NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|755498527|ref|XP_011237550|]
View 

disintegrin and metalloproteinase domain-containing protein 33 isoform X2 [Mus musculus]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 10136411)

protein containing domains ZnMc_adamalysin_II_like, DISIN, and ACR

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 75-272 3.39e-81

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: 255.23  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  75 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 154
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 155 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGC-CvqadaE 232
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755498527 233 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 272
Cdd:cd04269  156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
367-509 5.93e-44

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 154.06  E-value: 5.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527   367 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 446
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498527   447 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 509
Cdd:smart00608  80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 291-365 2.04e-33

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


:

Pssm-ID: 214490  Cd Length: 75  Bit Score: 122.41  E-value: 2.04e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498527   291 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 365
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 75-272 3.39e-81

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: 255.23  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  75 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 154
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 155 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGC-CvqadaE 232
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755498527 233 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 272
Cdd:cd04269  156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 75-272 3.81e-79

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: 249.91  E-value: 3.81e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527   75 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 153
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  154 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPE--GCCVQada 231
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 755498527  232 EQGGCVMEAATGHPFPRVFSACSRRQLRTFFRKGGGPCLSN 272
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ACR smart00608
ADAM Cysteine-Rich Domain;
367-509 5.93e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 154.06  E-value: 5.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527   367 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 446
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498527   447 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 509
Cdd:smart00608  80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 368-476 8.52e-36

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 130.04  E-value: 8.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  368 DGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQdHKGSFLPCAQRDALCGKLLCQGGE 447
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*....
gi 755498527  448 PNPLVPHIVTMDSTILlegREVVCRGAFV 476
Cdd:pfam08516  80 ELPLLGEHATVIYTNI---NGVTCWGTDY 105
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 291-365 2.04e-33

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 122.41  E-value: 2.04e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498527   291 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 365
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
291-363 3.45e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 116.19  E-value: 3.45e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498527  291 EAGEECDCGSGQKC-PDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPAD 363
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 75-272 3.39e-81

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: 255.23  E-value: 3.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  75 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 154
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 155 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGC-CvqadaE 232
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755498527 233 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 272
Cdd:cd04269  156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 75-272 3.81e-79

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: 249.91  E-value: 3.81e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527   75 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 153
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  154 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPE--GCCVQada 231
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 755498527  232 EQGGCVMEAATGHPFPRVFSACSRRQLRTFFRKGGGPCLSN 272
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ACR smart00608
ADAM Cysteine-Rich Domain;
367-509 5.93e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 154.06  E-value: 5.93e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527   367 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 446
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498527   447 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 509
Cdd:smart00608  80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 368-476 8.52e-36

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 130.04  E-value: 8.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  368 DGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQdHKGSFLPCAQRDALCGKLLCQGGE 447
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*....
gi 755498527  448 PNPLVPHIVTMDSTILlegREVVCRGAFV 476
Cdd:pfam08516  80 ELPLLGEHATVIYTNI---NGVTCWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 75-263 3.51e-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: 131.77  E-value: 3.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  75 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLD----IQLVLTGLEVW-TEQDLSRITQDANETLWAFLQ 149
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 150 WRRGVWARrpHDSTQLLTGRTF-QGTTVGLAPVEGICRAESSGGVSTDHSELPIgTAATMAHEIGHSLGLHHDPEGCCVQ 228
Cdd:cd04267   81 WRAEGPIR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGGDELAF 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755498527 229 ADAEQGGCVMEAATGHPFPRVFSACSRRQLRTFFR 263
Cdd:cd04267  158 ECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 291-365 2.04e-33

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 122.41  E-value: 2.04e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498527   291 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 365
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
291-363 3.45e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 116.19  E-value: 3.45e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498527  291 EAGEECDCGSGQKC-PDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPAD 363
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 75-270 1.32e-29

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: 116.18  E-value: 1.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  75 RYLELYIVADHTLFLLQHQNlnHTRQRLLEVANCVDQILR--TL--DIQLVLTGLEVWT-EQDLSRITQDANETLWAFLQ 149
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEdEESGLLISGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 150 WRRGVWARRP-----HDSTQLLTGRTFQG-----TTVGLAPVEGICRAESSGGVSTDHselPIGTAATMAHEIGHSLGLH 219
Cdd:cd04273   79 WQKKLNPPNDsdpehHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSINEDT---GLSSAFTIAHELGHVLGMP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755498527 220 HDPEG--CcvqADAEQGGCVMEAATGHPFPRVF-SACSRRQLRTFFRKGGGPCL 270
Cdd:cd04273  156 HDGDGnsC---GPEGKDGHIMSPTLGANTGPFTwSKCSRRYLTSFLDTGDGNCL 206
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 107-221 5.58e-15

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: 71.63  E-value: 5.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  107 NCVDQILRT-LDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGVWARRPHDSTQLLTGRTFQGTTvGLAPVEGIC 185
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGG-GIAYVGGVC 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755498527  186 RAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHD 221
Cdd:pfam13582  87 NSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
79-243 9.76e-15

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 73.22  E-value: 9.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527   79 LYIVADHTlFLLQHQNlNHTRQRLLEVANCVDQIL-RTLDIQLVLTGLEVWTEQDLS----RITQDANETLWAFlQWRRG 153
Cdd:pfam13688   7 LLVAADCS-YVAAFGG-DAAQANIINMVNTASNVYeRDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEF-QDFSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  154 VWARRPHDSTQLLTGRTFQGTtvGLAPVEGICRAESSGGVSTDHSE--LPIGTAA---TMAHEIGHSLGLHHDPegccvQ 228
Cdd:pfam13688  84 WRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGnnVVVSTATewqVFAHEIGHNFGAVHDC-----D 156

                         170
                  ....*....|....*
gi 755498527  229 ADAEQGGCVMEAATG 243
Cdd:pfam13688 157 SSTSSQCCPPSNSTC 171
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 75-261 3.66e-14

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: 70.63  E-value: 3.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  75 RYLELYIVADHtlfllQHQNLNHTRQRLLEVANCVDQILRT-LDIQLVLTGLEVwteqdlsritqdanetlwaflqwrrg 153
Cdd:cd00203    1 KVIPYVVVADD-----RDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 154 vwarRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGCCVQADAE- 232
Cdd:cd00203   50 ----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTi 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755498527 233 ---------QGGCVMEAATG---HPFPRVFSACSRRQLRTF 261
Cdd:cd00203  126 ddtlnaeddDYYSVMSYTKGsfsDGQRKDFSQCDIDQINKL 166
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 76-270 2.22e-11

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 63.91  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  76 YLELYIVADHtlfllQHQNLNHTRQRLLE----VANCVDQILRTL---DIQLVLTGLEVWTEQD-------LSRITQDAN 141
Cdd:cd04272    2 YPELFVVVDY-----DHQSEFFSNEQLIRylavMVNAANLRYRDLkspRIRLLLVGITISKDPDfepyihpINYGYIDAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 142 ETLWAFLQWRRGVWARRPHDSTQLLTGR---TFQG-----TTVGLAPVEGICrAESSGGVSTDHSELPIGtAATMAHEIG 213
Cdd:cd04272   77 ETLENFNEYVKKKRDYFNPDVVFLVTGLdmsTYSGgslqtGTGGYAYVGGAC-TENRVAMGEDTPGSYYG-VYTMTHELA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755498527 214 HSLGLHHDPEGCC--VQADAEQGGC----------VMEAATGHPfprvFSACSRRQLRTFFRKGGGPCL 270
Cdd:cd04272  155 HLLGAPHDGSPPPswVKGHPGSLDCpwddgyimsyVVNGERQYR----FSQCSQRQIRNVFRRLGASCL 219
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 79-276 3.76e-10

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 60.85  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  79 LYIVADHTLFllQH---QNLNHTRQRLLEVANCVDQILRTLD--------IQLVLTGLEVWTEQDlsRITQDANETLWAF 147
Cdd:cd04270    5 LLLVADHRFY--KYmgrGEEETTINYLISHIDRVDDIYRNTDwdgggfkgIGFQIKRIRIHTTPD--EVDPGNKFYNKSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 148 LQWRRGVWARRpHDSTQ---------LLTGRTFQGTTVGLAPVeGICRAESSGGVSTDHSELPIGTAA------------ 206
Cdd:cd04270   81 PNWGVEKFLVK-LLLEQfsddvclahLFTYRDFDMGTLGLAYV-GSPRDNSAGGICEKAYYYSNGKKKylntgltttvny 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 207 -----------TMAHEIGHSLGLHHDPEGC-CVQADAEQGGCVM--EAATG-HPFPRVFSACSRRQLRTFFRKGGGPCLS 271
Cdd:cd04270  159 gkrvptkesdlVTAHELGHNFGSPHDPDIAeCAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSCFV 238


                 ....*
gi 755498527 272 NTSAP 276
Cdd:cd04270  239 ERSQS 243
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 98-260 8.27e-07

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: 49.93  E-value: 8.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527   98 TRQRLLEVANCVDQI--LRTLDIQLVLTGL----------EVWTEQDLSRITQDANETLwaFLQWRrgvwARRPHDSTQL 165
Cdd:pfam13574   3 VTENLVNVVNRVNQIyePDDININGGLVNPgeipattsasDSGNNYCNSPTTIVRRLNF--LSQWR----GEQDYCLAHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527  166 LTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATM---------AHEIGHSLGLHHDPEG-----CCVQADA 231
Cdd:pfam13574  77 VTMGTFSGGELGLAYVGQICQKGASSPKTNTGLSTTTNYGSFNyptqewdvvAHEVGHNFGATHDCDGsqyasSGCERNA 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 755498527  232 EQGGC------VMeAATGHPFPRVFSACSRRQLRT 260
Cdd:pfam13574 157 ATSVCsangsfIM-NPASKSNNDLFSPCSISLICD 190
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 139-271 7.88e-05

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 44.72  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498527 139 DANETLWAFLQWRrgvwARRPHDSTQLLTGRTF--QGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAAT-----MAHE 211
Cdd:cd04271   77 DIDDRLSIFSQWR----GQQPDDGNAFWTLMTAcpSGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHE 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498527 212 IGHSLGLHHD-PEGCCVQADAEQGGC--------------VMEAATGHPFPRvFSACSRRQLRTFFRKGG--GPCLS 271
Cdd:cd04271  153 IGHTFGAVHDcTSGTCSDGSVGSQQCcplststcdangqyIMNPSSSSGITE-FSPCTIGNICSLLGRNPvrTSCLS 228
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 170-230 8.05e-05

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 44.64  E-value: 8.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755498527 170 TFQGTTVGLAPVEGIC--RAESSGGVSTDhselPIGTAATMAHEIGHSLGLHH---DPEGCCVQAD 230
Cdd:cd04275  105 TFPDSLVSLAFITDGVviNPSSLPGGSAA----PYNLGDTATHEVGHWLGLYHtfqGGSPCCTTGD 166
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH