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Conserved domains on  [gi|157951646|ref|NP_033751|]
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A disintegrin and metalloproteinase with thrombospondin motifs 1 preproprotein [Mus musculus]

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) ...
 259-464 3.03e-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: 336.13  E-value: 3.03e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 259 RYVETMLVADQSMADF-HGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQ 337
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 338 KQHNSPSDRDPEHYDTAILFTRQDLCGSH-TCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 415
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157951646 416 KHCASlngVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECL 464
Cdd:cd04273  161 NSCGP---EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 727-843 7.21e-38

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: 137.32  E-value: 7.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  727 KMSGIVTSTR-PGYHDIVTIPAGATNIEVKHRNqrgsrNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGS 805
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 157951646  806 SAALERIRSFSPLKEPLTIQVLMV-GHALRPKIKFTYFM 843
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 ...
 479-547 3.24e-25

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: 99.34  E-value: 3.24e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  479 PGTLYDANRQCQFTFGEESKHCPDA-ASTCTTLWCTGTSGGllVCQTKHFPWADGTSCGEGKWCVSGKCV 547
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGS--TCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 72-194 7.81e-25

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: 100.47  E-value: 7.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   72 PGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSpGSEAQHLDPTGDlaHCFYSGTVNGDPGSAAALSLCEG 151
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDG-GTGVESPPVQTD--HCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 157951646  152 VRGAFYLQGEEFFIQPAPGvaterlapavPEEESSARPqfHIL 194
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLEK----------YSREEGGHP--HVV 127
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 563-615 8.35e-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: 72.23  E-value: 8.35e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157951646   563 WGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCP 615
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 859-910 2.30e-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: 68.25  E-value: 2.30e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157951646  859 WVIEEWGECSKTCGSGWQRRVVQCRDINGH---PASECAKEVKPASTRPCADLPC 910
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 913-967 1.45e-13

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.94  E-value: 1.45e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157951646  913 WQVGDWSPCSKTCGKGYKKRTLKCV-SHDGGVLSNESCDPLKKPkHYIDFCTLTQC 967
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 ...
 622-725 2.67e-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: 55.87  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  622 FREEQC-EAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPD------STSVCVQ 694
Cdd:pfam19236   5 FMSQQCaRTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 157951646  695 GQCVKAGCDRIIDSKKKFDKCGVCGGNGSTC 725
Cdd:pfam19236  85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 259-464 3.03e-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: 336.13  E-value: 3.03e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 259 RYVETMLVADQSMADF-HGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQ 337
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 338 KQHNSPSDRDPEHYDTAILFTRQDLCGSH-TCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 415
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157951646 416 KHCASlngVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECL 464
Cdd:cd04273  161 NSCGP---EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 727-843 7.21e-38

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: 137.32  E-value: 7.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  727 KMSGIVTSTR-PGYHDIVTIPAGATNIEVKHRNqrgsrNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGS 805
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 157951646  806 SAALERIRSFSPLKEPLTIQVLMV-GHALRPKIKFTYFM 843
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 ...
 479-547 3.24e-25

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: 99.34  E-value: 3.24e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  479 PGTLYDANRQCQFTFGEESKHCPDA-ASTCTTLWCTGTSGGllVCQTKHFPWADGTSCGEGKWCVSGKCV 547
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGS--TCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 72-194 7.81e-25

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: 100.47  E-value: 7.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   72 PGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSpGSEAQHLDPTGDlaHCFYSGTVNGDPGSAAALSLCEG 151
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDG-GTGVESPPVQTD--HCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 157951646  152 VRGAFYLQGEEFFIQPAPGvaterlapavPEEESSARPqfHIL 194
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLEK----------YSREEGGHP--HVV 127
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 259-468 1.40e-23

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: 99.30  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  259 RYVETMLVADQSMADFHGSGLKHYLLTLFSVAA---RFYKHPSIRnsislVVVKILVIYEEQKGPEVTSNAALTLRNFCS 335
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNlvnSIYKELNIR-----VVLVGLEIWTDEDKIDVSGDANDTLRNFLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  336 WQKQHNSPSDRdpehYDTAILFTRQDLCGShtcdTLGMADVGTVCDPSRSCSVIED---DGLQAAFTTAHELGHVFNMPH 412
Cdd:pfam01421  76 WRQEYLKKRKP----HDVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157951646  413 DDAK---HCAslngvSGDSHLMASMLSSlDHSQPWSPCSAYMVTSFLDNGHGECLMDKP 468
Cdd:pfam01421 148 DDFNggcKCP-----PGGGCIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 563-615 8.35e-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: 72.23  E-value: 8.35e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157951646   563 WGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCP 615
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 859-910 2.30e-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: 68.25  E-value: 2.30e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157951646  859 WVIEEWGECSKTCGSGWQRRVVQCRDINGH---PASECAKEVKPASTRPCADLPC 910
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 913-967 1.45e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.94  E-value: 1.45e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157951646  913 WQVGDWSPCSKTCGKGYKKRTLKCV-SHDGGVLSNESCDPLKKPkHYIDFCTLTQC 967
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ACR smart00608
ADAM Cysteine-Rich Domain;
469-549 1.70e-11

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 62.76  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   469 QNPIKLPSD----LPGTLYDANRQCQFTFGEESK----HCPDAAST------------------------CTTLWCTGTS 516
Cdd:smart00608   1 QDGTPCDNGqgycYNGRCPTRDNQCQALFGPGAKvapdSCYEELNTkgdrfgncgrengtyipcapedvkCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157951646   517 G---------------GLLVCQTKHFP---------WADGTSCGEGKWCVSGKCVNK 549
Cdd:smart00608  81 ElpllgehatviysniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 622-725 2.67e-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: 55.87  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  622 FREEQC-EAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPD------STSVCVQ 694
Cdd:pfam19236   5 FMSQQCaRTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 157951646  695 GQCVKAGCDRIIDSKKKFDKCGVCGGNGSTC 725
Cdd:pfam19236  85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
564-614 1.48e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 1.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157951646  564 GPWGPWGDCSRTCGGGVQYTMRECDNPVPknGGKYCEGKRVRYRSCNIEDC 614
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 857-911 7.46e-08

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: 49.51  E-value: 7.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157951646   857 SEWviEEWGECSKTCGSGWQRRVVQCRDING-HPASECAKEVKpaSTRPCADLPCP 911
Cdd:smart00209   2 SEW--SEWSPCSVTCGGGVQTRTRSCCSPPPqNGGGPCTGEDV--ETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 912-954 6.32e-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: 41.42  E-value: 6.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 157951646   912 HWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSnESCDPLKK 954
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGG-GPCTGEDV 42
ACR smart00608
ADAM Cysteine-Rich Domain;
530-699 8.83e-03

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 37.72  E-value: 8.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   530 ADGTSCGEGKW-CVSGKCvnkTDMKHfatpvhgswgpwgpwgDCSRTCGGGVQYTMRECDNPVPKNGGK--YCEGKRVRY 606
Cdd:smart00608   1 QDGTPCDNGQGyCYNGRC---PTRDN----------------QCQALFGPGAKVAPDSCYEELNTKGDRfgNCGRENGTY 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   607 RSCNIED--CpdnnGKTfreeQCEahNEFSKASFGNEPTVEWTPKYagvspkdrcKLTCeaKGIGYFFVLQPK---VVDG 681
Cdd:smart00608  62 IPCAPEDvkC----GKL----QCT--NVSELPLLGEHATVIYSNIG---------GLVC--WSLDYHLGTDPDigmVKDG 120

                          170
                   ....*....|....*...
gi 157951646   682 TPCSPDstSVCVQGQCVK 699
Cdd:smart00608 121 TKCGPG--KVCINGQCVD 136
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 259-464 3.03e-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: 336.13  E-value: 3.03e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 259 RYVETMLVADQSMADF-HGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQ 337
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 338 KQHNSPSDRDPEHYDTAILFTRQDLCGSH-TCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDA- 415
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSNgNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157951646 416 KHCASlngVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECL 464
Cdd:cd04273  161 NSCGP---EGKDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 259-457 7.77e-41

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: 148.72  E-value: 7.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 259 RYVETMLVADQSM---ADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCS 335
Cdd:cd04267    1 REIELVVVADHRMvsyFNSDENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 336 WQKqhnspsdRDPEHYDTAILFTRQDLCGshtCDTLGMADVGTVCDPSRSCSVIEDDG--LQAAFTTAHELGHVFNMPHD 413
Cdd:cd04267   81 WRA-------EGPIRHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHD 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 157951646 414 DAkHCASLNGVSGDSHLMASMLSSLDhSQPWSPCSAYMVTSFLD 457
Cdd:cd04267  151 GG-DELAFECDGGGNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 727-843 7.21e-38

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: 137.32  E-value: 7.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  727 KMSGIVTSTR-PGYHDIVTIPAGATNIEVKHRNqrgsrNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGS 805
Cdd:pfam05986   1 TVSGSFTEGRaKGYVTFVTIPAGATHIHIVNRK-----PSFTHLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 157951646  806 SAALERIRSFSPLKEPLTIQVLMV-GHALRPKIKFTYFM 843
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFI 114
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 259-466 1.16e-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: 119.64  E-value: 1.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 259 RYVETMLVADQSMADFHGSGL---KHYLLTLFSVAARFYKHPSIRnsislVVVKILVIYEEQKGPEVTSNAALTLRNFCS 335
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPLNIR-----VVLVGLEIWTDKDKISVSGDAGETLNRFLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 336 WQKqhnspSDRDPEH-YDTAILFTRQDLCGshtcDTLGMADVGTVCDPSRSCSVIEDDG---LQAAFTTAHELGHVFNMP 411
Cdd:cd04269   76 WKR-----SNLLPRKpHDNAQLLTGRDFDG----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGME 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157951646 412 HDDAK-HCaslngvSGDSHLMASmlSSLDHSQPWSPCSAYMVTSFLDNGHGECLMD 466
Cdd:cd04269  147 HDDGGcTC------GRSTCIMAP--SPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 479-547 3.24e-25

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: 99.34  E-value: 3.24e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  479 PGTLYDANRQCQFTFGEESKHCPDA-ASTCTTLWCTGTSGGllVCQTKHFPWADGTSCGEGKWCVSGKCV 547
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGGS--TCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 72-194 7.81e-25

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: 100.47  E-value: 7.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   72 PGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSpGSEAQHLDPTGDlaHCFYSGTVNGDPGSAAALSLCEG 151
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDG-GTGVESPPVQTD--HCYYQGHVEGHPDSSVALSTCSG 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 157951646  152 VRGAFYLQGEEFFIQPAPGvaterlapavPEEESSARPqfHIL 194
Cdd:pfam01562  97 LRGFIRTENEEYLIEPLEK----------YSREEGGHP--HVV 127
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 259-468 1.40e-23

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: 99.30  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  259 RYVETMLVADQSMADFHGSGLKHYLLTLFSVAA---RFYKHPSIRnsislVVVKILVIYEEQKGPEVTSNAALTLRNFCS 335
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNlvnSIYKELNIR-----VVLVGLEIWTDEDKIDVSGDANDTLRNFLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  336 WQKQHNSPSDRdpehYDTAILFTRQDLCGShtcdTLGMADVGTVCDPSRSCSVIED---DGLQAAFTTAHELGHVFNMPH 412
Cdd:pfam01421  76 WRQEYLKKRKP----HDVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQH 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157951646  413 DDAK---HCAslngvSGDSHLMASMLSSlDHSQPWSPCSAYMVTSFLDNGHGECLMDKP 468
Cdd:pfam01421 148 DDFNggcKCP-----PGGGCIMNPSAGS-SFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 563-615 8.35e-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: 72.23  E-value: 8.35e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157951646   563 WGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCP 615
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 342-449 3.13e-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: 74.48  E-value: 3.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 342 SPSDRDPEHYDTAILFTRQDlcgsHTCDTLGMADVGTVCDPSRSCSVIEDDGL---QAAFTTAHELGHVFNMPHDDA--- 415
Cdd:cd00203   43 VLVGVEIDKADIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSgtkEGAQTIAHELGHALGFYHDHDrkd 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157951646 416 ------KHCASLNGVSGDSHLMASMLSSLDHSQ--PWSPCSA 449
Cdd:cd00203  119 rddyptIDDTLNAEDDDYYSVMSYTKGSFSDGQrkDFSQCDI 160
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 859-910 2.30e-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: 68.25  E-value: 2.30e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157951646  859 WVIEEWGECSKTCGSGWQRRVVQCRDINGH---PASECAKEVKPASTRPCADLPC 910
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGsivPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 913-967 1.45e-13

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.94  E-value: 1.45e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157951646  913 WQVGDWSPCSKTCGKGYKKRTLKCV-SHDGGVLSNESCDPLKKPkHYIDFCTLTQC 967
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqKGGGSIVPDSECSAQKKP-PETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 260-464 1.19e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 68.15  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 260 YVETMLVADQsmaDFHGSG-----LKHYLLTLFSVAARFYKhpSIRN-SISLVVVKILV-------IYEEQKGPEVTsNA 326
Cdd:cd04272    2 YPELFVVVDY---DHQSEFfsneqLIRYLAVMVNAANLRYR--DLKSpRIRLLLVGITIskdpdfePYIHPINYGYI-DA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 327 ALTLRNFCSWQKQhnspsDRDPEHYDTAILFTRQDLC----GSHTCDTLGMADVGTVCDpSRSCSVIEDDG--LQAAFTT 400
Cdd:cd04272   76 AETLENFNEYVKK-----KRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDTPgsYYGVYTM 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157951646 401 AHELGHVFNMPHDDAKHCASLNGVSG-------DSHLMASMLSSLDHSQpWSPCSAYMVTSFLDNGHGECL 464
Cdd:cd04272  150 THELAHLLGAPHDGSPPPSWVKGHPGsldcpwdDGYIMSYVVNGERQYR-FSQCSQRQIRNVFRRLGASCL 219
ACR smart00608
ADAM Cysteine-Rich Domain;
469-549 1.70e-11

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 62.76  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   469 QNPIKLPSD----LPGTLYDANRQCQFTFGEESK----HCPDAAST------------------------CTTLWCTGTS 516
Cdd:smart00608   1 QDGTPCDNGqgycYNGRCPTRDNQCQALFGPGAKvapdSCYEELNTkgdrfgncgrengtyipcapedvkCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157951646   517 G---------------GLLVCQTKHFP---------WADGTSCGEGKWCVSGKCVNK 549
Cdd:smart00608  81 ElpllgehatviysniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVDV 137
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 302-413 1.29e-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: 56.99  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  302 SISLVVVKIlVIYEEQKGPEVTSNAALTLRNFCSWQKQHnspsdRDPEHYDTAILFTRQDLCGshtcdTLGMADVGTVCD 381
Cdd:pfam13582  19 GIRLQLAAI-IITTSADTPYTSSDALEILDELQEVNDTR-----IGQYGYDLGHLFTGRDGGG-----GGGIAYVGGVCN 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 157951646  382 PSRSCSVIEDD---GLQAAFTTAHELGHVFNMPHD 413
Cdd:pfam13582  88 SGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 622-725 2.67e-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: 55.87  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  622 FREEQC-EAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPD------STSVCVQ 694
Cdd:pfam19236   5 FMSQQCaRTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 157951646  695 GQCVKAGCDRIIDSKKKFDKCGVCGGNGSTC 725
Cdd:pfam19236  85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
257-425 3.49e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 57.43  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  257 SPRYVETMLVADQS-MADFHGSGLKHYLLTLFSVAARFYKHPSirnSISLVVVKIlVIYEEQK----GPEVTSNAALTLR 331
Cdd:pfam13688   1 STRTVALLVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNL-TISDSTCpytpPACSTGDSSDRLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646  332 NFCSwqkqhnSPSDRDPEHYDTAILFTRQDlcgshtCDTLGMADVGTVCDPSRSCSVIEDDG--------LQAAFTTAHE 403
Cdd:pfam13688  77 EFQD------FSAWRGTQNDDLAYLFLMTN------CSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHE 144

                         170       180
                  ....*....|....*....|..
gi 157951646  404 LGHVFNMPHDdakHCASLNGVS 425
Cdd:pfam13688 145 IGHNFGAVHD---CDSSTSSQC 163
TSP_1 pfam00090
Thrombospondin type 1 domain;
564-614 1.48e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.65  E-value: 1.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157951646  564 GPWGPWGDCSRTCGGGVQYTMRECDNPVPknGGKYCEGKRVRYRSCNIEDC 614
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 857-911 7.46e-08

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: 49.51  E-value: 7.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 157951646   857 SEWviEEWGECSKTCGSGWQRRVVQCRDING-HPASECAKEVKpaSTRPCADLPCP 911
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 ...
 564-614 8.25e-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: 46.50  E-value: 8.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157951646  564 GPWGPWGDCSRTCGGGVQYTMRECDNPvPKNGGKYCEGKRVRyRSCNIEDC 614
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 857-910 8.96e-06

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: 43.81  E-value: 8.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157951646  857 SEWviEEWGECSKTCGSGWQRRVvqcRDINGHPA---SECAKEVKpasTRPCADLPC 910
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 ...
 567-614 4.09e-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: 42.05  E-value: 4.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157951646  567 GPWGDCSRTCGGGVQYTMRECDNPVPK--NGGKYCEGKR--VRYRSCNIEDC 614
Cdd:pfam19030   4 GPWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKkpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 912-954 6.32e-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: 41.42  E-value: 6.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 157951646   912 HWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSnESCDPLKK 954
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGG-GPCTGEDV 42
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 354-472 1.41e-03

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: 41.59  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646 354 AILFTRQDLCGShtcdTLGMADVGTVCDPSRS--CSVIE----------DDGL-------------QAAFTTAHELGHVF 408
Cdd:cd04270  104 AHLFTYRDFDMG----TLGLAYVGSPRDNSAGgiCEKAYyysngkkkylNTGLtttvnygkrvptkESDLVTAHELGHNF 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157951646 409 NMPHD-DAKHCASlNGVSGDSHLMASMLSSLDH--SQPWSPCSAYMVTSFLDNGHGECLMDkPQNPI 472
Cdd:cd04270  180 GSPHDpDIAECAP-GESQGGNYIMYARATSGDKenNKKFSPCSKKSISKVLEVKSNSCFVE-RSQSF 244
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 916-933 2.97e-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: 36.49  E-value: 2.97e-03
                          10
                  ....*....|....*...
gi 157951646  916 GDWSPCSKTCGKGYKKRT 933
Cdd:pfam19028   7 SEWSECSVTCGGGVQTRT 24
TSP_1 pfam00090
Thrombospondin type 1 domain;
916-938 3.43e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.24  E-value: 3.43e-03
                          10        20
                  ....*....|....*....|...
gi 157951646  916 GDWSPCSKTCGKGYKKRTLKCVS 938
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTCKS 26
ACR smart00608
ADAM Cysteine-Rich Domain;
530-699 8.83e-03

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 37.72  E-value: 8.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   530 ADGTSCGEGKW-CVSGKCvnkTDMKHfatpvhgswgpwgpwgDCSRTCGGGVQYTMRECDNPVPKNGGK--YCEGKRVRY 606
Cdd:smart00608   1 QDGTPCDNGQGyCYNGRC---PTRDN----------------QCQALFGPGAKVAPDSCYEELNTKGDRfgNCGRENGTY 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951646   607 RSCNIED--CpdnnGKTfreeQCEahNEFSKASFGNEPTVEWTPKYagvspkdrcKLTCeaKGIGYFFVLQPK---VVDG 681
Cdd:smart00608  62 IPCAPEDvkC----GKL----QCT--NVSELPLLGEHATVIYSNIG---------GLVC--WSLDYHLGTDPDigmVKDG 120

                          170
                   ....*....|....*...
gi 157951646   682 TPCSPDstSVCVQGQCVK 699
Cdd:smart00608 121 TKCGPG--KVCINGQCVD 136
 
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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