NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|46909598|ref|NP_997079|]
View 

disintegrin and metalloproteinase domain-containing protein 15 isoform 5 preproprotein [Homo sapiens]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 213-411 3.51e-82

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: 262.17  E-value: 3.51e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 213 KTVELVIVADHSEAQKY-RDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 291
Cdd:cd04269   1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 292 LLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 371
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46909598 372 paKTCIMEASTDFLPgLNFSNCSRRALEKALLDGMGSCLF 411
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
508-649 3.16e-45

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 159.06  E-value: 3.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598    508 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGSYVSCTPRDAICGQLQCQTGR 587
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46909598    588 TQPLLGSIRDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLVCIDHRCQRV 649
Cdd:smart00608  81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 430-504 2.61e-35

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: 128.19  E-value: 2.61e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46909598    430 EPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDV 504
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDP 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 62-154 2.50e-15

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: 73.12  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598    62 QTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRG 141
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                          90
                  ....*....|...
gi 46909598   142 LVVlTPERSYTLE 154
Cdd:pfam01562 100 FIR-TENEEYLIE 111
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 213-411 3.51e-82

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: 262.17  E-value: 3.51e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 213 KTVELVIVADHSEAQKY-RDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 291
Cdd:cd04269   1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 292 LLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 371
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46909598 372 paKTCIMEASTDFLPgLNFSNCSRRALEKALLDGMGSCLF 411
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 213-413 3.43e-72

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: 235.66  E-value: 3.43e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   213 KTVELVIVADHSEAQKYR-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGsDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   292 LLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPgpa 371
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 46909598   372 PAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFER 413
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
ACR smart00608
ADAM Cysteine-Rich Domain;
508-649 3.16e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 159.06  E-value: 3.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598    508 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGSYVSCTPRDAICGQLQCQTGR 587
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46909598    588 TQPLLGSIRDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLVCIDHRCQRV 649
Cdd:smart00608  81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 430-504 2.61e-35

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: 128.19  E-value: 2.61e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46909598    430 EPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDV 504
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDP 74
Disintegrin pfam00200
Disintegrin;
430-503 1.21e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 123.51  E-value: 1.21e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46909598   430 EPGEQCDCGFLDDC-VDPCCDSLTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 503
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 508-617 1.41e-33

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: 124.65  E-value: 1.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   508 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPsGSYVSCTPRDAICGQLQCQTGR 587
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 46909598   588 TQPLLGSIRDLLWETIdvngTELNCSWVHL 617
Cdd:pfam08516  80 ELPLLGEHATVIYTNI----NGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 62-154 2.50e-15

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: 73.12  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598    62 QTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRG 141
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                          90
                  ....*....|...
gi 46909598   142 LVVlTPERSYTLE 154
Cdd:pfam01562 100 FIR-TENEEYLIE 111
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 213-411 3.51e-82

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: 262.17  E-value: 3.51e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 213 KTVELVIVADHSEAQKY-RDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 291
Cdd:cd04269   1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 292 LLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 371
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46909598 372 paKTCIMEASTDFLPgLNFSNCSRRALEKALLDGMGSCLF 411
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 213-413 3.43e-72

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: 235.66  E-value: 3.43e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   213 KTVELVIVADHSEAQKYR-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGsDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   292 LLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPgpa 371
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 46909598   372 PAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFER 413
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
ACR smart00608
ADAM Cysteine-Rich Domain;
508-649 3.16e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 159.06  E-value: 3.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598    508 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGSYVSCTPRDAICGQLQCQTGR 587
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46909598    588 TQPLLGSIRDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLVCIDHRCQRV 649
Cdd:smart00608  81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 430-504 2.61e-35

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: 128.19  E-value: 2.61e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46909598    430 EPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDV 504
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDP 74
Disintegrin pfam00200
Disintegrin;
430-503 1.21e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 123.51  E-value: 1.21e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46909598   430 EPGEQCDCGFLDDC-VDPCCDSLTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 503
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 508-617 1.41e-33

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: 124.65  E-value: 1.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   508 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPsGSYVSCTPRDAICGQLQCQTGR 587
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 46909598   588 TQPLLGSIRDLLWETIdvngTELNCSWVHL 617
Cdd:pfam08516  80 ELPLLGEHATVIYTNI----NGVTCWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 213-402 2.55e-29

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: 115.60  E-value: 2.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 213 KTVELVIVADHSEAQKYR-DFQHLLNRTLEVALLLDTFFR----PLNVRVALVGLEAW-TQRDLVEISPNPAVTLENFLH 286
Cdd:cd04267   1 REIELVVVADHRMVSYFNsDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 287 WRRAHLlPRlpHDSAQLVTGTSF-SGPTVGMAIQNSICSPDFSGGVNMDHSTSILgVASSIAHELGHSLGLDHDlPGNSC 365
Cdd:cd04267  81 WRAEGP-IR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHD-GGDEL 155

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 46909598 366 PCPGPApAKTCIMEASTDFLPGLNFSNCSRRALEKAL 402
Cdd:cd04267 156 AFECDG-GGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 213-411 5.13e-27

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: 109.25  E-value: 5.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 213 KTVELVIVADHSEAQKY--RDFQH----LLNrtlEVALLL-DTFFRPlNVRVALVGLEAWTQR-DLVEISPNPAVTLENF 284
Cdd:cd04273   1 RYVETLVVADSKMVEFHhgEDLEHyiltLMN---IVASLYkDPSLGN-SINIVVVRLIVLEDEeSGLLISGNAQKSLKSF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 285 LHWRRAHLLPR----LPHDSAQLVTGTSFSGP-----TVGMAIQNSICSPDFSGGVNMDHStsiLGVASSIAHELGHSLG 355
Cdd:cd04273  77 CRWQKKLNPPNdsdpEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELGHVLG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46909598 356 LDHDLPGNSCpcpGPAPAKTCIMEASTDFLPG-LNFSNCSRRALEKALLDGMGSCLF 411
Cdd:cd04273 154 MPHDGDGNSC---GPEGKDGHIMSPTLGANTGpFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 62-154 2.50e-15

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: 73.12  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598    62 QTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRG 141
Cdd:pfam01562  20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99

                          90
                  ....*....|...
gi 46909598   142 LVVlTPERSYTLE 154
Cdd:pfam01562 100 FIR-TENEEYLIE 111
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
212-378 1.09e-13

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 70.53  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   212 TKTVELVIVADHSeaqkYRDfQHLLNRTLEVALLL-----DTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLH 286
Cdd:pfam13688   2 TRTVALLVAADCS----YVA-AFGGDAAQANIINMvntasNVYERDFNISLGLVNLTISDSTCPYTPPACSTGDSSDRLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   287 -------WRRAHllprlPHDSAQLVTGTSFSGPtvGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHSL 354
Cdd:pfam13688  77 efqdfsaWRGTQ-----NDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHNF 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 46909598   355 GLDHD----LPGNSCP-----CPGPApakTCIM 378
Cdd:pfam13688 150 GAVHDcdssTSSQCCPpsnstCPAGG---RYIM 179
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 251-359 6.29e-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: 60.46  E-value: 6.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   251 RPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAhllpRLPH---DSAQLVTGTSFSGpTVGMAIQNSICSPDF 327
Cdd:pfam13582  16 RDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQygyDLGHLFTGRDGGG-GGGIAYVGGVCNSGS 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 46909598   328 SGGVNMDHSTSILGVASSIAHELGHSLGLDHD 359
Cdd:pfam13582  91 KFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 213-402 1.15e-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: 61.00  E-value: 1.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 213 KTVELVIVADHseaqKYRDFQHLLNRTLEVALLLDTFFR-PLNVRVALVGLEawtqrdlveispnpavtlenflhwrrah 291
Cdd:cd00203   1 KVIPYVVVADD----RDVEEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVE---------------------------- 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 292 llpRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlPGNSCPCPGPA 371
Cdd:cd00203  49 ---IDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHD-HDRKDRDDYPT 124

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 46909598 372 PAKT---------CIMEASTDFLPGLN---FSNCSRRALEKAL 402
Cdd:cd00203 125 IDDTlnaedddyySVMSYTKGSFSDGQrkdFSQCDIDQINKLY 167
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 282-395 3.22e-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: 54.56  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   282 ENFLH-WRRAHllprlPHDSAQLVTGTSFSGPTVGMAIQNSIC-------------SPDFSGGVNMDHSTSILgvasSIA 347
Cdd:pfam13574  59 LNFLSqWRGEQ-----DYCLAHLVTMGTFSGGELGLAYVGQICqkgasspktntglSTTTNYGSFNYPTQEWD----VVA 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 46909598   348 HELGHSLGLDHDLPGNSCPCPG-PAPAKTCIMEASTDFL----PGLN---FSNCSR 395
Cdd:pfam13574 130 HEVGHNFGATHDCDGSQYASSGcERNAATSVCSANGSFImnpaSKSNndlFSPCSI 185
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 214-396 6.48e-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: 6.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 214 TVELVIVADhseaqkyRDFQHLLNRTLEVALLLDTFFRPLN----------VRVALVGLE----AWTQRDLVEISP---N 276
Cdd:cd04272   2 YPELFVVVD-------YDHQSEFFSNEQLIRYLAVMVNAANlryrdlksprIRLLLVGITiskdPDFEPYIHPINYgyiD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 277 PAVTLENF-LHWRRAHLLPRlpHDSAQLVTG----TSFSGP----TVGMAIQNSICSpDFSGGVNMDHSTSILGVaSSIA 347
Cdd:cd04272  75 AAETLENFnEYVKKKRDYFN--PDVVFLVTGldmsTYSGGSlqtgTGGYAYVGGACT-ENRVAMGEDTPGSYYGV-YTMT 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46909598 348 HELGHSLGLDHD-LPGNSCPCPGPApAKTC------IMeaSTDF--LPGLNFSNCSRR 396
Cdd:cd04272 151 HELAHLLGAPHDgSPPPSWVKGHPG-SLDCpwddgyIM--SYVVngERQYRFSQCSQR 205
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 301-413 3.09e-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: 3.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 301 AQLVTGTSFSGPTVGMAIQNS--------ICSPD--FSGGVN----------MDHSTSILGVASSI--AHELGHSLGLDH 358
Cdd:cd04270 104 AHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAyyYSNGKKkylntgltttVNYGKRVPTKESDLvtAHELGHNFGSPH 183

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46909598 359 DLPGNSCpCPGPAPAKTCIMEA---STDFLPGLNFSNCSRRALEKALLDGMGSCLFER 413
Cdd:cd04270 184 DPDIAEC-APGESQGGNYIMYAratSGDKENNKKFSPCSKKSISKVLEVKSNSCFVER 240
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 213-396 9.59e-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: 404471  Cd Length: 203  Bit Score: 47.23  E-value: 9.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   213 KTVELVIVADHSEAQKYRDFQHLLNRTLE-VALLLDTFFRPLNVRVALVGleawtQRDLVEISPNPA-----VTLENFLH 286
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRANINAtVTTANEVYGRDFNVSLALIS-----DRDVIYTDSSTDsfnadCSGGDLGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598   287 WRRAHL---LPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSggvNMDHStsilGVASS------IAHELGHSLGLD 357
Cdd:pfam13583  78 WRLATLtswRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQ---NAKAS----GVARSrdewdiFAHEIGHTFGAV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 46909598   358 HDLpGNSCPcpgPAPAKTC------IME-ASTDFLPglNFSNCSRR 396
Cdd:pfam13583 151 HDC-SSQGE---GLSSSTEdgsgqtIMSyASTASQT--AFSPCTIR 190
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 310-382 1.53e-05

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: 47.03  E-value: 1.53e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46909598 310 SGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEAST 382
Cdd:cd04271 108 SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHTFGAVHDCTSGTCSDGSVGSQQCCPLSTST 185
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 330-358 5.36e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 38.37  E-value: 5.36e-03
                          10        20
                  ....*....|....*....|....*....
gi 46909598   330 GVNMDHSTSILGVAssiAHELGHSLGLDH 358
Cdd:pfam00413  99 GSDPPHGINLFLVA---AHEIGHALGLGH 124
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 278-358 5.41e-03

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 38.63  E-value: 5.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46909598 278 AVTLENFLHWRRA---HLLPRLPHDSAQLVTGTS--FSGPTVGMAIQNSICSPD----FSGGVNMDHSTSILGVASS--- 345
Cdd:cd04268  18 AAILDAIEAWNKAfaiGFKNANDVDPADIRYSVIrwIPYNDGTWSYGPSQVDPLtgeiLLARVYLYSSFVEYSGARLrnt 97

                        90
                ....*....|...
gi 46909598 346 IAHELGHSLGLDH 358
Cdd:cd04268  98 AEHELGHALGLRH 110
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH