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Conserved domains on  [gi|256773268|ref|NP_001157961|]
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disintegrin and metalloproteinase domain-containing protein 8 isoform 2 precursor [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 200-400 7.71e-102

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: 311.16  E-value: 7.71e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  200 RYVELYVVVDNAEFQMLGS-EAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQ 278
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  279 RTRRHLHDNVQLITGVDFTGTTVGFARVSAMCS-HSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENVQGCRCQerf 357
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSlEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 256773268  358 EAGRCIMAGSIGSSFPRMFSDCSQAYLESFLERPQSVCLANAP 400
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 30-155 4.95e-44

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: 154.39  E-value: 4.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268   30 EVVLPWRLPGPRVRRALPSHlGLHPERVSYVLGATGHNFTLHLRKNRDLLGSGYTETYTAANGSEVTEQPRGQDHCFYQG 109
Cdd:pfam01562   1 EVVIPVRLDPSRRRRSLASE-STYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 256773268  110 HVEGYPDSAASLSTCAGLRGFFQVGSDLHLIEPLDEGG--EGGR-HAVY 155
Cdd:pfam01562  80 HVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSreEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 417-491 3.42e-34

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


:

Pssm-ID: 214490  Cd Length: 75  Bit Score: 125.11  E-value: 3.42e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773268   417 ERGEQCDCGPPEDCRNRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPEDAF 491
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ACR smart00608
ADAM Cysteine-Rich Domain;
494-605 2.34e-28

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 110.53  E-value: 2.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268   494 NGTPCSG--GYCYNGACPTLAQQCQAFWGPGGQAAEESCFSYDILPG-----C--KASRY-----RADMCGVLQCKGGQQ 559
Cdd:smart00608   2 DGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgrENGTYipcapEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256773268   560 P--LGRAICIV------DVCHALTTEDGTAYEP--VPEGTRCGPEKVCWKGRCQDL 605
Cdd:smart00608  82 LplLGEHATVIysniggLVCWSLDYHLGTDPDIgmVKDGTKCGPGKVCINGQCVDV 137
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 200-400 7.71e-102

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: 311.16  E-value: 7.71e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  200 RYVELYVVVDNAEFQMLGS-EAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQ 278
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  279 RTRRHLHDNVQLITGVDFTGTTVGFARVSAMCS-HSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENVQGCRCQerf 357
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSlEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 256773268  358 EAGRCIMAGSIGSSFPRMFSDCSQAYLESFLERPQSVCLANAP 400
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 200-398 2.84e-83

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 262.55  E-value: 2.84e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 200 RYVELYVVVDNAEFQMLGS-EAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQ 278
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 279 RTRRHLHDNVQLITGVDFTGTTVGFARVSAMCS-HSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENvqGCRCQErf 357
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSpKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG--GCTCGR-- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 256773268 358 eaGRCIMAGSIgSSFPRMFSDCSQAYLESFLERPQSVCLAN 398
Cdd:cd04269  157 --STCIMAPSP-SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 30-155 4.95e-44

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: 154.39  E-value: 4.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268   30 EVVLPWRLPGPRVRRALPSHlGLHPERVSYVLGATGHNFTLHLRKNRDLLGSGYTETYTAANGSEVTEQPRGQDHCFYQG 109
Cdd:pfam01562   1 EVVIPVRLDPSRRRRSLASE-STYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 256773268  110 HVEGYPDSAASLSTCAGLRGFFQVGSDLHLIEPLDEGG--EGGR-HAVY 155
Cdd:pfam01562  80 HVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSreEGGHpHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 417-491 3.42e-34

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 125.11  E-value: 3.42e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773268   417 ERGEQCDCGPPEDCRNRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPEDAF 491
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
417-489 3.04e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 116.57  E-value: 3.04e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256773268  417 ERGEQCDCGPPEDCR-NRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPED 489
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ACR smart00608
ADAM Cysteine-Rich Domain;
494-605 2.34e-28

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 110.53  E-value: 2.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268   494 NGTPCSG--GYCYNGACPTLAQQCQAFWGPGGQAAEESCFSYDILPG-----C--KASRY-----RADMCGVLQCKGGQQ 559
Cdd:smart00608   2 DGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgrENGTYipcapEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256773268   560 P--LGRAICIV------DVCHALTTEDGTAYEP--VPEGTRCGPEKVCWKGRCQDL 605
Cdd:smart00608  82 LplLGEHATVIysniggLVCWSLDYHLGTDPDIgmVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 494-559 1.89e-12

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: 64.17  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  494 NGTPC--SGGYCYNGACPTLAQQCQAFWGPGGQAAEESCFSY-----DILPGC--KASRYRA----D-MCGVLQCKGGQQ 559
Cdd:pfam08516   1 DGTPCnnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvnskgDRFGNCgrTNGGYVKcekrDvLCGKLQCTNVKE 80
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 200-400 7.71e-102

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: 311.16  E-value: 7.71e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  200 RYVELYVVVDNAEFQMLGS-EAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQ 278
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  279 RTRRHLHDNVQLITGVDFTGTTVGFARVSAMCS-HSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENVQGCRCQerf 357
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSlEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 256773268  358 EAGRCIMAGSIGSSFPRMFSDCSQAYLESFLERPQSVCLANAP 400
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 200-398 2.84e-83

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 262.55  E-value: 2.84e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 200 RYVELYVVVDNAEFQMLGS-EAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQ 278
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 279 RTRRHLHDNVQLITGVDFTGTTVGFARVSAMCS-HSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENvqGCRCQErf 357
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSpKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG--GCTCGR-- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 256773268 358 eaGRCIMAGSIgSSFPRMFSDCSQAYLESFLERPQSVCLAN 398
Cdd:cd04269  157 --STCIMAPSP-SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 30-155 4.95e-44

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: 154.39  E-value: 4.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268   30 EVVLPWRLPGPRVRRALPSHlGLHPERVSYVLGATGHNFTLHLRKNRDLLGSGYTETYTAANGSEVTEQPRGQDHCFYQG 109
Cdd:pfam01562   1 EVVIPVRLDPSRRRRSLASE-STYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 256773268  110 HVEGYPDSAASLSTCAGLRGFFQVGSDLHLIEPLDEGG--EGGR-HAVY 155
Cdd:pfam01562  80 HVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSreEGGHpHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 200-389 3.92e-39

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: 143.33  E-value: 3.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 200 RYVELYVVVDNAEF-QMLGSEAAVRHRVLEVVNHVDKLYQK----LNFRVVLVGLEIWNSQDRFHV-SPDPSVTLENLLT 273
Cdd:cd04267    1 REIELVVVADHRMVsYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 274 WQARQRTRrhlHDNVQLITGVDFT-GTTVGFARVSAMC-SHSSGAVNQDHSKNPVgVACTMAHEMGHNLGMDHDENvqGC 351
Cdd:cd04267   81 WRAEGPIR---HDNAVLLTAQDFIeGDILGLAYVGSMCnPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGG--DE 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 256773268 352 RCQERFEAGRCIMAGSIGSSFPRMFSDCSQAYLESFLE 389
Cdd:cd04267  155 LAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 200-396 1.65e-37

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: 139.30  E-value: 1.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 200 RYVELYVVVDNAEFQMLGSEAaVRHRVLEVVNHVDKLYQK----LNFRVVLVGLEIW-NSQDRFHVSPDPSVTLENLLTW 274
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGED-LEHYILTLMNIVASLYKDpslgNSINIVVVRLIVLeDEESGLLISGNAQKSLKSFCRW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 275 QARQRTRR----HLHDNVQLITGVDF-----TGTTVGFARVSAMCS-HSSGAVNQDhskNPVGVACTMAHEMGHNLGMDH 344
Cdd:cd04273   80 QKKLNPPNdsdpEHHDHAILLTRQDIcrsngNCDTLGLAPVGGMCSpSRSCSINED---TGLSSAFTIAHELGHVLGMPH 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 256773268 345 DENvqGCRCQERFEAGrCIMAGSIGS-SFPRMFSDCSQAYLESFLERPQSVCL 396
Cdd:cd04273  157 DGD--GNSCGPEGKDG-HIMSPTLGAnTGPFTWSKCSRRYLTSFLDTGDGNCL 206
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 417-491 3.42e-34

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 125.11  E-value: 3.42e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256773268   417 ERGEQCDCGPPEDCRNRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPEDAF 491
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
417-489 3.04e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 116.57  E-value: 3.04e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256773268  417 ERGEQCDCGPPEDCR-NRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPED 489
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ACR smart00608
ADAM Cysteine-Rich Domain;
494-605 2.34e-28

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 110.53  E-value: 2.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268   494 NGTPCSG--GYCYNGACPTLAQQCQAFWGPGGQAAEESCFSYDILPG-----C--KASRY-----RADMCGVLQCKGGQQ 559
Cdd:smart00608   2 DGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgrENGTYipcapEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 256773268   560 P--LGRAICIV------DVCHALTTEDGTAYEP--VPEGTRCGPEKVCWKGRCQDL 605
Cdd:smart00608  82 LplLGEHATVIysniggLVCWSLDYHLGTDPDIgmVKDGTKCGPGKVCINGQCVDV 137
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 200-388 2.51e-17

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: 79.87  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 200 RYVELYVVVDNAEFqmlgSEAAVRHRVLEVVNHVDKLY-QKLNFRVVLVGLEIWNsqdrfhvspdpsvtlenlltwqarq 278
Cdd:cd00203    1 KVIPYVVVADDRDV----EEENLSAQIQSLILIAMQIWrDYLNIRFVLVGVEIDK------------------------- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 279 rtrrhlHDNVQLITGVDFTGTTVGFARVSAMC-SHSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENVQGCRCQERF 357
Cdd:cd00203   52 ------ADIAILVTRQDFDGGTGGWAYLGRVCdSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTI 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 256773268 358 E--------AGRCIM---AGSIGSSFPRMFSDCSQAYLESFL 388
Cdd:cd00203  126 DdtlnaeddDYYSVMsytKGSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 201-396 1.98e-16

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 78.93  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 201 YVELYVVVDNAEFQMLGSEAAVRHRVLEVVNHVDKLYQKLN---FRVVLVGLEI----WNSQDRFHVSP---DPSVTLEN 270
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITIskdpDFEPYIHPINYgyiDAAETLEN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 271 LLTwQARQRTRRHLHDNVQLITGVDFTGT--------TVGFARVSAMCSHSSGAVNQDHSKNPVGVAcTMAHEMGHNLGM 342
Cdd:cd04272   82 FNE-YVKKKRDYFNPDVVFLVTGLDMSTYsggslqtgTGGYAYVGGACTENRVAMGEDTPGSYYGVY-TMTHELAHLLGA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256773268 343 DHDENVQGCRCQERFEAGRC------IMagSIGSSFPRM--FSDCSQAYLESFLERPQSVCL 396
Cdd:cd04272  160 PHDGSPPPSWVKGHPGSLDCpwddgyIM--SYVVNGERQyrFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
199-377 5.01e-16

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 77.07  E-value: 5.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  199 TRYVELYVVVDNAEFQMLGSEAAVRhRVLEVVNHVDKLYQK-LNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLT--WQ 275
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGDAAQA-NIINMVNTASNVYERdFNISLGLVNLTISDSTCPYTPPACSTGDSSDRLSefQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  276 ARQRTRRHLHDNVQLITGVDFTGTtvGFARVSAMCSH-SSGAVNQDHSKNPVGVAC-----TMAHEMGHNLGMDHD---- 345
Cdd:pfam13688  81 FSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSgSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDcdss 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 256773268  346 ENVQGCRCQERFEA--GRCIMAGSIGSSFpRMFS 377
Cdd:pfam13688 159 TSSQCCPPSNSTCPagGRYIMNPSSSPNS-TDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 225-345 1.04e-15

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 73.94  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  225 RVLEVVNHVDKLYQK-LNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQaRQRTRRHLHDNVQLITGVDFTGTTvGF 303
Cdd:pfam13582   2 RIVSLVNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVN-DTRIGQYGYDLGHLFTGRDGGGGG-GI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 256773268  304 ARVSAMCSHSSGA-VNQDHSKNPVGVACTMAHEMGHNLGMDHD 345
Cdd:pfam13582  80 AYVGGVCNSGSKFgVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 494-559 1.89e-12

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: 64.17  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  494 NGTPC--SGGYCYNGACPTLAQQCQAFWGPGGQAAEESCFSY-----DILPGC--KASRYRA----D-MCGVLQCKGGQQ 559
Cdd:pfam08516   1 DGTPCnnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvnskgDRFGNCgrTNGGYVKcekrDvLCGKLQCTNVKE 80
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 200-383 1.68e-10

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 61.10  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  200 RYVELYVVVDNAEFQMLGSEAAVRHRVLEVVNHVDKLYQK-LNFRVVLVGLEIWNSQDRfhvSPDPSVTL---ENLLTW- 274
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYGRdFNVSLALISDRDVIYTDS---STDSFNADcsgGDLGNWr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  275 QARQRTRRHL--HDNVQLITGVDFTGTTVGFARVSAMCSHSSgavnQDHSKNpvGVAC------TMAHEMGHNLGMDHDE 346
Cdd:pfam13583  80 LATLTSWRDSlnYDLAYLTLMTGPSGQNVGVAWVGALCSSAR----QNAKAS--GVARsrdewdIFAHEIGHTFGAVHDC 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 256773268  347 NVQGCRCQERFEAGR--CIMA-GSIGS----SFPRM----FSDCSQAY 383
Cdd:pfam13583 154 SSQGEGLSSSTEDGSgqTIMSyASTASqtafSPCTIrninGNPCSQAN 201
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 220-380 8.08e-09

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: 56.10  E-value: 8.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  220 AAVRHRVLEVVNHVDKLY--QKLNFRVVLVG----LEIWNSQD----RFHVSPDPSVTLENLLTWQARQRtrrhlHDNVQ 289
Cdd:pfam13574   1 GNVTENLVNVVNRVNQIYepDDININGGLVNpgeiPATTSASDsgnnYCNSPTTIVRRLNFLSQWRGEQD-----YCLAH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  290 LITGVDFTGTTVGFARVSAMCSHSSGAVnqdhsKNPVGVACT---------------MAHEMGHNLGMDHDENVQG--CR 352
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICQKGASSP-----KTNTGLSTTtnygsfnyptqewdvVAHEVGHNFGATHDCDGSQyaSS 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 256773268  353 CQERFEA-------GRCIMAGSiGSSFPRMFSDCS 380
Cdd:pfam13574 151 GCERNAAtsvcsanGSFIMNPA-SKSNNDLFSPCS 184
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 217-390 5.54e-06

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: 48.19  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 217 GSEAAVRHRVLEVVNHVDKLYQK-LNFRVVLVGLEIWNSQD--------RFHVSPDPSVTLENLLTWQARQRTRRHLHDN 287
Cdd:cd04271   18 GSVEEARRNILNNVNSASQLYESsFNISLGLRNLTISDASCpstavdsaPWNLPCNSRIDIDDRLSIFSQWRGQQPDDGN 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 288 V--QLITGVDfTGTTVGFARVSAMC--SHSSGAVNQDHSKNPVGVACT----MAHEMGHNLGMDHDENVQGCRcQERFEA 359
Cdd:cd04271   98 AfwTLMTACP-SGSEVGVAWLGQLCrtGASDQGNETVAGTNVVVRTSNewqvFAHEIGHTFGAVHDCTSGTCS-DGSVGS 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 256773268 360 GRC--------------IMAGSIGSSFPRmFSDCSQAYLESFLER 390
Cdd:cd04271  176 QQCcplststcdangqyIMNPSSSSGITE-FSPCTIGNICSLLGR 219
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 204-380 6.23e-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: 48.14  E-value: 6.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 204 LYVVVDNAEFQMLGS--EAAVRHRVLEVVNHVDKLYQKLNFRVVL---VGLEIwnSQDRFHVSPDPSVTLENLLT----- 273
Cdd:cd04270    5 LLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGGGfkgIGFQI--KRIRIHTTPDEVDPGNKFYNksfpn 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 274 -----WQARQRTRRHLHDN--VQLITGVDFTGTTVGFARVSAMCSHSSGAVNQDHSKNPVGVA----------------- 329
Cdd:cd04270   83 wgvekFLVKLLLEQFSDDVclAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKKkylntgltttvnygkrv 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268 330 ------CTMAHEMGHNLGMDHDENVQGCRCQERfEAGRCIM-AGSIGSSFP--RMFSDCS 380
Cdd:cd04270  163 ptkesdLVTAHELGHNFGSPHDPDIAECAPGES-QGGNYIMyARATSGDKEnnKKFSPCS 221
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 510-602 3.40e-04

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 39.64  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256773268  510 TLAQQCQAFWGPGGQaaeeSCFSYDilpgckasryrADMCGVLQCKGGQQPlgraicivdVCHalttedgTAYEPVPEGT 589
Cdd:pfam17771   6 SADEQCRLIFGPGST----FCPNGD-----------EDVCSKLWCSNPGGS---------TCT-------TKNLPAADGT 54

                          90
                  ....*....|...
gi 256773268  590 RCGPEKVCWKGRC 602
Cdd:pfam17771  55 PCGNKKWCLNGKC 67
 
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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