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Conserved domains on  [gi|755498523|ref|XP_006498639|]
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disintegrin and metalloproteinase domain-containing protein 33 isoform X1 [Mus musculus]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10480700)

disintegrin and metalloproteinase domain-containing protein such as snake venom metalloproteinases that impairs hemostasis in envenomed animals

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 ...
 211-395 8.60e-73

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: 235.59  E-value: 8.60e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSG-------------AATMAHEIGHSLGLHHDPEGC-CvqadaE 355
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGgvvqdhsrnlllfAVTMAHELGHNLGMEHDDGGCtC-----G 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755498523 356 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 395
Cdd:cd04269  156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
490-632 1.46e-44

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 156.75  E-value: 1.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523   490 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 569
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498523   570 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 632
Cdd:smart00608  80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 414-488 2.59e-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: 125.50  E-value: 2.59e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498523   414 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 488
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-153 5.22e-28

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: 109.33  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523   39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562   1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498523  119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 211-395 8.60e-73

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: 235.59  E-value: 8.60e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSG-------------AATMAHEIGHSLGLHHDPEGC-CvqadaE 355
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGgvvqdhsrnlllfAVTMAHELGHNLGMEHDDGGCtC-----G 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755498523 356 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 395
Cdd:cd04269  156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 211-395 2.42e-70

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: 229.49  E-value: 2.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 289
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  290 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSG-------------AATMAHEIGHSLGLHHDPE--GCCVQada 354
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGgvnedhsknlesfAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 755498523  355 EQGGCVMEAATGHPFPRVFSACSRRQLRTFFRKGGGPCLSN 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ACR smart00608
ADAM Cysteine-Rich Domain;
490-632 1.46e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 156.75  E-value: 1.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523   490 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 569
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498523   570 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 632
Cdd:smart00608  80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 491-599 2.54e-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: 132.35  E-value: 2.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  491 DGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQdHKGSFLPCAQRDALCGKLLCQGGE 570
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*....
gi 755498523  571 PNPLVPHIVTMDSTILlegREVVCRGAFV 599
Cdd:pfam08516  80 ELPLLGEHATVIYTNI---NGVTCWGTDY 105
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 414-488 2.59e-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: 125.50  E-value: 2.59e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498523   414 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 488
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
414-486 4.25e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.88  E-value: 4.25e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498523  414 EAGEECDCGSGQKC-PDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPAD 486
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-153 5.22e-28

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: 109.33  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523   39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562   1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498523  119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 327-343 7.72e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 37.33  E-value: 7.72e-03
                           10
                   ....*....|....*..
gi 755498523   327 GAATMAHEIGHSLGLHH 343
Cdd:smart00235  84 NTGVAAHELGHALGLYH 100
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 211-395 8.60e-73

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: 235.59  E-value: 8.60e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSG-------------AATMAHEIGHSLGLHHDPEGC-CvqadaE 355
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGgvvqdhsrnlllfAVTMAHELGHNLGMEHDDGGCtC-----G 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755498523 356 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 395
Cdd:cd04269  156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 211-395 2.42e-70

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: 229.49  E-value: 2.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 289
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  290 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSG-------------AATMAHEIGHSLGLHHDPE--GCCVQada 354
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGgvnedhsknlesfAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 755498523  355 EQGGCVMEAATGHPFPRVFSACSRRQLRTFFRKGGGPCLSN 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ACR smart00608
ADAM Cysteine-Rich Domain;
490-632 1.46e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 156.75  E-value: 1.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523   490 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 569
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498523   570 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 632
Cdd:smart00608  80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 491-599 2.54e-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: 132.35  E-value: 2.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  491 DGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQdHKGSFLPCAQRDALCGKLLCQGGE 570
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*....
gi 755498523  571 PNPLVPHIVTMDSTILlegREVVCRGAFV 599
Cdd:pfam08516  80 ELPLLGEHATVIYTNI---NGVTCWGTDY 105
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 414-488 2.59e-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: 125.50  E-value: 2.59e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498523   414 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 488
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
414-486 4.25e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.88  E-value: 4.25e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755498523  414 EAGEECDCGSGQKC-PDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPAD 486
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 211-386 3.99e-30

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: 117.52  E-value: 3.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLD----IQLVLTGLEVW-TEQDLSRITQDANETLWAFLQ 285
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 286 WRRGVWARrpHDSTQLLTGRTF-QGTTVGLAPVEGICRAESSG------------AATMAHEIGHSLGLHHDPEGCCVQA 352
Cdd:cd04267   81 WRAEGPIR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVgvvedtgftlltALTMAHELGHNLGAEHDGGDELAFE 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 755498523 353 DAEQGGCVMEAATGHPFPRVFSACSRRQLRTFFR 386
Cdd:cd04267  159 CDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 211-393 2.64e-28

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: 113.10  E-value: 2.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 211 RYLELYIVADHTLFLLQHQNlnHTRQRLLEVANCVDQILR--TL--DIQLVLTGLEVWT-EQDLSRITQDANETLWAFLQ 285
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEdEESGLLISGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 286 WRRGVWARRP-----HDSTQLLTGRTFQG-----TTVGLAPVEGICRAESS---------GAA-TMAHEIGHSLGLHHDP 345
Cdd:cd04273   79 WQKKLNPPNDsdpehHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRScsinedtglSSAfTIAHELGHVLGMPHDG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755498523 346 EG--CcvqADAEQGGCVMEAATGHPFPRVF-SACSRRQLRTFFRKGGGPCL 393
Cdd:cd04273  159 DGnsC---GPEGKDGHIMSPTLGANTGPFTwSKCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-153 5.22e-28

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: 109.33  E-value: 5.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523   39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562   1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498523  119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
215-366 2.93e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 66.29  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  215 LYIVADHTlFLLQHQNlNHTRQRLLEVANCVDQIL-RTLDIQLVLTGLEVWTEQDLS----RITQDANETLWAFlQWRRG 289
Cdd:pfam13688   7 LLVAADCS-YVAAFGG-DAAQANIINMVNTASNVYeRDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEF-QDFSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  290 VWARRPHDSTQLLTGRTFQGTtvGLAPVEGICRAESSGAATM------------------AHEIGHSLGLHHDPegccvQ 351
Cdd:pfam13688  84 WRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTrvsgnnvvvstatewqvfAHEIGHNFGAVHDC-----D 156

                         170
                  ....*....|....*
gi 755498523  352 ADAEQGGCVMEAATG 366
Cdd:pfam13688 157 SSTSSQCCPPSNSTC 171
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 212-393 3.35e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 66.61  E-value: 3.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 212 YLELYIVADHtlfllQHQNLNHTRQRLLE----VANCVDQILRTL---DIQLVLTGLEVWTEQD-------LSRITQDAN 277
Cdd:cd04272    2 YPELFVVVDY-----DHQSEFFSNEQLIRylavMVNAANLRYRDLkspRIRLLLVGITISKDPDfepyihpINYGYIDAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 278 ETLWAFLQWRRGVWARRPHDSTQLLTGR---TFQG-----TTVGLAPVEGICRAES-----------SGAATMAHEIGHS 338
Cdd:cd04272   77 ETLENFNEYVKKKRDYFNPDVVFLVTGLdmsTYSGgslqtGTGGYAYVGGACTENRvamgedtpgsyYGVYTMTHELAHL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498523 339 LGLHHDPEGCC--VQADAEQGGC----------VMEAATGHPfprvFSACSRRQLRTFFRKGGGPCL 393
Cdd:cd04272  157 LGAPHDGSPPPswVKGHPGSLDCpwddgyimsyVVNGERQYR----FSQCSQRQIRNVFRRLGASCL 219
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 243-344 1.80e-10

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: 58.92  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  243 NCVDQILRT-LDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGVWARRPHDSTQLLTGRTFQGTTvGLAPVEGIC 321
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGG-GIAYVGGVC 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 755498523  322 RAESS-------------GAATMAHEIGHSLGLHHD 344
Cdd:pfam13582  87 NSGSKfgvnsgsgpvgdtGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 211-384 2.90e-10

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: 59.84  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 211 RYLELYIVADHtlfllQHQNLNHTRQRLLEVANCVDQILRT-LDIQLVLTGLEVwteqdlsritqdanetlwaflqwrrg 289
Cdd:cd00203    1 KVIPYVVVADD-----RDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 290 vwarRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESS-------------GAATMAHEIGHSLGLHHDPEGCCVQADAE- 355
Cdd:cd00203   50 ----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGvgvlqdnqsgtkeGAQTIAHELGHALGFYHDHDRKDRDDYPTi 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755498523 356 ---------QGGCVMEAATG---HPFPRVFSACSRRQLRTF 384
Cdd:cd00203  126 ddtlnaeddDYYSVMSYTKGsfsDGQRKDFSQCDIDQINKL 166
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 215-399 1.87e-06

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: 50.06  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 215 LYIVADHTLFllQH---QNLNHTRQRLLEVANCVDQILRTLD--------IQLVLTGLEVWTEQDlsRITQDANETLWAF 283
Cdd:cd04270    5 LLLVADHRFY--KYmgrGEEETTINYLISHIDRVDDIYRNTDwdgggfkgIGFQIKRIRIHTTPD--EVDPGNKFYNKSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 284 LQWRRGVWARRpHDSTQ---------LLTGRTFQGTTVGLAPVE--------GICRAE---SSGAA-------------- 329
Cdd:cd04270   81 PNWGVEKFLVK-LLLEQfsddvclahLFTYRDFDMGTLGLAYVGsprdnsagGICEKAyyySNGKKkylntgltttvnyg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 330 ----------TMAHEIGHSLGLHHDPEGC-CVQADAEQGGCVM--EAATG-HPFPRVFSACSRRQLRTFFRKGGGPCLSN 395
Cdd:cd04270  160 krvptkesdlVTAHELGHNFGSPHDPDIAeCAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSCFVE 239


                 ....
gi 755498523 396 TSAP 399
Cdd:cd04270  240 RSQS 243
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 234-383 4.53e-06

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: 48.01  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  234 TRQRLLEVANCVDQILRTLDI----QLVLTG-LEVWTE-------QDLSRITQDANETLwaFLQWRrgvwARRPHDSTQL 301
Cdd:pfam13574   3 VTENLVNVVNRVNQIYEPDDIningGLVNPGeIPATTSasdsgnnYCNSPTTIVRRLNF--LSQWR----GEQDYCLAHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523  302 LTGRTFQGTTVGLAPVEGICRAESS------GAAT----------------MAHEIGHSLGLHHDPEG-----CCVQADA 354
Cdd:pfam13574  77 VTMGTFSGGELGLAYVGQICQKGASspktntGLSTttnygsfnyptqewdvVAHEVGHNFGATHDCDGsqyasSGCERNA 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 755498523  355 EQGGC------VMeAATGHPFPRVFSACSRRQLRT 383
Cdd:pfam13574 157 ATSVCsangsfIM-NPASKSNNDLFSPCSISLICD 190
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 275-394 2.34e-03

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: 40.48  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498523 275 DANETLWAFLQWRrgvwARRPHDSTQLLTGRTF--QGTTVGLAPVEGICRAESSG------------AAT------MAHE 334
Cdd:cd04271   77 DIDDRLSIFSQWR----GQQPDDGNAFWTLMTAcpSGSEVGVAWLGQLCRTGASDqgnetvagtnvvVRTsnewqvFAHE 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755498523 335 IGHSLGLHHD-PEGCCVQADAEQGGC--------------VMEAATGHPFPRvFSACSRRQLRTFFRKGG--GPCLS 394
Cdd:cd04271  153 IGHTFGAVHDcTSGTCSDGSVGSQQCcplststcdangqyIMNPSSSSGITE-FSPCTIGNICSLLGRNPvrTSCLS 228
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 330-353 2.96e-03

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: 40.02  E-value: 2.96e-03
                         10        20
                 ....*....|....*....|....*..
gi 755498523 330 TMAHEIGHSLGLHH---DPEGCCVQAD 353
Cdd:cd04275  140 TATHEVGHWLGLYHtfqGGSPCCTTGD 166
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 327-343 7.72e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 37.33  E-value: 7.72e-03
                           10
                   ....*....|....*..
gi 755498523   327 GAATMAHEIGHSLGLHH 343
Cdd:smart00235  84 NTGVAAHELGHALGLYH 100
 
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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