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Conserved domains on  [gi|57222280|ref|NP_001009547|]
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a disintegrin and metalloprotease domain 26b precursor [Mus musculus]

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 ...
 195-383 4.83e-70

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: 226.73  E-value: 4.83e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 195 RFIEYFVVIDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTALEIWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 275 FGNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTP-YNCGVSSFLSDVMSDMAHIVAHEMGHNLGMKHDGIGCTCGLKDCL 352
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 57222280 353 MAPYKTNSPK-FSNCSYEEMYSVVTKR--SCLYD 383
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
477-613 1.78e-52

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 177.55  E-value: 1.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280    477 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELADVLCGRIQCENVI 555
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 57222280    556 QLPQRRNHETVHYTHFSNVTCWTMDYHFGITiDDIGAVSDGTACAPYHICVDRKCVSK 613
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
401-473 2.20e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 130.82  E-value: 2.20e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57222280   401 EEGEECDCGSTESCLQDPCC-SSDCVLKPGAQCAFGLCCQDCQFLKTGTVCREEKNECDLPEWCNGTSAECPGD 473
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 29-147 6.63e-22

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: 91.61  E-value: 6.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280    29 EVVTPLRVTVTR------GNNTSPGWLSYSLNIGGQRHIITMKPKKNLMSRNLILLTYTQQGDLLEQRPFVPNDCYYHGY 102
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 57222280   103 VDEDPESLVILNTCFGsLQGTLEINGTTYEIMP----KSSTSTFEHLAY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 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 ...
 195-383 4.83e-70

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: 226.73  E-value: 4.83e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 195 RFIEYFVVIDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTALEIWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 275 FGNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTP-YNCGVSSFLSDVMSDMAHIVAHEMGHNLGMKHDGIGCTCGLKDCL 352
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 57222280 353 MAPYKTNSPK-FSNCSYEEMYSVVTKR--SCLYD 383
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
477-613 1.78e-52

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 177.55  E-value: 1.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280    477 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELADVLCGRIQCENVI 555
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 57222280    556 QLPQRRNHETVHYTHFSNVTCWTMDYHFGITiDDIGAVSDGTACAPYHICVDRKCVSK 613
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 195-385 5.46e-48

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: 167.86  E-value: 5.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   195 RFIEYFVVIDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTALEIWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   275 FGNRIRHDIIHLLV-RQGYGLYLGLAYLADVCTP-YNCGVSSFLSDVMSDMAHIVAHEMGHNLGMKHDGI--GCTCGLKD 350
Cdd:pfam01421  81 LKKRKPHDVAQLLSgVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 57222280   351 -CLMAPYKTNSP--KFSNCSYEEMYSVVTKR--SCLYDIP 385
Cdd:pfam01421 161 gCIMNPSAGSSFprKFSNCSQEDFEQFLTKQkgACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 478-581 9.77e-45

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: 155.08  E-value: 9.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   478 DGIPCS-GEGYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELADVLCGRIQCENVIQ 556
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 57222280   557 LPQRRNHETVHYTHFSNVTCWTMDY 581
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
401-473 2.20e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 130.82  E-value: 2.20e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57222280   401 EEGEECDCGSTESCLQDPCC-SSDCVLKPGAQCAFGLCCQDCQFLKTGTVCREEKNECDLPEWCNGTSAECPGD 473
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 401-475 3.22e-33

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 122.03  E-value: 3.22e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57222280    401 EEGEECDCGSTESClQDPCC-SSDCVLKPGAQCAFGLCCQDCQFLKTGTVCREEKNECDLPEWCNGTSAECPGDVY 475
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 29-147 6.63e-22

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: 91.61  E-value: 6.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280    29 EVVTPLRVTVTR------GNNTSPGWLSYSLNIGGQRHIITMKPKKNLMSRNLILLTYTQQGDLLEQRPFVPNDCYYHGY 102
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 57222280   103 VDEDPESLVILNTCFGsLQGTLEINGTTYEIMP----KSSTSTFEHLAY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 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 ...
 195-383 4.83e-70

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: 226.73  E-value: 4.83e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 195 RFIEYFVVIDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTALEIWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 275 FGNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTP-YNCGVSSFLSDVMSDMAHIVAHEMGHNLGMKHDGIGCTCGLKDCL 352
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 57222280 353 MAPYKTNSPK-FSNCSYEEMYSVVTKR--SCLYD 383
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
477-613 1.78e-52

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 177.55  E-value: 1.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280    477 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELADVLCGRIQCENVI 555
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 57222280    556 QLPQRRNHETVHYTHFSNVTCWTMDYHFGITiDDIGAVSDGTACAPYHICVDRKCVSK 613
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 195-385 5.46e-48

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: 167.86  E-value: 5.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   195 RFIEYFVVIDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTALEIWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   275 FGNRIRHDIIHLLV-RQGYGLYLGLAYLADVCTP-YNCGVSSFLSDVMSDMAHIVAHEMGHNLGMKHDGI--GCTCGLKD 350
Cdd:pfam01421  81 LKKRKPHDVAQLLSgVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 57222280   351 -CLMAPYKTNSP--KFSNCSYEEMYSVVTKR--SCLYDIP 385
Cdd:pfam01421 161 gCIMNPSAGSSFprKFSNCSQEDFEQFLTKQkgACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 478-581 9.77e-45

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: 155.08  E-value: 9.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   478 DGIPCS-GEGYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELADVLCGRIQCENVIQ 556
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 57222280   557 LPQRRNHETVHYTHFSNVTCWTMDY 581
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
401-473 2.20e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 130.82  E-value: 2.20e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57222280   401 EEGEECDCGSTESCLQDPCC-SSDCVLKPGAQCAFGLCCQDCQFLKTGTVCREEKNECDLPEWCNGTSAECPGD 473
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 401-475 3.22e-33

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 122.03  E-value: 3.22e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57222280    401 EEGEECDCGSTESClQDPCC-SSDCVLKPGAQCAFGLCCQDCQFLKTGTVCREEKNECDLPEWCNGTSAECPGDVY 475
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 195-368 3.51e-22

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: 94.79  E-value: 3.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 195 RFIEYFVVIDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDT----DVVLTALEIWNEKNYINV-ELSIFKVLGDFCT 269
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 270 WKQnmfGNRIRHDIIHLLVRQGYGL--YLGLAYLADVCTPY-NCGVSSFLSDVMsDMAHIVAHEMGHNLGMKHDGIGCTC 346
Cdd:cd04267  81 WRA---EGPIRHDNAVLLTAQDFIEgdILGLAYVGSMCNPYsSVGVVEDTGFTL-LTALTMAHELGHNLGAEHDGGDELA 156

                       170       180
                ....*....|....*....|....*...
gi 57222280 347 GLKD----CLMAPY--KTNSPKFSNCSY 368
Cdd:cd04267 157 FECDgggnYIMAPVdsGLNSYRFSQCSI 184
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 29-147 6.63e-22

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: 91.61  E-value: 6.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280    29 EVVTPLRVTVTR------GNNTSPGWLSYSLNIGGQRHIITMKPKKNLMSRNLILLTYTQQGDLLEQRPFVPNDCYYHGY 102
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 57222280   103 VDEDPESLVILNTCFGsLQGTLEINGTTYEIMP----KSSTSTFEHLAY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 195-373 2.64e-19

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: 86.91  E-value: 2.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 195 RFIEYFVVIDHK--QYVHRNNnittcIQDM-LQIVNGVNGYY----LQIDTDVVLTALEIW-NEKNYINVELSIFKVLGD 266
Cdd:cd04273   1 RYVETLVVADSKmvEFHHGED-----LEHYiLTLMNIVASLYkdpsLGNSINIVVVRLIVLeDEESGLLISGNAQKSLKS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 267 FCTW--KQNMFG--NRIRHDIIHLLVRQGYGLY------LGLAYLADVCTPYN-CGVSSflsDVMSDMAHIVAHEMGHNL 335
Cdd:cd04273  76 FCRWqkKLNPPNdsDPEHHDHAILLTRQDICRSngncdtLGLAPVGGMCSPSRsCSINE---DTGLSSAFTIAHELGHVL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 57222280 336 GMKHDGIGCTCGLKD---CLMAPYKT-NSPKF--SNCSYEEMYS 373
Cdd:cd04273 153 GMPHDGDGNSCGPEGkdgHIMSPTLGaNTGPFtwSKCSRRYLTS 196
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 225-340 1.36e-11

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: 62.00  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   225 IVNGVNGYY-LQIDTDVVLTALEIWNEKNYINVELSIFKVLGDFCTWKQNmfgnRIRH---DIIHLLVRQGYGLYLGLAY 300
Cdd:pfam13582   6 LVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQygyDLGHLFTGRDGGGGGGIAY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 57222280   301 LADVCTPYN-CGVSSFLSDVMSDMAHIVAHEMGHNLGMKHD 340
Cdd:pfam13582  82 VGGVCNSGSkFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 195-368 2.85e-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: 59.46  E-value: 2.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 195 RFIEYFVVIDHKQYvhRNNNITTCIQDMlqivngvngyylqidtdvVLTALEIWNEKNYINVELSIfkvlgdfctwkqnm 274
Cdd:cd00203   1 KVIPYVVVADDRDV--EEENLSAQIQSL------------------ILIAMQIWRDYLNIRFVLVG-------------- 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 275 fGNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTPYN-CGVSSFLSDVMSDMAHIVAHEMGHNLGMKHDG----------I 342
Cdd:cd00203  47 -VEIDKADIAILVTRQDFdGGTGGWAYLGRVCDSLRgVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHdrkdrddyptI 125

                       170       180       190
                ....*....|....*....|....*....|....*
gi 57222280 343 GCTCGLKD----CLMAPYKT-----NSPKFSNCSY 368
Cdd:cd00203 126 DDTLNAEDddyySVMSYTKGsfsdgQRKDFSQCDI 160
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
194-364 5.60e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 56.27  E-value: 5.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   194 HRFIEYFVVIDHKqYV--HRNNNITTCIQDMLQIVNGVngYYLQIDTDVVLTALEIWNEKN----YINVELSIFKVLGDF 267
Cdd:pfam13688   2 TRTVALLVAADCS-YVaaFGGDAAQANIINMVNTASNV--YERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   268 CTwkQNMFGNRIRHDIIHLLVRQ--GYGlylGLAYLADVCTP---YNCGVSSFLSDVMSDMA---HIVAHEMGHNLGMKH 339
Cdd:pfam13688  79 QD--FSAWRGTQNDDLAYLFLMTncSGG---GLAWLGQLCNSgsaGSVSTRVSGNNVVVSTAtewQVFAHEIGHNFGAVH 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 57222280   340 DgigCTCGLKD---------------CLMAPY-KTNSPKFS 364
Cdd:pfam13688 154 D---CDSSTSSqccppsnstcpaggrYIMNPSsSPNSTDFS 191
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 196-381 7.04e-08

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 53.51  E-value: 7.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 196 FIEYFVVIDHKQYVHRNNNITTcIQDMLQIVNGVNGYYLQIDT---DVVLTALEI----WNEKN-------YINVELSIf 261
Cdd:cd04272   2 YPELFVVVDYDHQSEFFSNEQL-IRYLAVMVNAANLRYRDLKSpriRLLLVGITIskdpDFEPYihpinygYIDAAETL- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 262 KVLGDFCTWKQNMFgnriRHDIIHLLVRQGYGLY---------LGLAYLADVCTPYNCGV-----SSFlsdvmsDMAHIV 327
Cdd:cd04272  80 ENFNEYVKKKRDYF----NPDVVFLVTGLDMSTYsggslqtgtGGYAYVGGACTENRVAMgedtpGSY------YGVYTM 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57222280 328 AHEMGHNLGMKHDG------IGCTCGLKDC------LMApYKTNSP---KFSNCSYEEMYSVV--TKRSCL 381
Cdd:cd04272 150 THELAHLLGAPHDGspppswVKGHPGSLDCpwddgyIMS-YVVNGErqyRFSQCSQRQIRNVFrrLGASCL 219
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 271-375 1.43e-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: 49.16  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280   271 KQNMFGNRI---RHDIIHLLVRQGY-GLYLGLAYLADVC-TPYNC-----GVSSFLS--DVMSDMAHI--VAHEMGHNLG 336
Cdd:pfam13574  58 RLNFLSQWRgeqDYCLAHLVTMGTFsGGELGLAYVGQICqKGASSpktntGLSTTTNygSFNYPTQEWdvVAHEVGHNFG 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 57222280   337 MKHDgigCTCGLKDC------------------LMAPY-KTNSPKFSNCSYEEMYSVV 375
Cdd:pfam13574 138 ATHD---CDGSQYASsgcernaatsvcsangsfIMNPAsKSNNDLFSPCSISLICDVL 192
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 296-380 2.81e-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: 49.29  E-value: 2.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222280 296 LGLAYLAD--------VCTPY-----------NCGVSSFL---SDVMSDMAHIV-AHEMGHNLGMKHD--GIGCTCGLKD 350
Cdd:cd04270 117 LGLAYVGSprdnsaggICEKAyyysngkkkylNTGLTTTVnygKRVPTKESDLVtAHELGHNFGSPHDpdIAECAPGESQ 196

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 57222280 351 ---CLMAPYKT-----NSPKFSNCSYEEMYSV--VTKRSC 380
Cdd:cd04270 197 ggnYIMYARATsgdkeNNKKFSPCSKKSISKVleVKSNSC 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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