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Conserved domains on  [gi|125490361|ref|NP_035912|]
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A disintegrin and metalloproteinase with thrombospondin motifs 5 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) ...
 269-473 9.40e-102

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: 315.72  E-value: 9.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 269 VELLLVADSSMARMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTDKDTSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273    3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 425
Cdd:cd04273   83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 125490361 426 CEENFgttEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 473
Cdd:cd04273  163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 733-852 9.47e-33

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: 122.69  E-value: 9.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  733 KIIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGW 811
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 125490361  812 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 852
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 487-554 8.46e-23

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


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.41  E-value: 8.46e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  487 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRVCLQGKCV 554
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 570-622 6.29e-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: 72.62  E-value: 6.29e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 125490361   570 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCP 622
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 68-182 9.92e-16

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: 74.66  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361   68 QRRS-GGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDTVGAAGSIVT----AGGGLSASSGHRGHCFYRGTVDGSP 142
Cdd:pfam01562  13 RRRSlASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTyyldGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 125490361  143 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEYER---IY 182
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHphvVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 879-930 3.60e-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: 64.78  E-value: 3.60e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 125490361  879 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 930
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 628-731 2.59e-12

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


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.34  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  628 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 697
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 125490361  698 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 731
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 269-473 9.40e-102

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: 315.72  E-value: 9.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 269 VELLLVADSSMARMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTDKDTSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273    3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 425
Cdd:cd04273   83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 125490361 426 CEENFgttEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 473
Cdd:cd04273  163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 733-852 9.47e-33

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: 122.69  E-value: 9.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  733 KIIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGW 811
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 125490361  812 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 852
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 269-476 1.55e-28

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: 113.55  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  269 VELLLVADSSMARMYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLTDKDtSLEVSKNAATTLKNFCKWQ 345
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDED-KIDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  346 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 422
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 125490361  423 SK---FCEENFGTtedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 476
Cdd:pfam01421 150 FNggcKCPPGGGC-----IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 487-554 8.46e-23

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.41  E-value: 8.46e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  487 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRVCLQGKCV 554
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 570-622 6.29e-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: 72.62  E-value: 6.29e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 125490361   570 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCP 622
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 68-182 9.92e-16

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: 74.66  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361   68 QRRS-GGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDTVGAAGSIVT----AGGGLSASSGHRGHCFYRGTVDGSP 142
Cdd:pfam01562  13 RRRSlASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTyyldGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 125490361  143 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEYER---IY 182
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHphvVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 879-930 3.60e-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: 64.78  E-value: 3.60e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 125490361  879 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 930
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 628-731 2.59e-12

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


Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.34  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  628 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 697
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 125490361  698 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 731
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
573-621 4.84e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 4.84e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 125490361  573 WGPWGQCSRSCGGGVQFAYRHCNNPAPRNSgrYCTGKRAIYRSCSVTPC 621
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 879-930 3.05e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.80  E-value: 3.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 125490361   879 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCLLSQRPSAFKQCLLKKC 930
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 269-473 9.40e-102

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: 315.72  E-value: 9.40e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 269 VELLLVADSSMARMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTDKDTSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273    3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 425
Cdd:cd04273   83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 125490361 426 CEENFgttEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 473
Cdd:cd04273  163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 269-465 2.16e-35

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: 132.93  E-value: 2.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 269 VELLLVADSSMaRMYGRG----LQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTDKDTSLEVSKNAATTLKNFCKW 344
Cdd:cd04267    3 IELVVVADHRM-VSYFNSdeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 345 QHQHNQlgddheeHYDAAILFTREDLCGhhsCDTLGMADVGTICSPERSCAVIEDDG--LHAAFTVAHEIGHLLGLSHDD 422
Cdd:cd04267   82 RAEGPI-------RHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHDG 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 125490361 423 SKFCEENFGtTEDKRLMSSILTSIDaSKPWSKCTSATITEFLD 465
Cdd:cd04267  152 GDELAFECD-GGGNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 269-474 2.15e-33

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: 127.35  E-value: 2.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 269 VELLLVADSSMARMYGRGL---QHYLLTLASIANRLYSHAsienHIRLAVVKVVVLTDKDtSLEVSKNAATTLKNFCKWQ 345
Cdd:cd04269    3 VELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPL----NIRVVLVGLEIWTDKD-KISVSGDAGETLNRFLDWK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 346 HqhNQLGDDHeeHYDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDD 422
Cdd:cd04269   78 R--SNLLPRK--PHDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSRNlllFAVTMAHELGHNLGMEHDD 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 125490361 423 SK-FCEENFGttedkrLMSSILTSIdaSKPWSKCTSATITEFLDDGHGNCLLD 474
Cdd:cd04269  150 GGcTCGRSTC------IMAPSPSSL--TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 733-852 9.47e-33

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: 122.69  E-value: 9.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  733 KIIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGW 811
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 125490361  812 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 852
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 269-476 1.55e-28

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: 113.55  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  269 VELLLVADSSMARMYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLTDKDtSLEVSKNAATTLKNFCKWQ 345
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDED-KIDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  346 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 422
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 125490361  423 SK---FCEENFGTtedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 476
Cdd:pfam01421 150 FNggcKCPPGGGC-----IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 487-554 8.46e-23

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


Pssm-ID: 465496  Cd Length: 68  Bit Score: 92.41  E-value: 8.46e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  487 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRVCLQGKCV 554
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 570-622 6.29e-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: 72.62  E-value: 6.29e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 125490361   570 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCP 622
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 68-182 9.92e-16

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: 74.66  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361   68 QRRS-GGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDTVGAAGSIVT----AGGGLSASSGHRGHCFYRGTVDGSP 142
Cdd:pfam01562  13 RRRSlASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTyyldGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 125490361  143 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEYER---IY 182
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHphvVY 128
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 269-464 1.85e-14

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 73.54  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 269 VELLLVADSSMARMYGRGLQ--HYLLTLASIANRLYShaSIEN-HIRLAVVKVVVLTDKDTSL----EVSKN--AATTLK 339
Cdd:cd04272    3 PELFVVVDYDHQSEFFSNEQliRYLAVMVNAANLRYR--DLKSpRIRLLLVGITISKDPDFEPyihpINYGYidAAETLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 340 NFckwqhQHNQLGDDHEEHYDAAILFTREDLC----GHHSCDTLGMADVGTICSpERSCAVIED-----DGLHaafTVAH 410
Cdd:cd04272   81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDtpgsyYGVY---TMTH 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125490361 411 EIGHLLGLSHDDS---KFCEENFGTT----EDKRLMSSILTSIDASKpWSKCTSATITEFL 464
Cdd:cd04272  152 ELAHLLGAPHDGSpppSWVKGHPGSLdcpwDDGYIMSYVVNGERQYR-FSQCSQRQIRNVF 211
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 311-421 8.47e-14

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: 68.94  E-value: 8.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  311 IRLAVVKVVVLTDKDTSlEVSKNAATTLKNFCKWQHQHNQLGDdheehYDAAILFTREDLCGhhscdTLGMADVGTICSP 390
Cdd:pfam13582  20 IRLQLAAIIITTSADTP-YTSSDALEILDELQEVNDTRIGQYG-----YDLGHLFTGRDGGG-----GGGIAYVGGVCNS 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 125490361  391 ERSCAVIEDD---GLHAAFTVAHEIGHLLGLSHD 421
Cdd:pfam13582  89 GSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 360-464 1.29e-13

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: 69.47  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361 360 DAAILFTREDlcghHSCDTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDDSKFCEENFGTTEDK 436
Cdd:cd00203   53 DIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDT 128

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 125490361 437 R---------LMSSILTSIDA--SKPWSKCTSATITEFL 464
Cdd:cd00203  129 LnaedddyysVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 879-930 3.60e-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: 64.78  E-value: 3.60e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 125490361  879 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 930
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 628-731 2.59e-12

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


Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.34  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  628 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 697
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 125490361  698 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 731
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
268-421 9.80e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 64.75  E-value: 9.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  268 QVELLLVADSS-MARMYGRGLQHYLLTLASIANRLYSHASienHIRLAVVKVVVLTDKDT---SLEVSKNAATTLKNFC- 342
Cdd:pfam13688   4 TVALLVAADCSyVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPytpPACSTGDSSDRLSEFQd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  343 --KWQHQHNqlgddheehYDAAILFTredlcgHHSCDTLGMADVGTICSPERSCAVIEDDGLH--------AAFTVAHEI 412
Cdd:pfam13688  81 fsAWRGTQN---------DDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEI 145


                  ....*....
gi 125490361  413 GHLLGLSHD 421
Cdd:pfam13688 146 GHNFGAVHD 154
TSP_1 pfam00090
Thrombospondin type 1 domain;
573-621 4.84e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 4.84e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 125490361  573 WGPWGQCSRSCGGGVQFAYRHCNNPAPRNSgrYCTGKRAIYRSCSVTPC 621
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 571-621 3.81e-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: 44.58  E-value: 3.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 125490361  571 GSWGPWGQCSRSCGGGVQFAYRHCNNPaPRNSGRYCTGKRAIyRSCSVTPC 621
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 291-464 1.00e-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: 47.24  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  291 LLTLASIANRLYSHASIENHIRLA-VVKVVVLTDKDTSLEVSKNAATT----LKNFCKWQHQHNqlgddheehYDAAILF 365
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDININGGLVnPGEIPATTSASDSGNNYCNSPTTivrrLNFLSQWRGEQD---------YCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  366 TREDLCGhhscDTLGMADVGTICSPERSCaVIEDDGLHAAFT-------------VAHEIGHLLGLSHD------DSKFC 426
Cdd:pfam13574  78 TMGTFSG----GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdgsqyASSGC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 125490361  427 EENFGTTEDKRLMSSIL--TSIDASKPWSKCTSATITEFL 464
Cdd:pfam13574 153 ERNAATSVCSANGSFIMnpASKSNNDLFSPCSISLICDVL 192
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 574-621 2.03e-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: 42.83  E-value: 2.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 125490361  574 GPWGQCSRSCGGGVQfaYR--HCNNPAPR--NSGRYCTGKRA--IYRSCSVTPC 621
Cdd:pfam19030   4 GPWGECSVTCGGGVQ--TRlvQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 269-460 1.02e-04

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 44.53  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  269 VELLLVADSSMARMYGR--GLQHYLLTLASIANRLYSHaSIENHIRLAVVKVVVLTDKDTSLEVSKNAATTLKN-----F 341
Cdd:pfam13583   5 YRVAVATDCTYSASFGSvdELRANINATVTTANEVYGR-DFNVSLALISDRDVIYTDSSTDSFNADCSGGDLGNwrlatL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125490361  342 CKWQHQHNqlgddheehYDAAILFtREDLCGHHSCdtlGMADVGTICSPER-----SCAVIEDDGLHaafTVAHEIGHLL 416
Cdd:pfam13583  84 TSWRDSLN---------YDLAYLT-LMTGPSGQNV---GVAWVGALCSSARqnakaSGVARSRDEWD---IFAHEIGHTF 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 125490361  417 GLSHDDSKFCEENFGTTEDKRlMSSILT--SIDASKPWSKCTSATI 460
Cdd:pfam13583 148 GAVHDCSSQGEGLSSSTEDGS-GQTIMSyaSTASQTAFSPCTIRNI 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 879-930 3.05e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.80  E-value: 3.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 125490361   879 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCLLSQRPSAFKQCLLKKC 930
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 406-420 6.91e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 38.37  E-value: 6.91e-03
                          10
                  ....*....|....*.
gi 125490361  406 FTVA-HEIGHLLGLSH 420
Cdd:pfam00413 109 FLVAaHEIGHALGLGH 124
 
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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