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Conserved domains on  [gi|530400098|ref|XP_005268859|]
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otogelin-like protein isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_ABD_OTOGL cd23401
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and ...
 1216-1369 1.14e-101

Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and similar proteins; OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOGL gene may cause hearing loss. OTOGL contains an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.


:

Pssm-ID: 467811  Cd Length: 154  Bit Score: 322.58  E-value: 1.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1216 YYNEGLGEGPYMLASYGQSGLVLGANMTSRSVFCLPRSSVHTSLFFYFMITPGLFKEKVSSLALVSLESAERPNYFLYVH 1295
Cdd:cd23401     1 YYNQGLGEGPYTLSSYGQSDCVLGANLTSGEVFPLPKISAQGSTFFHFMITPGLFKDKASSLPVVSLESAERPNYFLCVH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400098 1296 DNDTLSLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYDDSEEFKHSSSFSIEE 1369
Cdd:cd23401    81 DNRTLRLEQWQPSSEFRRRATFFHHQGLWIPGYSSFELHSKKGFFITLTHSGAKASKYDDSEEFKTSSSFSIEE 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 131-276 1.32e-30

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: 119.40  E-value: 1.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   131 CKTWGQYHFETFDGIYYYFPGNCSYIFAKDCGDlEPRYTVWVHNSPKCLGSVYSCYRSISLFFSNQeEIRIY-GHEIKKN 209
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGVCLKSVTVIVGDL-EITLQkGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   210 GISLTLPQTIGQIFIEKL-ADYILVKTTFGFSL--AWDGISGIYLKLSEDHKGKSCGLCGNYNDIQSDDF 276
Cdd:pfam00094   79 GQKVSLPYKSDGGEVEILgSGFVVVDLSPGVGLqvDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDF 148
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 480-642 4.62e-30

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: 117.89  E-value: 4.62e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    480 WNCTEQDCPVQCSVVGDSHFTTFDGRHYSFIGMCQYILVKG-TGKDKFTITLQKAPCEQnlGLVCLQSITLILED----- 553
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcSSEPTFSVLLKNVPCGG--GATCLKSVKVELNGdeiel 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    554 -DFNKQVTLgrGGQILTSPNQGFnlNGIVEIQTLSSlFILLKTTFGLKILfAIDGE-RIYIQLTSAWKRRTLGLCGTFNG 631
Cdd:smart00216   79 kDDNGKVTV--NGQQVSLPYKTS--DGSIQIRSSGG-YLVVITSLGLIQV-TFDGLtLLSVQLPSKYRGKTCGLCGNFDG 152

                           170
                    ....*....|.
gi 530400098    632 NIRDDFLSPSG 642
Cdd:smart00216  153 EPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 947-1102 2.19e-29

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


:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 115.96  E-value: 2.19e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    947 CTYYPCPAVCTIYGDRHYYSFDGLEYDYISDCQVFLIKSADDS-DISVIAQNKKCfDNDIVCSKSVLISVGDTEIYLNDT 1025
Cdd:smart00216    3 CTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC-GGGATCLKSVKVELNGDEIELKDD 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1026 PYKQKQSGF-----FLENKSTYQLWKAGYYIVVYFPEKDITILWDRKTTIHIKVGPQWKNKLSGLCGNFDKCTSNDMTTS 1100
Cdd:smart00216   82 NGKVTVNGQqvslpYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 530400098   1101 NN 1102
Cdd:smart00216  162 DG 163
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1741-1810 2.86e-17

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: 78.15  E-value: 2.86e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400098   1741 TEHDCSQCIDLLNRR-IFIPCHDKVSPEDFCEKMWI---NYTYFWNYECDALSAYVALCNKFDICIQ-WRTPDYC 1810
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYdtcACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1137-1210 2.67e-16

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


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.45  E-value: 2.67e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   1137 FPYAKKECSILYSD--IFASCRNVIDVTSFAKNCHEDTCNCnlGGDCECLCTSIAAYAYKCCQEGISIH-WRSSTVC 1210
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
VWD super family cl47031
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1534-1707 1.24e-15

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.


The actual alignment was detected with superfamily member smart00216:

Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 76.67  E-value: 1.24e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1534 CCPEWECPCRCSMLSELSIITFDGNNAALYSMASYILVRIpgeiivahiekCSMNQNGNSLKKLAPSGRiSGLCFKKLNV 1613
Cdd:smart00216    2 CCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-----------CSSEPTFSVLLKNVPCGG-GATCLKSVKV 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1614 TTPIHKIIVNRLARKVEVDSIVVPLPF--SSQELSIEDSGSMYVITTPAGLI-IKWSHLTGI-IDIHFGFRFNlssyTEG 1689
Cdd:smart00216   70 ELNGDEIELKDDNGKVTVNGQQVSLPYktSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLsVQLPSKYRGK----TCG 145

                           170
                    ....*....|....*...
gi 530400098   1690 LCGICNEDPDDDLRMQNG 1707
Cdd:smart00216  146 LCGNFDGEPEDDFRTPDG 163
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 328-388 7.14e-13

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


:

Pssm-ID: 462584  Cd Length: 68  Bit Score: 65.48  E-value: 7.14e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400098   328 KCQILL-QFPFLSCHEYIDPYLYIASCVNDLCKTD-DDETYCRAATEYARACSHAGYPIQDWR 388
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGgDDECLCAALAAYARACQAAGVCIGDWR 63
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 685-749 3.73e-11

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: 60.47  E-value: 3.73e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400098   685 HCDVI-HQELFAPCHIYISPGLYYQLCRHDACKCG--SSCLCNALAHYAYLCGQHGVPIDFRTQISFC 749
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGgdDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2285-2361 9.66e-09

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


:

Pssm-ID: 214482  Cd Length: 82  Bit Score: 54.33  E-value: 9.66e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   2285 IRKQDCMSqSPINVASCDGKCPSATIYNINIESHlrFCKCCRENGVRNLSVPLYCSgNGTEIMYTLQEPIDCTCQWN 2361
Cdd:smart00041    8 ITYNGCTS-VTVKNAFCEGKCGSASSYSIQDVQH--SCSCCQPHKTKTRQVRLRCP-DGSTVKKTVMHIEECGCEPN 80
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 753-808 1.38e-06

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 1.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530400098  753 CQKGMLYHHCSSFCLHSCISLSSPEQCSDDCAEGCNCPEGkFYEDTLNFCVPIFHC 808
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEG-YVRNSGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 398-451 2.53e-05

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.84  E-value: 2.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530400098  398 CDDSFVHRDCISCCPPTCTFEKQCLGSNLHCLDGCYCPDGLVMD-NGTCISLENC 451
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 851-916 4.09e-05

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


:

Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.07  E-value: 4.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098  851 CPEGKEYFDCrfpdpelpagGVNCETTCANLAMNFTCTpsSPCISGCVCAPGMAEHR-GKCYVPESC 916
Cdd:cd19941     1 CPPNEVYSEC----------GSACPPTCANPNAPPPCT--KQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1814-1872 8.55e-03

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: 36.53  E-value: 8.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530400098 1814 CPEGKEYQPCVRPCEaRTCLNQWFYGH--TSClnlREDCVCKVGTILHrpHSAQCIPEKEC 1872
Cdd:cd19941     1 CPPNEVYSECGSACP-PTCANPNAPPPctKQC---VEGCFCPEGYVRN--SGGKCVPPSQC 55
 
Name Accession Description Interval E-value
beta-trefoil_ABD_OTOGL cd23401
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and ...
 1216-1369 1.14e-101

Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and similar proteins; OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOGL gene may cause hearing loss. OTOGL contains an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467811  Cd Length: 154  Bit Score: 322.58  E-value: 1.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1216 YYNEGLGEGPYMLASYGQSGLVLGANMTSRSVFCLPRSSVHTSLFFYFMITPGLFKEKVSSLALVSLESAERPNYFLYVH 1295
Cdd:cd23401     1 YYNQGLGEGPYTLSSYGQSDCVLGANLTSGEVFPLPKISAQGSTFFHFMITPGLFKDKASSLPVVSLESAERPNYFLCVH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400098 1296 DNDTLSLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYDDSEEFKHSSSFSIEE 1369
Cdd:cd23401    81 DNRTLRLEQWQPSSEFRRRATFFHHQGLWIPGYSSFELHSKKGFFITLTHSGAKASKYDDSEEFKTSSSFSIEE 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 131-276 1.32e-30

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: 119.40  E-value: 1.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   131 CKTWGQYHFETFDGIYYYFPGNCSYIFAKDCGDlEPRYTVWVHNSPKCLGSVYSCYRSISLFFSNQeEIRIY-GHEIKKN 209
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGVCLKSVTVIVGDL-EITLQkGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   210 GISLTLPQTIGQIFIEKL-ADYILVKTTFGFSL--AWDGISGIYLKLSEDHKGKSCGLCGNYNDIQSDDF 276
Cdd:pfam00094   79 GQKVSLPYKSDGGEVEILgSGFVVVDLSPGVGLqvDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDF 148
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 129-276 2.22e-30

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: 119.04  E-value: 2.22e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    129 GICKTWGQYHFETFDGIYYYFPGNCSYIFAKDCGDlEPRYTVWVHNSPKCLGSvySCYRSISLFFSNQEEIRIY-GHEIK 207
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS-EPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIELKDdNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400098    208 KNGISLTLPQT--IGQIFIEKLADYILVKTTFG-FSLAWDGISGIYLKLSEDHKGKSCGLCGNYNDIQSDDF 276
Cdd:smart00216   87 VNGQQVSLPYKtsDGSIQIRSSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 480-642 4.62e-30

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: 117.89  E-value: 4.62e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    480 WNCTEQDCPVQCSVVGDSHFTTFDGRHYSFIGMCQYILVKG-TGKDKFTITLQKAPCEQnlGLVCLQSITLILED----- 553
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcSSEPTFSVLLKNVPCGG--GATCLKSVKVELNGdeiel 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    554 -DFNKQVTLgrGGQILTSPNQGFnlNGIVEIQTLSSlFILLKTTFGLKILfAIDGE-RIYIQLTSAWKRRTLGLCGTFNG 631
Cdd:smart00216   79 kDDNGKVTV--NGQQVSLPYKTS--DGSIQIRSSGG-YLVVITSLGLIQV-TFDGLtLLSVQLPSKYRGKTCGLCGNFDG 152

                           170
                    ....*....|.
gi 530400098    632 NIRDDFLSPSG 642
Cdd:smart00216  153 EPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 947-1102 2.19e-29

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 115.96  E-value: 2.19e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    947 CTYYPCPAVCTIYGDRHYYSFDGLEYDYISDCQVFLIKSADDS-DISVIAQNKKCfDNDIVCSKSVLISVGDTEIYLNDT 1025
Cdd:smart00216    3 CTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC-GGGATCLKSVKVELNGDEIELKDD 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1026 PYKQKQSGF-----FLENKSTYQLWKAGYYIVVYFPEKDITILWDRKTTIHIKVGPQWKNKLSGLCGNFDKCTSNDMTTS 1100
Cdd:smart00216   82 NGKVTVNGQqvslpYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 530400098   1101 NN 1102
Cdd:smart00216  162 DG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 491-643 3.25e-28

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: 112.46  E-value: 3.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   491 CSVVGDSHFTTFDGRHYSFIGMCQYILVKGTGKD---KFTITLQKAPCEQNlgLVCLQSITLILEDDfnkQVTLGRGGQI 567
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGAS--GVCLKSVTVIVGDL---EITLQKGGTV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   568 LTSpNQGFNL---NGIVEIQTLSSLFILLKTTFGLKILFAIDG-ERIYIQLTSAWKRRTLGLCGTFNGNIRDDFLSPSGM 643
Cdd:pfam00094   76 LVN-GQKVSLpykSDGGEVEILGSGFVVVDLSPGVGLQVDGDGrGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 956-1103 1.82e-25

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: 104.37  E-value: 1.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   956 CTIYGDRHYYSFDGLEYDYISDCQVFLIKSAD-DSDISVIAQNKKC-FDNDIVCSKSVLISVGDTEIYLNDT-------- 1025
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSeEPDFSFSVTNKNCnGGASGVCLKSVTVIVGDLEITLQKGgtvlvngq 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1026 ----PYKqkqsgfflENKSTYQLWKAGYYIVVYFPEKDITILWDRKTTIHIKVGPQWKNKLSGLCGNFDKCTSNDMTTSN 1101
Cdd:pfam00094   81 kvslPYK--------SDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152


                   ..
gi 530400098  1102 NL 1103
Cdd:pfam00094  153 GT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1741-1810 2.86e-17

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: 78.15  E-value: 2.86e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400098   1741 TEHDCSQCIDLLNRR-IFIPCHDKVSPEDFCEKMWI---NYTYFWNYECDALSAYVALCNKFDICIQ-WRTPDYC 1810
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYdtcACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1137-1210 2.67e-16

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.45  E-value: 2.67e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   1137 FPYAKKECSILYSD--IFASCRNVIDVTSFAKNCHEDTCNCnlGGDCECLCTSIAAYAYKCCQEGISIH-WRSSTVC 1210
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1534-1707 1.24e-15

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: 76.67  E-value: 1.24e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1534 CCPEWECPCRCSMLSELSIITFDGNNAALYSMASYILVRIpgeiivahiekCSMNQNGNSLKKLAPSGRiSGLCFKKLNV 1613
Cdd:smart00216    2 CCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-----------CSSEPTFSVLLKNVPCGG-GATCLKSVKV 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1614 TTPIHKIIVNRLARKVEVDSIVVPLPF--SSQELSIEDSGSMYVITTPAGLI-IKWSHLTGI-IDIHFGFRFNlssyTEG 1689
Cdd:smart00216   70 ELNGDEIELKDDNGKVTVNGQQVSLPYktSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLsVQLPSKYRGK----TCG 145

                           170
                    ....*....|....*...
gi 530400098   1690 LCGICNEDPDDDLRMQNG 1707
Cdd:smart00216  146 LCGNFDGEPEDDFRTPDG 163
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1144-1210 2.66e-13

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 66.63  E-value: 2.66e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530400098  1144 CSIL-YSDIFASCRNVIDVTSFAKNCHEDTCNCnlGGDCECLCTSIAAYAYKCCQEGISI-HWRSSTVC 1210
Cdd:pfam08742    2 CGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1544-1708 3.96e-13

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: 68.94  E-value: 3.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1544 CSMLSELSIITFDGnnaALYSM---ASYILVRIPGE----IIVAHIEKCSMNQNGNslkklapsgrisglCFKKLNVTTP 1616
Cdd:pfam00094    1 CSVSGDPHYVTFDG---VKYTFpgtCTYVLAKDCSEepdfSFSVTNKNCNGGASGV--------------CLKSVTVIVG 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1617 IHKIIVNRlARKVEVDSIVVPLPFSS--QELSIEDSGSMYVITTPA-GLIIKWSHLtGIIDIHFGFRFNlsSYTEGLCGI 1693
Cdd:pfam00094   64 DLEITLQK-GGTVLVNGQKVSLPYKSdgGEVEILGSGFVVVDLSPGvGLQVDGDGR-GQLFVTLSPSYQ--GKTCGLCGN 139

                          170
                   ....*....|....*
gi 530400098  1694 CNEDPDDDLRMQNGT 1708
Cdd:pfam00094  140 YNGNQEDDFMTPDGT 154
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 328-388 7.14e-13

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 65.48  E-value: 7.14e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400098   328 KCQILL-QFPFLSCHEYIDPYLYIASCVNDLCKTD-DDETYCRAATEYARACSHAGYPIQDWR 388
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGgDDECLCAALAAYARACQAAGVCIGDWR 63
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 685-749 3.73e-11

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: 60.47  E-value: 3.73e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400098   685 HCDVI-HQELFAPCHIYISPGLYYQLCRHDACKCG--SSCLCNALAHYAYLCGQHGVPIDFRTQISFC 749
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGgdDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 328-389 1.40e-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: 1.40e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400098    328 KCQILL--QFPFLSCHEYIDPYLYIASCVNDLCKTDDDETY-CRAATEYARACSHAGYPIQDWRD 389
Cdd:smart00832    7 QCGILLspRGPFAACHSVVDPEPFFENCVYDTCACGGDCEClCDALAAYAAACAEAGVCISPWRT 71
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2285-2361 9.66e-09

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 54.33  E-value: 9.66e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   2285 IRKQDCMSqSPINVASCDGKCPSATIYNINIESHlrFCKCCRENGVRNLSVPLYCSgNGTEIMYTLQEPIDCTCQWN 2361
Cdd:smart00041    8 ITYNGCTS-VTVKNAFCEGKCGSASSYSIQDVQH--SCSCCQPHKTKTRQVRLRCP-DGSTVKKTVMHIEECGCEPN 80
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 686-750 4.56e-08

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: 51.96  E-value: 4.56e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    686 CDVIHQEL--FAPCHIYISPGLYYQLCRHDACKCG--SSCLCNALAHYAYLCGQHGVPI-DFRTQiSFCA 750
Cdd:smart00832    8 CGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGgdCECLCDALAAYAAACAEAGVCIsPWRTP-TFCP 76
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 753-808 1.38e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 1.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530400098  753 CQKGMLYHHCSSFCLHSCISLSSPEQCSDDCAEGCNCPEGkFYEDTLNFCVPIFHC 808
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEG-YVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 753-808 2.47e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 2.47e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530400098   753 CQKGMLYHHCSSFCLHSCISLSSPEQCSDDCAEGCNCPEGkFYEDTLNFCVPIFHC 808
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPG-FVRNSGGKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1751-1810 4.65e-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: 46.22  E-value: 4.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400098  1751 LLNRRIFIPCHDKVSPEDFCEKMWINYTYFWNYE---CDALSAYVALCNKFDICIQ-WRTPDYC 1810
Cdd:pfam08742    5 LSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDeclCAALAAYARACQAAGVCIGdWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 398-451 2.53e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.84  E-value: 2.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530400098  398 CDDSFVHRDCISCCPPTCTFEKQCLGSNLHCLDGCYCPDGLVMD-NGTCISLENC 451
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 851-916 4.09e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.07  E-value: 4.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098  851 CPEGKEYFDCrfpdpelpagGVNCETTCANLAMNFTCTpsSPCISGCVCAPGMAEHR-GKCYVPESC 916
Cdd:cd19941     1 CPPNEVYSEC----------GSACPPTCANPNAPPPCT--KQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 403-451 5.12e-05

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 42.76  E-value: 5.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 530400098   403 VHRDCISCCPPTCTFEKQCLGSNLHCLDGCYCPDGLVMD-NGTCISLENC 451
Cdd:pfam01826    6 VYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 851-916 3.07e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 40.45  E-value: 3.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   851 CPEGKEYFDCrfpdpelpagGVNCETTCANLAMNFTCTpsSPCISGCVCAPGMAEHR-GKCYVPESC 916
Cdd:pfam01826    1 CPANEVYSEC----------GSACPPTCANLSPPDVCP--EPCVEGCVCPPGFVRNSgGKCVPPSDC 55
AbfB pfam05270
Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal ...
 1280-1367 3.68e-04

Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal alpha-L-arabinofuranosidase B proteins. L-Arabinose is a constituent of plant-cell-wall poly-saccharides. It is found in a polymeric form in L-arabinan, in which the backbone is formed by 1,5-a- linked l-arabinose residues that can be branched via 1,2-a- and 1,3-a-linked l-arabinofuranose side chains. AbfB hydrolyses 1,5-a, 1,3-a and 1,2-a linkages in both oligosaccharides and polysaccharides, which contain terminal non-reducing l-arabinofuranoses in side chains.


Pssm-ID: 428401  Cd Length: 137  Bit Score: 42.91  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1280 VSLESAERPNYFLyVHDNDTLSLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYDDSEEF 1359
Cdd:pfam05270   51 VSFESVNFPGSYL-RHYNFRLRLDANDGSALFREDATFCPRAGLGDSGSVSLESYNYPGRYIRHYNYELYIDPNGGTASF 129


                   ....*...
gi 530400098  1360 KHSSSFSI 1367
Cdd:pfam05270  130 RADATFVV 137
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1814-1872 8.55e-03

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: 36.53  E-value: 8.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530400098 1814 CPEGKEYQPCVRPCEaRTCLNQWFYGH--TSClnlREDCVCKVGTILHrpHSAQCIPEKEC 1872
Cdd:cd19941     1 CPPNEVYSECGSACP-PTCANPNAPPPctKQC---VEGCFCPEGYVRN--SGGKCVPPSQC 55
 
Name Accession Description Interval E-value
beta-trefoil_ABD_OTOGL cd23401
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and ...
 1216-1369 1.14e-101

Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and similar proteins; OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOGL gene may cause hearing loss. OTOGL contains an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467811  Cd Length: 154  Bit Score: 322.58  E-value: 1.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1216 YYNEGLGEGPYMLASYGQSGLVLGANMTSRSVFCLPRSSVHTSLFFYFMITPGLFKEKVSSLALVSLESAERPNYFLYVH 1295
Cdd:cd23401     1 YYNQGLGEGPYTLSSYGQSDCVLGANLTSGEVFPLPKISAQGSTFFHFMITPGLFKDKASSLPVVSLESAERPNYFLCVH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400098 1296 DNDTLSLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYDDSEEFKHSSSFSIEE 1369
Cdd:cd23401    81 DNRTLRLEQWQPSSEFRRRATFFHHQGLWIPGYSSFELHSKKGFFITLTHSGAKASKYDDSEEFKTSSSFSIEE 154
beta-trefoil_ABD_OTOG-like cd23398
Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The ...
 1221-1367 1.71e-63

Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The OTOG family includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOG or OTOGL gene may cause hearing loss. Members of this family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467808  Cd Length: 143  Bit Score: 212.95  E-value: 1.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1221 LGEGPYMLASYGQSGLVLGANMTSRSVFCLPRSSVhTSLFFYFMITPGLFKEKVSslaLVSLESAERPNYFLYVHDNDTL 1300
Cdd:cd23398     1 LGEGPYKLSSYNYPGYLLGANDDSGVVSLIPTENS-PSGGVSFMVTPGLNGDKAN---LVSFESAERPNYFLCVQANGTL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098 1301 SLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYDDSEEFKHSSSFSI 1367
Cdd:cd23398    77 KLVKWENSALFRNAASFFLRQGTWIPGYVAFESTSKPGYFIRHSNSSLKLQKYDHTEEFRRSSSFKL 143
beta-trefoil_ABD_OTOG cd23400
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar ...
 1216-1365 4.02e-43

Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar proteins; OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. Mutations in the OTOG gene may cause hearing loss. OTOG contains an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467810  Cd Length: 152  Bit Score: 154.93  E-value: 4.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1216 YYNEGLGEGPYMLASYGQSGLVLGANMTSRSVFCLPRSSVHTSLFFYFMITPGLFKEKVSSLALVSLESAERPNYFLYVH 1295
Cdd:cd23400     1 YFNKALGKGPYKLVTYLAGGALLAANKTGGLVFPVRGEDSVDEDLISFMLTPGLYKPKAHDSSLVSFEAADRPNYFLHVG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1296 DNDTLSLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYDDSEEFKHSSSF 1365
Cdd:cd23400    81 ANGSLRLAKWEDSEEFQDRATFVLHRDTWIPGYDALESFAKPGFFLHFMGSALQLQKYEHTERFRRATLF 150
beta-trefoil_ABD_ABFB-like cd23265
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
 1221-1365 4.15e-33

Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467807  Cd Length: 135  Bit Score: 125.47  E-value: 4.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1221 LGEGPYMLASYGQSGLVLGANMTSRSVFCLPRSSVHTslfFYFMITPGLFKEkvsslALVSLESAERPNYFLyVHDNDTL 1300
Cdd:cd23265     1 DGGTPVRLRSASDPGYYIRHDGGSGSVTSDDDDSAED---AFFRVVPGLAGE-----GTVSFESVDKPGYYL-RHRGGEL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400098 1301 SLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYdDSEEFKHSSSF 1365
Cdd:cd23265    72 RLEKNDGSAAFREDATFRPRPGLADPGGVSFESVNYPGYYLRHRNNRLVLGKV-DSTAFKEDATF 135
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 131-276 1.32e-30

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: 119.40  E-value: 1.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   131 CKTWGQYHFETFDGIYYYFPGNCSYIFAKDCGDlEPRYTVWVHNSPKCLGSVYSCYRSISLFFSNQeEIRIY-GHEIKKN 209
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSE-EPDFSFSVTNKNCNGGASGVCLKSVTVIVGDL-EITLQkGGTVLVN 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   210 GISLTLPQTIGQIFIEKL-ADYILVKTTFGFSL--AWDGISGIYLKLSEDHKGKSCGLCGNYNDIQSDDF 276
Cdd:pfam00094   79 GQKVSLPYKSDGGEVEILgSGFVVVDLSPGVGLqvDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDF 148
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 129-276 2.22e-30

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: 119.04  E-value: 2.22e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    129 GICKTWGQYHFETFDGIYYYFPGNCSYIFAKDCGDlEPRYTVWVHNSPKCLGSvySCYRSISLFFSNQEEIRIY-GHEIK 207
Cdd:smart00216   10 PTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSS-EPTFSVLLKNVPCGGGA--TCLKSVKVELNGDEIELKDdNGKVT 86

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400098    208 KNGISLTLPQT--IGQIFIEKLADYILVKTTFG-FSLAWDGISGIYLKLSEDHKGKSCGLCGNYNDIQSDDF 276
Cdd:smart00216   87 VNGQQVSLPYKtsDGSIQIRSSGGYLVVITSLGlIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDF 158
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 480-642 4.62e-30

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: 117.89  E-value: 4.62e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    480 WNCTEQDCPVQCSVVGDSHFTTFDGRHYSFIGMCQYILVKG-TGKDKFTITLQKAPCEQnlGLVCLQSITLILED----- 553
Cdd:smart00216    1 WCCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDcSSEPTFSVLLKNVPCGG--GATCLKSVKVELNGdeiel 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    554 -DFNKQVTLgrGGQILTSPNQGFnlNGIVEIQTLSSlFILLKTTFGLKILfAIDGE-RIYIQLTSAWKRRTLGLCGTFNG 631
Cdd:smart00216   79 kDDNGKVTV--NGQQVSLPYKTS--DGSIQIRSSGG-YLVVITSLGLIQV-TFDGLtLLSVQLPSKYRGKTCGLCGNFDG 152

                           170
                    ....*....|.
gi 530400098    632 NIRDDFLSPSG 642
Cdd:smart00216  153 EPEDDFRTPDG 163
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 947-1102 2.19e-29

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


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 115.96  E-value: 2.19e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    947 CTYYPCPAVCTIYGDRHYYSFDGLEYDYISDCQVFLIKSADDS-DISVIAQNKKCfDNDIVCSKSVLISVGDTEIYLNDT 1025
Cdd:smart00216    3 CTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCSSEpTFSVLLKNVPC-GGGATCLKSVKVELNGDEIELKDD 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1026 PYKQKQSGF-----FLENKSTYQLWKAGYYIVVYFPEKDITILWDRKTTIHIKVGPQWKNKLSGLCGNFDKCTSNDMTTS 1100
Cdd:smart00216   82 NGKVTVNGQqvslpYKTSDGSIQIRSSGGYLVVITSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161


                    ..
gi 530400098   1101 NN 1102
Cdd:smart00216  162 DG 163
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 491-643 3.25e-28

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: 112.46  E-value: 3.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   491 CSVVGDSHFTTFDGRHYSFIGMCQYILVKGTGKD---KFTITLQKAPCEQNlgLVCLQSITLILEDDfnkQVTLGRGGQI 567
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEpdfSFSVTNKNCNGGAS--GVCLKSVTVIVGDL---EITLQKGGTV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   568 LTSpNQGFNL---NGIVEIQTLSSLFILLKTTFGLKILFAIDG-ERIYIQLTSAWKRRTLGLCGTFNGNIRDDFLSPSGM 643
Cdd:pfam00094   76 LVN-GQKVSLpykSDGGEVEILGSGFVVVDLSPGVGLQVDGDGrGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPDGT 154
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 956-1103 1.82e-25

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: 104.37  E-value: 1.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   956 CTIYGDRHYYSFDGLEYDYISDCQVFLIKSAD-DSDISVIAQNKKC-FDNDIVCSKSVLISVGDTEIYLNDT-------- 1025
Cdd:pfam00094    1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSeEPDFSFSVTNKNCnGGASGVCLKSVTVIVGDLEITLQKGgtvlvngq 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1026 ----PYKqkqsgfflENKSTYQLWKAGYYIVVYFPEKDITILWDRKTTIHIKVGPQWKNKLSGLCGNFDKCTSNDMTTSN 1101
Cdd:pfam00094   81 kvslPYK--------SDGGEVEILGSGFVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152


                   ..
gi 530400098  1102 NL 1103
Cdd:pfam00094  153 GT 154
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1741-1810 2.86e-17

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: 78.15  E-value: 2.86e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400098   1741 TEHDCSQCIDLLNRR-IFIPCHDKVSPEDFCEKMWI---NYTYFWNYECDALSAYVALCNKFDICIQ-WRTPDYC 1810
Cdd:smart00832    1 KYYACSQCGILLSPRgPFAACHSVVDPEPFFENCVYdtcACGGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 1137-1210 2.67e-16

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


Pssm-ID: 214843  Cd Length: 76  Bit Score: 75.45  E-value: 2.67e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   1137 FPYAKKECSILYSD--IFASCRNVIDVTSFAKNCHEDTCNCnlGGDCECLCTSIAAYAYKCCQEGISIH-WRSSTVC 1210
Cdd:smart00832    1 KYYACSQCGILLSPrgPFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCISpWRTPTFC 75
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 1534-1707 1.24e-15

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: 76.67  E-value: 1.24e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1534 CCPEWECPCRCSMLSELSIITFDGNNAALYSMASYILVRIpgeiivahiekCSMNQNGNSLKKLAPSGRiSGLCFKKLNV 1613
Cdd:smart00216    2 CCTQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQD-----------CSSEPTFSVLLKNVPCGG-GATCLKSVKV 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098   1614 TTPIHKIIVNRLARKVEVDSIVVPLPF--SSQELSIEDSGSMYVITTPAGLI-IKWSHLTGI-IDIHFGFRFNlssyTEG 1689
Cdd:smart00216   70 ELNGDEIELKDDNGKVTVNGQQVSLPYktSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLsVQLPSKYRGK----TCG 145

                           170
                    ....*....|....*...
gi 530400098   1690 LCGICNEDPDDDLRMQNG 1707
Cdd:smart00216  146 LCGNFDGEPEDDFRTPDG 163
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1144-1210 2.66e-13

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 66.63  E-value: 2.66e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530400098  1144 CSIL-YSDIFASCRNVIDVTSFAKNCHEDTCNCnlGGDCECLCTSIAAYAYKCCQEGISI-HWRSSTVC 1210
Cdd:pfam08742    2 CGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSC--GGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 1544-1708 3.96e-13

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: 68.94  E-value: 3.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1544 CSMLSELSIITFDGnnaALYSM---ASYILVRIPGE----IIVAHIEKCSMNQNGNslkklapsgrisglCFKKLNVTTP 1616
Cdd:pfam00094    1 CSVSGDPHYVTFDG---VKYTFpgtCTYVLAKDCSEepdfSFSVTNKNCNGGASGV--------------CLKSVTVIVG 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1617 IHKIIVNRlARKVEVDSIVVPLPFSS--QELSIEDSGSMYVITTPA-GLIIKWSHLtGIIDIHFGFRFNlsSYTEGLCGI 1693
Cdd:pfam00094   64 DLEITLQK-GGTVLVNGQKVSLPYKSdgGEVEILGSGFVVVDLSPGvGLQVDGDGR-GQLFVTLSPSYQ--GKTCGLCGN 139

                          170
                   ....*....|....*
gi 530400098  1694 CNEDPDDDLRMQNGT 1708
Cdd:pfam00094  140 YNGNQEDDFMTPDGT 154
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 328-388 7.14e-13

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


Pssm-ID: 462584  Cd Length: 68  Bit Score: 65.48  E-value: 7.14e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400098   328 KCQILL-QFPFLSCHEYIDPYLYIASCVNDLCKTD-DDETYCRAATEYARACSHAGYPIQDWR 388
Cdd:pfam08742    1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDMCSCGgDDECLCAALAAYARACQAAGVCIGDWR 63
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 685-749 3.73e-11

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: 60.47  E-value: 3.73e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400098   685 HCDVI-HQELFAPCHIYISPGLYYQLCRHDACKCG--SSCLCNALAHYAYLCGQHGVPIDFRTQISFC 749
Cdd:pfam08742    1 KCGLLsDSGPFAPCHSVVDPEPYFEACVYDMCSCGgdDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 328-389 1.40e-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: 1.40e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400098    328 KCQILL--QFPFLSCHEYIDPYLYIASCVNDLCKTDDDETY-CRAATEYARACSHAGYPIQDWRD 389
Cdd:smart00832    7 QCGILLspRGPFAACHSVVDPEPFFENCVYDTCACGGDCEClCDALAAYAAACAEAGVCISPWRT 71
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 2285-2361 9.66e-09

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 54.33  E-value: 9.66e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   2285 IRKQDCMSqSPINVASCDGKCPSATIYNINIESHlrFCKCCRENGVRNLSVPLYCSgNGTEIMYTLQEPIDCTCQWN 2361
Cdd:smart00041    8 ITYNGCTS-VTVKNAFCEGKCGSASSYSIQDVQH--SCSCCQPHKTKTRQVRLRCP-DGSTVKKTVMHIEECGCEPN 80
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 686-750 4.56e-08

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: 51.96  E-value: 4.56e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098    686 CDVIHQEL--FAPCHIYISPGLYYQLCRHDACKCG--SSCLCNALAHYAYLCGQHGVPI-DFRTQiSFCA 750
Cdd:smart00832    8 CGILLSPRgpFAACHSVVDPEPFFENCVYDTCACGgdCECLCDALAAYAAACAEAGVCIsPWRTP-TFCP 76
beta-trefoil_ABD_ABFB cd23399
Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF ...
 1263-1365 7.52e-07

Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF B) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. The family also includes Hungateiclostridium thermocellum anti-sigma-I factor RsgI5. It negatively regulates SigI5 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI5 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI5. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467809  Cd Length: 138  Bit Score: 50.67  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098 1263 FMITPGLfkekvSSLALVSLESAERPNYFLyVHDNDTLSLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFII 1342
Cdd:cd23399    42 FKVVPGL-----ADSGCVSFESVNYPGYYL-RHYNFRLRLDKNDGSALFKEDATFCPRPGLADGGGVSFRSYNYPGRYIR 115

                          90       100
                  ....*....|....*....|...
gi 530400098 1343 FTDSSVKASKYDDSEEFKHSSSF 1365
Cdd:cd23399   116 HRNFELWLDPNDGTALFRQDATF 138
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 753-808 1.38e-06

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 47.31  E-value: 1.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530400098  753 CQKGMLYHHCSSFCLHSCISLSSPEQCSDDCAEGCNCPEGkFYEDTLNFCVPIFHC 808
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEG-YVRNSGGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 753-808 2.47e-06

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 46.61  E-value: 2.47e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530400098   753 CQKGMLYHHCSSFCLHSCISLSSPEQCSDDCAEGCNCPEGkFYEDTLNFCVPIFHC 808
Cdd:pfam01826    1 CPANEVYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPG-FVRNSGGKCVPPSDC 55
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 1751-1810 4.65e-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: 46.22  E-value: 4.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400098  1751 LLNRRIFIPCHDKVSPEDFCEKMWINYTYFWNYE---CDALSAYVALCNKFDICIQ-WRTPDYC 1810
Cdd:pfam08742    5 LSDSGPFAPCHSVVDPEPYFEACVYDMCSCGGDDeclCAALAAYARACQAAGVCIGdWRTPTFC 68
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 398-451 2.53e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.84  E-value: 2.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530400098  398 CDDSFVHRDCISCCPPTCTFEKQCLGSNLHCLDGCYCPDGLVMD-NGTCISLENC 451
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANPNAPPPCTKQCVEGCFCPEGYVRNsGGKCVPPSQC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 851-916 4.09e-05

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


Pssm-ID: 410995  Cd Length: 55  Bit Score: 43.07  E-value: 4.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098  851 CPEGKEYFDCrfpdpelpagGVNCETTCANLAMNFTCTpsSPCISGCVCAPGMAEHR-GKCYVPESC 916
Cdd:cd19941     1 CPPNEVYSEC----------GSACPPTCANPNAPPPCT--KQCVEGCFCPEGYVRNSgGKCVPPSQC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 403-451 5.12e-05

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 42.76  E-value: 5.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 530400098   403 VHRDCISCCPPTCTFEKQCLGSNLHCLDGCYCPDGLVMD-NGTCISLENC 451
Cdd:pfam01826    6 VYSECGSACPPTCANLSPPDVCPEPCVEGCVCPPGFVRNsGGKCVPPSDC 55
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 851-916 3.07e-04

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


Pssm-ID: 460351  Cd Length: 55  Bit Score: 40.45  E-value: 3.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400098   851 CPEGKEYFDCrfpdpelpagGVNCETTCANLAMNFTCTpsSPCISGCVCAPGMAEHR-GKCYVPESC 916
Cdd:pfam01826    1 CPANEVYSEC----------GSACPPTCANLSPPDVCP--EPCVEGCVCPPGFVRNSgGKCVPPSDC 55
AbfB pfam05270
Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal ...
 1280-1367 3.68e-04

Alpha-L-arabinofuranosidase B (ABFB) domain; This family consists of several fungal alpha-L-arabinofuranosidase B proteins. L-Arabinose is a constituent of plant-cell-wall poly-saccharides. It is found in a polymeric form in L-arabinan, in which the backbone is formed by 1,5-a- linked l-arabinose residues that can be branched via 1,2-a- and 1,3-a-linked l-arabinofuranose side chains. AbfB hydrolyses 1,5-a, 1,3-a and 1,2-a linkages in both oligosaccharides and polysaccharides, which contain terminal non-reducing l-arabinofuranoses in side chains.


Pssm-ID: 428401  Cd Length: 137  Bit Score: 42.91  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400098  1280 VSLESAERPNYFLyVHDNDTLSLELWEANSAFHRRATFFHHQGLWIPGYSAFELYSKKGFFIIFTDSSVKASKYDDSEEF 1359
Cdd:pfam05270   51 VSFESVNFPGSYL-RHYNFRLRLDANDGSALFREDATFCPRAGLGDSGSVSLESYNYPGRYIRHYNYELYIDPNGGTASF 129


                   ....*...
gi 530400098  1360 KHSSSFSI 1367
Cdd:pfam05270  130 RADATFVV 137
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 1814-1872 8.55e-03

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: 36.53  E-value: 8.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530400098 1814 CPEGKEYQPCVRPCEaRTCLNQWFYGH--TSClnlREDCVCKVGTILHrpHSAQCIPEKEC 1872
Cdd:cd19941     1 CPPNEVYSECGSACP-PTCANPNAPPPctKQC---VEGCFCPEGYVRN--SGGKCVPPSQC 55
 
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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