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Conserved domains on  [gi|2499181|sp|Q28983|]
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RecName: Full=Zonadhesin; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 145-310 2.49e-52

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: 181.77  E-value: 2.49e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      145 SFPQCDFEDNahPFCDWVQASQDGGYWRQGNKNTFIqpAGPFGISLNGEGHYIFLETDKFSQaGQSFRLVSRPFCAPA-V 223
Cdd:smart00137    2 SPGNCDFEEG--STCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGNGHFMFFETSSGAE-GQTARLLSPPLYENRsT 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      224 ICVTFTYHMYGLGQGTkLRLLLGSPAGSPPSSLWERVGPQSPEWLNTSVTIPSgHQQPMQLIFEAVRGTNTAFVVALGFV 303
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 2499181      304 LINHGTC 310
Cdd:smart00137  155 LLSNGPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1186-1339 6.04e-52

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: 180.26  E-value: 6.04e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1186 CTVSGDPHYLTFDGALHHFTGTCTYTLTKPCWLRSlenSFLVSATNEFRGGNLEASYVRAVQVQVFNLRISLIKGRKVTL 1265
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1266 DGRRVALPLWPAQGRVSITSSG-SFILLYTDFGLQVRYDGDHLVEVTVPSSYAGRLCGLCGNYNNNSLDDILQPD 1339
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 801-953 7.77e-52

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: 179.87  E-value: 7.77e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     801 CSVYGDPHYLTFDGRRFNFMGKCTYILAQPCGNLTEHFFRVLVKKEERGQEGVsCLSKVYVTLPESTVTLLKGRHTLVGG 880
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     881 QRVTLPAIPSRG-VFLAPSGR-FVELQTAFGLRVRWDGDQQLFVSVPSTFSGKLCGLCGDYDGDSSNDNQKPDGS 953
Cdd:pfam00094   80 QKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1970-2124 1.94e-44

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: 158.69  E-value: 1.94e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1970 CSVFGDPHYRTFDGLSYRFQGRMTYTLVKTLDVLPDgvePLVVEGRNKVYPSLTPVFLQEIIVMVYGYTVQLQAELELVV 2049
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181    2050 NGQKVSIPYKPNE-YLQVTLRGR-RLYLVTDFELVVSFNGRNNAVIAMPSTYLGLVRGLCGNYDKNKRNDFMLPNGS 2124
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1575-1727 9.52e-44

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: 156.76  E-value: 9.52e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1575 CRIPDTSHYVSFDGSYHAVRGNCTYVLVKICHSTMDlpfFKISGENGKREGQPPAFYLRQVYVDIFNTLVTL-KQDQVLI 1653
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLqKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1654 NGTRVSLPATTQIRGVRVISRDGYTV-LTINIGVQVKFDGRGFLEVEIPKAYYGRTCGVCGNFNDEEEDELMMPS 1727
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 992-1067 9.73e-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: 88.17  E-value: 9.73e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499181      992 TMSGPEFCGQLVAPHGVFEACLPHLRASSFFKSCTFDMCNFQGLQHMLCAHMSALTENCQDAGYTVKPWRGPQFCP 1067
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1386-1453 1.29e-20

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 87.78  E-value: 1.29e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181     1386 CDVLMNPQGPFSQCHRVVAPQSSFSSCLYGQCATKGDTLTLCRSLQAYASLCARAGQALT-WRNGTFCP 1453
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2180-2254 1.32e-20

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 87.78  E-value: 1.32e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     2180 TQACGVLVDPQGPFAACHQIVAPGPFQEHCVFDLCAAPGPKEQEelrCQVLSGYAIICQESGPTLAGWRDHTHCA 2254
Cdd:smart00832    5 CSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECL---CDALAAYAAACAEAGVCISPWRTPTFCP 76
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 9-141 1.37e-17

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: 82.04  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     9 GPMAMPHPPLIPSTPTllafsfPGGFYMLLDPKNAKPRQRSALLSPLI---QSSGClsLSFQYTQRGQASGaTLMVYASV 85
Cdd:cd06263   25 GSTPSPGTPPDHTHGT------GSGHYLYVESSSGREGQKARLLSPLLpppRSSHC--LSFWYHMYGSGVG-TLNVYVRE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181    86 LGSIRKHTLF--SGQPGPSWQPVSVNY-TSQGQIQFTLVGVFGKIPEPAVAVDAISIAP 141
Cdd:cd06263   96 EGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 741-794 1.29e-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: 1.29e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2499181     741 CFYNDNYYKLGTDWFSPNCTEHCHCrPSSRMECQTFKCGTHTVCQLKNGQYGCH 794
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1909-1963 2.52e-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: 69.25  E-value: 2.52e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1909 CRDARGTFLPVGRFRLSSGCSQMCVCTAGAIECRPFTCPSGSQCEPNeDGKDFCQ 1963
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1513-1568 1.69e-13

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: 66.94  E-value: 1.69e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2499181    1513 CTTQRGSYHPVGESWYTDNsCSRLCTCSaHNNISCRQASCKPSQMCWPQDGLIRCR 1568
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1070-1123 6.37e-13

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: 65.42  E-value: 6.37e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181  1070 CPRNSRYTLCARLCPDTCHSEFSGRACKDRCVEGCECDPGFVLS-GLQCVSRSEC 1123
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1780-1847 4.74e-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: 63.17  E-value: 4.74e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181    1780 QCQAAFQAPAWANCATRVVLSPYVRSCTHKLCEFGGLNRAFCESLQAFGAACQAQGIKPPVWRNSSFC 1847
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1456-1511 8.91e-12

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


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 62.02  E-value: 8.91e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181    1456 CPSGSSYSTCANPCPATCLSLNNPSYCPstLPCAEGCECQKGHILS-GTSCVPLSQC 1511
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP--EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 311-580 1.14e-11

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 70.49  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    311 RGPSETSVSTEKPVAPTEkpTVPSEIytipTEKPMVHME-KPI---VHTEKPTVP--TEKPTIPTE----KSTVPTKKPT 380
Cdd:PTZ00449  534 HEDSKESDEPKEGGKPGE--TKEGEV----GKKPGPAKEhKPSkipTLSKKPEFPkdPKHPKDPEEpkkpKRPRSAQRPT 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    381 VFKEPTLP-----------PEGPT-----VPAERPTTP--PEGPAV-----PPKGPTVLTEwPT-------SHTEKSTVH 430
Cdd:PTZ00449  608 RPKSPKLPelldipkspkrPESPKspkrpPPPQRPSSPerPEGPKIikspkPPKSPKPPFD-PKfkekfydDYLDAAAKS 686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    431 TE-KPILPTGKSTIPTEKPMVPTKRTTTPTERTTIPAEKPTVPiEKPMVPTERttiPTERTTIPTEKPTVPTEKLTVPTE 509
Cdd:PTZ00449  687 KEtKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDE-EFPFEPIGD---PDAEQPDDIEFFTPPEEERTFFHE 762

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2499181    510 KPiVPTEKPIVPTEKhtIPTEKLTvltertttpterttIPTEKPTVPTEKPSVPTE-KPTVPTEEPTIPTEK 580
Cdd:PTZ00449  763 TP-ADTPLPDILAEE--FKEEDIH--------------AETGEPDEAMKRPDSPSEhEDKPPGDHPSLPKKR 817
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2257-2310 3.36e-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: 3.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    2257 CPANTVYQSCMTPCPASCATLAVPRACDGPCVEGCASLPGYIYS-GAQSLPMAHC 2310
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1851-1907 3.13e-10

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 57.71  E-value: 3.13e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181  1851 CSAHSVYTSCVPSCLPSCQDPEGQ--CTgagapSTCEEGCICEPGYVLSEQ-QCVARSQC 1907
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPppCT-----KQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2312-2365 5.69e-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: 56.93  E-value: 5.69e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2499181    2312 CTNNGVYYQQGDSFVTENCSQRCTCaSSGVLLCEPLSCRPGEICTLGNLTRGCF 2365
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 690-739 6.06e-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: 53.93  E-value: 6.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     690 CPPNAHFERC--ACPVSCQSPTP--NCELFCKPGCVCDPGFLFS-GSHCVNASSC 739
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPpdVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 1125-1179 5.78e-08

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 51.15  E-value: 5.78e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1125 CLDSTAGYVKVGERWFKPGCRQLCICEGNNrTRCVLWRCQAQEFCGQQDGIYGCH 1179
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2370-2399 8.10e-05

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


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.60  E-value: 8.10e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2499181    2370 CLQNPCQNDGRCREQGTHFTCECELGYGGD 2399
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 145-310 2.49e-52

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: 181.77  E-value: 2.49e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      145 SFPQCDFEDNahPFCDWVQASQDGGYWRQGNKNTFIqpAGPFGISLNGEGHYIFLETDKFSQaGQSFRLVSRPFCAPA-V 223
Cdd:smart00137    2 SPGNCDFEEG--STCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGNGHFMFFETSSGAE-GQTARLLSPPLYENRsT 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      224 ICVTFTYHMYGLGQGTkLRLLLGSPAGSPPSSLWERVGPQSPEWLNTSVTIPSgHQQPMQLIFEAVRGTNTAFVVALGFV 303
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 2499181      304 LINHGTC 310
Cdd:smart00137  155 LLSNGPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1186-1339 6.04e-52

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: 180.26  E-value: 6.04e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1186 CTVSGDPHYLTFDGALHHFTGTCTYTLTKPCWLRSlenSFLVSATNEFRGGNLEASYVRAVQVQVFNLRISLIKGRKVTL 1265
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1266 DGRRVALPLWPAQGRVSITSSG-SFILLYTDFGLQVRYDGDHLVEVTVPSSYAGRLCGLCGNYNNNSLDDILQPD 1339
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 801-953 7.77e-52

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: 179.87  E-value: 7.77e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     801 CSVYGDPHYLTFDGRRFNFMGKCTYILAQPCGNLTEHFFRVLVKKEERGQEGVsCLSKVYVTLPESTVTLLKGRHTLVGG 880
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     881 QRVTLPAIPSRG-VFLAPSGR-FVELQTAFGLRVRWDGDQQLFVSVPSTFSGKLCGLCGDYDGDSSNDNQKPDGS 953
Cdd:pfam00094   80 QKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 149-311 3.31e-45

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: 161.38  E-value: 3.31e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     149 CDFEDNAhpFCDWVQASQDGGYWRQGNKntFIQPAGPFGIS--LNGEGHYIFLETDKFsQAGQSFRLVSRPFCAPA-VIC 225
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSG--PSVKTGPSSDHtqGTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     226 VTFTYHMYGLGQGTkLRLLLGSPAGSPPSSLWERVGPQSPEWLNTSVTIPSGhQQPMQLIFEAVRGTNTAFVVALGFVLI 305
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 2499181     306 NHGTCR 311
Cdd:pfam00629  154 SSGPCP 159
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1178-1339 8.26e-45

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: 160.26  E-value: 8.26e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1178 CHAQGSATCTVSGDPHYLTFDGALHHFTGTCTYTLTKPCwlrSLENSFLVSATNEFRGGNleASYVRAVQVQVFNLRISL 1257
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1258 IK-GRKVTLDGRRVALPLWPAQGRVSITSSGSFILLYTDFGL-QVRYDGDHLVEVTVPSSYAGRLCGLCGNYNNNSLDDI 1335
Cdd:smart00216   79 KDdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....
gi 2499181     1336 LQPD 1339
Cdd:smart00216  159 RTPD 162
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 793-952 1.38e-44

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: 159.49  E-value: 1.38e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      793 CHPYGSaTCSVYGDPHYLTFDGRRFNFMGKCTYILAQPCGnlTEHFFRVLVKKEERGQeGVSCLSKVYVTLPESTVTLLK 872
Cdd:smart00216    5 QEECSP-TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS--SEPTFSVLLKNVPCGG-GATCLKSVKVELNGDEIELKD 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      873 GRHT-LVGGQRVTLPAIPSRGVFLA-PSGRFVELQTAFGL-RVRWDGDQQLFVSVPSTFSGKLCGLCGDYDGDSSNDNQK 949
Cdd:smart00216   81 DNGKvTVNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRT 160


                    ...
gi 2499181      950 PDG 952
Cdd:smart00216  161 PDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1970-2124 1.94e-44

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: 158.69  E-value: 1.94e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1970 CSVFGDPHYRTFDGLSYRFQGRMTYTLVKTLDVLPDgvePLVVEGRNKVYPSLTPVFLQEIIVMVYGYTVQLQAELELVV 2049
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181    2050 NGQKVSIPYKPNE-YLQVTLRGR-RLYLVTDFELVVSFNGRNNAVIAMPSTYLGLVRGLCGNYDKNKRNDFMLPNGS 2124
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1575-1727 9.52e-44

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: 156.76  E-value: 9.52e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1575 CRIPDTSHYVSFDGSYHAVRGNCTYVLVKICHSTMDlpfFKISGENGKREGQPPAFYLRQVYVDIFNTLVTL-KQDQVLI 1653
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLqKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1654 NGTRVSLPATTQIRGVRVISRDGYTV-LTINIGVQVKFDGRGFLEVEIPKAYYGRTCGVCGNFNDEEEDELMMPS 1727
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1573-1727 4.22e-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: 144.08  E-value: 4.22e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1573 GVCRIPDTSHYVSFDGSYHAVRGNCTYVLVKICHSTmdlPFFKISGENGKREGQPpaFYLRQVYVDIFNTLVTLKQDQ-- 1650
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIELKDDNgk 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181     1651 VLINGTRVSLPATTQIRGVRVISRDGYTVLTINIGV-QVKFDGRGFLEVEIPKAYYGRTCGVCGNFNDEEEDELMMPS 1727
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1970-2123 3.91e-38

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: 141.00  E-value: 3.91e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1970 CSVFGDPHYRTFDGLSYRFQGRMTYTLVKTLDVLPDgvepLVVEGRNKVYPSlTPVFLQEIIVMVYGYTVQL-QAELELV 2048
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGG-GATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181     2049 VNGQKVSIPYKPNEY-LQVTLRGRRLYLVTDFELV-VSFNGRNNAVIAMPSTYLGLVRGLCGNYDKNKRNDFMLPNG 2123
Cdd:smart00216   87 VNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 149-310 4.72e-38

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: 140.59  E-value: 4.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181   149 CDFEDnahPFCDWVQASQDGGYWRQGNKNTFIQPAGPFGISLNGEGHYIFLETDkFSQAGQSFRLVSRPFCAPA-VICVT 227
Cdd:cd06263    1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESS-SGREGQKARLLSPLLPPPRsSHCLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181   228 FTYHMYGLGQGTkLRLLLGSPAGSPPSSLWERVGPQSPEWLNTSVTIPSGHqQPMQLIFEAVRGTNTAFVVALGFVLINH 307
Cdd:cd06263   77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                 ...
gi 2499181   308 GTC 310
Cdd:cd06263  155 GPC 157
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 992-1067 9.73e-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: 88.17  E-value: 9.73e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499181      992 TMSGPEFCGQLVAPHGVFEACLPHLRASSFFKSCTFDMCNFQGLQHMLCAHMSALTENCQDAGYTVKPWRGPQFCP 1067
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1386-1453 1.29e-20

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 87.78  E-value: 1.29e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181     1386 CDVLMNPQGPFSQCHRVVAPQSSFSSCLYGQCATKGDTLTLCRSLQAYASLCARAGQALT-WRNGTFCP 1453
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2180-2254 1.32e-20

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 87.78  E-value: 1.32e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     2180 TQACGVLVDPQGPFAACHQIVAPGPFQEHCVFDLCAAPGPKEQEelrCQVLSGYAIICQESGPTLAGWRDHTHCA 2254
Cdd:smart00832    5 CSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECL---CDALAAYAAACAEAGVCISPWRTPTFCP 76
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 9-141 1.37e-17

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: 82.04  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     9 GPMAMPHPPLIPSTPTllafsfPGGFYMLLDPKNAKPRQRSALLSPLI---QSSGClsLSFQYTQRGQASGaTLMVYASV 85
Cdd:cd06263   25 GSTPSPGTPPDHTHGT------GSGHYLYVESSSGREGQKARLLSPLLpppRSSHC--LSFWYHMYGSGVG-TLNVYVRE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181    86 LGSIRKHTLF--SGQPGPSWQPVSVNY-TSQGQIQFTLVGVFGKIPEPAVAVDAISIAP 141
Cdd:cd06263   96 EGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1386-1452 3.58e-17

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: 77.81  E-value: 3.58e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181    1386 CDVLMNpQGPFSQCHRVVAPQSSFSSCLYGQCATKGDTLTLCRSLQAYASLCARAGQALT-WRNGTFC 1452
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2183-2253 4.65e-17

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: 77.42  E-value: 4.65e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2499181    2183 CGVLVDpQGPFAACHQIVAPGPFQEHCVFDLCAAPGpkeQEELRCQVLSGYAIICQESGPTLAGWRDHTHC 2253
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGG---DDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 741-794 1.29e-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: 1.29e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2499181     741 CFYNDNYYKLGTDWFSPNCTEHCHCrPSSRMECQTFKCGTHTVCQLKNGQYGCH 794
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 998-1066 8.41e-15

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: 70.87  E-value: 8.41e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181     998 FCGQLVApHGVFEACLPHLRASSFFKSCTFDMCNFQGLQHMLCAHMSALTENCQDAGYTVKPWRGPQFC 1066
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 31-142 2.41e-14

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: 72.78  E-value: 2.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      31 PGGFYMLLDPKNAKPRQRSALLSPLIQ---SSGClsLSFQYTQRGQASGaTLMVYASVLGSIRKHTLFS--GQPGPSWQP 105
Cdd:pfam00629   42 GSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC--LRFWYHMSGSGVG-TLRVYVRENGGTLDTLLWSisGDQGPSWKE 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2499181     106 VSVNYTS-QGQIQFTLVGVFGKIPEPAVAVDAISIA--PC 142
Cdd:pfam00629  119 ARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSsgPC 158
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1909-1963 2.52e-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: 69.25  E-value: 2.52e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1909 CRDARGTFLPVGRFRLSSGCSQMCVCTAGAIECRPFTCPSGSQCEPNeDGKDFCQ 1963
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1513-1568 1.69e-13

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: 66.94  E-value: 1.69e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2499181    1513 CTTQRGSYHPVGESWYTDNsCSRLCTCSaHNNISCRQASCKPSQMCWPQDGLIRCR 1568
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1070-1123 6.37e-13

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: 65.42  E-value: 6.37e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181  1070 CPRNSRYTLCARLCPDTCHSEFSGRACKDRCVEGCECDPGFVLS-GLQCVSRSEC 1123
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1780-1847 4.74e-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: 63.17  E-value: 4.74e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181    1780 QCQAAFQAPAWANCATRVVLSPYVRSCTHKLCEFGGLNRAFCESLQAFGAACQAQGIKPPVWRNSSFC 1847
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1456-1511 8.91e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 62.02  E-value: 8.91e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181    1456 CPSGSSYSTCANPCPATCLSLNNPSYCPstLPCAEGCECQKGHILS-GTSCVPLSQC 1511
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP--EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 311-580 1.14e-11

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 70.49  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    311 RGPSETSVSTEKPVAPTEkpTVPSEIytipTEKPMVHME-KPI---VHTEKPTVP--TEKPTIPTE----KSTVPTKKPT 380
Cdd:PTZ00449  534 HEDSKESDEPKEGGKPGE--TKEGEV----GKKPGPAKEhKPSkipTLSKKPEFPkdPKHPKDPEEpkkpKRPRSAQRPT 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    381 VFKEPTLP-----------PEGPT-----VPAERPTTP--PEGPAV-----PPKGPTVLTEwPT-------SHTEKSTVH 430
Cdd:PTZ00449  608 RPKSPKLPelldipkspkrPESPKspkrpPPPQRPSSPerPEGPKIikspkPPKSPKPPFD-PKfkekfydDYLDAAAKS 686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    431 TE-KPILPTGKSTIPTEKPMVPTKRTTTPTERTTIPAEKPTVPiEKPMVPTERttiPTERTTIPTEKPTVPTEKLTVPTE 509
Cdd:PTZ00449  687 KEtKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDE-EFPFEPIGD---PDAEQPDDIEFFTPPEEERTFFHE 762

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2499181    510 KPiVPTEKPIVPTEKhtIPTEKLTvltertttpterttIPTEKPTVPTEKPSVPTE-KPTVPTEEPTIPTEK 580
Cdd:PTZ00449  763 TP-ADTPLPDILAEE--FKEEDIH--------------AETGEPDEAMKRPDSPSEhEDKPPGDHPSLPKKR 817
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1456-1511 1.82e-11

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 61.18  E-value: 1.82e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181  1456 CPSGSSYSTCANPCPATCLSLNNPSYCpsTLPCAEGCECQKGHILS-GTSCVPLSQC 1511
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPPPC--TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1070-1123 2.28e-11

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 60.86  E-value: 2.28e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1070 CPRNSRYTLCARLCPDTCHSEFSGRACKDRCVEGCECDPGFVLSGL-QCVSRSEC 1123
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2257-2310 3.36e-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: 3.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    2257 CPANTVYQSCMTPCPASCATLAVPRACDGPCVEGCASLPGYIYS-GAQSLPMAHC 2310
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1851-1907 3.13e-10

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 57.71  E-value: 3.13e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181  1851 CSAHSVYTSCVPSCLPSCQDPEGQ--CTgagapSTCEEGCICEPGYVLSEQ-QCVARSQC 1907
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPppCT-----KQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1851-1907 3.77e-10

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 57.40  E-value: 3.77e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181    1851 CSAHSVYTSCVPSCLPSCQDPEgqcTGAGAPSTCEEGCICEPGYVLS-EQQCVARSQC 1907
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS---PPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2312-2365 5.69e-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: 56.93  E-value: 5.69e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2499181    2312 CTNNGVYYQQGDSFVTENCSQRCTCaSSGVLLCEPLSCRPGEICTLGNLTRGCF 2365
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1791-1848 1.31e-09

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: 56.58  E-value: 1.31e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181     1791 ANCATRVVLSPYVRSCTHKLCEFGGLNRAFCESLQAFGAACQAQGIKPPVWRNSSFCP 1848
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2257-2300 1.33e-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: 55.79  E-value: 1.33e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 2499181  2257 CPANTVYQSCMTPCPASCATLAVPRACDGPCVEGCASLPGYIYS 2300
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRN 44
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 341-527 2.33e-09

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: 63.01  E-value: 2.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     341 TEKPMVHMEKPIVHTEKPTVPTEKPTIPTEKSTVP--TKKPTVFKEPTlpPEGPTVPAERPTTPPegPAVPPKGPTVLTE 418
Cdd:pfam05109  415 TTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPssTHVPTNLTAPA--STGPTVSTADVTSPT--PAGTTSGASPVTP 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     419 WPT-------SHTEKSTVHTEKPILPTGKSTIPTEKPMVPTKRTTTPTERTTIPAEKPTVPIEKPMVPTERTTIPTERTT 491
Cdd:pfam05109  491 SPSprdngteSKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNAT 570

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2499181     492 IPTEKPTVPTEKLTVPTEKPIVPT---EKPIVPTEKHTI 527
Cdd:pfam05109  571 IPTLGKTSPTSAVTTPTPNATSPTvgeTSPQANTTNHTL 609
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 690-739 6.06e-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: 53.93  E-value: 6.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     690 CPPNAHFERC--ACPVSCQSPTP--NCELFCKPGCVCDPGFLFS-GSHCVNASSC 739
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPpdVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 690-739 6.49e-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: 53.86  E-value: 6.49e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181   690 CPPNAHFERC--ACPVSCQSPT--PNCELFCKPGCVCDPGFLFS-GSHCVNASSC 739
Cdd:cd19941    1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2312-2375 8.40e-09

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 54.11  E-value: 8.40e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2499181     2312 CTNNGVYYQQGDSFVtENCsQRCTCASSGVlLCEPLSCRPGEiCTLGNLTRGCFRDSP-------CLQNPC 2375
Cdd:smart00215    1 CWNNGSYYPPGAKWD-DDC-NRCTCLNGRV-SCTKVWCGPKP-CLLHNLSGECPLGQGcvpslsdCLSSPC 67
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1125-1179 5.78e-08

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 51.15  E-value: 5.78e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1125 CLDSTAGYVKVGERWFKPGCRQLCICEGNNrTRCVLWRCQAQEFCGQQDGIYGCH 1179
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 341-572 1.45e-06

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 53.62  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    341 TEKPMVhmeKPIVHTEKPTVPTEkPTIPTEKSTVPTKKPTVFKEPTLPPEGPTVPAErpttpPEGPAvPPKGPTVLTEWP 420
Cdd:NF033839  283 TPKEPG---NKKPSAPKPGMQPS-PQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQ-----PEKPK-PEVKPQLETPKP 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    421 TSHTEKSTVHTE-KPILPTGKSTIP----TEKPMVPTKRTTTPterttiPAEKPTVPIEKPMVPTERTT-----IPTERT 490
Cdd:NF033839  353 EVKPQPEKPKPEvKPQPEKPKPEVKpqpeTPKPEVKPQPEKPK------PEVKPQPEKPKPEVKPQPEKpkpevKPQPEK 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    491 TIPTEKPTVPTEKltvPTEKPIVPTEKPIVPTEKHTIPTEkltvLTERTTTPTERTTIPTEKPTVPTEKPSVPTEKPTVP 570
Cdd:NF033839  427 PKPEVKPQPEKPK---PEVKPQPEKPKPEVKPQPETPKPE----VKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTP 499


                  ..
gi 2499181    571 TE 572
Cdd:NF033839  500 NN 501
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 329-579 6.31e-06

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 51.69  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    329 KPTVPSEIYTIPTEKPMVHMEKPIVHTEKPTVPTEKPTIPTEkstvpTKKPTVFKEPTLPPEGPTVPAERPTTPPEGPAV 408
Cdd:NF033839  241 KKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQD-----TPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    409 PPKgPTVLTEWPTSHTEKSTvHTEKPiLPTGKSTIPTEKPMVPTKRTTTPterttiPAEKPTVPIEKPMVPTE-RTTIPT 487
Cdd:NF033839  316 TPK-PEVKPQLEKPKPEVKP-QPEKP-KPEVKPQLETPKPEVKPQPEKPK------PEVKPQPEKPKPEVKPQpETPKPE 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    488 ERTTIPTEKPTV-PTEKLTVPTEKPIVPTEKPIVPTEKHTiPTEKLtvltertttpterttipteKPTVPTEKPSVpteK 566
Cdd:NF033839  387 VKPQPEKPKPEVkPQPEKPKPEVKPQPEKPKPEVKPQPEK-PKPEV-------------------KPQPEKPKPEV---K 443

                         250
                  ....*....|...
gi 2499181    567 PTVPTEEPTIPTE 579
Cdd:NF033839  444 PQPEKPKPEVKPQ 456
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2370-2399 8.10e-05

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.60  E-value: 8.10e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2499181    2370 CLQNPCQNDGRCREQGTHFTCECELGYGGD 2399
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2373-2402 7.67e-03

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 7.67e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 2499181  2373 NPCQNDGRCREQGTHFTCECELGYGGDLCT 2402
Cdd:cd00054    9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 145-310 2.49e-52

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: 181.77  E-value: 2.49e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      145 SFPQCDFEDNahPFCDWVQASQDGGYWRQGNKNTFIqpAGPFGISLNGEGHYIFLETDKFSQaGQSFRLVSRPFCAPA-V 223
Cdd:smart00137    2 SPGNCDFEEG--STCGWHQDSNDDGHWERVSSATGI--PGPNRDHTTGNGHFMFFETSSGAE-GQTARLLSPPLYENRsT 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      224 ICVTFTYHMYGLGQGTkLRLLLGSPAGSPPSSLWERVGPQSPEWLNTSVTIPSgHQQPMQLIFEAVRGTNTAFVVALGFV 303
Cdd:smart00137   77 HCLTFWYYMYGSGSGT-LNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGKGHSGYIALDDI 154


                    ....*..
gi 2499181      304 LINHGTC 310
Cdd:smart00137  155 LLSNGPC 161
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1186-1339 6.04e-52

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: 180.26  E-value: 6.04e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1186 CTVSGDPHYLTFDGALHHFTGTCTYTLTKPCWLRSlenSFLVSATNEFRGGNLEASYVRAVQVQVFNLRISLIKGRKVTL 1265
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEP---DFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1266 DGRRVALPLWPAQGRVSITSSG-SFILLYTDFGLQVRYDGDHLVEVTVPSSYAGRLCGLCGNYNNNSLDDILQPD 1339
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 801-953 7.77e-52

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: 179.87  E-value: 7.77e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     801 CSVYGDPHYLTFDGRRFNFMGKCTYILAQPCGNLTEHFFRVLVKKEERGQEGVsCLSKVYVTLPESTVTLLKGRHTLVGG 880
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     881 QRVTLPAIPSRG-VFLAPSGR-FVELQTAFGLRVRWDGDQQLFVSVPSTFSGKLCGLCGDYDGDSSNDNQKPDGS 953
Cdd:pfam00094   80 QKVSLPYKSDGGeVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 149-311 3.31e-45

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: 161.38  E-value: 3.31e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     149 CDFEDNAhpFCDWVQASQDGGYWRQGNKntFIQPAGPFGIS--LNGEGHYIFLETDKFsQAGQSFRLVSRPFCAPA-VIC 225
Cdd:pfam00629    1 CDFEDGN--LCGWTQDSSDDFDWERVSG--PSVKTGPSSDHtqGTGSGHFMYVDTSSG-APGQTARLLSPLLPPSRsPQC 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     226 VTFTYHMYGLGQGTkLRLLLGSPAGSPPSSLWERVGPQSPEWLNTSVTIPSGhQQPMQLIFEAVRGTNTAFVVALGFVLI 305
Cdd:pfam00629   76 LRFWYHMSGSGVGT-LRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIRGGGSRGGIALDDISL 153


                   ....*.
gi 2499181     306 NHGTCR 311
Cdd:pfam00629  154 SSGPCP 159
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1178-1339 8.26e-45

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: 160.26  E-value: 8.26e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1178 CHAQGSATCTVSGDPHYLTFDGALHHFTGTCTYTLTKPCwlrSLENSFLVSATNEFRGGNleASYVRAVQVQVFNLRISL 1257
Cdd:smart00216    4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDC---SSEPTFSVLLKNVPCGGG--ATCLKSVKVELNGDEIEL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1258 IK-GRKVTLDGRRVALPLWPAQGRVSITSSGSFILLYTDFGL-QVRYDGDHLVEVTVPSSYAGRLCGLCGNYNNNSLDDI 1335
Cdd:smart00216   79 KDdNGKVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158


                    ....
gi 2499181     1336 LQPD 1339
Cdd:smart00216  159 RTPD 162
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 793-952 1.38e-44

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: 159.49  E-value: 1.38e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      793 CHPYGSaTCSVYGDPHYLTFDGRRFNFMGKCTYILAQPCGnlTEHFFRVLVKKEERGQeGVSCLSKVYVTLPESTVTLLK 872
Cdd:smart00216    5 QEECSP-TCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS--SEPTFSVLLKNVPCGG-GATCLKSVKVELNGDEIELKD 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      873 GRHT-LVGGQRVTLPAIPSRGVFLA-PSGRFVELQTAFGL-RVRWDGDQQLFVSVPSTFSGKLCGLCGDYDGDSSNDNQK 949
Cdd:smart00216   81 DNGKvTVNGQQVSLPYKTSDGSIQIrSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRT 160


                    ...
gi 2499181      950 PDG 952
Cdd:smart00216  161 PDG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1970-2124 1.94e-44

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: 158.69  E-value: 1.94e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1970 CSVFGDPHYRTFDGLSYRFQGRMTYTLVKTLDVLPDgvePLVVEGRNKVYPSLTPVFLQEIIVMVYGYTVQLQAELELVV 2049
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181    2050 NGQKVSIPYKPNE-YLQVTLRGR-RLYLVTDFELVVSFNGRNNAVIAMPSTYLGLVRGLCGNYDKNKRNDFMLPNGS 2124
Cdd:pfam00094   78 NGQKVSLPYKSDGgEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1575-1727 9.52e-44

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: 156.76  E-value: 9.52e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    1575 CRIPDTSHYVSFDGSYHAVRGNCTYVLVKICHSTMDlpfFKISGENGKREGQPPAFYLRQVYVDIFNTLVTL-KQDQVLI 1653
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPD---FSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLqKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1654 NGTRVSLPATTQIRGVRVISRDGYTV-LTINIGVQVKFDGRGFLEVEIPKAYYGRTCGVCGNFNDEEEDELMMPS 1727
Cdd:pfam00094   78 NGQKVSLPYKSDGGEVEILGSGFVVVdLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1573-1727 4.22e-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: 144.08  E-value: 4.22e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1573 GVCRIPDTSHYVSFDGSYHAVRGNCTYVLVKICHSTmdlPFFKISGENGKREGQPpaFYLRQVYVDIFNTLVTLKQDQ-- 1650
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE---PTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIELKDDNgk 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181     1651 VLINGTRVSLPATTQIRGVRVISRDGYTVLTINIGV-QVKFDGRGFLEVEIPKAYYGRTCGVCGNFNDEEEDELMMPS 1727
Cdd:smart00216   85 VTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1970-2123 3.91e-38

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: 141.00  E-value: 3.91e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     1970 CSVFGDPHYRTFDGLSYRFQGRMTYTLVKTLDVLPDgvepLVVEGRNKVYPSlTPVFLQEIIVMVYGYTVQL-QAELELV 2048
Cdd:smart00216   12 CSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEPT----FSVLLKNVPCGG-GATCLKSVKVELNGDEIELkDDNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181     2049 VNGQKVSIPYKPNEY-LQVTLRGRRLYLVTDFELV-VSFNGRNNAVIAMPSTYLGLVRGLCGNYDKNKRNDFMLPNG 2123
Cdd:smart00216   87 VNGQQVSLPYKTSDGsIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPDG 163
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 149-310 4.72e-38

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: 140.59  E-value: 4.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181   149 CDFEDnahPFCDWVQASQDGGYWRQGNKNTFIQPAGPFGISLNGEGHYIFLETDkFSQAGQSFRLVSRPFCAPA-VICVT 227
Cdd:cd06263    1 CDFED---GLCGWTQDSTDDFDWTRVSGSTPSPGTPPDHTHGTGSGHYLYVESS-SGREGQKARLLSPLLPPPRsSHCLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181   228 FTYHMYGLGQGTkLRLLLGSPAGSPPSSLWERVGPQSPEWLNTSVTIPSGHqQPMQLIFEAVRGTNTAFVVALGFVLINH 307
Cdd:cd06263   77 FWYHMYGSGVGT-LNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRGSGSRGDIALDDISLSP 154


                 ...
gi 2499181   308 GTC 310
Cdd:cd06263  155 GPC 157
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 992-1067 9.73e-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: 88.17  E-value: 9.73e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499181      992 TMSGPEFCGQLVAPHGVFEACLPHLRASSFFKSCTFDMCNFQGLQHMLCAHMSALTENCQDAGYTVKPWRGPQFCP 1067
Cdd:smart00832    1 KYYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1386-1453 1.29e-20

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 87.78  E-value: 1.29e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181     1386 CDVLMNPQGPFSQCHRVVAPQSSFSSCLYGQCATKGDTLTLCRSLQAYASLCARAGQALT-WRNGTFCP 1453
Cdd:smart00832    8 CGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFCP 76
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 2180-2254 1.32e-20

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 87.78  E-value: 1.32e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     2180 TQACGVLVDPQGPFAACHQIVAPGPFQEHCVFDLCAAPGPKEQEelrCQVLSGYAIICQESGPTLAGWRDHTHCA 2254
Cdd:smart00832    5 CSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECL---CDALAAYAAACAEAGVCISPWRTPTFCP 76
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 9-141 1.37e-17

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: 82.04  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     9 GPMAMPHPPLIPSTPTllafsfPGGFYMLLDPKNAKPRQRSALLSPLI---QSSGClsLSFQYTQRGQASGaTLMVYASV 85
Cdd:cd06263   25 GSTPSPGTPPDHTHGT------GSGHYLYVESSSGREGQKARLLSPLLpppRSSHC--LSFWYHMYGSGVG-TLNVYVRE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181    86 LGSIRKHTLF--SGQPGPSWQPVSVNY-TSQGQIQFTLVGVFGKIPEPAVAVDAISIAP 141
Cdd:cd06263   96 EGGGLGTLLWsaSGGQGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSP 154
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1386-1452 3.58e-17

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: 77.81  E-value: 3.58e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181    1386 CDVLMNpQGPFSQCHRVVAPQSSFSSCLYGQCATKGDTLTLCRSLQAYASLCARAGQALT-WRNGTFC 1452
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGdWRTPTFC 68
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 2183-2253 4.65e-17

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: 77.42  E-value: 4.65e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2499181    2183 CGVLVDpQGPFAACHQIVAPGPFQEHCVFDLCAAPGpkeQEELRCQVLSGYAIICQESGPTLAGWRDHTHC 2253
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGG---DDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 741-794 1.29e-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: 1.29e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2499181     741 CFYNDNYYKLGTDWFSPNCTEHCHCrPSSRMECQTFKCGTHTVCQLKNGQYGCH 794
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 998-1066 8.41e-15

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: 70.87  E-value: 8.41e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2499181     998 FCGQLVApHGVFEACLPHLRASSFFKSCTFDMCNFQGLQHMLCAHMSALTENCQDAGYTVKPWRGPQFC 1066
Cdd:pfam08742    1 KCGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 31-142 2.41e-14

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: 72.78  E-value: 2.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181      31 PGGFYMLLDPKNAKPRQRSALLSPLIQ---SSGClsLSFQYTQRGQASGaTLMVYASVLGSIRKHTLFS--GQPGPSWQP 105
Cdd:pfam00629   42 GSGHFMYVDTSSGAPGQTARLLSPLLPpsrSPQC--LRFWYHMSGSGVG-TLRVYVRENGGTLDTLLWSisGDQGPSWKE 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2499181     106 VSVNYTS-QGQIQFTLVGVFGKIPEPAVAVDAISIA--PC 142
Cdd:pfam00629  119 ARVTLSSsTQPFQVVFEGIRGGGSRGGIALDDISLSsgPC 158
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1909-1963 2.52e-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: 69.25  E-value: 2.52e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1909 CRDARGTFLPVGRFRLSSGCSQMCVCTAGAIECRPFTCPSGSQCEPNeDGKDFCQ 1963
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGNIQCQPFQCPPGTVCKDN-DGSSNCH 54
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1513-1568 1.69e-13

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: 66.94  E-value: 1.69e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2499181    1513 CTTQRGSYHPVGESWYTDNsCSRLCTCSaHNNISCRQASCKPSQMCWPQDGLIRCR 1568
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCT-GGNIQCQPFQCPPGTVCKDNDGSSNCH 54
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1070-1123 6.37e-13

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: 65.42  E-value: 6.37e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181  1070 CPRNSRYTLCARLCPDTCHSEFSGRACKDRCVEGCECDPGFVLS-GLQCVSRSEC 1123
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1780-1847 4.74e-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: 63.17  E-value: 4.74e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181    1780 QCQAAFQAPAWANCATRVVLSPYVRSCTHKLCEFGGLNRAFCESLQAFGAACQAQGIKPPVWRNSSFC 1847
Cdd:pfam08742    1 KCGLLSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1456-1511 8.91e-12

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 62.02  E-value: 8.91e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181    1456 CPSGSSYSTCANPCPATCLSLNNPSYCPstLPCAEGCECQKGHILS-GTSCVPLSQC 1511
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCP--EPCVEGCVCPPGFVRNsGGKCVPPSDC 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 311-580 1.14e-11

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 70.49  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    311 RGPSETSVSTEKPVAPTEkpTVPSEIytipTEKPMVHME-KPI---VHTEKPTVP--TEKPTIPTE----KSTVPTKKPT 380
Cdd:PTZ00449  534 HEDSKESDEPKEGGKPGE--TKEGEV----GKKPGPAKEhKPSkipTLSKKPEFPkdPKHPKDPEEpkkpKRPRSAQRPT 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    381 VFKEPTLP-----------PEGPT-----VPAERPTTP--PEGPAV-----PPKGPTVLTEwPT-------SHTEKSTVH 430
Cdd:PTZ00449  608 RPKSPKLPelldipkspkrPESPKspkrpPPPQRPSSPerPEGPKIikspkPPKSPKPPFD-PKfkekfydDYLDAAAKS 686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    431 TE-KPILPTGKSTIPTEKPMVPTKRTTTPTERTTIPAEKPTVPiEKPMVPTERttiPTERTTIPTEKPTVPTEKLTVPTE 509
Cdd:PTZ00449  687 KEtKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDE-EFPFEPIGD---PDAEQPDDIEFFTPPEEERTFFHE 762

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2499181    510 KPiVPTEKPIVPTEKhtIPTEKLTvltertttpterttIPTEKPTVPTEKPSVPTE-KPTVPTEEPTIPTEK 580
Cdd:PTZ00449  763 TP-ADTPLPDILAEE--FKEEDIH--------------AETGEPDEAMKRPDSPSEhEDKPPGDHPSLPKKR 817
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1456-1511 1.82e-11

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 61.18  E-value: 1.82e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181  1456 CPSGSSYSTCANPCPATCLSLNNPSYCpsTLPCAEGCECQKGHILS-GTSCVPLSQC 1511
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPPPC--TKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1070-1123 2.28e-11

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 60.86  E-value: 2.28e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1070 CPRNSRYTLCARLCPDTCHSEFSGRACKDRCVEGCECDPGFVLSGL-QCVSRSEC 1123
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 2257-2310 3.36e-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: 3.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    2257 CPANTVYQSCMTPCPASCATLAVPRACDGPCVEGCASLPGYIYS-GAQSLPMAHC 2310
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1851-1907 3.13e-10

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 57.71  E-value: 3.13e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181  1851 CSAHSVYTSCVPSCLPSCQDPEGQ--CTgagapSTCEEGCICEPGYVLSEQ-QCVARSQC 1907
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPppCT-----KQCVEGCFCPEGYVRNSGgKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1851-1907 3.77e-10

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 57.40  E-value: 3.77e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181    1851 CSAHSVYTSCVPSCLPSCQDPEgqcTGAGAPSTCEEGCICEPGYVLS-EQQCVARSQC 1907
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLS---PPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 2312-2365 5.69e-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: 56.93  E-value: 5.69e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2499181    2312 CTNNGVYYQQGDSFVTENCSQRCTCaSSGVLLCEPLSCRPGEICTLGNLTRGCF 2365
Cdd:pfam12714    2 KDAQGNYIPAGKTWFSSGCTQSCTC-TGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1791-1848 1.31e-09

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: 56.58  E-value: 1.31e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2499181     1791 ANCATRVVLSPYVRSCTHKLCEFGGLNRAFCESLQAFGAACQAQGIKPPVWRNSSFCP 1848
Cdd:smart00832   19 AACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 2257-2300 1.33e-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: 55.79  E-value: 1.33e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 2499181  2257 CPANTVYQSCMTPCPASCATLAVPRACDGPCVEGCASLPGYIYS 2300
Cdd:cd19941    1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRN 44
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 341-527 2.33e-09

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: 63.01  E-value: 2.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     341 TEKPMVHMEKPIVHTEKPTVPTEKPTIPTEKSTVP--TKKPTVFKEPTlpPEGPTVPAERPTTPPegPAVPPKGPTVLTE 418
Cdd:pfam05109  415 TTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPssTHVPTNLTAPA--STGPTVSTADVTSPT--PAGTTSGASPVTP 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     419 WPT-------SHTEKSTVHTEKPILPTGKSTIPTEKPMVPTKRTTTPTERTTIPAEKPTVPIEKPMVPTERTTIPTERTT 491
Cdd:pfam05109  491 SPSprdngteSKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNAT 570

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2499181     492 IPTEKPTVPTEKLTVPTEKPIVPT---EKPIVPTEKHTI 527
Cdd:pfam05109  571 IPTLGKTSPTSAVTTPTPNATSPTvgeTSPQANTTNHTL 609
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 690-739 6.06e-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: 53.93  E-value: 6.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181     690 CPPNAHFERC--ACPVSCQSPTP--NCELFCKPGCVCDPGFLFS-GSHCVNASSC 739
Cdd:pfam01826    1 CPANEVYSECgsACPPTCANLSPpdVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 690-739 6.49e-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: 53.86  E-value: 6.49e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181   690 CPPNAHFERC--ACPVSCQSPT--PNCELFCKPGCVCDPGFLFS-GSHCVNASSC 739
Cdd:cd19941    1 CPPNEVYSECgsACPPTCANPNapPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
2312-2375 8.40e-09

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 54.11  E-value: 8.40e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2499181     2312 CTNNGVYYQQGDSFVtENCsQRCTCASSGVlLCEPLSCRPGEiCTLGNLTRGCFRDSP-------CLQNPC 2375
Cdd:smart00215    1 CWNNGSYYPPGAKWD-DDC-NRCTCLNGRV-SCTKVWCGPKP-CLLHNLSGECPLGQGcvpslsdCLSSPC 67
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 331-578 1.40e-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: 1.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     331 TVPSEIYTIPTEKPMVHMEKPIVHTEKPTVPTEKPTIPTEKSTVPTKKpTVFKEPTLPPEGPTVPAErpttppegpavpp 410
Cdd:pfam05109  398 TAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTT-TGLPSSTHVPTNLTAPAS------------- 463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     411 KGPTVLTEWPTSHTEKSTVHTEKPILPTgkstiPTekpmvptkrtttpterttiPAEKPTVPIEKPMV-PTERTTIPTER 489
Cdd:pfam05109  464 TGPTVSTADVTSPTPAGTTSGASPVTPS-----PS-------------------PRDNGTESKAPDMTsPTSAVTTPTPN 519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     490 TTIPTEKPTVPTEKLTVPTEKPIVPTEKPIVPTEKHTIPTEKLTVltertttpterttiPTEKPTVPTEKPSVPTEKPTV 569
Cdd:pfam05109  520 ATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTT--------------PTPNATIPTLGKTSPTSAVTT 585


                   ....*....
gi 2499181     570 PTEEPTIPT 578
Cdd:pfam05109  586 PTPNATSPT 594
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 1125-1179 5.78e-08

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 51.15  E-value: 5.78e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    1125 CLDSTAGYVKVGERWFKPGCRQLCICEGNNrTRCVLWRCQAQEFCGQQDGIYGCH 1179
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 341-572 1.45e-06

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 53.62  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    341 TEKPMVhmeKPIVHTEKPTVPTEkPTIPTEKSTVPTKKPTVFKEPTLPPEGPTVPAErpttpPEGPAvPPKGPTVLTEWP 420
Cdd:NF033839  283 TPKEPG---NKKPSAPKPGMQPS-PQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQ-----PEKPK-PEVKPQLETPKP 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    421 TSHTEKSTVHTE-KPILPTGKSTIP----TEKPMVPTKRTTTPterttiPAEKPTVPIEKPMVPTERTT-----IPTERT 490
Cdd:NF033839  353 EVKPQPEKPKPEvKPQPEKPKPEVKpqpeTPKPEVKPQPEKPK------PEVKPQPEKPKPEVKPQPEKpkpevKPQPEK 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    491 TIPTEKPTVPTEKltvPTEKPIVPTEKPIVPTEKHTIPTEkltvLTERTTTPTERTTIPTEKPTVPTEKPSVPTEKPTVP 570
Cdd:NF033839  427 PKPEVKPQPEKPK---PEVKPQPEKPKPEVKPQPETPKPE----VKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTP 499


                  ..
gi 2499181    571 TE 572
Cdd:NF033839  500 NN 501
PHA03247 PHA03247
large tegument protein UL36; Provisional
 311-579 2.87e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    311 RGPSETSVSTEKPVAPTEKPTVPSEIYTIPTEKPMVHMEKPIVHTEKPTVPTEKPTIPTEKSTVPTKKPTVFKEPTLPPE 390
Cdd:PHA03247 2602 VDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ 2681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    391 GPTVPAERPTT--------PPEGPAVPPKGPTVLTEWPTSHTEKSTVHTEKPILPTGKSTIPtekpmvptkrtttptert 462
Cdd:PHA03247 2682 RPRRRAARPTVgsltsladPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA------------------ 2743

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    463 tiPAEKPTVPIEKPMVPTERTTIPTERTTIPTEKPTVPTEKLTVPTEKPIVPTekpivpTEKHTIPTEKLTVLTERTTTP 542
Cdd:PHA03247 2744 --VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSES------RESLPSPWDPADPPAAVLAPA 2815

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2499181    543 TERTTIPTEKPTVPTEKPSVPTEKPTVPTE-EPTIPTE 579
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGPpPPSLPLG 2853
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 247-442 5.94e-06

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 5.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     247 SPAGSPPSSLWERVGPQSPewlNTSVTIPSGHQQPMQLIFEAVRG--TNTAFVvalgfvlinhgTCRGPSETSvSTEKPV 324
Cdd:pfam05109  424 APESTTTSPTLNTTGFAAP---NTTTGLPSSTHVPTNLTAPASTGptVSTADV-----------TSPTPAGTT-SGASPV 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     325 APTEKP------------TVPSEIYTIPTekPMVHMEKPIVHTEKP---------TVPTEKPTIPTEKSTVPTKKPTV-F 382
Cdd:pfam05109  489 TPSPSPrdngteskapdmTSPTSAVTTPT--PNATSPTPAVTTPTPnatsptlgkTSPTSAVTTPTPNATSPTPAVTTpT 566

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     383 KEPTLPPEGPTVPAERPTTPPEGPAVPPKGPTVLTEWPTSHTEKSTVHTEKPILPTGKST 442
Cdd:pfam05109  567 PNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNAT 626
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 329-579 6.31e-06

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 51.69  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    329 KPTVPSEIYTIPTEKPMVHMEKPIVHTEKPTVPTEKPTIPTEkstvpTKKPTVFKEPTLPPEGPTVPAERPTTPPEGPAV 408
Cdd:NF033839  241 KKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQD-----TPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    409 PPKgPTVLTEWPTSHTEKSTvHTEKPiLPTGKSTIPTEKPMVPTKRTTTPterttiPAEKPTVPIEKPMVPTE-RTTIPT 487
Cdd:NF033839  316 TPK-PEVKPQLEKPKPEVKP-QPEKP-KPEVKPQLETPKPEVKPQPEKPK------PEVKPQPEKPKPEVKPQpETPKPE 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    488 ERTTIPTEKPTV-PTEKLTVPTEKPIVPTEKPIVPTEKHTiPTEKLtvltertttpterttipteKPTVPTEKPSVpteK 566
Cdd:NF033839  387 VKPQPEKPKPEVkPQPEKPKPEVKPQPEKPKPEVKPQPEK-PKPEV-------------------KPQPEKPKPEV---K 443

                         250
                  ....*....|...
gi 2499181    567 PTVPTEEPTIPTE 579
Cdd:NF033839  444 PQPEKPKPEVKPQ 456
PHA03247 PHA03247
large tegument protein UL36; Provisional
 248-571 1.36e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    248 PAGSPPSSlweRVGPQSPEWLNTSVTIPSGHQQPMQLIFEAVRGTNTAFVVALGfvlinhGTCRGPSETSVSTEKPVAPT 327
Cdd:PHA03247 2703 PPPPTPEP---APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG------PARPARPPTTAGPPAPAPPA 2773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    328 EKPTVPSEIYTIPTEKPMVHMEKPIVHTEKPTVPTEKPTIPTekstvPTKKPTVFKEPTLPPEGPTVPAERPTTPPEGPA 407
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-----AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    408 VPPKGPTVLTEWPTSHTEKSTVHTEKPILPTGKSTIPTEKPmvptkrtttpterttiPAEKPTVPIEKPMVPTERTTIPt 487
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP----------------AVSRSTESFALPPDQPERPPQP- 2911

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    488 ERTTIPTEKPTVPTEKLTVPTEKPIVPTEKPIVPTEKHTIPTEKLTVLTERTTTPTERTTIPTEKPTVPTEKPSVPTEKP 567
Cdd:PHA03247 2912 QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS 2991


                  ....
gi 2499181    568 TVPT 571
Cdd:PHA03247 2992 STPP 2995
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 315-533 1.46e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.46  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    315 ETSVSTEKPVAPTeKPTVPseiytiptEKPmvhmEKP-IVHTEKPTVPTEKPTIPT---------------EKSTVPTKK 378
Cdd:PTZ00449  628 ESPKSPKRPPPPQ-RPSSP--------ERP----EGPkIIKSPKPPKSPKPPFDPKfkekfyddyldaaakSKETKTTVV 694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    379 PTVFKEPTLPPEGPTVPAERPTTPPEGPAVPPKGPTVLTEWPTSHTEKSTVHTEKPILPTGKSTIPTEKpmvptkrtttp 458
Cdd:PTZ00449  695 LDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHET----------- 763

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2499181    459 terttiPAEKPTVPIEKPMVPTERTTIPTERTTIPTEKPTVPTEkltvptEKPIVPTEKPIVPTEKHTIPTEKLT 533
Cdd:PTZ00449  764 ------PADTPLPDILAEEFKEEDIHAETGEPDEAMKRPDSPSE------HEDKPPGDHPSLPKKRHRLDGLALS 826
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 313-693 3.60e-05

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 48.80  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     313 PSETSVSTEKPVAPTEKPTVPSEIYTIPTekpmvhmekpivhTEKPTVPTE-KPTIPTEKSTVPTKKptvfkEPTLPPEG 391
Cdd:pfam17823  118 AASSSPSSAAQSLPAAIAALPSEAFSAPR-------------AAACRANASaAPRAAIAAASAPHAA-----SPAPRTAA 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     392 PTVPAERPTTPPEGPAVPPKGPTVLTEWPTSHTEKSTVHTEKPILPTGKSTIPTEKPMvptKRTTTPTERTTIPAEKPTV 471
Cdd:pfam17823  180 SSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPA---AGTVTAAVGTVTPAALATL 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     472 PIEKPMVPTERTTI----PTERTTIPTEK-PTVPTEKLTVPTEKPI-------VPTEKPIVPTEKHTIPTEKLTVLTERT 539
Cdd:pfam17823  257 AAAAGTVASAAGTInmgdPHARRLSPAKHmPSDTMARNPAAPMGAQaqgpiiqVSTDQPVHNTAGEPTPSPSNTTLEPNT 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     540 TTPTERTTIPTEKPT-VPTEKPSVPTeKPTVPTEepTIPTEKLTvptertttptkrtttptirtttptirtttptERttt 618
Cdd:pfam17823  337 PKSVASTNLAVVTTTkAQAKEPSASP-VPVLHTS--MIPEVEAT-------------------------------SP--- 379

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181     619 ptirtttpterttiptkkTTVPTekTIIPTERTIAPTTPQpsptlVPTQPAAVVMPSTSATTVTPRT-------TIASCP 691
Cdd:pfam17823  380 ------------------TTQPS--PLLPTQGAAGPGILL-----APEQVATEATAGTASAGPTPRSsgdpktlAMASCQ 434


                   ..
gi 2499181     692 PN 693
Cdd:pfam17823  435 LS 436
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 292-523 6.32e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.53  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    292 TNTAFVVALGFVLINHGTCRGPSETSVSTEKPVAPTeKPTVPSEIYTIPTEkpmvhmekpivhtekptvPTEKPTIPTEK 371
Cdd:PTZ00449  689 TKTTVVLDESFESILKETLPETPGTPFTTPRPLPPK-LPRDEEFPFEPIGD------------------PDAEQPDDIEF 749

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    372 STVPTKKPTVFKEPTLPPEGPTVPAERPTTP-----PEGPAVPPKGPtvltEWPTSHTEKSTvhTEKPILPTGK------ 440
Cdd:PTZ00449  750 FTPPEEERTFFHETPADTPLPDILAEEFKEEdihaeTGEPDEAMKRP----DSPSEHEDKPP--GDHPSLPKKRhrldgl 823

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    441 --STI------------PTEKPMVPTKRTTTPTERTTIPAEKPTVPIEKPMVPTERTTIPTERTTIPTEKptvptEKLTV 506
Cdd:PTZ00449  824 alSTTdlesdagriakdASGKIVKLKRSKSFDDLTTVEEAEEMGAEARKIVVDDDGTEADDEDTHPPEEK-----HKSEV 898

                         250
                  ....*....|....*..
gi 2499181    507 PTEKPIVPTEKPIVPTE 523
Cdd:PTZ00449  899 RRRRPPKKPSKPKKPSK 915
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2370-2399 8.10e-05

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 41.60  E-value: 8.10e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2499181    2370 CLQNPCQNDGRCREQGTHFTCECELGYGGD 2399
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 341-576 1.73e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.84  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    341 TEKPMVHMEKPIVHTEKPTVPTEKPTIPTEKSTVPTKKptvfkeptLPPEGPTVPAERptTPPEGPAVPPKGPTVLTEW- 419
Cdd:PLN03209  309 TTAPLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKP--------VTPEAPSPPIEE--EPPQPKAVVPRPLSPYTAYe 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    420 ----PTSHTekstvhtekPILPTGKSTIPTEkpmVPTKRTTTPTERTTIPAEKPTVPIEKPMVPTERTTIPT------ER 489
Cdd:PLN03209  379 dlkpPTSPI---------PTPPSSSPASSKS---VDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLspyaryED 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    490 TTIPTE-KPTVPTEKLTVPTEKPIVP----TEKPIVPTEKHTIPTEKLTVLtertttPTERTTIPTEKPTVPTEKPSVPT 564
Cdd:PLN03209  447 LKPPTSpSPTAPTGVSPSVSSTSSVPavpdTAPATAATDAAAPPPANMRPL------SPYAVYDDLKPPTSPSPAAPVGK 520

                         250
                  ....*....|..
gi 2499181    565 EKPTVPTEEPTI 576
Cdd:PLN03209  521 VAPSSTNEVVKV 532
VWC smart00214
von Willebrand factor (vWF) type C domain;
2312-2358 2.73e-04

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 40.96  E-value: 2.73e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2499181     2312 CTNNGVYYQQGDSFVTENCsQRCTCASSGVLLCEPLSCRPGEICTLG 2358
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPC-QICTCLDGTTVLCDPVECPPPPDCPNP 46
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 355-510 1.89e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 43.01  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    355 TEKPTVPTEKPTIPTEKSTVPTKKPTVFKEPTLPPEGPTVPAERPTTPPEGPAVPPKgptvltewptshteKSTVHTEKP 434
Cdd:PTZ00436  216 SAKAAAPAKAAAAPAKAAAPPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAAAPPA--------------KAAAPPAKA 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2499181    435 ILPTGKSTIPTEKPMVPTKRTTTPterttiPAEKPTVPIEKPMVPTERTTIPTERTTIPTEKPTVPTEKLTVPTEK 510
Cdd:PTZ00436  282 AAPPAKAAAPPAKAAAAPAKAAAA------PAKAAAAPAKAAAPPAKAAAPPAKAATPPAKAAAPPAKAAAAPVGK 351
PHA03379 PHA03379
EBNA-3A; Provisional
 309-517 5.95e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.97  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    309 TCRGPSETSVSTEKPVAPTEKPTVPSEIYTIPT-------EKPMVHMEKPI----VHTEKPTVPTEKPTIPTEKSTVPTK 377
Cdd:PHA03379  404 ALEKASEPTYGTPRPPVEKPRPEVPQSLETATShgsaqvpEPPPVHDLEPGplhdQHSMAPCPVAQLPPGPLQDLEPGDQ 483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2499181    378 KPTVFKEPT---LPPEGPTVPAERP--TTPPEGPAVPPkGPTVLTEWPTSHTEKSTVHTEKPILPtgkstIPTEKPMVPT 452
Cdd:PHA03379  484 LPGVVQDGRpacAPVPAPAGPIVRPweASLSQVPGVAF-APVMPQPMPVEPVPVPTVALERPVCP-----APPLIAMQGP 557

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2499181    453 KRTTTPTERTTIPAEKPTVPIE-KPMVP-----------TERTTIPTERTTIPTEKPTVPTEKltvPTEKPIVPTEK 517
Cdd:PHA03379  558 GETSGIVRVRERWRPAPWTPNPpRSPSQmsvrdrlarlrAEAQPYQASVEVQPPQLTQVSPQQ---PMEYPLEPEQQ 631
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2373-2402 7.67e-03

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 7.67e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 2499181  2373 NPCQNDGRCREQGTHFTCECELGYGGDLCT 2402
Cdd:cd00054    9 NPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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