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Conserved domains on  [gi|297707703|ref|XP_002830631|]
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A disintegrin and metalloproteinase with thrombospondin motifs 5 [Pongo abelii]

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 8.02e-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: 8.02e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 269 VELLLVADASMARLY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273    3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 425
Cdd:cd04273   83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 297707703 426 CEETFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 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 1.54e-32

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: 121.92  E-value: 1.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  733 KIVGTFNK-KSKGYTDVVRIPEGSTHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 811
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 297707703  812 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkplDVRYSFFVP 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 2.14e-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: 94.33  E-value: 2.14e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  487 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 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 1.15e-14

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 68.77  E-value: 1.15e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 297707703   570 WGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCS 622
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 66-182 1.35e-14

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.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 71.19  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703   66 QRRRSKGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDGSVGIAGFV-----PAGGGTSAPWRHRSHCFYRGTVDGSP 140
Cdd:pfam01562  13 RRRSLASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 297707703  141 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGpwAEEETGR---VY 182
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKY--SREEGGHphvVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 879-930 1.71e-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: 65.55  E-value: 1.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 297707703  879 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCPLSQRPSAFKQCLLKKC 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 1.92e-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: 64.73  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  628 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 697
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 297707703  698 CVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 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 8.02e-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: 8.02e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 269 VELLLVADASMARLY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273    3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 425
Cdd:cd04273   83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 297707703 426 CEETFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 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 1.54e-32

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: 121.92  E-value: 1.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  733 KIVGTFNK-KSKGYTDVVRIPEGSTHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 811
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 297707703  812 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkplDVRYSFFVP 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 3.62e-27

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: 109.70  E-value: 3.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  269 VELLLVADASMARLYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLGDKDKsLEVSKNAATTLKNFCKWQ 345
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  346 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 422
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 297707703  423 SK---FCEETFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 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 2.14e-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: 94.33  E-value: 2.14e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  487 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 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 1.15e-14

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 68.77  E-value: 1.15e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 297707703   570 WGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCS 622
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 66-182 1.35e-14

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: 71.19  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703   66 QRRRSKGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDGSVGIAGFV-----PAGGGTSAPWRHRSHCFYRGTVDGSP 140
Cdd:pfam01562  13 RRRSLASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 297707703  141 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGpwAEEETGR---VY 182
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKY--SREEGGHphvVY 128
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 879-930 1.71e-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: 65.55  E-value: 1.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 297707703  879 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCPLSQRPSAFKQCLLKKC 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 1.92e-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: 64.73  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  628 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 697
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 297707703  698 CVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 731
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 571-621 7.85e-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: 7.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 297707703  571 GSWGSWGQCSRSCGGGVQFAYRHCNNPaPRNNGRYCTGKRAIyRSCSLMPC 621
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 879-930 1.05e-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: 37.95  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 297707703   879 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCPLSQRPSAFKQCLLKKC 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 8.02e-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: 8.02e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 269 VELLLVADASMARLY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 347
Cdd:cd04273    3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 348 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 425
Cdd:cd04273   83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 297707703 426 CEETFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 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 2.05e-34

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


Pssm-ID: 239795  Cd Length: 192  Bit Score: 130.23  E-value: 2.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 269 VELLLVADASMARLYGRG---LQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQ 345
Cdd:cd04267    3 IELVVVADHRMVSYFNSDeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 346 HQHNQlgddheeHYDAAILFTREDLCGhhsCDTLGMADVGTICSPERSCAVIEDDG--LHAAFTVAHEIGHLLGLSHDDS 423
Cdd:cd04267   83 AEGPI-------RHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHDGG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 297707703 424 KFCEETFGStEDKRLMSSILTSIDaSKPWSKCTSATITEFLD 465
Cdd:cd04267  153 DELAFECDG-GGNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 733-852 1.54e-32

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: 121.92  E-value: 1.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  733 KIVGTFNK-KSKGYTDVVRIPEGSTHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 811
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 297707703  812 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkplDVRYSFFVP 852
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 269-474 3.40e-32

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: 123.88  E-value: 3.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 269 VELLLVADASMARLYGRGL---QHYLLTLASIANRLYSHAsienHIRLAVVKVVVLGDKDKsLEVSKNAATTLKNFCKWQ 345
Cdd:cd04269    3 VELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPL----NIRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLDWK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 346 HqhNQLGDDHeeHYDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDD 422
Cdd:cd04269   78 R--SNLLPRK--PHDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSRNlllFAVTMAHELGHNLGMEHDD 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297707703 423 SK-FCEETFGstedkrLMSSILTSIdaSKPWSKCTSATITEFLDDGHGNCLLD 474
Cdd:cd04269  150 GGcTCGRSTC------IMAPSPSSL--TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 269-476 3.62e-27

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: 109.70  E-value: 3.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  269 VELLLVADASMARLYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLGDKDKsLEVSKNAATTLKNFCKWQ 345
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  346 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 422
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 297707703  423 SK---FCEETFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 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 2.14e-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: 94.33  E-value: 2.14e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  487 PGQTYDATQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 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 1.15e-14

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 68.77  E-value: 1.15e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 297707703   570 WGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCS 622
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 66-182 1.35e-14

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: 71.19  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703   66 QRRRSKGLVQNIDQLYsgggkvgYLVYAGGRRFLLDLERDGSVGIAGFV-----PAGGGTSAPWRHRSHCFYRGTVDGSP 140
Cdd:pfam01562  13 RRRSLASESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 297707703  141 RSLAVFDLCGGLDGFFAVKHARYTLKPLLRGpwAEEETGR---VY 182
Cdd:pfam01562  86 DSSVALSTCSGLRGFIRTENEEYLIEPLEKY--SREEGGHphvVY 128
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 269-464 2.04e-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: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 269 VELLLVADASMARLYGRGLQ--HYLLTLASIANRLYShaSIEN-HIRLAVVKVVVlgDKDKSLEV--------SKNAATT 337
Cdd:cd04272    3 PELFVVVDYDHQSEFFSNEQliRYLAVMVNAANLRYR--DLKSpRIRLLLVGITI--SKDPDFEPyihpinygYIDAAET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 338 LKNFckwqhQHNQLGDDHEEHYDAAILFTREDLC----GHHSCDTLGMADVGTICSpERSCAVIED-----DGLHaafTV 408
Cdd:cd04272   79 LENF-----NEYVKKKRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDtpgsyYGVY---TM 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297707703 409 AHEIGHLLGLSHDDS---KFCEETFGST----EDKRLMSSILTSIDASKpWSKCTSATITEFL 464
Cdd:cd04272  150 THELAHLLGAPHDGSpppSWVKGHPGSLdcpwDDGYIMSYVVNGERQYR-FSQCSQRQIRNVF 211
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 879-930 1.71e-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: 65.55  E-value: 1.71e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 297707703  879 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCPLSQRPSAFKQCLLKKC 930
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 360-464 4.24e-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: 68.32  E-value: 4.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703 360 DAAILFTREDlcghHSCDTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDDSKFCEE---TFGST 433
Cdd:cd00203   53 DIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDdypTIDDT 128

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 297707703 434 ---EDKR---LMSSILTSIDA--SKPWSKCTSATITEFL 464
Cdd:cd00203  129 lnaEDDDyysVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 628-731 1.92e-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: 64.73  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  628 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpADVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 697
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 297707703  698 CVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 731
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 311-421 3.79e-12

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: 63.93  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  311 IRLAVVKVVVLgDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDdheehYDAAILFTREDLCGhhscdTLGMADVGTICSP 390
Cdd:pfam13582  20 IRLQLAAIIIT-TSADTPYTSSDALEILDELQEVNDTRIGQYG-----YDLGHLFTGRDGGG-----GGGIAYVGGVCNS 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 297707703  391 ERSCAVIEDD---GLHAAFTVAHEIGHLLGLSHD 421
Cdd:pfam13582  89 GSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
268-421 1.78e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 61.28  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  268 QVELLLVADASMARLYGR-GLQHYLLTLASIANRLYSHASienHIRLAVVKVVVL---GDKDKSLEVSKNAATTLKNFC- 342
Cdd:pfam13688   4 TVALLVAADCSYVAAFGGdAAQANIINMVNTASNVYERDF---NISLGLVNLTISdstCPYTPPACSTGDSSDRLSEFQd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  343 --KWQHQHNqlgddheehYDAAILFTredlcgHHSCDTLGMADVGTICSPERSCAVIEDDGLH--------AAFTVAHEI 412
Cdd:pfam13688  81 fsAWRGTQN---------DDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEI 145


                  ....*....
gi 297707703  413 GHLLGLSHD 421
Cdd:pfam13688 146 GHNFGAVHD 154
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 571-621 7.85e-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: 7.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 297707703  571 GSWGSWGQCSRSCGGGVQFAYRHCNNPaPRNNGRYCTGKRAIyRSCSLMPC 621
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
573-621 5.35e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.33  E-value: 5.35e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 297707703  573 WGSWGQCSRSCGGGVQFAYRHCNNPAPrnNGRYCTGKRAIYRSCSLMPC 621
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 574-621 4.82e-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: 41.67  E-value: 4.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 297707703  574 GSWGQCSRSCGGGVQfaYR--HCNNPAPR--NNGRYCTGKRA--IYRSCSLMPC 621
Cdd:pfam19030   4 GPWGECSVTCGGGVQ--TRlvQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 291-464 4.09e-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: 372637  Cd Length: 193  Bit Score: 42.62  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  291 LLTLASIANRLYSHASIEnhIRLAVVKVVvlgdkdkSLEVSKNAATTLKNFCK---WQHQHNQLGDD--HEEHYDAAILF 365
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDIN--INGGLVNPG-------EIPATTSASDSGNNYCNsptTIVRRLNFLSQwrGEQDYCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  366 TREDLCGhhscDTLGMADVGTICSPERSCaVIEDDGLHAAFT-------------VAHEIGHLLGLSHD------DSKFC 426
Cdd:pfam13574  78 TMGTFSG----GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdgsqyASSGC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 297707703  427 EETFGSTEDKRLMSSIL--TSIDASKPWSKCTSATITEFL 464
Cdd:pfam13574 153 ERNAATSVCSANGSFIMnpASKSNNDLFSPCSISLICDVL 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 879-930 1.05e-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: 37.95  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 297707703   879 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCPLSQRPSAFKQCLLKKC 930
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 356-460 1.13e-03

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 41.45  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297707703  356 EEHYDAAILFtREDLCGHHSCdtlGMADVGTICSPER-----SCAVIEDDGLHaafTVAHEIGHLLGLSHDDSKFCEETF 430
Cdd:pfam13583  89 SLNYDLAYLT-LMTGPSGQNV---GVAWVGALCSSARqnakaSGVARSRDEWD---IFAHEIGHTFGAVHDCSSQGEGLS 161

                          90       100       110
                  ....*....|....*....|....*....|..
gi 297707703  431 GSTEDKRlMSSILT--SIDASKPWSKCTSATI 460
Cdd:pfam13583 162 SSTEDGS-GQTIMSyaSTASQTAFSPCTIRNI 192
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 297707703  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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