPCKEGCLCQPGYVVH-NHKCVLQIHC 4225
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4642-4700 2.37e-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: 2.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4642 CPAHSLYTNCLPSCLPSCSDPEglcggTSPEVPSTCKEGCFCQSGYVLHKN-KCMLRIHC 4700
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
PHA03255 PHA03255
BDLF3; Provisional
 751-906 2.64e-05

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 49.13  E-value: 2.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  751 EETILTTLYTEVPTVPTEVTGVhTEVTNVSPEETSVPTEETiSTEVTTVSPEETTlptevPTVSTEVTNVSPEETSVPPE 830
Cdd:PHA03255    19 ETSLIWTSSGSSTASAGNVTGT-TAVTTPSPSASGPSTNQS-TTLTTTSAPITTT-----AILSTNTTTVTSTGTTVTPV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  831 ETI----LTEITTVSPEETVFPIE---GTTLPT--EVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPeet 901
Cdd:PHA03255    92 PTTsnasTINVTTKVTAQNITATEagtGTSTGVtsNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAELP--- 168


                   ....*
gi 1907162178  902 SIPTE 906
Cdd:PHA03255   169 TVPDE 173
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2958-3016 2.91e-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: 2.91e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 2958 CPAHSHFTNCLPPCQPSC--LDSEGHCegsttkaPSACQEGCVCEPDYVV-LNNKCVPRIEC 3016
Cdd:cd19941      1 CPPNEVYSECGSACPPTCanPNAPPPC-------TKQCVEGCFCPEGYVRnSGGKCVPPSQC 55
YbbR COG4856
Cyclic di-AMP synthase regulator CdaR, YbbR domain [Signal transduction mechanisms];
610-879 3.71e-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: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  610 SPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILT----EVTTVSPEETTV----------PTEVPIVLIEATAFPTG 675
Cdd:COG4856     71 PRSVLLSLSASDIKAYVDLSGLKPGTHTVPVKVEGNLpsgvEVVEVSPSTITVtlekkvtkevPVEVEVKGKPAEGYEVG 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  676 ETTLytEVPTVptEVTGVHTEVTNVSPEETSVPTE---ETISTEVT-------------TVSPEETTLptEVPTVSTEVT 739
Cdd:COG4856    151 EVSV--SPSTV--TVSGPESVVNQIDSVKATVDVSgatEDFTKSVPvkaydangneldvTISPSTVEV--TVPVLPSKTV 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  740 NVSPEETSVPPEETILTTLYTEVPTVptEVTGVHTEVTNVSpeetSVPTE--------ETISTEVTTVSPEETTLPTEVP 811
Cdd:COG4856    225 PVKVNTTGEPAEGYSVTSITVSPSTV--TIYGPEEVLDSIS----SIETEpidlsgltESTTVEVKLKLPEGVTLVDPPS 298

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  812 TVstEVT-NVSPEETSVPPEETILTE------ITTVSPEETVFPIEGT-----TLPTEVLTVPIEVTTFPTGETTVPTEV 879
Cdd:COG4856    299 TV--TVTvEVEKKTTKTFENIPITVEnlpdglTASISPGTVDVTVSGPksvldSLTASDIKAYVDLSGLGPGEYTVPVQV 376
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 4402-4460 4.44e-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: 4.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 4402 CPAHSHHTYCLPSCIPSCSNvndrcESTSLQRPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4460
Cdd:pfam01826    1 CPANEVYSECGSACPPTCAN-----LSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3795-3853 4.94e-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: 4.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3795 CPTHSNYTDCLPFCLPSCLDPSalcggTSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3853
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
 508-845 5.71e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 5.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  508 LISHGPCRVLLQTEIPSSPLLP--PTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTPTEEATIPTEtttvptevinvsp 585
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPaaPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR------------- 2781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  586 keTSIPPEVTIPTEVITVSPeeiiSPTEVTPVPTDVTA-AYVEATNASPEETSVPPevtilTEVTTVSPEETTVPTEVPI 664
Cdd:PHA03247  2782 --RLTRPAVASLSESRESLP----SPWDPADPPAAVLApAAALPPAASPAGPLPPP-----TSAQPTAPPPPPGPPPPSL 2850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  665 VLIEATAfPTGETTLY-TEVPTVPTEVTGVHTEVTNVSPEETSVPTEetiSTEVTTVSPEETTLPtEVPTVSTEVTNVSP 743
Cdd:PHA03247  2851 PLGGSVA-PGGDVRRRpPSRSPAAKPAAPARPPVRRLARPAVSRSTE---SFALPPDQPERPPQP-QAPPPPQPQPQPPP 2925

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  744 EETSVPPEEtilTTLYTEVPTVPTEVTGVHTEVTNVSPE---------ETSVPTEETISTEVTTVSPEETTLP---TEVP 811
Cdd:PHA03247  2926 PPQPQPPPP---PPPRPQPPLAPTTDPAGAGEPSGAVPQpwlgalvpgRVAVPRFRVPQPAPSREAPASSTPPltgHSLS 3002

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1907162178  812 TVSTEVTNVSPEETSVPPEETILTeiTTVSPEET 845
Cdd:PHA03247  3003 RVSSWASSLALHEETDPPPVSLKQ--TLWPPDDT 3034
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2015-2070 6.15e-05

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 43.45  E-value: 6.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 2015 CSDQDGSYHLLGESWYTEKtCTTLCTCSaHSNITCSPTACKANHVCLRQEGLLRCA 2070
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 519-724 6.78e-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: 6.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  519 QTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTKATTVT-----------------------IEIPTTPTEEATIPTEttt 575
Cdd:pfam11596   12 ETDIPTTTTATTTPTGSGTITLISTGNSSVSTKAGSSItvagtsstgsdnddddddetdceTEIPTVPTGTTTIDPT--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  576 vptevinVSPKETSIPPEVTIPTEviTVSPEEIIsptevTPVPTDVTAAYVEATNaspeeTSVPPEVTILTEVTTVSPEE 655
Cdd:pfam11596   89 -------GNGTITGIPTASDTDDE--TDCETETD-----TVEPSIGTATTGVTTT-----TVISDGVTTTQTVTTVAPVP 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162178  656 TTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVhtEVTNVSPEETSVPTEETISTEVT-----TVSPEE 724
Cdd:pfam11596  150 TQTHTETETVTITYTGAGQTFTTYLTQSGEICDETVTY--TVTTTCPTTTVAQGGGVYTTTVTvitthTVYPED 221
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 588-915 7.26e-05

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


Pssm-ID: 444243 [Multi-domain]  Cd Length: 613  Bit Score: 49.30  E-value: 7.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  588 TSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLI 667
Cdd:COG5492    116 TATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNTVV 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  668 EATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETS 747
Cdd:COG5492    196 VTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGSGS 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  748 VPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSV 827
Cdd:COG5492    276 TTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPTSV 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  828 ppeetILTEITTVSPEETVFPIEGTTLP-------TEVLTVPIE--VTTFPTGETTVptevpTVSTEMTGVHTEVT-TVF 897
Cdd:COG5492    356 -----TLAVGQTLTLTATVTPANATNKNvtwsssdPSVATVDSNglVTAVAAGTATI-----TATTKDGGKTATCTvTVT 425

                          330
                   ....*....|....*...
gi 1907162178  898 PEETSIPTEVATVLPASI 915
Cdd:COG5492    426 AAGSTGTVVVVSLAATSA 443
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 4402-4460 9.83e-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: 9.83e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178 4402 CPAHSHHTYCLPSCIPSCSNVND--RCestslqrPSTCIEGCLCHSGFVFSKD-KCVPRTQC 4460
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAppPC-------TKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
Cu_amine_oxidN1 pfam07833
Copper amine oxidase N-terminal domain; Copper amine oxidases catalyze the oxidative ...
 1357-1418 1.25e-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: 1.25e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907162178 1357 KVVISLPETTVTMISGRHTL-IGDQEVTL---PAILSDDTYVGLsgRFVElrTTFGLRVRWDGDQQ 1418
Cdd:pfam07833   28 TVTITKGGTTIKLTIGSNTAtVNGQEITLdvpPVLINGRTYVPL--RFVA--EALGAKVDWDEATR 89
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3795-3853 1.50e-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: 1.50e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3795 CPTHSNYTDCLPFCLPSCLDPSAlcggtSPKGPSTCKEGCVCQPGYVLDKD-KCILKIEC 3853
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNA-----PPPCTKQCVEGCFCPEGYVRNSGgKCVPPSQC 55
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 587-803 1.67e-04

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


Pssm-ID: 371619 [Multi-domain]  Cd Length: 241  Bit Score: 46.61  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  587 ETSIPP---EVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNAS-----PEETSVPPEV-TILTEVTTVSPEETT 657
Cdd:pfam11596   12 ETDIPTtttATTTPTGSGTITLISTGNSSVSTKAGSSITVAGTSSTGSDnddddDDETDCETEIpTVPTGTTTIDPTGNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  658 VPTEVPIVlIEATAFPTGETTLYTEVPTVPTEVTGVHTEvtnvspeeTSVPTEETISTEVTTVSPEETTLPTEVPTVSTE 737
Cdd:pfam11596   92 TITGIPTA-SDTDDETDCETETDTVEPSIGTATTGVTTT--------TVISDGVTTTQTVTTVAPVPTQTHTETETVTIT 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162178  738 VTNVSpeetsvppeeTILTTLYTEVPTVPTEVTGVhtEVTNVSPEETSVPTEETISTEVT-----TVSPEE 803
Cdd:pfam11596  163 YTGAG----------QTFTTYLTQSGEICDETVTY--TVTTTCPTTTVAQGGGVYTTTVTvitthTVYPED 221
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 3555-3613 1.86e-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: 1.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3555 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLSNN-KCLLRNRC 3613
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS-----PPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 493-749 1.96e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  493 TRGTSTAFVVALNFILISHGPCRVLLQTEIPSSPLLPPTGPSESTVPTLPMEQPTSPTkatTVTIEIPTTPTEEATipte 572
Cdd:PTZ00449   686 SKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQ---PDDIEFFTPPEEERT---- 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  573 tttvpteVINVSPKETSIPPEVT--IPTEVITV---SPEEII----SPTEVTPVPTdvtaayveATNAS-PEETSVPPEV 642
Cdd:PTZ00449   759 -------FFHETPADTPLPDILAeeFKEEDIHAetgEPDEAMkrpdSPSEHEDKPP--------GDHPSlPKKRHRLDGL 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  643 TI-LTEVTTVSPEETTVPTEVPIVLIEATAFptGETTLYTEVPTVPTEVTG--VHTEVTNVSPEETSvPTEETISTEVTT 719
Cdd:PTZ00449   824 ALsTTDLESDAGRIAKDASGKIVKLKRSKSF--DDLTTVEEAEEMGAEARKivVDDDGTEADDEDTH-PPEEKHKSEVRR 900

                          250       260       270
                   ....*....|....*....|....*....|
gi 1907162178  720 VSPEETtlPTEVPTVSTEVTNVSPEETSVP 749
Cdd:PTZ00449   901 RRPPKK--PSKPKKPSKPKKPKKPDSAFIP 928
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 523-869 2.04e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.99  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  523 PSSPLLPPTGPSESTVPTLPMEQP---------TSPTKATTVTIEIPTTPTEEATIPTETttvptevinvspkeTSIPP- 592
Cdd:pfam05109  509 PTSAVTTPTPNATSPTPAVTTPTPnatsptlgkTSPTSAVTTPTPNATSPTPAVTTPTPN--------------ATIPTl 574

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  593 EVTIPTEVITVSPEEIISPT--EVTPvPTDVTAAYVEATNASPEETSVPPEVT--ILTEVTTVSPEETTVPTEVPIVLIE 668
Cdd:pfam05109  575 GKTSPTSAVTTPTPNATSPTvgETSP-QANTTNHTLGGTSSTPVVTSPPKNATsaVTTGQHNITSSSTSSMSLRPSSISE 653

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  669 aTAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSvpteetiSTEVTTVSPEETtlptevPTVSTEVTNVSPEETSV 748
Cdd:pfam05109  654 -TLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTS-------THHVSTSSPAPR------PGTTSQASGPGNSSTST 719

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  749 PPEETILTTlytevPTVPTEVTGVHTEvtnvSPEETSVPTEETISTEVTTVSPEETTLPTEVPTvSTEVTNVSPEETSVP 828
Cdd:pfam05109  720 KPGEVNVTK-----GTPPKNATSPQAP----SGQKTAVPTVTSTGGKANSTTGGKHTTGHGART-STEPTTDYGGDSTTP 789

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1907162178  829 PEETILTEITTVSPEETVFPIEGTTLP---TEVLTVPIEVTTFP 869
Cdd:pfam05109  790 RTRYNATTYLPPSTSSKLRPRWTFTSPpvtTAQATVPVPPTSQP 833
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 3555-3613 2.31e-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: 2.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178 3555 CPAHSLFTNCLPSCLPSCLDPDglckgASPKVPSSCKEGCICQSGYVLS-NNKCLLRNRC 3613
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPN-----APPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 550-910 3.02e-04

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


Pssm-ID: 444243 [Multi-domain]  Cd Length: 613  Bit Score: 47.38  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  550 TKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEAT 629
Cdd:COG5492    114 TGTATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTTASGSLNT 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  630 NASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPT 709
Cdd:COG5492    194 VVVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATSSASTLGS 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  710 EETISTEVTTVSPEETTLPTEV-----PTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEET 784
Cdd:COG5492    274 GSTTSTNTVTAGVGDTGVSVAVasssaATTSAVVGTLSSSGGGGGVVTAAATTGVTVVTASSVATTVDVVPVTGVTLNPT 353

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  785 SV--PTEETISTEVtTVSPEETTLPT--------EVPTVSTE--VTNVSPEETSVppeeTILTE------ITTVspeeTV 846
Cdd:COG5492    354 SVtlAVGQTLTLTA-TVTPANATNKNvtwsssdpSVATVDSNglVTAVAAGTATI----TATTKdggktaTCTV----TV 424

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162178  847 FPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPTEVATV 910
Cdd:COG5492    425 TAAGSTGTVVVVSLAATSAVSASVVLTPAGTVNAGASTASLNVNATDGVSTTVGVANVVSAVTV 488
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 681-900 5.41e-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: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  681 TEVPTVPTEVTgvhtevtnVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYT 760
Cdd:pfam11596   13 TDIPTTTTATT--------TPTGSGTITLISTGNSSVSTKAGSSITVAGTSSTGSDNDDDDDDETDCETEIPTVPTGTTT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  761 EVPTVPTEVTGVHT--EVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEIT 838
Cdd:pfam11596   85 IDPTGNGTITGIPTasDTDDETDCETETDTVEPSIGTATTGVTTTTVISDGVTTTQTVTTVAPVPTQTHTETETVTITYT 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907162178  839 TVSPEETVFPIEGTTLPTEVLTVPIeVTTFPTgeTTVPTEVPTVSTEMTGVHTEvtTVFPEE 900
Cdd:pfam11596  165 GAGQTFTTYLTQSGEICDETVTYTV-TTTCPT--TTVAQGGGVYTTTVTVITTH--TVYPED 221
rne PRK10811
ribonuclease E; Reviewed
 774-923 7.24e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 46.19  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  774 TEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEV-PTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGT 852
Cdd:PRK10811   848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSaPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQ 927

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162178  853 TLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEMTGVHTEVTTVFPEETSIPTEVATVLPASIPPEETTTP 923
Cdd:PRK10811   928 PQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
751-860 9.64e-04

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 45.61  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  751 EETILTTlyteVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVspEETSVPPE 830
Cdd:PRK11907    28 AEEIVTT----TPATSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETSDPTSEATDTTTS--EARTVTPA 101

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907162178  831 ETilteittvspeETVFPIEGTTLPTEVLT 860
Cdd:PRK11907   102 AT-----------ETSKPVEGQTVDVRILS 120
DUF3246 pfam11596
Protein of unknown function (DUF3246); This is a small family of fungal proteins one of whose ...
 729-910 1.19e-03

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


Pssm-ID: 371619 [Multi-domain]  Cd Length: 241  Bit Score: 44.30  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  729 TEVPTVSTEVTNVSPEETSvppeeTILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVsPEETTlpT 808
Cdd:pfam11596   13 TDIPTTTTATTTPTGSGTI-----TLISTGNSSVSTKAGSSITVAGTSSTGSDNDDDDDDETDCETEIPTV-PTGTT--T 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  809 EVPTVSTEVTNVsPEETSVPPEETILTEITTV--SPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEM 886
Cdd:pfam11596   85 IDPTGNGTITGI-PTASDTDDETDCETETDTVepSIGTATTGVTTTTVISDGVTTTQTVTTVAPVPTQTHTETETVTITY 163

                          170       180
                   ....*....|....*....|....
gi 1907162178  887 TGVHTEVTTVFPEETSIPTEVATV 910
Cdd:pfam11596  164 TGAGQTFTTYLTQSGEICDETVTY 187
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 600-910 1.22e-03

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


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 45.35  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  600 VITVSPE-EIISPTEVTPVPTDVTAAYVEATNASPEETSVPPEVTIltEVTTVSPEETTVPTEVPIVLIEATafptGETT 678
Cdd:COG4932    219 TETKAPEgYVLDTKDPTGATITVTVNAGGTVTVTLKNTPKYTKGSV--TVTKTDADTGEPLAGATFTLTDAD----GNTV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  679 LYTEVptVPTEVTGvHTEVTNVSP-----EETSVPT-----EETISTEVTTVSPEETTLPTE---VPTVSTEVTNVSPEE 745
Cdd:COG4932    293 VTTTV--TVTDADG-SYTFTDLPPgtytvTETKAPAgydldGEAVKVTITAGQTTTVTVTNGnneVKTGSVTLTKVDADD 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  746 TSVPPEE---TILTTLYTEVPTVPTEVTGVHTeVTNVSP-----EETSVPTEETISTEVT--TVSPEETTLPTEV----P 811
Cdd:COG4932    370 GEAPLAGaefTLTDADGTVVATITTDADGTAS-FKGLAPgtytlTETKAPEGYTLDSTPItvTVTDGGTGAIDTItnerK 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  812 TVSTEVTNVSP-----EETSVPPEETILTEITTVSPEETVFPIEGTTLPTEVLTVPIEVTTFPTGETTVPTEVPTVSTEM 886
Cdd:COG4932    449 KGSVQVTKVDAplagaTFTLTDADGTVVTLTTDADLAGATFEADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITDD 528

                          330       340
                   ....*....|....*....|....
gi 1907162178  887 TGVHTEVTTVFPEETSIPTEVATV 910
Cdd:COG4932    529 TDGTVGDEATGTDPEVTVTGKSTT 552
YjdB COG5492
Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction ...
 549-910 1.38e-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: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  549 PTKATTVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEA 628
Cdd:COG5492     27 STAGVTSSSVTANLSVLASNDTSTTSSVASVVSTAGSGGTANTSSTVAVSGAALAAGAVSTVGVDATTVAQTVATASLEA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  629 TNASPEETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVP 708
Cdd:COG5492    107 GGVSSTGTGTATTETVGTAATADAQIVKAASTGSGSVTAAVAVGSVGVASAGTSVTTTVATATSASLVSTLVVTSVGLTT 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  709 TEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPT 788
Cdd:COG5492    187 ASGSLNTVVVTSVVGNGATDASTASAVVAAVTAVTSAGSLTSAASVTTAGDDGTGVVATTVTTTISTSSSTTLTVTGATS 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  789 EETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTEITTVSPEETVFPIEGTTlptevltvpiEVTTF 868
Cdd:COG5492    267 SASTLGSGSTTSTNTVTAGVGDTGVSVAVASSSAATTSAVVGTLSSSGGGGGVVTAAATTGVTVV----------TASSV 336

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907162178  869 PTGETTVP-TEV---PTVSTEMTGVHTEVT-TVFPEE--------TSIPTEVATV 910
Cdd:COG5492    337 ATTVDVVPvTGVtlnPTSVTLAVGQTLTLTaTVTPANatnknvtwSSSDPSVATV 391
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
665-778 2.05e-03

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


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 44.84  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  665 VLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVspE 744
Cdd:PRK11907    17 LLTASNPKLAQAEEIVTTTPATSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETSDPTSEATDTTTS--E 94

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907162178  745 ETSVPPEETIlTTLYTEVPTVPTEV---TGVHTEVTN 778
Cdd:PRK11907    95 ARTVTPAATE-TSKPVEGQTVDVRIlstTDLHTNLVN 130
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
554-822 2.19e-03

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


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 43.89  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  554 TVTIEIPTTPTEEATIPTETTTVPTEVINVSPKETSIPPEVTIPTEVITVSPEEIISPTEVTPVPTDVTAAYVEATNASP 633
Cdd:COG3291     57 TVTDAAGCSDTTTKTITVGAPNPGVTTVTTSTTVTTLANTANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGTTTTT 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  634 EETSVPPEVTILTEVTTVSPEETTVPTEVPIVLIEATAFPTGETTLYTEVPTVPTEVTGVHTEVTNVSPEETSVPTEETI 713
Cdd:COG3291    137 GTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTSASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  714 STEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEETILTTLYTEVPTVPTEVTGVHTEVTNVSPeETSVPTEETIS 793
Cdd:COG3291    217 GTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTVTTSGANTAGTSTITGGTSGVVTTSAATGTSTNG-TGGLGTTTAIT 295

                          250       260
                   ....*....|....*....|....*....
gi 1907162178  794 TEVTTVSPEETTLPTEVPTVSTEVTNVSP 822
Cdd:COG3291    296 PGNVSTTADVTGGTATLAVSSTLTTNDTT 324
PHA03255 PHA03255
BDLF3; Provisional
 493-689 4.09e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.58  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  493 TRGTSTAfVVALnfILIshgpCRV-LLQTEIPSSPLlPPTGPSESTVPTLPMEQPTSPTKATTVTIEIPTTP-TEEATIP 570
Cdd:PHA03255     4 ARDKAGA-VLAM--ILI----CETsLIWTSSGSSTA-SAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPiTTTAILS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  571 TETTTVPTEVINVSPKETSipPEVTIPTEVITVSPEEIISPTEVTPVPTDVTaayveaTNASPEETSVPPEVTILTEVTT 650
Cdd:PHA03255    76 TNTTTVTSTGTTVTPVPTT--SNASTINVTTKVTAQNITATEAGTGTSTGVT------SNVTTRSSSTTSATTRITNATT 147

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907162178  651 VSPEETTVptevpivlieaTAFPTGETTlyTEVPTVPTE 689
Cdd:PHA03255   148 LAPTLSSK-----------GTSNATKTT--AELPTVPDE 173
COG1470 COG1470
Uncharacterized membrane protein [Function unknown];
705-914 5.76e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 441079 [Multi-domain]  Cd Length: 475  Bit Score: 42.92  E-value: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  705 TSVPTEETISTEVTTVSPEETTLPTEVPTVSTEVTNVSPEETSVPPEE--TILTTLYTEVPTVPTEVTgVHTEVTNVSPE 782
Cdd:COG1470      4 AGLVASSTVAAGALAALLDLTTPLVGSTVALTSTASALSGERTTLAALaaTGGLVTATPVSPTSATLT-LSVEVPSNATV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162178  783 ETSVPTEETISTEVTTVSPEETTL---PTEVPTVSTEVTNVSPEETSVPPE-ETILTEITTVSPEETVFPIEgttlPTEV 858
Cdd:COG1470     83 GTYLPITVTVAPYGLTLSVESPSLevaPGETVTYTVTLTNTGDEPDTVSLSaEGLPEGWTVTFTPDTSVSLA----PGES 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907162178  859 LTVPIEVT---TFPTGETTVPTEVPTVSTEMTGVhTEVTTVFPEETSIpteVATVLPAS 914
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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