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Conserved domains on  [gi|442616511|ref|NP_001259590|]
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mind-meld, isoform H [Drosophila melanogaster]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10480592)

disintegrin and metalloproteinase domain-containing protein also contains an ADAM domain and belongs to the ADAM family of membrane-anchored metalloproteases; ADAMs (A Disintegrin And Metalloprotease) are glycoproteins that play roles in cell signaling, cell fusion, and cell-cell interactions

Graphical summary

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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 ...
 270-471 7.84e-59

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: 200.92  E-value: 7.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  270 KYIETAIIVDKAMFDKRNGSTrAEVIHDAIQVANIADLYFRTLNTRVSVVYIETWG-KNQAVIdgSKDISKAISNFNDYT 348
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNL-SKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISV--SGDAGETLNRFLDWK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  349 SRNLFQ-IERDTTQLLTGETFAGGEAGMAVPETVCTP-RAVGISVDVNVyEPHLLAGTMAHMIGHNIGMGHDDGreECFC 426
Cdd:cd04269    78 RSNLLPrKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDG--GCTC 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 442616511  427 RDwHGCIMAQSIVGqenvQPYKFSECSKKDYIDALRTGHGLCLLN 471
Cdd:cd04269   155 GR-STCIMAPSPSS----LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
566-713 1.13e-43

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 155.21  E-value: 1.13e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511    566 NGSPCGlsktGISGYCFQGYCPTLSLQCEAIWGYGGSAADRQCYEQFNSKGSINGHCGRDaNEHYIKCEPENVQCGTLQC 645
Cdd:smart00608    2 DGTPCD----NGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQC 76

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616511    646 KDGERQPVNDGIDqlysrTIISIKGQEFECKATSGQVGSNsyPEHGLVKDGTPCGDNLICLNQTCVSL 713
Cdd:smart00608   77 TNVSELPLLGEHA-----TVIYSNIGGLVCWSLDYHLGTD--PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
488-561 1.66e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.36  E-value: 1.66e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616511   488 EEDEECDCGTFEECALDQCCDGITCKLKSEAQCASGACCDQCRLRPKDYICRDSNNECDLPEYCDGEIGQCPSD 561
Cdd:pfam00200    1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 104-214 1.16e-29

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: 114.72  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   104 NRGRTKKHFHRTSLLIKAFNHKFRLDLELNSQLLSPNIQQKHYHVGGYLVDGNRHDIEHCYYHGTVKDYPGASAAFHTCN 183
Cdd:pfam01562   16 SLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCS 95

                           90       100       110
                   ....*....|....*....|....*....|...
gi 442616511   184 GVSGVIHIGNETFVIHPFYGGDLS--KHPHVIF 214
Cdd:pfam01562   96 GLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 270-471 7.84e-59

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: 200.92  E-value: 7.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  270 KYIETAIIVDKAMFDKRNGSTrAEVIHDAIQVANIADLYFRTLNTRVSVVYIETWG-KNQAVIdgSKDISKAISNFNDYT 348
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNL-SKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISV--SGDAGETLNRFLDWK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  349 SRNLFQ-IERDTTQLLTGETFAGGEAGMAVPETVCTP-RAVGISVDVNVyEPHLLAGTMAHMIGHNIGMGHDDGreECFC 426
Cdd:cd04269    78 RSNLLPrKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDG--GCTC 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 442616511  427 RDwHGCIMAQSIVGqenvQPYKFSECSKKDYIDALRTGHGLCLLN 471
Cdd:cd04269   155 GR-STCIMAPSPSS----LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 270-473 3.50e-50

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: 176.34  E-value: 3.50e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   270 KYIETAIIVDKAMFdKRNGSTRAEVIHDAIQVANIADLYFRTLNTRVSVVYIETWG-KNQavIDGSKDISKAISNFNDYT 348
Cdd:pfam01421    1 KYIELFIVVDKQLF-QKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDK--IDVSGDANDTLRNFLKWR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   349 SRNLFQ-IERDTTQLLTGETFAGGEAGMAVPETVCTP-RAVGISVDVNVyEPHLLAGTMAHMIGHNIGMGHDDGREECFC 426
Cdd:pfam01421   78 QEYLKKrKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSK-NLESFAVTMAHELGHNLGMQHDDFNGGCKC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 442616511   427 RDWHGCIMAQSIVgqeNVQPYKFSECSKKDYIDALRTGHGLCLLNKP 473
Cdd:pfam01421  157 PPGGGCIMNPSAG---SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
566-713 1.13e-43

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 155.21  E-value: 1.13e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511    566 NGSPCGlsktGISGYCFQGYCPTLSLQCEAIWGYGGSAADRQCYEQFNSKGSINGHCGRDaNEHYIKCEPENVQCGTLQC 645
Cdd:smart00608    2 DGTPCD----NGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQC 76

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616511    646 KDGERQPVNDGIDqlysrTIISIKGQEFECKATSGQVGSNsyPEHGLVKDGTPCGDNLICLNQTCVSL 713
Cdd:smart00608   77 TNVSELPLLGEHA-----TVIYSNIGGLVCWSLDYHLGTD--PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
488-561 1.66e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.36  E-value: 1.66e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616511   488 EEDEECDCGTFEECALDQCCDGITCKLKSEAQCASGACCDQCRLRPKDYICRDSNNECDLPEYCDGEIGQCPSD 561
Cdd:pfam00200    1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 488-563 6.87e-34

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: 125.11  E-value: 6.87e-34
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442616511    488 EEDEECDCGTFEECAlDQCCDGITCKLKSEAQCASGACCDQCRLRPKDYICRDSNNECDLPEYCDGEIGQCPSDVF 563
Cdd:smart00050    1 EEGEECDCGSPKECT-DPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 104-214 1.16e-29

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: 114.72  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   104 NRGRTKKHFHRTSLLIKAFNHKFRLDLELNSQLLSPNIQQKHYHVGGYLVDGNRHDIEHCYYHGTVKDYPGASAAFHTCN 183
Cdd:pfam01562   16 SLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCS 95

                           90       100       110
                   ....*....|....*....|....*....|...
gi 442616511   184 GVSGVIHIGNETFVIHPFYGGDLS--KHPHVIF 214
Cdd:pfam01562   96 GLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 566-678 7.73e-29

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: 111.55  E-value: 7.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   566 NGSPCGLSKtgisGYCFQGYCPTLSLQCEAIWGYGGSAADRQCYEQFNSKGSINGHCGRDANEhYIKCEPENVQCGTLQC 645
Cdd:pfam08516    1 DGTPCNNGQ----AYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGG-YVKCEKRDVLCGKLQC 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 442616511   646 KDGERQPVNDGIdqlysRTIISIKGQEFECKAT 678
Cdd:pfam08516   76 TNVKELPLLGEH-----ATVIYTNINGVTCWGT 103
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 270-471 7.84e-59

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: 200.92  E-value: 7.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  270 KYIETAIIVDKAMFDKRNGSTrAEVIHDAIQVANIADLYFRTLNTRVSVVYIETWG-KNQAVIdgSKDISKAISNFNDYT 348
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNL-SKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISV--SGDAGETLNRFLDWK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  349 SRNLFQ-IERDTTQLLTGETFAGGEAGMAVPETVCTP-RAVGISVDVNVyEPHLLAGTMAHMIGHNIGMGHDDGreECFC 426
Cdd:cd04269    78 RSNLLPrKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDG--GCTC 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 442616511  427 RDwHGCIMAQSIVGqenvQPYKFSECSKKDYIDALRTGHGLCLLN 471
Cdd:cd04269   155 GR-STCIMAPSPSS----LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 270-473 3.50e-50

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: 176.34  E-value: 3.50e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   270 KYIETAIIVDKAMFdKRNGSTRAEVIHDAIQVANIADLYFRTLNTRVSVVYIETWG-KNQavIDGSKDISKAISNFNDYT 348
Cdd:pfam01421    1 KYIELFIVVDKQLF-QKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDK--IDVSGDANDTLRNFLKWR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   349 SRNLFQ-IERDTTQLLTGETFAGGEAGMAVPETVCTP-RAVGISVDVNVyEPHLLAGTMAHMIGHNIGMGHDDGREECFC 426
Cdd:pfam01421   78 QEYLKKrKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSK-NLESFAVTMAHELGHNLGMQHDDFNGGCKC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 442616511   427 RDWHGCIMAQSIVgqeNVQPYKFSECSKKDYIDALRTGHGLCLLNKP 473
Cdd:pfam01421  157 PPGGGCIMNPSAG---SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
566-713 1.13e-43

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 155.21  E-value: 1.13e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511    566 NGSPCGlsktGISGYCFQGYCPTLSLQCEAIWGYGGSAADRQCYEQFNSKGSINGHCGRDaNEHYIKCEPENVQCGTLQC 645
Cdd:smart00608    2 DGTPCD----NGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQC 76

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616511    646 KDGERQPVNDGIDqlysrTIISIKGQEFECKATSGQVGSNsyPEHGLVKDGTPCGDNLICLNQTCVSL 713
Cdd:smart00608   77 TNVSELPLLGEHA-----TVIYSNIGGLVCWSLDYHLGTD--PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
488-561 1.66e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.36  E-value: 1.66e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442616511   488 EEDEECDCGTFEECALDQCCDGITCKLKSEAQCASGACCDQCRLRPKDYICRDSNNECDLPEYCDGEIGQCPSD 561
Cdd:pfam00200    1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 488-563 6.87e-34

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: 125.11  E-value: 6.87e-34
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442616511    488 EEDEECDCGTFEECAlDQCCDGITCKLKSEAQCASGACCDQCRLRPKDYICRDSNNECDLPEYCDGEIGQCPSDVF 563
Cdd:smart00050    1 EEGEECDCGSPKECT-DPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 104-214 1.16e-29

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: 114.72  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   104 NRGRTKKHFHRTSLLIKAFNHKFRLDLELNSQLLSPNIQQKHYHVGGYLVDGNRHDIEHCYYHGTVKDYPGASAAFHTCN 183
Cdd:pfam01562   16 SLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCS 95

                           90       100       110
                   ....*....|....*....|....*....|...
gi 442616511   184 GVSGVIHIGNETFVIHPFYGGDLS--KHPHVIF 214
Cdd:pfam01562   96 GLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 566-678 7.73e-29

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: 111.55  E-value: 7.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   566 NGSPCGLSKtgisGYCFQGYCPTLSLQCEAIWGYGGSAADRQCYEQFNSKGSINGHCGRDANEhYIKCEPENVQCGTLQC 645
Cdd:pfam08516    1 DGTPCNNGQ----AYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGG-YVKCEKRDVLCGKLQC 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 442616511   646 KDGERQPVNDGIdqlysRTIISIKGQEFECKAT 678
Cdd:pfam08516   76 TNVKELPLLGEH-----ATVIYTNINGVTCWGT 103
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 270-470 1.69e-20

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: 91.15  E-value: 1.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  270 KYIETAIIVDKAMFDKRNGStraEVIHDAIQVANIADLYFR--TL--NTRVSVVYIETWGKNQAVIDGSKDISKAISNFN 345
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGE---DLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEESGLLISGNAQKSLKSFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  346 DYTSR----NLFQIER-DTTQLLTGETFAGGE-----AGMAVPETVCTP-RAVGISVDVnvyepHL-LAGTMAHMIGHNI 413
Cdd:cd04273    78 RWQKKlnppNDSDPEHhDHAILLTRQDICRSNgncdtLGLAPVGGMCSPsRSCSINEDT-----GLsSAFTIAHELGHVL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442616511  414 GMGHDDGREECFCRDWHGCIMAQSIVGqeNVQPYKFSECSKKDYIDALRTGHGLCLL 470
Cdd:cd04273   153 GMPHDGDGNSCGPEGKDGHIMSPTLGA--NTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 270-462 2.10e-20

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: 90.56  E-value: 2.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  270 KYIETAIIVDKAMFDKRNGSTRAeVIHDAIQVANIADLYFR----TLNTRVSVVYIETWGKNQAVIDGSKDISKAISNFN 345
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDENI-LQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  346 DYTSRNLfqIERDTTQLLTGETFA-GGEAGMAVPETVCTP-RAVGISVDVNvyEPHLLAGTMAHMIGHNIGMGHDDGREE 423
Cdd:cd04267    80 FWRAEGP--IRHDNAVLLTAQDFIeGDILGLAYVGSMCNPySSVGVVEDTG--FTLLTALTMAHELGHNLGAEHDGGDEL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 442616511  424 CFCRDWHG-CIMAQSIVGqENvqPYKFSECSKKDYIDALR 462
Cdd:cd04267   156 AFECDGGGnYIMAPVDSG-LN--SYRFSQCSIGSIREFLD 192
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 337-455 5.59e-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: 5.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  337 ISKAISNFNDYTS-----RNLFQIERDTTQLLTGETFAGGEAGMAVPETVCTPRAVGISVDVNVYEPHLLAGTMAHMIGH 411
Cdd:cd00203    27 ILIAMQIWRDYLNirfvlVGVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGH 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442616511  412 NIGMGHDDGREECF-----------CRDWHGCIMAQSIVGQENVQPYKFSECSKK 455
Cdd:cd00203   107 ALGFYHDHDRKDRDdyptiddtlnaEDDDYYSVMSYTKGSFSDGQRKDFSQCDID 161
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 271-469 3.46e-10

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 61.60  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  271 YIETAIIVDKAmFDKRNGSTRAEVIHDAIQVaNIADLYFRTLNT---RVSVVYIETwGKNQAV-------IDGSKDISKA 340
Cdd:cd04272     2 YPELFVVVDYD-HQSEFFSNEQLIRYLAVMV-NAANLRYRDLKSpriRLLLVGITI-SKDPDFepyihpiNYGYIDAAET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  341 ISNFNDYTSRNLFQIERDTTQLLTGE---TFAGGEA-----GMAVPETVCTPRAVGISVDvnvyEPHLLAG--TMAHMIG 410
Cdd:cd04272    79 LENFNEYVKKKRDYFNPDVVFLVTGLdmsTYSGGSLqtgtgGYAYVGGACTENRVAMGED----TPGSYYGvyTMTHELA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442616511  411 HNIGMGHD---------DGREECFCRDWHGCIMAQsivGQENVQPYKFSECSKKDYIDALRTGHGLCL 469
Cdd:cd04272   155 HLLGAPHDgspppswvkGHPGSLDCPWDDGYIMSY---VVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 298-418 2.42e-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: 45.05  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   298 AIQVANIAdlYFRTLNTRVSVVYIETWgKNQAVIDGSKDISKAISNFNDYTSRNLFQIERDTTQLLTGETFAGGeAGMAV 377
Cdd:pfam13582    6 LVNRANTI--YERDLGIRLQLAAIIIT-TSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGG-GGIAY 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 442616511   378 PETVCTPR-AVGISVDVNVYePHLLAGTMAHMIGHNIGMGHD 418
Cdd:pfam13582   82 VGGVCNSGsKFGVNSGSGPV-GDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
275-418 7.94e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 45.10  E-value: 7.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511   275 AIIVDKAMFDKRNGSTRAEVIHDAIQVANiaDLYFRTLNTRVSVVYIETWGK---NQAVIDGSKDISKAISNFNDYTSRN 351
Cdd:pfam13688    8 LVAADCSYVAAFGGDAAQANIINMVNTAS--NVYERDFNISLGLVNLTISDStcpYTPPACSTGDSSDRLSEFQDFSAWR 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442616511   352 lFQIERDTTQLLTGETFAGGeaGMAVPETVCTPRAVGiSVDVNVYEPHLLAGT------MAHMIGHNIGMGHD 418
Cdd:pfam13688   86 -GTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAG-SVSTRVSGNNVVVSTatewqvFAHEIGHNFGAVHD 154
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 387-468 5.93e-04

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: 43.13  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616511  387 VGISVDVNvYEPHLLAG----TMAHMIGHNIGMGHDDGREECFCRDWHG--CIMAQSIVGQENVQPYKFSECSKKDYIDA 460
Cdd:cd04270   150 TGLTTTVN-YGKRVPTKesdlVTAHELGHNFGSPHDPDIAECAPGESQGgnYIMYARATSGDKENNKKFSPCSKKSISKV 228


                  ....*...
gi 442616511  461 LRTGHGLC 468
Cdd:cd04270   229 LEVKSNSC 236
 
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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