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Conserved domains on  [gi|155371891|ref|NP_001094550|]
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A disintegrin and metalloproteinase with thrombospondin motifs 1 [Bos taurus]

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) ...
 261-466 4.51e-109

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: 335.75  E-value: 4.51e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 261 RYVETMLVADQSMAEF-HGSDLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIYEEKKGPEVTSNAALTLRNFCSWQ 339
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 340 KQHNPPSDRDAEHYDTAILFTRQDLCGTQ-TCDTLGMADVGTICDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 417
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 155371891 418 KQCAginGLNRDSHMMASMLTNLDHNQPWSPCSASSITTFLDNGHGECL 466
Cdd:cd04273  161 NSCG---PEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 729-845 2.63e-37

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: 135.78  E-value: 2.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  729 KVSGSVTTAK-PGYHDIVTIPTGATNIEVKQRNhrgsrNNGSFLAIKAADGTYILNGDFTLSTLEQDITHKGSVLRYSGS 807
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 155371891  808 SAALERIRSFSPLKEPLTIQVLTV-GNAFRPKIKYTYFV 845
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 481-549 5.62e-24

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: 95.87  E-value: 5.62e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  481 PGTLYDASRQCQLTFGEESRHCPDA-ASTCMILWCTGTSGglPVCQTKHFPWADGTSCGEGKWCVNGQCL 549
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGG--STCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-163 7.43e-24

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: 97.77  E-value: 7.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891   74 TAHLRLDAFGRQLSLELHLDRGFLAPGFTLQTVGRRPEpdvQRSDPVGDLAHCFYSGTVNGDPSSAAALSLCDGVRGAFY 153
Cdd:pfam01562  26 TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGT---GVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102

                          90
                  ....*....|
gi 155371891  154 LQGEEYFIQP 163
Cdd:pfam01562 103 TENEEYLIEP 112
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 565-617 4.66e-16

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: 73.00  E-value: 4.66e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 155371891   565 WGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCP 617
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 861-912 1.94e-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: 1.94e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 155371891  861 WVIEEWGECSKSCGLGVQRRLVECRDING---QPASECAKEVKPASTRPCADLPC 912
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 915-969 6.51e-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: 61.31  E-value: 6.51e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891  915 WQLGDWSPCSKTCGKGYKKRTLQCL-SHDGGVLSHESCDPLKKPkHYIDFCTVAEC 969
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 661-727 1.13e-09

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: 57.03  E-value: 1.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 155371891  661 CKLICQAKGTGYFFVLQPKVVDGTPCSPD------STSVCVQGQCVKAGCDHIIDSKNKFDKCGICGGNGSTC 727
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 261-466 4.51e-109

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: 335.75  E-value: 4.51e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 261 RYVETMLVADQSMAEF-HGSDLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIYEEKKGPEVTSNAALTLRNFCSWQ 339
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 340 KQHNPPSDRDAEHYDTAILFTRQDLCGTQ-TCDTLGMADVGTICDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 417
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 155371891 418 KQCAginGLNRDSHMMASMLTNLDHNQPWSPCSASSITTFLDNGHGECL 466
Cdd:cd04273  161 NSCG---PEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 729-845 2.63e-37

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: 135.78  E-value: 2.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  729 KVSGSVTTAK-PGYHDIVTIPTGATNIEVKQRNhrgsrNNGSFLAIKAADGTYILNGDFTLSTLEQDITHKGSVLRYSGS 807
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 155371891  808 SAALERIRSFSPLKEPLTIQVLTV-GNAFRPKIKYTYFV 845
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 481-549 5.62e-24

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: 95.87  E-value: 5.62e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  481 PGTLYDASRQCQLTFGEESRHCPDA-ASTCMILWCTGTSGglPVCQTKHFPWADGTSCGEGKWCVNGQCL 549
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGG--STCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-163 7.43e-24

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: 97.77  E-value: 7.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891   74 TAHLRLDAFGRQLSLELHLDRGFLAPGFTLQTVGRRPEpdvQRSDPVGDLAHCFYSGTVNGDPSSAAALSLCDGVRGAFY 153
Cdd:pfam01562  26 TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGT---GVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102

                          90
                  ....*....|
gi 155371891  154 LQGEEYFIQP 163
Cdd:pfam01562 103 TENEEYLIEP 112
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 261-470 1.04e-21

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: 93.90  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  261 RYVETMLVADQSMAEFHGSDLKHYLLTLFSVAA---RLYKHPSIRnsvslVVVKILVIYEEKKGPEVTSNAALTLRNFCS 337
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNlvnSIYKELNIR-----VVLVGLEIWTDEDKIDVSGDANDTLRNFLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  338 WQKQHNPPSDRdaehYDTAILFTRQDLCGTqtcdTLGMADVGTICDPSRSCSVIED---DGLQAAFTTAHELGHVFNMPH 414
Cdd:pfam01421  76 WRQEYLKKRKP----HDVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQH 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 155371891  415 DDAK---QCAGINGLnrdshMMASMLTnldHNQP--WSPCSASSITTFLDNGHGECLMDEP 470
Cdd:pfam01421 148 DDFNggcKCPPGGGC-----IMNPSAG---SSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 565-617 4.66e-16

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: 73.00  E-value: 4.66e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 155371891   565 WGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCP 617
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 861-912 1.94e-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: 1.94e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 155371891  861 WVIEEWGECSKSCGLGVQRRLVECRDING---QPASECAKEVKPASTRPCADLPC 912
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 915-969 6.51e-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: 61.31  E-value: 6.51e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891  915 WQLGDWSPCSKTCGKGYKKRTLQCL-SHDGGVLSHESCDPLKKPkHYIDFCTVAEC 969
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 661-727 1.13e-09

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: 57.03  E-value: 1.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 155371891  661 CKLICQAKGTGYFFVLQPKVVDGTPCSPD------STSVCVQGQCVKAGCDHIIDSKNKFDKCGICGGNGSTC 727
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
566-616 8.47e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 8.47e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 155371891  566 GPWGPWGDCSRTCGGGVQYTMRECDNPVPknGGKYCEGKRVRYRSCNIEDC 616
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ACR smart00608
ADAM Cysteine-Rich Domain;
456-550 9.99e-09

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 54.67  E-value: 9.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891   456 TFLDNGHGECLMdepqlviqlpsdlpGTLYDASRQCQLTFGEESR----HCPDAAST----------------------- 508
Cdd:smart00608   4 TPCDNGQGYCYN--------------GRCPTRDNQCQALFGPGAKvapdSCYEELNTkgdrfgncgrengtyipcapedv 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 155371891   509 -CMILWCTGTSGGLP---------------VCQTKHFP---------WADGTSCGEGKWCVNGQCLD 550
Cdd:smart00608  70 kCGKLQCTNVSELPLlgehatviysnigglVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVD 136
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 859-913 3.48e-07

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: 47.97  E-value: 3.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891   859 SEWviEEWGECSKSCGLGVQRRLVECRDINGQ-PASECAKEVKpaSTRPCADLPCP 913
Cdd:smart00209   2 SEW--SEWSPCSVTCGGGVQTRTRSCCSPPPQnGGGPCTGEDV--ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 915-970 1.18e-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: 43.34  E-value: 1.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891   915 WQLGDWSPCSKTCGKGYKKRTLQCLSHDGGVlSHESCDPLKKPKHyidFCTVAECS 970
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQN-GGGPCTGEDVETR---ACNEQPCP 53
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 261-466 4.51e-109

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: 335.75  E-value: 4.51e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 261 RYVETMLVADQSMAEF-HGSDLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIYEEKKGPEVTSNAALTLRNFCSWQ 339
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 340 KQHNPPSDRDAEHYDTAILFTRQDLCGTQ-TCDTLGMADVGTICDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 417
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 155371891 418 KQCAginGLNRDSHMMASMLTNLDHNQPWSPCSASSITTFLDNGHGECL 466
Cdd:cd04273  161 NSCG---PEGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 261-459 2.77e-40

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: 147.18  E-value: 2.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 261 RYVETMLVADQSMAEF---HGSDLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIYEEKKGPEVTSNAALTLRNFCS 337
Cdd:cd04267    1 REIELVVVADHRMVSYfnsDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 338 WQKqhnppsdRDAEHYDTAILFTRQDLCGtqtCDTLGMADVGTICDPSRSCSVIEDDG--LQAAFTTAHELGHVFNMPHD 415
Cdd:cd04267   81 WRA-------EGPIRHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHD 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 155371891 416 DAKQCAGINGlNRDSHMMASMLTNLDhNQPWSPCSASSITTFLD 459
Cdd:cd04267  151 GGDELAFECD-GGGNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 729-845 2.63e-37

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: 135.78  E-value: 2.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  729 KVSGSVTTAK-PGYHDIVTIPTGATNIEVKQRNhrgsrNNGSFLAIKAADGTYILNGDFTLSTLEQDITHKGSVLRYSGS 807
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 155371891  808 SAALERIRSFSPLKEPLTIQVLTV-GNAFRPKIKYTYFV 845
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFI 114
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 261-468 7.68e-30

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: 117.33  E-value: 7.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 261 RYVETMLVADQSMAEFHGSDL---KHYLLTLFSVAARLYKHPSIRnsvslVVVKILVIYEEKKGPEVTSNAALTLRNFCS 337
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPLNIR-----VVLVGLEIWTDKDKISVSGDAGETLNRFLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 338 WQKqhnppSDRDAEH-YDTAILFTRQDLCGTqtcdTLGMADVGTICDPSRSCSVIEDDG---LQAAFTTAHELGHVFNMP 413
Cdd:cd04269   76 WKR-----SNLLPRKpHDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGME 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891 414 HDDAK-QCAginglnRDSHMMASmlTNLDHNQPWSPCSASSITTFLDNGHGECLMD 468
Cdd:cd04269  147 HDDGGcTCG------RSTCIMAP--SPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 481-549 5.62e-24

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: 95.87  E-value: 5.62e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  481 PGTLYDASRQCQLTFGEESRHCPDA-ASTCMILWCTGTSGglPVCQTKHFPWADGTSCGEGKWCVNGQCL 549
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGG--STCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-163 7.43e-24

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: 97.77  E-value: 7.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891   74 TAHLRLDAFGRQLSLELHLDRGFLAPGFTLQTVGRRPEpdvQRSDPVGDLAHCFYSGTVNGDPSSAAALSLCDGVRGAFY 153
Cdd:pfam01562  26 TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGT---GVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102

                          90
                  ....*....|
gi 155371891  154 LQGEEYFIQP 163
Cdd:pfam01562 103 TENEEYLIEP 112
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 261-470 1.04e-21

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: 93.90  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  261 RYVETMLVADQSMAEFHGSDLKHYLLTLFSVAA---RLYKHPSIRnsvslVVVKILVIYEEKKGPEVTSNAALTLRNFCS 337
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNlvnSIYKELNIR-----VVLVGLEIWTDEDKIDVSGDANDTLRNFLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  338 WQKQHNPPSDRdaehYDTAILFTRQDLCGTqtcdTLGMADVGTICDPSRSCSVIED---DGLQAAFTTAHELGHVFNMPH 414
Cdd:pfam01421  76 WRQEYLKKRKP----HDVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQH 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 155371891  415 DDAK---QCAGINGLnrdshMMASMLTnldHNQP--WSPCSASSITTFLDNGHGECLMDEP 470
Cdd:pfam01421 148 DDFNggcKCPPGGGC-----IMNPSAG---SSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 565-617 4.66e-16

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: 73.00  E-value: 4.66e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 155371891   565 WGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCP 617
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 354-458 6.34e-15

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: 73.33  E-value: 6.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 354 DTAILFTRQDLcgtqTCDTLGMADVGTICDPSRSCSVIEDDGL---QAAFTTAHELGHVFNMPHD-DAKQCAGINGLNRD 429
Cdd:cd00203   53 DIAILVTRQDF----DGGTGGWAYLGRVCDSLRGVGVLQDNQSgtkEGAQTIAHELGHALGFYHDhDRKDRDDYPTIDDT 128

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 155371891 430 ---------SHMMASMLTNLDHN-QPWSPCSASSITTFL 458
Cdd:cd00203  129 lnaedddyySVMSYTKGSFSDGQrKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 861-912 1.94e-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: 1.94e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 155371891  861 WVIEEWGECSKSCGLGVQRRLVECRDING---QPASECAKEVKPASTRPCADLPC 912
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGgsiVPDSECSAQKKPPETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 262-466 5.22e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 66.22  E-value: 5.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 262 YVETMLVADQSMA--EFHGSDLKHYLLTLFSVAARLYKhpSIRN-SVSLVVVKILV-------IYEEKKGPEVTsNAALT 331
Cdd:cd04272    2 YPELFVVVDYDHQseFFSNEQLIRYLAVMVNAANLRYR--DLKSpRIRLLLVGITIskdpdfePYIHPINYGYI-DAAET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 332 LRNFCSWQKQhnppsDRDAEHYDTAILFTRQDLC----GTQTCDTLGMADVGTICDpSRSCSVIEDDG--LQAAFTTAHE 405
Cdd:cd04272   79 LENFNEYVKK-----KRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDTPgsYYGVYTMTHE 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 155371891 406 LGHVFNMPHDDAKQCAGINGLN-------RDSHMMASMLTNLDHNQpWSPCSASSITTFLDNGHGECL 466
Cdd:cd04272  153 LAHLLGAPHDGSPPPSWVKGHPgsldcpwDDGYIMSYVVNGERQYR-FSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 915-969 6.51e-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: 61.31  E-value: 6.51e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891  915 WQLGDWSPCSKTCGKGYKKRTLQCL-SHDGGVLSHESCDPLKKPkHYIDFCTVAEC 969
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
259-422 4.41e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.82  E-value: 4.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  259 SPRYVETMLVADQSMAEFHGSD-LKHYLLTLFSVAARLYKHPSirnSVSLVVVKILVI---YEEKKGPEVTSNAALTLRN 334
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGGDaAQANIINMVNTASNVYERDF---NISLGLVNLTISdstCPYTPPACSTGDSSDRLSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  335 FcswQKQHnppSDRDAEHYDTAILFTrqdlcgTQTCDTLGMADVGTICDPSRSCSVIEDDG--------LQAAFTTAHEL 406
Cdd:pfam13688  78 F---QDFS---AWRGTQNDDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEI 145

                         170
                  ....*....|....*.
gi 155371891  407 GHVFNMPHDDAKQCAG 422
Cdd:pfam13688 146 GHNFGAVHDCDSSTSS 161
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 661-727 1.13e-09

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: 57.03  E-value: 1.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 155371891  661 CKLICQAKGTGYFFVLQPKVVDGTPCSPD------STSVCVQGQCVKAGCDHIIDSKNKFDKCGICGGNGSTC 727
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 304-415 2.27e-09

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: 56.22  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  304 SVSLVVVKIlVIYEEKKGPEVTSNAALTLRNFCSWQKQHnppsdRDAEHYDTAILFTRQDLCGTQtcdtlGMADVGTICD 383
Cdd:pfam13582  19 GIRLQLAAI-IITTSADTPYTSSDALEILDELQEVNDTR-----IGQYGYDLGHLFTGRDGGGGG-----GIAYVGGVCN 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 155371891  384 PSRSCSVIEDD---GLQAAFTTAHELGHVFNMPHD 415
Cdd:pfam13582  88 SGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP_1 pfam00090
Thrombospondin type 1 domain;
566-616 8.47e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 8.47e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 155371891  566 GPWGPWGDCSRTCGGGVQYTMRECDNPVPknGGKYCEGKRVRYRSCNIEDC 616
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ACR smart00608
ADAM Cysteine-Rich Domain;
456-550 9.99e-09

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 54.67  E-value: 9.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891   456 TFLDNGHGECLMdepqlviqlpsdlpGTLYDASRQCQLTFGEESR----HCPDAAST----------------------- 508
Cdd:smart00608   4 TPCDNGQGYCYN--------------GRCPTRDNQCQALFGPGAKvapdSCYEELNTkgdrfgncgrengtyipcapedv 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 155371891   509 -CMILWCTGTSGGLP---------------VCQTKHFP---------WADGTSCGEGKWCVNGQCLD 550
Cdd:smart00608  70 kCGKLQCTNVSELPLlgehatviysnigglVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVD 136
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 859-913 3.48e-07

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: 47.97  E-value: 3.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891   859 SEWviEEWGECSKSCGLGVQRRLVECRDINGQ-PASECAKEVKpaSTRPCADLPCP 913
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 ...
 566-616 6.16e-07

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: 46.89  E-value: 6.16e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 155371891  566 GPWGPWGDCSRTCGGGVQYTMRECDNPvPKNGGKYCEGKRVRyRSCNIEDC 616
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 356-471 3.00e-06

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: 49.68  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891 356 AILFTRQDLCGTqtcdTLGMADVGT--------ICDPSRSCSVIEDDGL-----------------QAAFTTAHELGHVF 410
Cdd:cd04270  104 AHLFTYRDFDMG----TLGLAYVGSprdnsaggICEKAYYYSNGKKKYLntgltttvnygkrvptkESDLVTAHELGHNF 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 155371891 411 NMPHD-DAKQCAGiNGLNRDSHMMASMLTNLDH--NQPWSPCSASSITTFLDNGHGECLMDEPQ 471
Cdd:cd04270  180 GSPHDpDIAECAP-GESQGGNYIMYARATSGDKenNKKFSPCSKKSISKVLEVKSNSCFVERSQ 242
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 915-970 1.18e-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: 43.34  E-value: 1.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 155371891   915 WQLGDWSPCSKTCGKGYKKRTLQCLSHDGGVlSHESCDPLKKPKHyidFCTVAECS 970
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQN-GGGPCTGEDVETR---ACNEQPCP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 859-912 2.40e-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: 42.65  E-value: 2.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 155371891  859 SEWviEEWGECSKSCGLGVQRRLvecRDINGQPA---SECAKEVKpasTRPCADLPC 912
Cdd:pfam19028   4 SEW--SEWSECSVTCGGGVQTRT---RTVIVEPQnggRPCPELLE---RRPCNLPPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 569-616 3.30e-05

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: 42.44  E-value: 3.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 155371891  569 GPWGDCSRTCGGGVQYTMRECDNPVPK--NGGKYCEGKR--VRYRSCNIEDC 616
Cdd:pfam19030   4 GPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKkpPETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 285-458 3.58e-05

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: 45.70  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  285 LLTLFSVAARLYKHPSIRNSVSLV-VVKILVIYEEKKGPEVTSNAALT----LRNFCSWQKQHNppsdrdaehYDTAILF 359
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDININGGLVnPGEIPATTSASDSGNNYCNSPTTivrrLNFLSQWRGEQD---------YCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371891  360 TRQDLCGTqtcdTLGMADVGTICDPSRSCsVIEDDGLQAAFTT-------------AHELGHVFNMPHDDAKQCAGINGL 426
Cdd:pfam13574  78 TMGTFSGG----ELGLAYVGQICQKGASS-PKTNTGLSTTTNYgsfnyptqewdvvAHEVGHNFGATHDCDGSQYASSGC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 155371891  427 NRDS----------HMMASmlTNLDHNQPWSPCSASSITTFL 458
Cdd:pfam13574 153 ERNAatsvcsangsFIMNP--ASKSNNDLFSPCSISLICDVL 192
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 918-935 2.47e-03

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: 36.87  E-value: 2.47e-03
                          10
                  ....*....|....*...
gi 155371891  918 GDWSPCSKTCGKGYKKRT 935
Cdd:pfam19028   7 SEWSECSVTCGGGVQTRT 24
 
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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