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Conserved domains on  [gi|51558724|ref|NP_112217|]
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A disintegrin and metalloproteinase with thrombospondin motifs 12 isoform 1 preproprotein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 246-453 1.84e-108

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


:

Pssm-ID: 239801  Cd Length: 207  Bit Score: 342.68  E-value: 1.84e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  246 RWVETLVVADTKMIEYHGSENVESYILTIMNMVTGLFHNPSIGNAIHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQ 325
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  326 KSINPKSDLNPVHHDVAVLLTRKDICAGfNRPCETLGLSHLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGK 405
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 51558724  406 ENDCEPVGRHPYIMSRQLQYDPTPLTWSKCSEEYITRFLDRGWGFCLD 453
Cdd:cd04273  160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 703-812 2.47e-34

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 127.69  E-value: 2.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    703 TVRKMFKQKEGSGYVDIGLIPKGARDIRVMEIEGAGNFLAIRSeDPEKYYLNGGFIIQ-WNGNYKLAGTVFQYDR-KGDL 780
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRsLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 51558724    781 EKLMATGPTNESVWIQLLFQ---VTNPGIKYEYTI 812
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 54-195 7.29e-33

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 124.35  E-value: 7.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724     54 VVGPVRVDASghflsyglhypitssRRKRDLDGSE---DWVYYRISHEEKDLFFNLTVNQGFLSNSYIMEKRYGNLSHVK 130
Cdd:pfam01562    2 VVIPVRLDPS---------------RRRRSLASEStylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVE 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    131 MMASSAPLCHLSGTVlqQGTRVGTAALSACHGLTGFFQLPHGDFFIEPVKKHPLVEGGyHPHIVY 195
Cdd:pfam01562   67 SPPVQTDHCYYQGHV--EGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG-HPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 468-532 1.24e-22

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.79  E-value: 1.24e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51558724    468 PGVIYDVHHQCQLQYGPNATFCQEV-ENVCQTLWCSVKGF--CRSKLDAAADGTQCGEKKWCMAGKCI 532
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGstCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 545-596 2.29e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 2.29e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 51558724     545 WGRWSPWSHCSRTCGAGVQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPC 596
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1475-1531 3.28e-15

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 71.33  E-value: 3.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51558724   1475 WATGNWDLCSTSCGGGFQKRTVQCVPSEGNKTEDQDQclCDHKPRPPEFKKCNQQAC 1531
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE--CSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1427-1472 4.03e-13

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.17  E-value: 4.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724   1427 WQVEPWSQCSRSCGGGVQERGVFC---------PGGLCDWTKRPTSTMSCNEHLC 1472
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-996 5.97e-12

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 5.97e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    948 WTVGNWSECSVSCGGGVRIRSVTCAK------NHDEPCDVTRKPNSRALCGLQQC 996
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsiVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 603-701 8.33e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 63.57  E-value: 8.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    603 FRQMQCSEFDTVPYKNE-----LYHW---FPIFNPAHPCELYCRPIDGQFSEKMLDAVIDGTPCFEGG----NSRNVCIN 670
Cdd:pfam19236    5 FMSQQCARTDGQPLRSSpggasFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredGTLSLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 51558724    671 GICKMVGCDYEIDSNATEDRCGVCLGDGSSC 701
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 828-882 2.90e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.90e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724    828 WQYGHWTECSVTCGTGIRRQTAHCIKK-GRGMVKATFCDPETQPNgRQKKCHEKAC 882
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgGGSIVPDSECSAQKKPP-ETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1317-1365 2.35e-09

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.77  E-value: 2.35e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724   1317 WIVGNWSECSTTCGLGAYWRRVEC------STQMDSDCAAIQRPDPAKRCHLRPC 1365
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1368-1424 5.09e-08

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 50.91  E-value: 5.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51558724   1368 WKVGNWSKCSRNCSGGFKIREIQCVDSRDHRNLRPFHCQFLAgiPPPLSMSCNPEPC 1424
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQK--KPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 886-940 5.09e-07

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 47.83  E-value: 5.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    886 WWAGEWEACSATCGPhGEKKRTVLCIQTMvsDEQALPPTDCQHLLKPKTLLSCNR 940
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQKG--GGSIVPDSECSAQKKPPETQSCNL 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 246-453 1.84e-108

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 342.68  E-value: 1.84e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  246 RWVETLVVADTKMIEYHGSENVESYILTIMNMVTGLFHNPSIGNAIHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQ 325
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  326 KSINPKSDLNPVHHDVAVLLTRKDICAGfNRPCETLGLSHLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGK 405
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 51558724  406 ENDCEPVGRHPYIMSRQLQYDPTPLTWSKCSEEYITRFLDRGWGFCLD 453
Cdd:cd04273  160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 703-812 2.47e-34

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 127.69  E-value: 2.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    703 TVRKMFKQKEGSGYVDIGLIPKGARDIRVMEIEGAGNFLAIRSeDPEKYYLNGGFIIQ-WNGNYKLAGTVFQYDR-KGDL 780
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRsLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 51558724    781 EKLMATGPTNESVWIQLLFQ---VTNPGIKYEYTI 812
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 54-195 7.29e-33

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 124.35  E-value: 7.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724     54 VVGPVRVDASghflsyglhypitssRRKRDLDGSE---DWVYYRISHEEKDLFFNLTVNQGFLSNSYIMEKRYGNLSHVK 130
Cdd:pfam01562    2 VVIPVRLDPS---------------RRRRSLASEStylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVE 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    131 MMASSAPLCHLSGTVlqQGTRVGTAALSACHGLTGFFQLPHGDFFIEPVKKHPLVEGGyHPHIVY 195
Cdd:pfam01562   67 SPPVQTDHCYYQGHV--EGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG-HPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 246-456 8.06e-29

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 115.09  E-value: 8.06e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    246 RWVETLVVADTKMIEYHGS--ENVESYILTIMNMVTglfhnpSIGNAIHIVVVrLILLE--EEEQGLKIVHHAEKTLSSF 321
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwTDEDKIDVSGDANDTLRNF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    322 CKWQKSINPKsdlnPVHHDVAVLLTRKDIcagfnrPCETLGLSHLSGMCQPHRSCNINED---SGLPLAFTIAHELGHSF 398
Cdd:pfam01421   74 LKWRQEYLKK----RKPHDVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNL 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51558724    399 GIQHD--GKENDCEPVGR---HPYIMSrqlqydPTPLTWSKCSEEYITRFLDRGWGFCLDDIP 456
Cdd:pfam01421  144 GMQHDdfNGGCKCPPGGGcimNPSAGS------SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 468-532 1.24e-22

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.79  E-value: 1.24e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51558724    468 PGVIYDVHHQCQLQYGPNATFCQEV-ENVCQTLWCSVKGF--CRSKLDAAADGTQCGEKKWCMAGKCI 532
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGstCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 545-596 2.29e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 2.29e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 51558724     545 WGRWSPWSHCSRTCGAGVQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPC 596
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1475-1531 3.28e-15

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 71.33  E-value: 3.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51558724   1475 WATGNWDLCSTSCGGGFQKRTVQCVPSEGNKTEDQDQclCDHKPRPPEFKKCNQQAC 1531
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE--CSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1427-1472 4.03e-13

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.17  E-value: 4.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724   1427 WQVEPWSQCSRSCGGGVQERGVFC---------PGGLCDWTKRPTSTMSCNEHLC 1472
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-996 5.97e-12

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 5.97e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    948 WTVGNWSECSVSCGGGVRIRSVTCAK------NHDEPCDVTRKPNSRALCGLQQC 996
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsiVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 603-701 8.33e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 63.57  E-value: 8.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    603 FRQMQCSEFDTVPYKNE-----LYHW---FPIFNPAHPCELYCRPIDGQFSEKMLDAVIDGTPCFEGG----NSRNVCIN 670
Cdd:pfam19236    5 FMSQQCARTDGQPLRSSpggasFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredGTLSLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 51558724    671 GICKMVGCDYEIDSNATEDRCGVCLGDGSSC 701
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 828-882 2.90e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.90e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724    828 WQYGHWTECSVTCGTGIRRQTAHCIKK-GRGMVKATFCDPETQPNgRQKKCHEKAC 882
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgGGSIVPDSECSAQKKPP-ETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1317-1365 2.35e-09

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.77  E-value: 2.35e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724   1317 WIVGNWSECSTTCGLGAYWRRVEC------STQMDSDCAAIQRPDPAKRCHLRPC 1365
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggSIVPDSECSAQKKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
548-596 5.04e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 5.04e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51558724    548 WSPWSHCSRTCGAGVQSAERLCNNPEPkfGGKYCTGERKRYRLCNVHPC 596
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1368-1424 5.09e-08

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 50.91  E-value: 5.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51558724   1368 WKVGNWSKCSRNCSGGFKIREIQCVDSRDHRNLRPFHCQFLAgiPPPLSMSCNPEPC 1424
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQK--KPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 886-940 5.09e-07

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 47.83  E-value: 5.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    886 WWAGEWEACSATCGPhGEKKRTVLCIQTMvsDEQALPPTDCQHLLKPKTLLSCNR 940
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQKG--GGSIVPDSECSAQKKPPETQSCNL 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 946-997 3.72e-05

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.57  E-value: 3.72e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724     946 SDWtvGNWSECSVSCGGGVRIRSVTC----AKNHDEPCDVTRKpnSRALCGLQQCP 997
Cdd:smart00209    2 SEW--SEWSPCSVTCGGGVQTRTRSCcsppPQNGGGPCTGEDV--ETRACNEQPCP 53
ACR smart00608
ADAM Cysteine-Rich Domain;
515-676 8.47e-05

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 44.27  E-value: 8.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724     515 ADGTQCGEKKW-CMAGKCITVGKkpesipggwgrwspwsHCSRTCGAGVQSAERLC----NNPEPKFGgkYCTGERKRYR 589
Cdd:smart00608    1 QDGTPCDNGQGyCYNGRCPTRDN----------------QCQALFGPGAKVAPDSCyeelNTKGDRFG--NCGRENGTYI 62

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724     590 lcnvhPCRSEAPTFRQMQCSEFDTVPYKNELY--HWFPIFNpahpceLYCRPIDGQFSEKMLDA-VIDGTPCFEGgnsrN 666
Cdd:smart00608   63 -----PCAPEDVKCGKLQCTNVSELPLLGEHAtvIYSNIGG------LVCWSLDYHLGTDPDIGmVKDGTKCGPG----K 127

                           170
                    ....*....|
gi 51558724     667 VCINGICKMV 676
Cdd:smart00608  128 VCINGQCVDV 137
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1474-1531 1.32e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.03  E-value: 1.32e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 51558724    1474 HWATGNWDLCSTSCGGGFQKRTVQCVpsegNKTEDQDQCLCDHKprPPEFKKCNQQAC 1531
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCC----SPPPQNGGGPCTGE--DVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 828-883 3.72e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.88  E-value: 3.72e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724     828 WQYGHWTECSVTCGTGIRRQTAHCIkKGRGMVKATFCDPetqPNGRQKKCHEKACP 883
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPCTG---EDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1427-1472 1.36e-03

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 1.36e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 51558724    1427 WQVEPWSQCSRSCGGGVQERGVFC-------PGGLCdwTKRPTSTMSCNEHLC 1472
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCcspppqnGGGPC--TGEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 246-453 1.84e-108

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 342.68  E-value: 1.84e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  246 RWVETLVVADTKMIEYHGSENVESYILTIMNMVTGLFHNPSIGNAIHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQ 325
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  326 KSINPKSDLNPVHHDVAVLLTRKDICAGfNRPCETLGLSHLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGK 405
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 51558724  406 ENDCEPVGRHPYIMSRQLQYDPTPLTWSKCSEEYITRFLDRGWGFCLD 453
Cdd:cd04273  160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 703-812 2.47e-34

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 127.69  E-value: 2.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    703 TVRKMFKQKEGSGYVDIGLIPKGARDIRVMEIEGAGNFLAIRSeDPEKYYLNGGFIIQ-WNGNYKLAGTVFQYDR-KGDL 780
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRsLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 51558724    781 EKLMATGPTNESVWIQLLFQ---VTNPGIKYEYTI 812
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 246-452 2.99e-34

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 130.43  E-value: 2.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  246 RWVETLVVADTKMIEYHGS--ENVESYILTIMNMVTGLFHNpsignaIHIVVVrLILLE---EEEQgLKIVHHAEKTLSS 320
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP------LNIRVV-LVGLEiwtDKDK-ISVSGDAGETLNR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  321 FCKWQKSinpksDLNP-VHHDVAVLLTRKDicagFNRPceTLGLSHLSGMCQPHRSCNINEDSG---LPLAFTIAHELGH 396
Cdd:cd04269   73 FLDWKRS-----NLLPrKPHDNAQLLTGRD----FDGN--TVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGH 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724  397 SFGIQHDGKENDCepvGRHPYIMSRQLQYDPTplTWSKCSEEYITRFLDRGWGFCL 452
Cdd:cd04269  142 NLGMEHDDGGCTC---GRSTCIMAPSPSSLTD--AFSNCSYEDYQKFLSRGGGQCL 192
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 246-445 1.79e-33

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 128.31  E-value: 1.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  246 RWVETLVVADTKMIEYHGS--ENVESYILTIMNMVTGLFHNPSIGNAIHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCK 323
Cdd:cd04267    1 REIELVVVADHRMVSYFNSdeNILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  324 WQKSinpksdlNPVHHDVAVLLTRKDICAgfnrpCETLGLSHLSGMCQPHRSCNINEDSGLPL--AFTIAHELGHSFGIQ 401
Cdd:cd04267   81 WRAE-------GPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 51558724  402 HDGK-ENDCEPVGRHPYIMSRQLQyDPTPLTWSKCSEEYITRFLD 445
Cdd:cd04267  149 HDGGdELAFECDGGGNYIMAPVDS-GLNSYRFSQCSIGSIREFLD 192
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 54-195 7.29e-33

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 124.35  E-value: 7.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724     54 VVGPVRVDASghflsyglhypitssRRKRDLDGSE---DWVYYRISHEEKDLFFNLTVNQGFLSNSYIMEKRYGNLSHVK 130
Cdd:pfam01562    2 VVIPVRLDPS---------------RRRRSLASEStylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVE 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    131 MMASSAPLCHLSGTVlqQGTRVGTAALSACHGLTGFFQLPHGDFFIEPVKKHPLVEGGyHPHIVY 195
Cdd:pfam01562   67 SPPVQTDHCYYQGHV--EGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG-HPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 246-456 8.06e-29

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 115.09  E-value: 8.06e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    246 RWVETLVVADTKMIEYHGS--ENVESYILTIMNMVTglfhnpSIGNAIHIVVVrLILLE--EEEQGLKIVHHAEKTLSSF 321
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwTDEDKIDVSGDANDTLRNF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    322 CKWQKSINPKsdlnPVHHDVAVLLTRKDIcagfnrPCETLGLSHLSGMCQPHRSCNINED---SGLPLAFTIAHELGHSF 398
Cdd:pfam01421   74 LKWRQEYLKK----RKPHDVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNL 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51558724    399 GIQHD--GKENDCEPVGR---HPYIMSrqlqydPTPLTWSKCSEEYITRFLDRGWGFCLDDIP 456
Cdd:pfam01421  144 GMQHDdfNGGCKCPPGGGcimNPSAGS------SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 468-532 1.24e-22

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.79  E-value: 1.24e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51558724    468 PGVIYDVHHQCQLQYGPNATFCQEV-ENVCQTLWCSVKGF--CRSKLDAAADGTQCGEKKWCMAGKCI 532
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGstCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 545-596 2.29e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.46  E-value: 2.29e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 51558724     545 WGRWSPWSHCSRTCGAGVQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPC 596
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1475-1531 3.28e-15

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 71.33  E-value: 3.28e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51558724   1475 WATGNWDLCSTSCGGGFQKRTVQCVPSEGNKTEDQDQclCDHKPRPPEFKKCNQQAC 1531
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE--CSAQKKPPETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 248-452 4.05e-15

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 76.24  E-value: 4.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  248 VETLVVADTKMIEYHGS-ENVESYILTIMNMVT---GLFHNPSIgnaiHIVVVRLILLEEEEQGLKIVHH------AEKT 317
Cdd:cd04272    3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANlryRDLKSPRI----RLLLVGITISKDPDFEPYIHPInygyidAAET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  318 LSSFckwqkSINPKSDLNPVHHDVAVLLTRKDICAGFNRPCET--LGLSHLSGMCQpHRSCNINEDSGLPL--AFTIAHE 393
Cdd:cd04272   79 LENF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHE 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51558724  394 LGHSFGIQHDGKEnDCEPVGRHP----------YIMSrQLQYDPTPLTWSKCSEEYITRFLDRGWGFCL 452
Cdd:cd04272  153 LAHLLGAPHDGSP-PPSWVKGHPgsldcpwddgYIMS-YVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 331-444 9.22e-14

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 70.63  E-value: 9.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  331 KSDLNPVHHDVAVLLTRKDicagfnRPCETLGLSHLSGMCQPHRSCNINEDSGLP---LAFTIAHELGHSFGIQHDGKEN 407
Cdd:cd00203   44 LVGVEIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRK 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 51558724  408 DCEP-----------VGRHPYIMSRQL--QYDPTPLTWSKCSEEYITRFL 444
Cdd:cd00203  118 DRDDyptiddtlnaeDDDYYSVMSYTKgsFSDGQRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1427-1472 4.03e-13

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.17  E-value: 4.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724   1427 WQVEPWSQCSRSCGGGVQERGVFC---------PGGLCDWTKRPTSTMSCNEHLC 1472
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggsivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 948-996 5.97e-12

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.09  E-value: 5.97e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    948 WTVGNWSECSVSCGGGVRIRSVTCAK------NHDEPCDVTRKPNSRALCGLQQC 996
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsiVPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 603-701 8.33e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 63.57  E-value: 8.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    603 FRQMQCSEFDTVPYKNE-----LYHW---FPIFNPAHPCELYCRPIDGQFSEKMLDAVIDGTPCFEGG----NSRNVCIN 670
Cdd:pfam19236    5 FMSQQCARTDGQPLRSSpggasFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredGTLSLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 51558724    671 GICKMVGCDYEIDSNATEDRCGVCLGDGSSC 701
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
244-420 7.22e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 63.21  E-value: 7.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    244 KERWVETLVVADTKMIEYHGSENVESYILTIMNMVTGLFHNPSignAIHIVVVRLILLEEEE---QGLKIVHHAEKTLSS 320
Cdd:pfam13688    1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCpytPPACSTGDSSDRLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    321 FCKWQKSINPKSDlnpvhhDVAVLLTrkdicagfNRPCETLGLSHLSGMCQPHRSCNINEDSGLP--------LAFTIAH 392
Cdd:pfam13688   78 FQDFSAWRGTQND------DLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAH 143

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 51558724    393 ELGHSFGIQHD---GKENDCEPVGRHP------YIMS 420
Cdd:pfam13688  144 EIGHNFGAVHDcdsSTSSQCCPPSNSTcpaggrYIMN 180
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 828-882 2.90e-10

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 57.08  E-value: 2.90e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724    828 WQYGHWTECSVTCGTGIRRQTAHCIKK-GRGMVKATFCDPETQPNgRQKKCHEKAC 882
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgGGSIVPDSECSAQKKPP-ETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1317-1365 2.35e-09

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 54.77  E-value: 2.35e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724   1317 WIVGNWSECSTTCGLGAYWRRVEC------STQMDSDCAAIQRPDPAKRCHLRPC 1365
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCvqkgggSIVPDSECSAQKKPPETQSCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
548-596 5.04e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.58  E-value: 5.04e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51558724    548 WSPWSHCSRTCGAGVQSAERLCNNPEPkfGGKYCTGERKRYRLCNVHPC 596
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1368-1424 5.09e-08

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 50.91  E-value: 5.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51558724   1368 WKVGNWSKCSRNCSGGFKIREIQCVDSRDHRNLRPFHCQFLAgiPPPLSMSCNPEPC 1424
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSECSAQK--KPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 886-940 5.09e-07

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 47.83  E-value: 5.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 51558724    886 WWAGEWEACSATCGPhGEKKRTVLCIQTMvsDEQALPPTDCQHLLKPKTLLSCNR 940
Cdd:pfam19030    1 WVAGPWGECSVTCGG-GVQTRLVQCVQKG--GGSIVPDSECSAQKKPPETQSCNL 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 946-997 3.72e-05

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 42.57  E-value: 3.72e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724     946 SDWtvGNWSECSVSCGGGVRIRSVTC----AKNHDEPCDVTRKpnSRALCGLQQCP 997
Cdd:smart00209    2 SEW--SEWSPCSVTCGGGVQTRTRSCcsppPQNGGGPCTGEDV--ETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 548-596 5.97e-05

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 41.88  E-value: 5.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 51558724    548 WSPWSHCSRTCGAGVQSAERLCNNPePKFGGKYCTGERKRyRLCNVHPC 596
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 251-451 7.22e-05

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 46.21  E-value: 7.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  251 LVVADTKMIEYHGSENVESYILTIMNMVTGL--------FHNPSIGNaIHIVVVRLILLEEEEqglKIVHHAEKTLSSFC 322
Cdd:cd04270    6 LLVADHRFYKYMGRGEEETTINYLISHIDRVddiyrntdWDGGGFKG-IGFQIKRIRIHTTPD---EVDPGNKFYNKSFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  323 KWQKSINPKSDLNPVHHD---VAVLLTRKDICAGfnrpceTLGLSHLS--------GMCQPH--------RSCN------ 377
Cdd:cd04270   82 NWGVEKFLVKLLLEQFSDdvcLAHLFTYRDFDMG------TLGLAYVGsprdnsagGICEKAyyysngkkKYLNtglttt 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724  378 INEDSGLPLA---FTIAHELGHSFGIQHDGKENDCEPVGRH--PYIMSRQLQ--YDPTPLTWSKCSEEYITRFLDRGWGF 450
Cdd:cd04270  156 VNYGKRVPTKesdLVTAHELGHNFGSPHDPDIAECAPGESQggNYIMYARATsgDKENNKKFSPCSKKSISKVLEVKSNS 235


                 .
gi 51558724  451 C 451
Cdd:cd04270  236 C 236
ACR smart00608
ADAM Cysteine-Rich Domain;
515-676 8.47e-05

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 44.27  E-value: 8.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724     515 ADGTQCGEKKW-CMAGKCITVGKkpesipggwgrwspwsHCSRTCGAGVQSAERLC----NNPEPKFGgkYCTGERKRYR 589
Cdd:smart00608    1 QDGTPCDNGQGyCYNGRCPTRDN----------------QCQALFGPGAKVAPDSCyeelNTKGDRFG--NCGRENGTYI 62

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724     590 lcnvhPCRSEAPTFRQMQCSEFDTVPYKNELY--HWFPIFNpahpceLYCRPIDGQFSEKMLDA-VIDGTPCFEGgnsrN 666
Cdd:smart00608   63 -----PCAPEDVKCGKLQCTNVSELPLLGEHAtvIYSNIGG------LVCWSLDYHLGTDPDIGmVKDGTKCGPG----K 127

                           170
                    ....*....|
gi 51558724     667 VCINGICKMV 676
Cdd:smart00608  128 VCINGQCVDV 137
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 549-596 1.17e-04

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 41.16  E-value: 1.17e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 51558724    549 SPWSHCSRTCGAGVqsAERLCNNPEpkfggkYCTGERKRyRLCNVHPC 596
Cdd:pfam19035    6 TEWSPCSKTCGMGV--STRVSNDNA------ECKLVTET-RLCQLRPC 44
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1474-1531 1.32e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 41.03  E-value: 1.32e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 51558724    1474 HWATGNWDLCSTSCGGGFQKRTVQCVpsegNKTEDQDQCLCDHKprPPEFKKCNQQAC 1531
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCC----SPPPQNGGGPCTGE--DVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 828-883 3.72e-04

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 39.88  E-value: 3.72e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 51558724     828 WQYGHWTECSVTCGTGIRRQTAHCIkKGRGMVKATFCDPetqPNGRQKKCHEKACP 883
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPCTG---EDVETRACNEQPCP 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 349-403 5.55e-04

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 41.20  E-value: 5.55e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51558724    349 DICAGFNR--PCETLGLSHLSGMCQPHRSCNINEDS---GLPLAFTIAHELGHSFGIQHD 403
Cdd:pfam13582   63 DLGHLFTGrdGGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 946-996 6.65e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.18  E-value: 6.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 51558724    946 SDWTvgNWSECSVSCGGGVRIRS---VTCAKNHDEPCDVTRKpnSRAlCGLQQC 996
Cdd:pfam19028    4 SEWS--EWSECSVTCGGGVQTRTrtvIVEPQNGGRPCPELLE--RRP-CNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
946-979 8.72e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.55  E-value: 8.72e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 51558724    946 SDWTvgNWSECSVSCGGGVRIRSVTCAKNHD--EPC 979
Cdd:pfam00090    1 SPWS--PWSPCSVTCGKGIQVRQRTCKSPFPggEPC 34
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1427-1472 1.36e-03

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 38.34  E-value: 1.36e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 51558724    1427 WQVEPWSQCSRSCGGGVQERGVFC-------PGGLCdwTKRPTSTMSCNEHLC 1472
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCcspppqnGGGPC--TGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 550-596 8.16e-03

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 36.28  E-value: 8.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 51558724    550 PWSHCSRTCGAGVQSAERLCNNPEPK--FGGKYCTGERK--RYRLCNVHPC 596
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 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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