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Conserved domains on  [gi|148539874|ref|NP_034215|]
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disintegrin and metalloproteinase domain-containing protein 26A preproprotein [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 3.61e-67

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: 219.02  E-value: 3.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 195 RFIEYFVVLDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTTLEVWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 275 FGNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTP-YNCGVSSVLSDVMSDMAHIVAHEMGHNFGMKHDGIGCTCGLKDCL 352
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148539874 353 MAPYKTNSPK-FSNCSYEEMYSVVTKR--SCLYD 383
Cdd:cd04269  161 MAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
477-613 1.62e-52

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 177.55  E-value: 1.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874   477 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRQGDRFGNCGNDSSTYRTCQIADVLCGQIQCENVI 555
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539874   556 QLPQRRNHETVHYTHFSNITCWTMDYHFGITiDDIGAVSDGTAYAPDHICVDRKCVSK 613
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
401-473 4.67e-37

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.75  E-value: 4.67e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539874  401 EEGEQCDCGNSESCLQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKAGTVCRKEKNECDLPEWCNGTSAECPGD 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 1.27e-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: 93.92  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874   29 EVVTPLRVTVTR------GNNISPGWLSYSLNIGGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEQHHFVQNDCYYHGY 102
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 148539874  103 VDEDLESPVIVNTCFGsLQGTLEINGTSYEIMP----KSSTSTFEHLVY 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 3.61e-67

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: 219.02  E-value: 3.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 195 RFIEYFVVLDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTTLEVWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 275 FGNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTP-YNCGVSSVLSDVMSDMAHIVAHEMGHNFGMKHDGIGCTCGLKDCL 352
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148539874 353 MAPYKTNSPK-FSNCSYEEMYSVVTKR--SCLYD 383
Cdd:cd04269  161 MAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
477-613 1.62e-52

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 177.55  E-value: 1.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874   477 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRQGDRFGNCGNDSSTYRTCQIADVLCGQIQCENVI 555
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539874   556 QLPQRRNHETVHYTHFSNITCWTMDYHFGITiDDIGAVSDGTAYAPDHICVDRKCVSK 613
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 195-385 3.36e-45

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: 160.16  E-value: 3.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  195 RFIEYFVVLDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTTLEVWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  275 FGNRIRHDIIHLLV-RQGYGLYLGLAYLADVCTP-YNCGVSSVLSDVMSDMAHIVAHEMGHNFGMKHDGI--GCTCGLKD 350
Cdd:pfam01421  81 LKKRKPHDVAQLLSgVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 148539874  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 5.32e-44

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: 153.15  E-value: 5.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  478 DGIPCS-GEGYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRQGDRFGNCGNDSSTYRTCQIADVLCGQIQCENVIQ 556
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 148539874  557 LPQRRNHETVHYTHFSNITCWTMDY 581
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
401-473 4.67e-37

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.75  E-value: 4.67e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539874  401 EEGEQCDCGNSESCLQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKAGTVCRKEKNECDLPEWCNGTSAECPGD 473
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 401-475 3.88e-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: 124.73  E-value: 3.88e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539874   401 EEGEQCDCGNSESClQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKAGTVCRKEKNECDLPEWCNGTSAECPGDVY 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 1.27e-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: 93.92  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874   29 EVVTPLRVTVTR------GNNISPGWLSYSLNIGGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEQHHFVQNDCYYHGY 102
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 148539874  103 VDEDLESPVIVNTCFGsLQGTLEINGTSYEIMP----KSSTSTFEHLVY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 395-432 8.98e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 34.66  E-value: 8.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148539874  395 CGNKVVEEGEQCDCGNSESclqDPCCSSDCVLKPGAQC 432
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTTS---GDGCSATCRLEEGFAC 38
 
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 3.61e-67

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: 219.02  E-value: 3.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 195 RFIEYFVVLDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTTLEVWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 275 FGNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTP-YNCGVSSVLSDVMSDMAHIVAHEMGHNFGMKHDGIGCTCGLKDCL 352
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148539874 353 MAPYKTNSPK-FSNCSYEEMYSVVTKR--SCLYD 383
Cdd:cd04269  161 MAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
477-613 1.62e-52

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 177.55  E-value: 1.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874   477 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRQGDRFGNCGNDSSTYRTCQIADVLCGQIQCENVI 555
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539874   556 QLPQRRNHETVHYTHFSNITCWTMDYHFGITiDDIGAVSDGTAYAPDHICVDRKCVSK 613
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 195-385 3.36e-45

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: 160.16  E-value: 3.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  195 RFIEYFVVLDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDTDVVLTTLEVWNEKNYINVELSIFKVLGDFCTWKQNM 274
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  275 FGNRIRHDIIHLLV-RQGYGLYLGLAYLADVCTP-YNCGVSSVLSDVMSDMAHIVAHEMGHNFGMKHDGI--GCTCGLKD 350
Cdd:pfam01421  81 LKKRKPHDVAQLLSgVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 148539874  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 5.32e-44

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: 153.15  E-value: 5.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  478 DGIPCS-GEGYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRQGDRFGNCGNDSSTYRTCQIADVLCGQIQCENVIQ 556
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 148539874  557 LPQRRNHETVHYTHFSNITCWTMDY 581
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
401-473 4.67e-37

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.75  E-value: 4.67e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148539874  401 EEGEQCDCGNSESCLQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKAGTVCRKEKNECDLPEWCNGTSAECPGD 473
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 401-475 3.88e-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: 124.73  E-value: 3.88e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539874   401 EEGEQCDCGNSESClQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKAGTVCRKEKNECDLPEWCNGTSAECPGDVY 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 1.27e-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: 93.92  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874   29 EVVTPLRVTVTR------GNNISPGWLSYSLNIGGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEQHHFVQNDCYYHGY 102
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 148539874  103 VDEDLESPVIVNTCFGsLQGTLEINGTSYEIMP----KSSTSTFEHLVY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 195-368 4.12e-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: 94.41  E-value: 4.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 195 RFIEYFVVLDHKQYVHRNNNITTCIQDMLQIVNGVNGYYLQIDT----DVVLTTLEVWNEKNYINV-ELSIFKVLGDFCT 269
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 270 WKQnmfGNRIRHDIIHLLVRQGYGL--YLGLAYLADVCTPYNCGVSSVLSDVMSDMAHIVAHEMGHNFGMKHDGIGCTCG 347
Cdd:cd04267   81 WRA---EGPIRHDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVVEDTGFTLLTALTMAHELGHNLGAEHDGGDELAF 157

                        170       180
                 ....*....|....*....|....*..
gi 148539874 348 LKD----CLMAPY--KTNSPKFSNCSY 368
Cdd:cd04267  158 ECDgggnYIMAPVdsGLNSYRFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 195-373 3.43e-20

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 89.22  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 195 RFIEYFVVLDHK--QYVHRNNnittcIQDM-LQIVNGVNGYY----LQIDTDVVLTTLEVW-NEKNYINVELSIFKVLGD 266
Cdd:cd04273    1 RYVETLVVADSKmvEFHHGED-----LEHYiLTLMNIVASLYkdpsLGNSINIVVVRLIVLeDEESGLLISGNAQKSLKS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 267 FCTW--KQNMFG--NRIRHDIIHLLVRQGYGLY------LGLAYLADVCTPYN-CgvsSVLSDVMSDMAHIVAHEMGHNF 335
Cdd:cd04273   76 FCRWqkKLNPPNdsDPEHHDHAILLTRQDICRSngncdtLGLAPVGGMCSPSRsC---SINEDTGLSSAFTIAHELGHVL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148539874 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 1.56e-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: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  225 IVNGVNGYY-LQIDTDVVLTTLEVWNEKNYINVELSIFKVLGDFCTWKQNmfgnRIRH---DIIHLLVRQGYGLYLGLAY 300
Cdd:pfam13582   6 LVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQygyDLGHLFTGRDGGGGGGIAY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 148539874  301 LADVCTPYN-CGVSSVLSDVMSDMAHIVAHEMGHNFGMKHD 340
Cdd:pfam13582  82 VGGVCNSGSkFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 276-368 2.87e-09

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: 56.76  E-value: 2.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 276 GNRIRHDIIHLLVRQGY-GLYLGLAYLADVCTPYN-CGVSSVLSDVMSDMAHIVAHEMGHNFGMKHDG----------IG 343
Cdd:cd00203   47 VEIDKADIAILVTRQDFdGGTGGWAYLGRVCDSLRgVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHdrkdrddyptID 126

                         90       100       110
                 ....*....|....*....|....*....|....
gi 148539874 344 CTCGLKD----CLMAPYKT-----NSPKFSNCSY 368
Cdd:cd00203  127 DTLNAEDddyySVMSYTKGsfsdgQRKDFSQCDI 160
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
194-364 2.89e-08

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 54.35  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  194 HRFIEYFVVLDHKqYV--HRNNNITTCIQDMLQIVNGVngYYLQIDTDVVLTTLEVWNEKN----YINVELSIFKVLGDF 267
Cdd:pfam13688   2 TRTVALLVAADCS-YVaaFGGDAAQANIINMVNTASNV--YERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  268 CTwkQNMFGNRIRHDIIHLLVRQ--GYGlylGLAYLADVCTP---YNCGVSSVLSDVMSDMA---HIVAHEMGHNFGMKH 339
Cdd:pfam13688  79 QD--FSAWRGTQNDDLAYLFLMTncSGG---GLAWLGQLCNSgsaGSVSTRVSGNNVVVSTAtewQVFAHEIGHNFGAVH 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 148539874  340 DgigCTCGLKD---------------CLMAPY-KTNSPKFS 364
Cdd:pfam13688 154 D---CDSSTSSqccppsnstcpaggrYIMNPSsSPNSTDFS 191
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 271-375 8.96e-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: 372637  Cd Length: 193  Bit Score: 53.02  E-value: 8.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  271 KQNMFGNRI---RHDIIHLLVRQGY-GLYLGLAYLADVC-TPYNC-----GVSSVLS--DVMSDMAHI--VAHEMGHNFG 336
Cdd:pfam13574  58 RLNFLSQWRgeqDYCLAHLVTMGTFsGGELGLAYVGQICqKGASSpktntGLSTTTNygSFNYPTQEWdvVAHEVGHNFG 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148539874  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 2.27e-07

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: 52.38  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 296 LGLAYLAD--------VCTPY-----------NCGVSSVL---SDVMSDMAHIV-AHEMGHNFGMKHD--GIGCTCGLKD 350
Cdd:cd04270  117 LGLAYVGSprdnsaggICEKAyyysngkkkylNTGLTTTVnygKRVPTKESDLVtAHELGHNFGSPHDpdIAECAPGESQ 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148539874 351 ---CLMAPYKT-----NSPKFSNCSYEEMYSV--VTKRSC 380
Cdd:cd04270  197 ggnYIMYARATsgdkeNNKKFSPCSKKSISKVleVKSNSC 236
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 196-381 2.55e-06

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 48.89  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 196 FIEYFVVLDHKQYVHRNNNITTcIQDMLQIVNGVNGYYLQIDT---DVVLTTLEV----WNEKN-------YINVELSIf 261
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNEQL-IRYLAVMVNAANLRYRDLKSpriRLLLVGITIskdpDFEPYihpinygYIDAAETL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 262 KVLGDFCTWKQNMFgnriRHDIIHLLVRQGYGLY---------LGLAYLADVCTPYNCGVSSVLSDVMSDMaHIVAHEMG 332
Cdd:cd04272   80 ENFNEYVKKKRDYF----NPDVVFLVTGLDMSTYsggslqtgtGGYAYVGGACTENRVAMGEDTPGSYYGV-YTMTHELA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539874 333 HNFGMKHDG------IGCTCGLKDC------LMApYKTNSP---KFSNCSYEEMYSVV--TKRSCL 381
Cdd:cd04272  155 HLLGAPHDGspppswVKGHPGSLDCpwddgyIMS-YVVNGErqyRFSQCSQRQIRNVFrrLGASCL 219
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 265-367 2.01e-03

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: 39.91  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874  265 GDFCTWKQNMFGNRI---RHDIIHLLVRQG-YGLYLGLAYLADVC-TPYNCGVSSVLSDVmSDMAHIVAHEMGHNFGMKH 339
Cdd:pfam13583  73 GDLGNWRLATLTSWRdslNYDLAYLTLMTGpSGQNVGVAWVGALCsSARQNAKASGVARS-RDEWDIFAHEIGHTFGAVH 151

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 148539874  340 DGIGCTCGLK--------DCLMAPYKTNS-PKFSNCS 367
Cdd:pfam13583 152 DCSSQGEGLSsstedgsgQTIMSYASTASqTAFSPCT 188
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 255-347 4.64e-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: 39.33  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539874 255 NVELSIFKVLGDFCTWKqnmfGNRIRHDII--HLLVRQGYGLYLGLAYLADVCTP-----YNCGVSSVLSDVM-SDMAHI 326
Cdd:cd04271   73 NSRIDIDDRLSIFSQWR----GQQPDDGNAfwTLMTACPSGSEVGVAWLGQLCRTgasdqGNETVAGTNVVVRtSNEWQV 148

                         90       100
                 ....*....|....*....|.
gi 148539874 327 VAHEMGHNFGMKHDGIGCTCG 347
Cdd:cd04271  149 FAHEIGHTFGAVHDCTSGTCS 169
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 395-432 8.98e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 34.66  E-value: 8.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148539874  395 CGNKVVEEGEQCDCGNSESclqDPCCSSDCVLKPGAQC 432
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTTS---GDGCSATCRLEEGFAC 38
 
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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