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Conserved domains on  [gi|312836829|ref|NP_001099890|]
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A disintegrin and metalloproteinase with thrombospondin motifs 12 precursor [Rattus norvegicus]

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) ...
 250-457 2.30e-107

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: 339.98  E-value: 2.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  250 RWVETLVVADTKMVEYHGSENVESYILTIMNMVTGLFHNPSIGNAVHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQ 329
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  330 KSINPKSDLNPVHHDVAVLITRKDICAGvNRPCETLGLSQLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGK 409
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 312836829  410 ENDCEPVGRHPYIMSQQIQYDPTPLTWSKCSKEYITRFLDRGRGFCLD 457
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 ...
 707-816 4.94e-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: 126.92  E-value: 4.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   707 TVKKVFRQKEGSGYIDIGLIPKGARDIRVMEIKAAGNFLAIRSeDPEKYYLNGGFIIQ-WNGNYKLAGTVFQYDR-KGDL 784
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRsLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 312836829   785 ERLMAPGPTNESVWLQLLFQ---VTNPGIKYEYTV 816
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 54-197 9.09e-34

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: 126.66  E-value: 9.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829    54 IVSPVQVDASghflsyglhhpvtgsRKKRAAGGSG---DQVYYRISHEEKNLFFNLTVNWEFLSNGYVVERRYGNLSHVK 130
Cdd:pfam01562    2 VVIPVRLDPS---------------RRRRSLASEStylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVE 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829   131 MAASSGQPCHLRGTVLQQGptirMGTAALSACQGLTGFFHLPHGDFFIEPVKKHPlTEEGYQPHVIY 197
Cdd:pfam01562   67 SPPVQTDHCYYQGHVEGHP----DSSVALSTCSGLRGFIRTENEEYLIEPLEKYS-REEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-536 1.88e-23

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: 95.10  E-value: 1.88e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829   472 PGVIYDVHHQCQLQYGPNATFCQEV-ENVCQTLWCSVKGF--CRSKLDAAADGTRCGEKKWCMAGKCI 536
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGstCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 549-600 1.83e-14

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: 69.15  E-value: 1.83e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 312836829    549 WGRWSPWSHCSRTCGAGAQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPC 600
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1480-1536 7.39e-14

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: 67.48  E-value: 7.39e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829  1480 WATGNWELCTTSCGGGSQKRTVHCIPSENSTTEDQDqcFCDHQARPPEFQNCNQQAC 1536
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDS--ECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1432-1477 3.02e-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: 62.86  E-value: 3.02e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829  1432 WKVEPWSQCSRSCGGGVQERGVFC---------PGGLCDWTKRPASTVPCNRHLC 1477
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 ...
 607-705 2.53e-11

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: 62.42  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   607 FRQMQCSEFDTVPYKNQ-----FYRW---FPVFNPAHPCELYCRPIDEQFSERMLEAVIDGTPCFEGG----NSRNVCIN 674
Cdd:pfam19236    5 FMSQQCARTDGQPLRSSpggasFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredGTLSLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 312836829   675 GICKRVGCDYEIDSNATEDRCGVCLGDGSAC 705
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 952-1000 6.63e-11

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: 59.00  E-value: 6.63e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829   952 WTVGNWSECSVSCGGGVRIRSVTCAK------NLNEPCDKTRKPNSRALCGLQQC 1000
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsiVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 832-886 1.30e-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: 55.15  E-value: 1.30e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829   832 WQFGRWTECSVTCGTGIRRQTAHCVKK-GHGIVKTTFCNPETQPSVRQkKCYEKDC 886
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgGGSIVPDSECSAQKKPPETQ-SCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1372-1429 2.73e-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: 51.68  E-value: 2.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829  1372 WRVGNWSKCSRNCSGGFKIREVQCMDGVDHHRSLRPFhCQFLAgvPPPLSMSCNLEPC 1429
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE-CSAQK--KPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1321-1369 8.41e-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: 50.14  E-value: 8.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829  1321 WIVGNWSKCSTTCGLGAYWRSVECSTGM------NADCAAIQRPDPAKKCHLRPC 1369
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 890-944 2.52e-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: 48.99  E-value: 2.52e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829   890 WWAGEWEACSMTCGpYGEKKRTVLCIQTMGSDEQalPATDCQHLLKPKTLVSCNR 944
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIV--PDSECSAQKKPPETQSCNL 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 250-457 2.30e-107

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: 339.98  E-value: 2.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  250 RWVETLVVADTKMVEYHGSENVESYILTIMNMVTGLFHNPSIGNAVHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQ 329
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  330 KSINPKSDLNPVHHDVAVLITRKDICAGvNRPCETLGLSQLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGK 409
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 312836829  410 ENDCEPVGRHPYIMSQQIQYDPTPLTWSKCSKEYITRFLDRGRGFCLD 457
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 ...
 707-816 4.94e-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: 126.92  E-value: 4.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   707 TVKKVFRQKEGSGYIDIGLIPKGARDIRVMEIKAAGNFLAIRSeDPEKYYLNGGFIIQ-WNGNYKLAGTVFQYDR-KGDL 784
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRsLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 312836829   785 ERLMAPGPTNESVWLQLLFQ---VTNPGIKYEYTV 816
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 54-197 9.09e-34

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: 126.66  E-value: 9.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829    54 IVSPVQVDASghflsyglhhpvtgsRKKRAAGGSG---DQVYYRISHEEKNLFFNLTVNWEFLSNGYVVERRYGNLSHVK 130
Cdd:pfam01562    2 VVIPVRLDPS---------------RRRRSLASEStylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVE 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829   131 MAASSGQPCHLRGTVLQQGptirMGTAALSACQGLTGFFHLPHGDFFIEPVKKHPlTEEGYQPHVIY 197
Cdd:pfam01562   67 SPPVQTDHCYYQGHVEGHP----DSSVALSTCSGLRGFIRTENEEYLIEPLEKYS-REEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 250-460 5.09e-30

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: 118.56  E-value: 5.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   250 RWVETLVVADTKMVEYHGS--ENVESYILTIMNMVTGLFHNPSIgnavHIVVVRLILLEEEEQgLKIVHHAEKTLSSFCK 327
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYKELNI----RVVLVGLEIWTDEDK-IDVSGDANDTLRNFLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   328 WQKSINPKsdlnPVHHDVAVLITrkdicaGVNRPCETLGLSQLSGMCQPHRSCNINED---SGLPLAFTIAHELGHSFGI 404
Cdd:pfam01421   76 WRQEYLKK----RKPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGM 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829   405 QHD--GKENDCEPVGRhpYIMSQQIQYdPTPLTWSKCSKEYITRFLDRGRGFCLDDVP 460
Cdd:pfam01421  146 QHDdfNGGCKCPPGGG--CIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-536 1.88e-23

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: 95.10  E-value: 1.88e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829   472 PGVIYDVHHQCQLQYGPNATFCQEV-ENVCQTLWCSVKGF--CRSKLDAAADGTRCGEKKWCMAGKCI 536
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGstCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 549-600 1.83e-14

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: 69.15  E-value: 1.83e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 312836829    549 WGRWSPWSHCSRTCGAGAQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPC 600
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1480-1536 7.39e-14

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: 67.48  E-value: 7.39e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829  1480 WATGNWELCTTSCGGGSQKRTVHCIPSENSTTEDQDqcFCDHQARPPEFQNCNQQAC 1536
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDS--ECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1432-1477 3.02e-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: 62.86  E-value: 3.02e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829  1432 WKVEPWSQCSRSCGGGVQERGVFC---------PGGLCDWTKRPASTVPCNRHLC 1477
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 ...
 607-705 2.53e-11

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: 62.42  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   607 FRQMQCSEFDTVPYKNQ-----FYRW---FPVFNPAHPCELYCRPIDEQFSERMLEAVIDGTPCFEGG----NSRNVCIN 674
Cdd:pfam19236    5 FMSQQCARTDGQPLRSSpggasFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredGTLSLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 312836829   675 GICKRVGCDYEIDSNATEDRCGVCLGDGSAC 705
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 952-1000 6.63e-11

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: 59.00  E-value: 6.63e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829   952 WTVGNWSECSVSCGGGVRIRSVTCAK------NLNEPCDKTRKPNSRALCGLQQC 1000
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsiVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 832-886 1.30e-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: 55.15  E-value: 1.30e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829   832 WQFGRWTECSVTCGTGIRRQTAHCVKK-GHGIVKTTFCNPETQPSVRQkKCYEKDC 886
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgGGSIVPDSECSAQKKPPETQ-SCNLKPC 55
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-600 2.01e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 2.01e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 312836829   552 WSPWSHCSRTCGAGAQSAERLCNNPEPkfGGKYCTGERKRYRLCNVHPC 600
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1372-1429 2.73e-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: 51.68  E-value: 2.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829  1372 WRVGNWSKCSRNCSGGFKIREVQCMDGVDHHRSLRPFhCQFLAgvPPPLSMSCNLEPC 1429
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE-CSAQK--KPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1321-1369 8.41e-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: 50.14  E-value: 8.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829  1321 WIVGNWSKCSTTCGLGAYWRSVECSTGM------NADCAAIQRPDPAKKCHLRPC 1369
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 890-944 2.52e-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: 48.99  E-value: 2.52e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829   890 WWAGEWEACSMTCGpYGEKKRTVLCIQTMGSDEQalPATDCQHLLKPKTLVSCNR 944
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIV--PDSECSAQKKPPETQSCNL 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 950-1001 1.08e-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: 41.42  E-value: 1.08e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829    950 SDWtvGNWSECSVSCGGGVRIRSVTC----AKNLNEPCDKTRKpnSRALCGLQQCP 1001
Cdd:smart00209    2 SEW--SEWSPCSVTCGGGVQTRTRSCcsppPQNGGGPCTGEDV--ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 832-887 4.63e-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: 39.49  E-value: 4.63e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829    832 WQFGRWTECSVTCGTGIRRQTAHCVkKGHGIVKTTFCnpeTQPSVRQKKCYEKDCP 887
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPC---TGEDVETRACNEQPCP 53
ACR smart00608
ADAM Cysteine-Rich Domain;
519-680 9.15e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 41.19  E-value: 9.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829    519 ADGTRCGEKKW-CMAGKCITVGKkpesipggwgrwspwsHCSRTCGAGAQSAERLC----NNPEPKFGgkYCTGERKRYR 593
Cdd:smart00608    1 QDGTPCDNGQGyCYNGRCPTRDN----------------QCQALFGPGAKVAPDSCyeelNTKGDRFG--NCGRENGTYI 62

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829    594 LCNvhpcRSDTPTFRqMQCSEFDTVPYKNQFYrwfpVFNPAHPCELYCRPIDEQFSERMLEA-VIDGTPCFEGgnsrNVC 672
Cdd:smart00608   63 PCA----PEDVKCGK-LQCTNVSELPLLGEHA----TVIYSNIGGLVCWSLDYHLGTDPDIGmVKDGTKCGPG----KVC 129


                    ....*...
gi 312836829    673 INGICKRV 680
Cdd:smart00608  130 INGQCVDV 137
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1429-1477 1.41e-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: 1.41e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829   1429 CEEWkvEPWSQCSRSCGGGVQERGVFC-------PGGLCdwTKRPASTVPCNRHLC 1477
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCcspppqnGGGPC--TGEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 250-457 2.30e-107

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: 339.98  E-value: 2.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  250 RWVETLVVADTKMVEYHGSENVESYILTIMNMVTGLFHNPSIGNAVHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCKWQ 329
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  330 KSINPKSDLNPVHHDVAVLITRKDICAGvNRPCETLGLSQLSGMCQPHRSCNINEDSGLPLAFTIAHELGHSFGIQHDGK 409
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 312836829  410 ENDCEPVGRHPYIMSQQIQYDPTPLTWSKCSKEYITRFLDRGRGFCLD 457
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 250-449 1.04e-34

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: 131.77  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  250 RWVETLVVADTKMVEYHGS--ENVESYILTIMNMVTGLFHNPSIGNAVHIVVVRLILLEEEEQGLKIVHHAEKTLSSFCK 327
Cdd:cd04267     1 REIELVVVADHRMVSYFNSdeNILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  328 WQKSinpksdlNPVHHDVAVLITRKDICAgvnrpCETLGLSQLSGMCQPHRSCNINEDSGLPL--AFTIAHELGHSFGIQ 405
Cdd:cd04267    81 WRAE-------GPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAE 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 312836829  406 HDGK-ENDCEPVGRHPYIMSQQIQyDPTPLTWSKCSKEYITRFLD 449
Cdd:cd04267   149 HDGGdELAFECDGGGNYIMAPVDS-GLNSYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 250-456 1.19e-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: 131.58  E-value: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  250 RWVETLVVADTKMVEYHGS--ENVESYILTIMNMVTGLFHNpsignaVHIVVVrLILLE---EEEQgLKIVHHAEKTLSS 324
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRP------LNIRVV-LVGLEiwtDKDK-ISVSGDAGETLNR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  325 FCKWQKSinpksDLNP-VHHDVAVLITrkdicaGVNRPCETLGLSQLSGMCQPHRSCNINEDSG---LPLAFTIAHELGH 400
Cdd:cd04269    73 FLDWKRS-----NLLPrKPHDNAQLLT------GRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGH 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829  401 SFGIQHDGKENDCepvGRHPYIMSQQIQYDPTplTWSKCSKEYITRFLDRGRGFCL 456
Cdd:cd04269   142 NLGMEHDDGGCTC---GRSTCIMAPSPSSLTD--AFSNCSYEDYQKFLSRGGGQCL 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 707-816 4.94e-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: 126.92  E-value: 4.94e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   707 TVKKVFRQKEGSGYIDIGLIPKGARDIRVMEIKAAGNFLAIRSeDPEKYYLNGGFIIQ-WNGNYKLAGTVFQYDR-KGDL 784
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRsLPAL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 312836829   785 ERLMAPGPTNESVWLQLLFQ---VTNPGIKYEYTV 816
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 54-197 9.09e-34

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: 126.66  E-value: 9.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829    54 IVSPVQVDASghflsyglhhpvtgsRKKRAAGGSG---DQVYYRISHEEKNLFFNLTVNWEFLSNGYVVERRYGNLSHVK 130
Cdd:pfam01562    2 VVIPVRLDPS---------------RRRRSLASEStylDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVE 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829   131 MAASSGQPCHLRGTVLQQGptirMGTAALSACQGLTGFFHLPHGDFFIEPVKKHPlTEEGYQPHVIY 197
Cdd:pfam01562   67 SPPVQTDHCYYQGHVEGHP----DSSVALSTCSGLRGFIRTENEEYLIEPLEKYS-REEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 250-460 5.09e-30

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: 118.56  E-value: 5.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   250 RWVETLVVADTKMVEYHGS--ENVESYILTIMNMVTGLFHNPSIgnavHIVVVRLILLEEEEQgLKIVHHAEKTLSSFCK 327
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYKELNI----RVVLVGLEIWTDEDK-IDVSGDANDTLRNFLK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   328 WQKSINPKsdlnPVHHDVAVLITrkdicaGVNRPCETLGLSQLSGMCQPHRSCNINED---SGLPLAFTIAHELGHSFGI 404
Cdd:pfam01421   76 WRQEYLKK----RKPHDVAQLLS------GVEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGM 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829   405 QHD--GKENDCEPVGRhpYIMSQQIQYdPTPLTWSKCSKEYITRFLDRGRGFCLDDVP 460
Cdd:pfam01421  146 QHDdfNGGCKCPPGGG--CIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 472-536 1.88e-23

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: 95.10  E-value: 1.88e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829   472 PGVIYDVHHQCQLQYGPNATFCQEV-ENVCQTLWCSVKGF--CRSKLDAAADGTRCGEKKWCMAGKCI 536
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGstCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 252-456 3.34e-17

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 82.40  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  252 VETLVVADTKMVEYHGS-ENVESYILTIMNMVT---GLFHNPSIgnavHIVVVRLILLEEEEQGLKIVHH------AEKT 321
Cdd:cd04272     3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANlryRDLKSPRI----RLLLVGITISKDPDFEPYIHPInygyidAAET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  322 LSSFckwqkSINPKSDLNPVHHDVAVLITRKDICAGVNRPCET--LGLSQLSGMCQpHRSCNINEDSGLPL--AFTIAHE 397
Cdd:cd04272    79 LENF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHE 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  398 LGHSFGIQHDGKEnDCEPVGRHP----------YIMSqQIQYDPTPLTWSKCSKEYITRFLdRGRGF-CL 456
Cdd:cd04272   153 LAHLLGAPHDGSP-PPSWVKGHPgsldcpwddgYIMS-YVVNGERQYRFSQCSQRQIRNVF-RRLGAsCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 335-448 1.58e-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: 72.94  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829  335 KSDLNPVHHDVAVLITRKDicagvnRPCETLGLSQLSGMCQPHRSCNINEDSGLP---LAFTIAHELGHSFGIQHDGKEN 411
Cdd:cd00203    44 LVGVEIDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRK 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 312836829  412 DCEP-----------VGRHPYIMSQQI--QYDPTPLTWSKCSKEYITRFL 448
Cdd:cd00203   118 DRDDyptiddtlnaeDDDYYSVMSYTKgsFSDGQRKDFSQCDIDQINKLY 167
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 549-600 1.83e-14

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: 69.15  E-value: 1.83e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 312836829    549 WGRWSPWSHCSRTCGAGAQSAERLCNNPEPKFGGKYCTGERKRYRLCNVHPC 600
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1480-1536 7.39e-14

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: 67.48  E-value: 7.39e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829  1480 WATGNWELCTTSCGGGSQKRTVHCIPSENSTTEDQDqcFCDHQARPPEFQNCNQQAC 1536
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDS--ECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1432-1477 3.02e-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: 62.86  E-value: 3.02e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829  1432 WKVEPWSQCSRSCGGGVQERGVFC---------PGGLCDWTKRPASTVPCNRHLC 1477
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 ...
 607-705 2.53e-11

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: 62.42  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   607 FRQMQCSEFDTVPYKNQ-----FYRW---FPVFNPAHPCELYCRPIDEQFSERMLEAVIDGTPCFEGG----NSRNVCIN 674
Cdd:pfam19236    5 FMSQQCARTDGQPLRSSpggasFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGpredGTLSLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 312836829   675 GICKRVGCDYEIDSNATEDRCGVCLGDGSAC 705
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 952-1000 6.63e-11

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: 59.00  E-value: 6.63e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829   952 WTVGNWSECSVSCGGGVRIRSVTCAK------NLNEPCDKTRKPNSRALCGLQQC 1000
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQkgggsiVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 832-886 1.30e-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: 55.15  E-value: 1.30e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829   832 WQFGRWTECSVTCGTGIRRQTAHCVKK-GHGIVKTTFCNPETQPSVRQkKCYEKDC 886
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgGGSIVPDSECSAQKKPPETQ-SCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
248-424 2.09e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 58.97  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   248 KERWVETLVVADTKMVEYHGSENVESYILTIMNMVTGLFHNPSignAVHIVVVRLILLEEEE---QGLKIVHHAEKTLSS 324
Cdd:pfam13688    1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCpytPPACSTGDSSDRLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   325 FCKWQKSINPKSDlnpvhhDVAVLITrkdicagvNRPCETLGLSQLSGMCQPHRSCNINEDSGLP--------LAFTIAH 396
Cdd:pfam13688   78 FQDFSAWRGTQND------DLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAH 143

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 312836829   397 ELGHSFGIQHD---GKENDCEPVGRHP------YIMS 424
Cdd:pfam13688  144 EIGHNFGAVHDcdsSTSSQCCPPSNSTcpaggrYIMN 180
TSP_1 pfam00090
Thrombospondin type 1 domain;
552-600 2.01e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 2.01e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 312836829   552 WSPWSHCSRTCGAGAQSAERLCNNPEPkfGGKYCTGERKRYRLCNVHPC 600
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1372-1429 2.73e-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: 51.68  E-value: 2.73e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 312836829  1372 WRVGNWSKCSRNCSGGFKIREVQCMDGVDHHRSLRPFhCQFLAgvPPPLSMSCNLEPC 1429
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSE-CSAQK--KPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1321-1369 8.41e-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: 50.14  E-value: 8.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829  1321 WIVGNWSKCSTTCGLGAYWRSVECSTGM------NADCAAIQRPDPAKKCHLRPC 1369
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 890-944 2.52e-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: 48.99  E-value: 2.52e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 312836829   890 WWAGEWEACSMTCGpYGEKKRTVLCIQTMGSDEQalPATDCQHLLKPKTLVSCNR 944
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIV--PDSECSAQKKPPETQSCNL 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 393-455 3.95e-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: 46.98  E-value: 3.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829  393 TIAHELGHSFGIQHDGKENDCEPVGRH--PYIMSQQIQ--YDPTPLTWSKCSKEYITRFLDRGRGFC 455
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECAPGESQggNYIMYARATsgDKENNKKFSPCSKKSISKVLEVKSNSC 236
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 950-1001 1.08e-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: 41.42  E-value: 1.08e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829    950 SDWtvGNWSECSVSCGGGVRIRSVTC----AKNLNEPCDKTRKpnSRALCGLQQCP 1001
Cdd:smart00209    2 SEW--SEWSPCSVTCGGGVQTRTRSCcsppPQNGGGPCTGEDV--ETRACNEQPCP 53
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 344-407 2.47e-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: 42.36  E-value: 2.47e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829   344 DVAVLITRKDicagvnrPCETLGLSQLSGMCQPHRSCNINEDS---GLPLAFTIAHELGHSFGIQHD 407
Cdd:pfam13582   63 DLGHLFTGRD-------GGGGGGIAYVGGVCNSGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 950-1000 4.04e-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: 39.57  E-value: 4.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 312836829   950 SDWTvgNWSECSVSCGGGVRIRS---VTCAKNLNEPC---DKTRKpnsralCGLQQC 1000
Cdd:pfam19028    4 SEWS--EWSECSVTCGGGVQTRTrtvIVEPQNGGRPCpelLERRP------CNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
950-983 4.26e-04

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 39.71  E-value: 4.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 312836829   950 SDWTvgNWSECSVSCGGGVRIRSVTCAKNL--NEPC 983
Cdd:pfam00090    1 SPWS--PWSPCSVTCGKGIQVRQRTCKSPFpgGEPC 34
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 832-887 4.63e-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: 39.49  E-value: 4.63e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829    832 WQFGRWTECSVTCGTGIRRQTAHCVkKGHGIVKTTFCnpeTQPSVRQKKCYEKDCP 887
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSCC-SPPPQNGGGPC---TGEDVETRACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 552-600 5.27e-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: 5.27e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 312836829   552 WSPWSHCSRTCGAGAQSAERLCNNPePKFGGKYCTGERKRyRLCNVHPC 600
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
ACR smart00608
ADAM Cysteine-Rich Domain;
519-680 9.15e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 41.19  E-value: 9.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829    519 ADGTRCGEKKW-CMAGKCITVGKkpesipggwgrwspwsHCSRTCGAGAQSAERLC----NNPEPKFGgkYCTGERKRYR 593
Cdd:smart00608    1 QDGTPCDNGQGyCYNGRCPTRDN----------------QCQALFGPGAKVAPDSCyeelNTKGDRFG--NCGRENGTYI 62

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829    594 LCNvhpcRSDTPTFRqMQCSEFDTVPYKNQFYrwfpVFNPAHPCELYCRPIDEQFSERMLEA-VIDGTPCFEGgnsrNVC 672
Cdd:smart00608   63 PCA----PEDVKCGK-LQCTNVSELPLLGEHA----TVIYSNIGGLVCWSLDYHLGTDPDIGmVKDGTKCGPG----KVC 129


                    ....*...
gi 312836829    673 INGICKRV 680
Cdd:smart00608  130 INGQCVDV 137
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 334-418 1.07e-03

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: 372637  Cd Length: 193  Bit Score: 41.85  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836829   334 PKSDLNPVHHDVAVLITR-----------KDICAGV---NRPCE--TLGLSQLSGMCQPHRSCnINEDSGLPLAFT---- 393
Cdd:pfam13574   40 SASDSGNNYCNSPTTIVRrlnflsqwrgeQDYCLAHlvtMGTFSggELGLAYVGQICQKGASS-PKTNTGLSTTTNygsf 118

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 312836829   394 ---------IAHELGHSFGIQHD--GKENDCEPVGR 418
Cdd:pfam13574  119 nyptqewdvVAHEVGHNFGATHDcdGSQYASSGCER 154
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 553-600 1.25e-03

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: 38.08  E-value: 1.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 312836829   553 SPWSHCSRTCGAGAqsAERLCNNPEpkfggkYCTGERKRyRLCNVHPC 600
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.
 1429-1477 1.41e-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: 1.41e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836829   1429 CEEWkvEPWSQCSRSCGGGVQERGVFC-------PGGLCdwTKRPASTVPCNRHLC 1477
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCcspppqnGGGPC--TGEDVETRACNEQPC 52
 
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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