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Conserved domains on  [gi|109109297|ref|XP_001113698|]
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A disintegrin and metalloproteinase with thrombospondin motifs 15 [Macaca mulatta]

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) ...
 218-424 4.03e-111

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: 340.76  E-value: 4.03e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 218 RYVETLVVADESMVKF-HGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLRDRDSGPKVTGNAALTLRNFCAWQ 296
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 297 KKLNKVSDKHPEYWDTAILFTRQDLCGA-TTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNV- 374
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109109297 375 KVCEEVFGKlraNHMMSPTLIQIDRANPWSACSAAIITDFLDSGHGDCLL 424
Cdd:cd04273  161 NSCGPEGKD---GHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 684-801 1.96e-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: 138.87  E-value: 1.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  684 KVTGLFTK-PMHGYNFVVAIPAGASSIDIRQRGYKGligddNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSLLRYSGT 762
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 109109297  763 GTAVESLQASRPILEPLTVEVLSV-GKMTPPRVRYSFYLP 801
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 24-149 7.11e-26

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: 103.55  E-value: 7.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297   24 EVVVPIRLDPDINGRRyywRGPEDSGDQGLIFQITAFQEDFYLHLTPDAQFLAPAFATEHLGVPLQGFTGSSSDLRRCFY 103
Cdd:pfam01562   1 EVVIPVRLDPSRRRRS---LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 109109297  104 SGDVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNASAPAAQR 149
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 438-505 2.92e-22

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: 90.87  E-value: 2.92e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  438 PGASYTLSQQCELAFGVGSKPCPYMQY--CTKLWCtgKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACV 505
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEdvCSKLWC--SNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 843-894 3.33e-15

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: 70.56  E-value: 3.33e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 109109297  843 WVAGSWGPCSVSCGSGLQKRAVDCRGSPGQRTVPA--CDAAHRPVETQACGE-PC 894
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDseCSAQKKPPETQSCNLkPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 519-571 1.24e-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: 1.24e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 109109297   519 WAKWEPYGPCSRTCGGGVQLARRQCTNPTPANGGKYCEGVRVKYRSCNLEPCP 571
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 897-950 2.26e-12

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


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.47  E-value: 2.26e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 109109297  897 WELSAWSPCSKSCGRGFKRRPLKCVG-HGGRLLARDQCNLRRKPQELDFCVLRPC 950
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 ...
 616-682 8.17e-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: 62.80  E-value: 8.17e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109109297  616 CKLICRANGTGYFYVLAPKVVDGTLCSPD------STSVCVQGKCIKAGCDGNLGSKKRFDKCGVCGGDNKSC 682
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 218-424 4.03e-111

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: 340.76  E-value: 4.03e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 218 RYVETLVVADESMVKF-HGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLRDRDSGPKVTGNAALTLRNFCAWQ 296
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 297 KKLNKVSDKHPEYWDTAILFTRQDLCGA-TTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNV- 374
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109109297 375 KVCEEVFGKlraNHMMSPTLIQIDRANPWSACSAAIITDFLDSGHGDCLL 424
Cdd:cd04273  161 NSCGPEGKD---GHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 684-801 1.96e-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: 138.87  E-value: 1.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  684 KVTGLFTK-PMHGYNFVVAIPAGASSIDIRQRGYKGligddNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSLLRYSGT 762
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 109109297  763 GTAVESLQASRPILEPLTVEVLSV-GKMTPPRVRYSFYLP 801
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 24-149 7.11e-26

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: 103.55  E-value: 7.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297   24 EVVVPIRLDPDINGRRyywRGPEDSGDQGLIFQITAFQEDFYLHLTPDAQFLAPAFATEHLGVPLQGFTGSSSDLRRCFY 103
Cdd:pfam01562   1 EVVIPVRLDPSRRRRS---LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 109109297  104 SGDVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNASAPAAQR 149
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 218-427 2.06e-24

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: 101.61  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  218 RYVETLVVADESMVKFHGADLEH---YLLTLLATAARLYRhpsilnPINIVVVKVLL--LRDRDSgPKVTGNAALTLRNF 292
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK------ELNIRVVLVGLeiWTDEDK-IDVSGDANDTLRNF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  293 CAWQKKLNKVSDKHpeywDTAILFTRQDLCGATTcdtlGMADVGTMCDPKRSCSVIEDdGLPS----AFTTAHELGHVFN 368
Cdd:pfam01421  74 LKWRQEYLKKRKPH----DVAQLLSGVEFGGTTV----GAAYVGGMCSLEYSGGVNED-HSKNlesfAVTMAHELGHNLG 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109109297  369 MPHDNVKV---CEEVFGKLranhmMSPTLIQIDrANPWSACSAAIITDFLDSGHGDCLLDQP 427
Cdd:pfam01421 145 MQHDDFNGgckCPPGGGCI-----MNPSAGSSF-PRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 438-505 2.92e-22

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: 90.87  E-value: 2.92e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  438 PGASYTLSQQCELAFGVGSKPCPYMQY--CTKLWCtgKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACV 505
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEdvCSKLWC--SNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 843-894 3.33e-15

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: 70.56  E-value: 3.33e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 109109297  843 WVAGSWGPCSVSCGSGLQKRAVDCRGSPGQRTVPA--CDAAHRPVETQACGE-PC 894
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDseCSAQKKPPETQSCNLkPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 519-571 1.24e-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: 1.24e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 109109297   519 WAKWEPYGPCSRTCGGGVQLARRQCTNPTPANGGKYCEGVRVKYRSCNLEPCP 571
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 897-950 2.26e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.47  E-value: 2.26e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 109109297  897 WELSAWSPCSKSCGRGFKRRPLKCVG-HGGRLLARDQCNLRRKPQELDFCVLRPC 950
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 ...
 616-682 8.17e-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: 62.80  E-value: 8.17e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109109297  616 CKLICRANGTGYFYVLAPKVVDGTLCSPD------STSVCVQGKCIKAGCDGNLGSKKRFDKCGVCGGDNKSC 682
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 846-895 8.24e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.81  E-value: 8.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 109109297   846 GSWGPCSVSCGSGLQKRAVDCRGSPGQRTVPACDAAHRpvETQAC-GEPCP 895
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDV--ETRACnEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
522-570 1.56e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.87  E-value: 1.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 109109297  522 WEPYGPCSRTCGGGVQLARRQCTNPTPanGGKYCEGVRVKYRSCNLEPC 570
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ACR smart00608
ADAM Cysteine-Rich Domain;
437-506 2.25e-05

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 45.04  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297   437 LPGASYTLSQQCELAFGVGSKPCPYMQY-----------------------------CTKLWCTGKAK------------ 475
Cdd:smart00608  14 YNGRCPTRDNQCQALFGPGAKVAPDSCYeelntkgdrfgncgrengtyipcapedvkCGKLQCTNVSElpllgehatviy 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 109109297   476 ---GQMVCQTRHFP---------WADGTSCGEGKFCLKGACVE 506
Cdd:smart00608  94 sniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVD 136
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 897-950 8.17e-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: 41.03  E-value: 8.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 109109297   897 WELSAWSPCSKSCGRGFKRRPLKCVGHGGRLLARdQCNLRRKpqELDFCVLRPC 950
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-PCTGEDV--ETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 218-424 4.03e-111

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: 340.76  E-value: 4.03e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 218 RYVETLVVADESMVKF-HGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLRDRDSGPKVTGNAALTLRNFCAWQ 296
Cdd:cd04273    1 RYVETLVVADSKMVEFhHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 297 KKLNKVSDKHPEYWDTAILFTRQDLCGA-TTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNV- 374
Cdd:cd04273   81 KKLNPPNDSDPEHHDHAILLTRQDICRSnGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDg 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109109297 375 KVCEEVFGKlraNHMMSPTLIQIDRANPWSACSAAIITDFLDSGHGDCLL 424
Cdd:cd04273  161 NSCGPEGKD---GHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 218-416 4.04e-39

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: 143.71  E-value: 4.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 218 RYVETLVVADESMVKFHGADLE---HYLLTLLATAARLYRHPSILNPINIVVVKVLLLRDRDSGPKVTGNAALTLRNFCA 294
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENilqAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 295 WQKKLNKvsdKHpeywDTAILFTRQDLCGattCDTLGMADVGTMCDPKRSCSVIEDDGLP--SAFTTAHELGHVFNMPHD 372
Cdd:cd04267   81 WRAEGPI---RH----DNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGFTllTALTMAHELGHNLGAEHD 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 109109297 373 NVKVCEEVFGKlRANHMMSPTLiqiDRANP--WSACSAAIITDFLD 416
Cdd:cd04267  151 GGDELAFECDG-GGNYIMAPVD---SGLNSyrFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 684-801 1.96e-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: 138.87  E-value: 1.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  684 KVTGLFTK-PMHGYNFVVAIPAGASSIDIRQRGYKGligddNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSLLRYSGT 762
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPSF-----THLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 109109297  763 GTAVESLQASRPILEPLTVEVLSV-GKMTPPRVRYSFYLP 801
Cdd:pfam05986  76 LPALEELHAPGPTQEDLEIQVLRQyGKGTNPGITYEYFIP 115
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 218-425 1.10e-29

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: 116.95  E-value: 1.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 218 RYVETLVVADESMVKFHGADLEHylltllaTAARLYRHPSILN----PINIVVVKVLLL----RDRDSgpkVTGNAALTL 289
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSK-------VRQRVIEIVNIVDsiyrPLNIRVVLVGLEiwtdKDKIS---VSGDAGETL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 290 RNFCAW-QKKLNKvSDKHpeywDTAILFTRQDLCGattcDTLGMADVGTMCDPKRSCSVIEDDG---LPSAFTTAHELGH 365
Cdd:cd04269   71 NRFLDWkRSNLLP-RKPH----DNAQLLTGRDFDG----NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGH 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109109297 366 VFNMPHDNVK-VCEevfgklRANHMMSPTLIQIDRAnpWSACSAAIITDFLDSGHGDCLLD 425
Cdd:cd04269  142 NLGMEHDDGGcTCG------RSTCIMAPSPSSLTDA--FSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 24-149 7.11e-26

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: 103.55  E-value: 7.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297   24 EVVVPIRLDPDINGRRyywRGPEDSGDQGLIFQITAFQEDFYLHLTPDAQFLAPAFATEHLGVPLQGFTGSSSDLRRCFY 103
Cdd:pfam01562   1 EVVIPVRLDPSRRRRS---LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 109109297  104 SGDVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNASAPAAQR 149
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 218-427 2.06e-24

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: 101.61  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  218 RYVETLVVADESMVKFHGADLEH---YLLTLLATAARLYRhpsilnPINIVVVKVLL--LRDRDSgPKVTGNAALTLRNF 292
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK------ELNIRVVLVGLeiWTDEDK-IDVSGDANDTLRNF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  293 CAWQKKLNKVSDKHpeywDTAILFTRQDLCGATTcdtlGMADVGTMCDPKRSCSVIEDdGLPS----AFTTAHELGHVFN 368
Cdd:pfam01421  74 LKWRQEYLKKRKPH----DVAQLLSGVEFGGTTV----GAAYVGGMCSLEYSGGVNED-HSKNlesfAVTMAHELGHNLG 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109109297  369 MPHDNVKV---CEEVFGKLranhmMSPTLIQIDrANPWSACSAAIITDFLDSGHGDCLLDQP 427
Cdd:pfam01421 145 MQHDDFNGgckCPPGGGCI-----MNPSAGSSF-PRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 438-505 2.92e-22

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: 90.87  E-value: 2.92e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  438 PGASYTLSQQCELAFGVGSKPCPYMQY--CTKLWCtgKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACV 505
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEdvCSKLWC--SNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 218-415 8.96e-16

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: 76.02  E-value: 8.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 218 RYVETLVVADESMvkFHGADLEHYLLTLLATAARLYRhpsilNPINIVVVKVLLLRDRDsgpkvtgnaaltlrnfcawqk 297
Cdd:cd00203    1 KVIPYVVVADDRD--VEEENLSAQIQSLILIAMQIWR-----DYLNIRFVLVGVEIDKA--------------------- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 298 klnkvsdkhpeywDTAILFTRQDLcgatTCDTLGMADVGTMCDPKRSCSVIEDDGLPS---AFTTAHELGHVFNMPHDNV 374
Cdd:cd00203   53 -------------DIAILVTRQDF----DGGTGGWAYLGRVCDSLRGVGVLQDNQSGTkegAQTIAHELGHALGFYHDHD 115

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109109297 375 KVCEEVFGKL---------RANHMMSPTLIQIDRAN--PWSACSAAIITDFL 415
Cdd:cd00203  116 RKDRDDYPTIddtlnaeddDYYSVMSYTKGSFSDGQrkDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 843-894 3.33e-15

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: 70.56  E-value: 3.33e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 109109297  843 WVAGSWGPCSVSCGSGLQKRAVDCRGSPGQRTVPA--CDAAHRPVETQACGE-PC 894
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDseCSAQKKPPETQSCNLkPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 519-571 1.24e-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: 1.24e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 109109297   519 WAKWEPYGPCSRTCGGGVQLARRQCTNPTPANGGKYCEGVRVKYRSCNLEPCP 571
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 219-423 1.90e-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: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 219 YVETLVVADESMVKfHGADLEHYLLTLLAT--AARLyRHPSILNP-INIVVVKVLLLRDRDSGPKVTGN------AALTL 289
Cdd:cd04272    2 YPELFVVVDYDHQS-EFFSNEQLIRYLAVMvnAANL-RYRDLKSPrIRLLLVGITISKDPDFEPYIHPInygyidAAETL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297 290 RNFcawqkKLNKVSDKHPEYWDTAILFTRQDLC----GATTCDTLGMADVGTMCDpKRSCSVIEDdgLPSAF----TTAH 361
Cdd:cd04272   80 ENF-----NEYVKKKRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGED--TPGSYygvyTMTH 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109109297 362 ELGHVFNMPHDNVKVCEEVFGKLRAN-------HMMSpTLIQIDRANPWSACSAAIITDFLDSGHGDCL 423
Cdd:cd04272  152 ELAHLLGAPHDGSPPPSWVKGHPGSLdcpwddgYIMS-YVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 897-950 2.26e-12

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 62.47  E-value: 2.26e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 109109297  897 WELSAWSPCSKSCGRGFKRRPLKCVG-HGGRLLARDQCNLRRKPQELDFCVLRPC 950
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 ...
 616-682 8.17e-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: 62.80  E-value: 8.17e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109109297  616 CKLICRANGTGYFYVLAPKVVDGTLCSPD------STSVCVQGKCIKAGCDGNLGSKKRFDKCGVCGGDNKSC 682
Cdd:pfam19236  43 CRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
217-372 4.99e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 59.74  E-value: 4.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  217 PRYVETLVVADESMVKFHGAD-LEHYLLTLLATAARLYRHPSilnPINIVVVKVLLLrDRD----SGPKVTGNAALTLRN 291
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGDaAQANIINMVNTASNVYERDF---NISLGLVNLTIS-DSTcpytPPACSTGDSSDRLSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  292 FCAwQKKLNkvsdkHPEYWDTAILFTrqdlcgATTCDTLGMADVGTMCDPKRSCSVIEDDGLPS--------AFTTAHEL 363
Cdd:pfam13688  78 FQD-FSAWR-----GTQNDDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNNvvvstateWQVFAHEI 145


                  ....*....
gi 109109297  364 GHVFNMPHD 372
Cdd:pfam13688 146 GHNFGAVHD 154
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 846-895 8.24e-07

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 46.81  E-value: 8.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 109109297   846 GSWGPCSVSCGSGLQKRAVDCRGSPGQRTVPACDAAHRpvETQAC-GEPCP 895
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDV--ETRACnEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
522-570 1.56e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.87  E-value: 1.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 109109297  522 WEPYGPCSRTCGGGVQLARRQCTNPTPanGGKYCEGVRVKYRSCNLEPC 570
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 522-570 3.08e-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: 44.96  E-value: 3.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 109109297  522 WEPYGPCSRTCGGGVQLARRQCTNPtPANGGKYCeGVRVKYRSCNLEPC 570
Cdd:pfam19028   6 WSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
ACR smart00608
ADAM Cysteine-Rich Domain;
437-506 2.25e-05

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 45.04  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297   437 LPGASYTLSQQCELAFGVGSKPCPYMQY-----------------------------CTKLWCTGKAK------------ 475
Cdd:smart00608  14 YNGRCPTRDNQCQALFGPGAKVAPDSCYeelntkgdrfgncgrengtyipcapedvkCGKLQCTNVSElpllgehatviy 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 109109297   476 ---GQMVCQTRHFP---------WADGTSCGEGKFCLKGACVE 506
Cdd:smart00608  94 sniGGLVCWSLDYHlgtdpdigmVKDGTKCGPGKVCINGQCVD 136
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 262-372 2.66e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 44.67  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109109297  262 INIVVVKVLLLRDRDSgPKVTGNAALTLRNFCAWqkklNKVSDKHPEYwDTAILFTRQDLCGattcdTLGMADVGTMCDP 341
Cdd:pfam13582  20 IRLQLAAIIITTSADT-PYTSSDALEILDELQEV----NDTRIGQYGY-DLGHLFTGRDGGG-----GGGIAYVGGVCNS 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 109109297  342 KRSCSVIEDD---GLPSAFTTAHELGHVFNMPHD 372
Cdd:pfam13582  89 GSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 894-950 5.12e-05

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 41.16  E-value: 5.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 109109297  894 CPTWElSAWSPCSKSCGRGFKRRplkcvghggRLLARDQCNLRrkpQELDFCVLRPC 950
Cdd:pfam19035   1 CEEQS-TEWSPCSKTCGMGVSTR---------VSNDNAECKLV---TETRLCQLRPC 44
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 524-570 6.36e-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: 41.28  E-value: 6.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109109297  524 PYGPCSRTCGGGVQLARRQCTNPTP--ANGGKYCEGVRvKY---RSCNLEPC 570
Cdd:pfam19030   5 PWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQK-KPpetQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 897-950 8.17e-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: 41.03  E-value: 8.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 109109297   897 WELSAWSPCSKSCGRGFKRRPLKCVGHGGRLLARdQCNLRRKpqELDFCVLRPC 950
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGG-PCTGEDV--ETRACNEQPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 900-937 2.30e-03

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 36.87  E-value: 2.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 109109297  900 SAWSPCSKSCGRGFKRR-------PLkcvgHGGR----LLARDQCNLRR 937
Cdd:pfam19028   7 SEWSECSVTCGGGVQTRtrtvivePQ----NGGRpcpeLLERRPCNLPP 51
TSP_1 pfam00090
Thrombospondin type 1 domain;
846-894 8.86e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 35.09  E-value: 8.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 109109297  846 GSWGPCSVSCGSGLQKRAVDCRGSPGQRtvPACDAAHrpVETQAC-GEPC 894
Cdd:pfam00090   4 SPWSPCSVTCGKGIQVRQRTCKSPFPGG--EPCTGDD--IETQACkMDKC 49
 
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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