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Conserved domains on  [gi|2038004112|ref|XP_041471228|]
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zonadhesin-like [Lytechinus variegatus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 400-556 2.07e-34

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: 129.41  E-value: 2.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  400 CEIMGDPHYTSFDGKRFDFQGDCEYTLLKPRSpetdELPDFHLYGNNVRSSPSSRVSILRQIFLTYNGTTFSVGQpsGRT 479
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS----EEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQK--GGT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  480 LRVDGLQVTAPVNQNGVSI---TYAFPLIIIETEFGLRVTYDGSHFAKVYLSPSFYGKTCGLCGNFDGNPDNDFTLPDGT 556
Cdd:pfam00094   75 VLVNGQKVSLPYKSDGGEVeilGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 805-959 7.74e-32

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: 122.09  E-value: 7.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  805 CTISGDPHYRTFDRFYHHFQGDCMYTLVKPCQASdlfPDFHIWGDPVKTHPSATVSWLRKVFLLLNGTTYTLGQGMAFLV 884
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEE---PDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038004112  885 DGvAQSNIDYRDGSVH---AWADSRYLTLETEFGVRIQFSGGSLAEISVSYDFWNNTCGLCGNFDGISTNEFTTSDGT 959
Cdd:pfam00094   78 NG-QKVSLPYKSDGGEveiLGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1072-1125 8.77e-16

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: 72.73  E-value: 8.77e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112 1072 CPEPQLYNPCGSPCPATCANPTAPENCQETCIETCSCPDGLLLD-GDSCVEPDRC 1125
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 676-729 8.36e-14

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: 66.96  E-value: 8.36e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  676 CPEGTGYRMCGTACPNTCADPTAADNCPRPCHETCLCPDGLVLD-GEKCVEIADC 729
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 731-785 2.55e-09

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


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 54.23  E-value: 2.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  731 CTLPNNVYISSGEVWITPDtCEERCDCQGGILTCEPLGCGDNEVCAVRNGVRGCY 785
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 600-667 2.66e-09

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: 54.69  E-value: 2.66e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038004112  600 CSIFdpdRNEGIFGDCSNFVDHFNFYTSCQFDLCYTHELNKVVCASVQEYIVLCQARnpGVVIGEWRN 667
Cdd:pfam08742    2 CGLL---SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAA--GVCIGDWRT 64
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 996-1057 1.30e-06

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: 47.34  E-value: 1.30e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038004112   996 TAAARACNNLQNINGPFQNCLDFADPTDIYTSCLFDACVLGADDDAVCDHYDQYTGTCQALG 1057
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAG 63
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 43-139 2.33e-05

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


The actual alignment was detected with superfamily member cd00041:

Pssm-ID: 412131 [Multi-domain]  Cd Length: 113  Bit Score: 44.71  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   43 PLQTTNLMECVWQVTAPPGQHVRLNVVFMQTDEHEE-----IAVYDHGTSIDdqylvSSIRGILLRSSSGNIVSSGAGLT 117
Cdd:cd00041     19 PNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNcsydyLEIYDGPSTSS-----PLLGRFCGSTLPPPIISSGNSLT 93

                           90       100
                   ....*....|....*....|..
gi 2038004112  118 VRYTADqeSLNPGIRFFAHTSF 139
Cdd:cd00041     94 VRFRSD--SSVTGRGFKATYSA 113
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 275-390 1.91e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


The actual alignment was detected with superfamily member cd00041:

Pssm-ID: 412131 [Multi-domain]  Cd Length: 113  Bit Score: 39.32  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  275 CGGSLVLA-EGTlptanIRSPydpNRPETSDCSIMCWWFITAPYGSQVQVDINDVTTT-----TNERVRITDGatPSNNP 348
Cdd:cd00041      1 CGGTLTAStSGT-----ISSP---NYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspncSYDYLEIYDG--PSTSS 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2038004112  349 SFERTFSGAgIAGETLFSQAGGVTIALedLSPEGPNGRGFSL 390
Cdd:cd00041     71 PLLGRFCGS-TLPPPIISSGNSLTVRF--RSDSSVTGRGFKA 109
CUB super family cl00049
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 150-262 2.17e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


The actual alignment was detected with superfamily member cd00041:

Pssm-ID: 412131 [Multi-domain]  Cd Length: 113  Bit Score: 39.32  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  150 CGGRIELNGNTVLEAP-----YNNHirpfigggyMSCVWTVVAPDDRRVRATWTRVDTLD------ERVGIFDHETlSED 218
Cdd:cd00041      1 CGGTLTASTSGTISSPnypnnYPNN---------LNCVWTIEAPPGYRIRLTFEDFDLESspncsyDYLEIYDGPS-TSS 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2038004112  219 HEVTRLQGliDWRMPAFTSIGNVIVVYLRQDAfqFVIGNGFSLQ 262
Cdd:cd00041     71 PLLGRFCG--STLPPPIISSGNSLTVRFRSDS--SVTGRGFKAT 110
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 400-556 2.07e-34

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: 129.41  E-value: 2.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  400 CEIMGDPHYTSFDGKRFDFQGDCEYTLLKPRSpetdELPDFHLYGNNVRSSPSSRVSILRQIFLTYNGTTFSVGQpsGRT 479
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS----EEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQK--GGT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  480 LRVDGLQVTAPVNQNGVSI---TYAFPLIIIETEFGLRVTYDGSHFAKVYLSPSFYGKTCGLCGNFDGNPDNDFTLPDGT 556
Cdd:pfam00094   75 VLVNGQKVSLPYKSDGGEVeilGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 397-555 1.86e-32

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: 124.05  E-value: 1.86e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   397 PGYCEIMGDPHYTSFDGKRFDFQGDCEYTLLKPRSPEtdelPDFHLYGNNVRSSPSSRvsILRQIFLTYNGTTFSVGQPs 476
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE----PTFSVLLKNVPCGGGAT--CLKSVKVELNGDEIELKDD- 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   477 GRTLRVDGLQVTAPVNQNGVSITY--AFPLIIIETEFGL-RVTYDGSHFAKVYLSPSFYGKTCGLCGNFDGNPDNDFTLP 553
Cdd:smart00216   82 NGKVTVNGQQVSLPYKTSDGSIQIrsSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 2038004112   554 DG 555
Cdd:smart00216  162 DG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 805-959 7.74e-32

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: 122.09  E-value: 7.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  805 CTISGDPHYRTFDRFYHHFQGDCMYTLVKPCQASdlfPDFHIWGDPVKTHPSATVSWLRKVFLLLNGTTYTLGQGMAFLV 884
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEE---PDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038004112  885 DGvAQSNIDYRDGSVH---AWADSRYLTLETEFGVRIQFSGGSLAEISVSYDFWNNTCGLCGNFDGISTNEFTTSDGT 959
Cdd:pfam00094   78 NG-QKVSLPYKSDGGEveiLGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 798-958 5.92e-29

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 114.04  E-value: 5.92e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   798 CVRAPAVCTISGDPHYRTFDRFYHHFQGDCMYTLVKPCQAsdlFPDFHIWGDPVktHPSATVSWLRKVFLLLNGTTYTLG 877
Cdd:smart00216    5 QEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS---EPTFSVLLKNV--PCGGGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   878 Q-GMAFLVDGVAQS-NIDYRDGSVHAWADSRYLTLETEFGV-RIQFSGGSLAEISVSYDFWNNTCGLCGNFDGISTNEFT 954
Cdd:smart00216   80 DdNGKVTVNGQQVSlPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159


                    ....
gi 2038004112   955 TSDG 958
Cdd:smart00216  160 TPDG 163
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1072-1125 8.77e-16

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: 72.73  E-value: 8.77e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112 1072 CPEPQLYNPCGSPCPATCANPTAPENCQETCIETCSCPDGLLLD-GDSCVEPDRC 1125
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1072-1125 2.62e-14

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 68.57  E-value: 2.62e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112 1072 CPEPQLYNPCGSPCPATCANPTAPENCQETCIETCSCPDGLLLD-GDSCVEPDRC 1125
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 676-729 8.36e-14

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: 66.96  E-value: 8.36e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  676 CPEGTGYRMCGTACPNTCADPTAADNCPRPCHETCLCPDGLVLD-GEKCVEIADC 729
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 676-729 9.50e-13

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: 63.95  E-value: 9.50e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  676 CPEGTGYRMCGTACPNTCADPTAADNCPRPCHETCLCPDGLVLDGE-KCVEIADC 729
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 731-785 2.55e-09

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 54.23  E-value: 2.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  731 CTLPNNVYISSGEVWITPDtCEERCDCQGGILTCEPLGCGDNEVCAVRNGVRGCY 785
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 600-667 2.66e-09

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: 54.69  E-value: 2.66e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038004112  600 CSIFdpdRNEGIFGDCSNFVDHFNFYTSCQFDLCYTHELNKVVCASVQEYIVLCQARnpGVVIGEWRN 667
Cdd:pfam08742    2 CGLL---SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAA--GVCIGDWRT 64
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 996-1057 1.30e-06

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: 47.34  E-value: 1.30e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038004112   996 TAAARACNNLQNINGPFQNCLDFADPTDIYTSCLFDACVLGADDDAVCDHYDQYTGTCQALG 1057
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAG 63
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1002-1057 1.74e-06

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: 46.60  E-value: 1.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038004112 1002 CNNLQNiNGPFQNCLDFADPTDIYTSCLFDACVLGADDDAVCDHYDQYTGTCQALG 1057
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAG 56
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 609-667 1.79e-06

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 46.95  E-value: 1.79e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038004112   609 EGIFGDCSNFVDHFNFYTSCQFDLCYTHELNKVVCASVQEYIVLCQArnPGVVIGEWRN 667
Cdd:smart00832   15 RGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAE--AGVCISPWRT 71
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 43-139 2.33e-05

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 44.71  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   43 PLQTTNLMECVWQVTAPPGQHVRLNVVFMQTDEHEE-----IAVYDHGTSIDdqylvSSIRGILLRSSSGNIVSSGAGLT 117
Cdd:cd00041     19 PNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNcsydyLEIYDGPSTSS-----PLLGRFCGSTLPPPIISSGNSLT 93

                           90       100
                   ....*....|....*....|..
gi 2038004112  118 VRYTADqeSLNPGIRFFAHTSF 139
Cdd:cd00041     94 VRFRSD--SSVTGRGFKATYSA 113
CUB pfam00431
CUB domain;
48-123 1.48e-03

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 39.59  E-value: 1.48e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038004112   48 NLMECVWQVTAPPGQHVRLNVVFMQTDEHEEIAvYDHGTSIDDQYLVSSIRGILLRSS-SGNIVSSGAGLTVRYTAD 123
Cdd:pfam00431   23 PNKDCVWLIRAPPGFRVKLTFQDFELEDHDECG-YDYVEIRDGPSASSPLLGRFCGSGiPEDIVSSSNQMTIKFVSD 98
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 275-390 1.91e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 39.32  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  275 CGGSLVLA-EGTlptanIRSPydpNRPETSDCSIMCWWFITAPYGSQVQVDINDVTTT-----TNERVRITDGatPSNNP 348
Cdd:cd00041      1 CGGTLTAStSGT-----ISSP---NYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspncSYDYLEIYDG--PSTSS 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2038004112  349 SFERTFSGAgIAGETLFSQAGGVTIALedLSPEGPNGRGFSL 390
Cdd:cd00041     71 PLLGRFCGS-TLPPPIISSGNSLTVRF--RSDSSVTGRGFKA 109
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 150-262 2.17e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 39.32  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  150 CGGRIELNGNTVLEAP-----YNNHirpfigggyMSCVWTVVAPDDRRVRATWTRVDTLD------ERVGIFDHETlSED 218
Cdd:cd00041      1 CGGTLTASTSGTISSPnypnnYPNN---------LNCVWTIEAPPGYRIRLTFEDFDLESspncsyDYLEIYDGPS-TSS 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2038004112  219 HEVTRLQGliDWRMPAFTSIGNVIVVYLRQDAfqFVIGNGFSLQ 262
Cdd:cd00041     71 PLLGRFCG--STLPPPIISSGNSLTVRFRSDS--SVTGRGFKAT 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 43-136 4.26e-03

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 38.14  E-value: 4.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112    43 PLQTTNLMECVWQVTAPPGQHVRLNVVFMQTDEHEE-----IAVYDhGTSIDDQYLV---SSIRGILLRSSSGNIvssga 114
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNceydyVEIYD-GPSASSPLLGrfcGSEAPPPVISSSSNS----- 82

                            90       100
                    ....*....|....*....|..
gi 2038004112   115 gLTVRYTADqeSLNPGIRFFAH 136
Cdd:smart00042   83 -LTLTFVSD--SSVQKRGFSAR 101
 
Name Accession Description Interval E-value
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 400-556 2.07e-34

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: 129.41  E-value: 2.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  400 CEIMGDPHYTSFDGKRFDFQGDCEYTLLKPRSpetdELPDFHLYGNNVRSSPSSRVSILRQIFLTYNGTTFSVGQpsGRT 479
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCS----EEPDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQK--GGT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  480 LRVDGLQVTAPVNQNGVSI---TYAFPLIIIETEFGLRVTYDGSHFAKVYLSPSFYGKTCGLCGNFDGNPDNDFTLPDGT 556
Cdd:pfam00094   75 VLVNGQKVSLPYKSDGGEVeilGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 397-555 1.86e-32

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: 124.05  E-value: 1.86e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   397 PGYCEIMGDPHYTSFDGKRFDFQGDCEYTLLKPRSPEtdelPDFHLYGNNVRSSPSSRvsILRQIFLTYNGTTFSVGQPs 476
Cdd:smart00216    9 SPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSE----PTFSVLLKNVPCGGGAT--CLKSVKVELNGDEIELKDD- 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   477 GRTLRVDGLQVTAPVNQNGVSITY--AFPLIIIETEFGL-RVTYDGSHFAKVYLSPSFYGKTCGLCGNFDGNPDNDFTLP 553
Cdd:smart00216   82 NGKVTVNGQQVSLPYKTSDGSIQIrsSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 2038004112   554 DG 555
Cdd:smart00216  162 DG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 805-959 7.74e-32

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: 122.09  E-value: 7.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  805 CTISGDPHYRTFDRFYHHFQGDCMYTLVKPCQASdlfPDFHIWGDPVKTHPSATVSWLRKVFLLLNGTTYTLGQGMAFLV 884
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEE---PDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLV 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038004112  885 DGvAQSNIDYRDGSVH---AWADSRYLTLETEFGVRIQFSGGSLAEISVSYDFWNNTCGLCGNFDGISTNEFTTSDGT 959
Cdd:pfam00094   78 NG-QKVSLPYKSDGGEveiLGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 798-958 5.92e-29

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 114.04  E-value: 5.92e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   798 CVRAPAVCTISGDPHYRTFDRFYHHFQGDCMYTLVKPCQAsdlFPDFHIWGDPVktHPSATVSWLRKVFLLLNGTTYTLG 877
Cdd:smart00216    5 QEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS---EPTFSVLLKNV--PCGGGATCLKSVKVELNGDEIELK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   878 Q-GMAFLVDGVAQS-NIDYRDGSVHAWADSRYLTLETEFGV-RIQFSGGSLAEISVSYDFWNNTCGLCGNFDGISTNEFT 954
Cdd:smart00216   80 DdNGKVTVNGQQVSlPYKTSDGSIQIRSSGGYLVVITSLGLiQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFR 159


                    ....
gi 2038004112   955 TSDG 958
Cdd:smart00216  160 TPDG 163
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1072-1125 8.77e-16

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: 72.73  E-value: 8.77e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112 1072 CPEPQLYNPCGSPCPATCANPTAPENCQETCIETCSCPDGLLLD-GDSCVEPDRC 1125
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 1072-1125 2.62e-14

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 68.57  E-value: 2.62e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112 1072 CPEPQLYNPCGSPCPATCANPTAPENCQETCIETCSCPDGLLLD-GDSCVEPDRC 1125
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 676-729 8.36e-14

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: 66.96  E-value: 8.36e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  676 CPEGTGYRMCGTACPNTCADPTAADNCPRPCHETCLCPDGLVLD-GEKCVEIADC 729
Cdd:cd19941      1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 676-729 9.50e-13

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: 63.95  E-value: 9.50e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  676 CPEGTGYRMCGTACPNTCADPTAADNCPRPCHETCLCPDGLVLDGE-KCVEIADC 729
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNSGgKCVPPSDC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 731-785 2.55e-09

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


Pssm-ID: 432736  Cd Length: 54  Bit Score: 54.23  E-value: 2.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038004112  731 CTLPNNVYISSGEVWITPDtCEERCDCQGGILTCEPLGCGDNEVCAVRNGVRGCY 785
Cdd:pfam12714    1 CKDAQGNYIPAGKTWFSSG-CTQSCTCTGGNIQCQPFQCPPGTVCKDNDGSSNCH 54
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 600-667 2.66e-09

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: 54.69  E-value: 2.66e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038004112  600 CSIFdpdRNEGIFGDCSNFVDHFNFYTSCQFDLCYTHELNKVVCASVQEYIVLCQARnpGVVIGEWRN 667
Cdd:pfam08742    2 CGLL---SDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAA--GVCIGDWRT 64
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 996-1057 1.30e-06

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: 47.34  E-value: 1.30e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038004112   996 TAAARACNNLQNINGPFQNCLDFADPTDIYTSCLFDACVLGADDDAVCDHYDQYTGTCQALG 1057
Cdd:smart00832    2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAG 63
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1002-1057 1.74e-06

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: 46.60  E-value: 1.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038004112 1002 CNNLQNiNGPFQNCLDFADPTDIYTSCLFDACVLGADDDAVCDHYDQYTGTCQALG 1057
Cdd:pfam08742    2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAG 56
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 609-667 1.79e-06

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 46.95  E-value: 1.79e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038004112   609 EGIFGDCSNFVDHFNFYTSCQFDLCYTHELNKVVCASVQEYIVLCQArnPGVVIGEWRN 667
Cdd:smart00832   15 RGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAE--AGVCISPWRT 71
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 43-139 2.33e-05

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 44.71  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112   43 PLQTTNLMECVWQVTAPPGQHVRLNVVFMQTDEHEE-----IAVYDHGTSIDdqylvSSIRGILLRSSSGNIVSSGAGLT 117
Cdd:cd00041     19 PNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNcsydyLEIYDGPSTSS-----PLLGRFCGSTLPPPIISSGNSLT 93

                           90       100
                   ....*....|....*....|..
gi 2038004112  118 VRYTADqeSLNPGIRFFAHTSF 139
Cdd:cd00041     94 VRFRSD--SSVTGRGFKATYSA 113
CUB pfam00431
CUB domain;
48-123 1.48e-03

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 39.59  E-value: 1.48e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038004112   48 NLMECVWQVTAPPGQHVRLNVVFMQTDEHEEIAvYDHGTSIDDQYLVSSIRGILLRSS-SGNIVSSGAGLTVRYTAD 123
Cdd:pfam00431   23 PNKDCVWLIRAPPGFRVKLTFQDFELEDHDECG-YDYVEIRDGPSASSPLLGRFCGSGiPEDIVSSSNQMTIKFVSD 98
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 275-390 1.91e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 39.32  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  275 CGGSLVLA-EGTlptanIRSPydpNRPETSDCSIMCWWFITAPYGSQVQVDINDVTTT-----TNERVRITDGatPSNNP 348
Cdd:cd00041      1 CGGTLTAStSGT-----ISSP---NYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspncSYDYLEIYDG--PSTSS 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2038004112  349 SFERTFSGAgIAGETLFSQAGGVTIALedLSPEGPNGRGFSL 390
Cdd:cd00041     71 PLLGRFCGS-TLPPPIISSGNSLTVRF--RSDSSVTGRGFKA 109
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 150-262 2.17e-03

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 39.32  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112  150 CGGRIELNGNTVLEAP-----YNNHirpfigggyMSCVWTVVAPDDRRVRATWTRVDTLD------ERVGIFDHETlSED 218
Cdd:cd00041      1 CGGTLTASTSGTISSPnypnnYPNN---------LNCVWTIEAPPGYRIRLTFEDFDLESspncsyDYLEIYDGPS-TSS 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2038004112  219 HEVTRLQGliDWRMPAFTSIGNVIVVYLRQDAfqFVIGNGFSLQ 262
Cdd:cd00041     71 PLLGRFCG--STLPPPIISSGNSLTVRFRSDS--SVTGRGFKAT 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 43-136 4.26e-03

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 38.14  E-value: 4.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038004112    43 PLQTTNLMECVWQVTAPPGQHVRLNVVFMQTDEHEE-----IAVYDhGTSIDDQYLV---SSIRGILLRSSSGNIvssga 114
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNceydyVEIYD-GPSASSPLLGrfcGSEAPPPVISSSSNS----- 82

                            90       100
                    ....*....|....*....|..
gi 2038004112   115 gLTVRYTADqeSLNPGIRFFAH 136
Cdd:smart00042   83 -LTLTFVSD--SSVQKRGFSAR 101
 
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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