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Conserved domains on  [gi|74184783|dbj|BAE27990|]
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unnamed protein product [Mus musculus]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 12023311)

disintegrin and metalloproteinase domain-containing protein, also called metalloproteinase-disintegrin (ADAM), is a membrane-spanning multi-domain protein which may serve as an integrin ligand

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 191-389 1.18e-85

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: 272.25  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   191 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 269
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   270 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD--SAHCCSASAa 347
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 74184783   348 dGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMP 389
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
482-630 4.01e-50

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 172.93  E-value: 4.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    482 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGlNGQYRKCSPRDAKCGKIQCQST 561
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    562 QARP-LESNAVSIDTTItlngRRIHCRGTHVYRGPEEeegegdmlDPGLVMTGTKCGHNHICFEGQCRNT 630
Cdd:smart00608  80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP--------DIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 25-143 2.23e-27

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: 107.79  E-value: 2.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    25 ELIIPQW-------RTSESPGRGKHPLraELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYH 97
Cdd:pfam01562   1 EVVIPVRldpsrrrRSLASESTYLDTL--SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 74184783    98 GTVRDVDESSVTLSTCRGIRGLIIVrSNLSYIIEPVPNSDS-----QHRIY 143
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSReegghPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 420-480 3.50e-27

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: 105.08  E-value: 3.50e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74184783    420 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYY 480
Cdd:smart00050  15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 191-389 1.18e-85

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: 272.25  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   191 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 269
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   270 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD--SAHCCSASAa 347
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 74184783   348 dGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMP 389
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 191-387 3.78e-83

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: 265.25  E-value: 3.78e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 191 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 269
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 270 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHC-CSASaad 348
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 74184783 349 gGCIMAAATGHPfPKVFSWCNRKELDRYLQTGGGMCLSN 387
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
482-630 4.01e-50

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 172.93  E-value: 4.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    482 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGlNGQYRKCSPRDAKCGKIQCQST 561
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    562 QARP-LESNAVSIDTTItlngRRIHCRGTHVYRGPEEeegegdmlDPGLVMTGTKCGHNHICFEGQCRNT 630
Cdd:smart00608  80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP--------DIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 483-591 4.43e-39

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: 140.44  E-value: 4.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   483 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKgLNGQYRKCSPRDAKCGKIQCQSTQ 562
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 74184783   563 ARP-LESNAVSIDTTItlngRRIHCRGTHV 591
Cdd:pfam08516  80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 25-143 2.23e-27

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: 107.79  E-value: 2.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    25 ELIIPQW-------RTSESPGRGKHPLraELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYH 97
Cdd:pfam01562   1 EVVIPVRldpsrrrRSLASESTYLDTL--SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 74184783    98 GTVRDVDESSVTLSTCRGIRGLIIVrSNLSYIIEPVPNSDS-----QHRIY 143
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSReegghPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 420-480 3.50e-27

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: 105.08  E-value: 3.50e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74184783    420 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYY 480
Cdd:smart00050  15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
420-478 2.24e-25

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 100.01  E-value: 2.24e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 74184783   420 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTN 478
Cdd:pfam00200  16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 191-389 1.18e-85

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: 272.25  E-value: 1.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   191 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 269
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   270 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD--SAHCCSASAa 347
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 74184783   348 dGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMP 389
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 191-387 3.78e-83

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: 265.25  E-value: 3.78e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 191 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 269
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 270 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHC-CSASaad 348
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 74184783 349 gGCIMAAATGHPfPKVFSWCNRKELDRYLQTGGGMCLSN 387
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
482-630 4.01e-50

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 172.93  E-value: 4.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    482 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGlNGQYRKCSPRDAKCGKIQCQST 561
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    562 QARP-LESNAVSIDTTItlngRRIHCRGTHVYRGPEEeegegdmlDPGLVMTGTKCGHNHICFEGQCRNT 630
Cdd:smart00608  80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP--------DIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 483-591 4.43e-39

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: 140.44  E-value: 4.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   483 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKgLNGQYRKCSPRDAKCGKIQCQSTQ 562
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 74184783   563 ARP-LESNAVSIDTTItlngRRIHCRGTHV 591
Cdd:pfam08516  80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 191-377 5.25e-33

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: 126.00  E-value: 5.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 191 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRS----LNIRIALVGLEVWtHGdKCEVSENPYS---TLWSF 263
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQIL-KG-EQFAPPIDSDasnTLNSF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 264 LSWRRKLLAqkSHDNAQLITGRSF-QGTTIGLAPLMAMCSVYQSGGVSMDHSENAIgVASTVAHEIGHNFGMSHDSAHCC 342
Cdd:cd04267  79 SFWRAEGPI--RHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGGDEL 155

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74184783 343 SASA-ADGGCIMAAATGHPFPKVFSWCNRKELDRYL 377
Cdd:cd04267 156 AFECdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 191-385 5.39e-33

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: 126.58  E-value: 5.39e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 191 KYVELYLVADyAEFQKNRHDQDaTKRKLMEIANYVDKFYR--SL--NIRIALVGLEVWTHGDK-CEVSENPYSTLWSFLS 265
Cdd:cd04273   1 RYVETLVVAD-SKMVEFHHGED-LEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 266 WRRKLLAQ-----KSHDNAQLITGRSFQG-----TTIGLAPLMAMCSVYQSGGVSMDhseNAIGVASTVAHEIGHNFGMS 335
Cdd:cd04273  79 WQKKLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSINED---TGLSSAFTIAHELGHVLGMP 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 74184783 336 HD-SAHCCSASAADgGCIMAAATGHPFPKvFSW--CNRKELDRYLQTGGGMCL 385
Cdd:cd04273 156 HDgDGNSCGPEGKD-GHIMSPTLGANTGP-FTWskCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 25-143 2.23e-27

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: 107.79  E-value: 2.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783    25 ELIIPQW-------RTSESPGRGKHPLraELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYH 97
Cdd:pfam01562   1 EVVIPVRldpsrrrRSLASESTYLDTL--SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 74184783    98 GTVRDVDESSVTLSTCRGIRGLIIVrSNLSYIIEPVPNSDS-----QHRIY 143
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSReegghPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 420-480 3.50e-27

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: 105.08  E-value: 3.50e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74184783    420 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYY 480
Cdd:smart00050  15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
420-478 2.24e-25

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 100.01  E-value: 2.24e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 74184783   420 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTN 478
Cdd:pfam00200  16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
193-359 2.58e-20

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 89.79  E-value: 2.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   193 VELYLVADYaEFQKNrHDQDATKRKLMEIANYVD-KFYRSLNIRIALVGLEVWTHGD----KCEVSENPYSTLWSFLSwR 267
Cdd:pfam13688   5 VALLVAADC-SYVAA-FGGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQD-F 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   268 RKLLAQKSHDNAQLITGRSFQGTtiGLAPLMAMCSVYQSGGVSMDHSENAIGVAS-----TVAHEIGHNFGMSHDSA--- 339
Cdd:pfam13688  82 SAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCDsst 159

                         170       180
                  ....*....|....*....|....*.
gi 74184783   340 --HCCSASA----ADGGCIMAAATGH 359
Cdd:pfam13688 160 ssQCCPPSNstcpAGGRYIMNPSSSP 185
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 191-376 4.64e-18

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: 82.57  E-value: 4.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 191 KYVELYLVADyaefqKNRHDQDATKRKLMEIANYVDKFYRS-LNIRIALVGLEVwthgdkcevsenpystlwsflswrrk 269
Cdd:cd00203   1 KVIPYVVVAD-----DRDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 270 llaqKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCC------- 342
Cdd:cd00203  50 ----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddypti 125

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 74184783 343 ----SASAADGGCIMaaatgHPFPKVFSWCNRKELDRY 376
Cdd:cd00203 126 ddtlNAEDDDYYSVM-----SYTKGSFSDGQRKDFSQC 158
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 223-337 2.23e-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: 73.17  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   223 NYVDKFYRS-LNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRKLLAQKSHDNAQLITGRSFQGTTiGLAPLMAMC 301
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGG-GIAYVGGVC 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 74184783   302 SVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD 337
Cdd:pfam13582  87 NSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 213-357 4.98e-12

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 65.73  E-value: 4.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   213 ATKRKLMEIANYVDKFYR--SLNIRIALVGLevwthgDKCEV------SENPYSTLWSFLSWRRKLLAQ----KSHDNAQ 280
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEpdDININGGLVNP------GEIPAttsasdSGNNYCNSPTTIVRRLNFLSQwrgeQDYCLAH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   281 LITGRSFQGTTIGLAPLMAMC-----SVYQSGGVSMDHSENAIGVAST----VAHEIGHNFGMSHDsahCCSASAADGGC 351
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICqkgasSPKTNTGLSTTTNYGSFNYPTQewdvVAHEVGHNFGATHD---CDGSQYASSGC 152


                  ....*.
gi 74184783   352 IMAAAT 357
Cdd:pfam13574 153 ERNAAT 158
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 195-384 1.61e-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: 62.39  E-value: 1.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 195 LYLVADYAEFQK-NRHDQDATKRKLMEIANYVDKFYRSL--------NIRIALVGLEVWTHGDKCEVSENPY---STLWS 262
Cdd:cd04270   5 LLLVADHRFYKYmGRGEEETTINYLISHIDRVDDIYRNTdwdgggfkGIGFQIKRIRIHTTPDEVDPGNKFYnksFPNWG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 263 FLSWRRKLLAQKSHDN---AQLITGRSFQGTTIGLAPLMA--------MCSVYQSGGVSMDHSENAiGVASTV------- 324
Cdd:cd04270  85 VEKFLVKLLLEQFSDDvclAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAYYYSNGKKKYLNT-GLTTTVnygkrvp 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74184783 325 --------AHEIGHNFGMSHDS--AHCCSASAADGGCIM--AAATG-HPFPKVFSWCNRKELDRYLQTGGGMC 384
Cdd:cd04270 164 tkesdlvtAHELGHNFGSPHDPdiAECAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSC 236
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 211-358 7.94e-10

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: 60.13  E-value: 7.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 211 QDATKRKLMEIANYVDKFYR-SLNIRIALVGLEVwthGDKCEVSENPYSTLWS---------------FLSWRrkllAQK 274
Cdd:cd04271  20 VEEARRNILNNVNSASQLYEsSFNISLGLRNLTI---SDASCPSTAVDSAPWNlpcnsrididdrlsiFSQWR----GQQ 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 275 SHDNAQLITGRSF--QGTTIGLAPLMAMC-SVYQSGGVSMDHSENAIGVAST----VAHEIGHNFGMSHD---------- 337
Cdd:cd04271  93 PDDGNAFWTLMTAcpSGSEVGVAWLGQLCrTGASDQGNETVAGTNVVVRTSNewqvFAHEIGHTFGAVHDctsgtcsdgs 172

                       170       180
                ....*....|....*....|....*..
gi 74184783 338 --SAHCCSASA----ADGGCIMAAATG 358
Cdd:cd04271 173 vgSQQCCPLSTstcdANGQYIMNPSSS 199
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 191-356 4.63e-08

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 54.16  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   191 KYVELYLVADYaEFQKNRHDQDATKRKLMEIANYVDKFY-RSLNIRIALvglevwtHGDKCEVSENPYSTLW-------- 261
Cdd:pfam13583   3 RVYRVAVATDC-TYSASFGSVDELRANINATVTTANEVYgRDFNVSLAL-------ISDRDVIYTDSSTDSFnadcsggd 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783   262 -------SFLSWRrkllAQKSHDNAQLITGRSFQGTTIGLAPLMAMC-SVYQS---GGVSMDHSEnaigvASTVAHEIGH 330
Cdd:pfam13583  75 lgnwrlaTLTSWR----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNakaSGVARSRDE-----WDIFAHEIGH 145

                         170       180       190
                  ....*....|....*....|....*....|.
gi 74184783   331 NFGMSHD-SAHCCSASAA----DGGCIMAAA 356
Cdd:pfam13583 146 TFGAVHDcSSQGEGLSSStedgSGQTIMSYA 176
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 192-385 6.27e-08

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 54.28  E-value: 6.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 192 YVELYLVADYaEFQKNRHDQDATKRKLMEIANYVDKFYRSLN---IRIALVGLEVWTHGDKCEVSENP-------YSTLW 261
Cdd:cd04272   2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPInygyidaAETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74184783 262 SFLSWRRKLLAQKSHDNAQLITGR--------SFQGTTIGLAPLMAMCSVYqsgGVSMdhSENAIGV---ASTVAHEIGH 330
Cdd:cd04272  81 NFNEYVKKKRDYFNPDVVFLVTGLdmstysggSLQTGTGGYAYVGGACTEN---RVAM--GEDTPGSyygVYTMTHELAH 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74184783 331 NFGMSHDSAHCCS---------ASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCL 385
Cdd:cd04272 156 LLGAPHDGSPPPSwvkghpgslDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
 
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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