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Conserved domains on  [gi|187954921|gb|AAI41205|]
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A disintegrin and metallopeptidase domain 34 [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 ...
 207-395 2.03e-66

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: 217.48  E-value: 2.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 207 RFIDYFVVIDHNRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEIRKVLGAFCNWKINA 286
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 287 IGNRVRHDIIHLFVRRSY-GTYLGLANVGTVClTLNCA--VNSFLSDSLSDMAFIIAHEMGHNLGMMHDGSSCTCGLSSC 363
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMC-SPKYSggVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187954921 364 IMAPYKSNSPK-FSNCSYEEMFSVVTKR--SCLYD 395
Cdd:cd04269  160 IMAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
492-628 2.04e-51

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 174.86  E-value: 2.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921   492 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSMYRRCNLADVLCGRIQCENVI 570
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954921   571 QLPQRRNHETVHYTHFSNVTCWTTDYHFGITiDDVGAVSDGTTCGPDYLCVHRKCVSK 628
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
416-488 4.57e-37

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.75  E-value: 4.57e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187954921  416 EEGEECDCGSTESCLQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKTGTVCREEKNECDLPEWCNGTSAECPGD 488
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 6.51e-24

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: 97.38  E-value: 6.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921   41 EVVTPLRVTVTR------GNNISPGWLSYSLNIEGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEEQPFVQNDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 187954921  115 VDEDPESLVIVNTCFGsLQGTLEINGTTYEIMP----KSTTSTFEHLAY 159
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 ...
 207-395 2.03e-66

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: 217.48  E-value: 2.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 207 RFIDYFVVIDHNRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEIRKVLGAFCNWKINA 286
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 287 IGNRVRHDIIHLFVRRSY-GTYLGLANVGTVClTLNCA--VNSFLSDSLSDMAFIIAHEMGHNLGMMHDGSSCTCGLSSC 363
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMC-SPKYSggVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187954921 364 IMAPYKSNSPK-FSNCSYEEMFSVVTKR--SCLYD 395
Cdd:cd04269  160 IMAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
492-628 2.04e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 174.86  E-value: 2.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921   492 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSMYRRCNLADVLCGRIQCENVI 570
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954921   571 QLPQRRNHETVHYTHFSNVTCWTTDYHFGITiDDVGAVSDGTTCGPDYLCVHRKCVSK 628
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 493-596 2.39e-45

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 157.01  E-value: 2.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  493 DGIPCS-GEGYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSMYRRCNLADVLCGRIQCENVIQ 571
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 187954921  572 LPQRRNHETVHYTHFSNVTCWTTDY 596
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 207-397 1.35e-43

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: 155.92  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  207 RFIDYFVVIDHNRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEIRKVLGAFCNWKINA 286
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  287 IGNRVRHDIIHLFVRRS-YGTYLGLANVGTVCLTL-NCAVNSFLSDSLSDMAFIIAHEMGHNLGMMHDGSS--CTCG-LS 361
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEfGGTTVGAAYVGGMCSLEySGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 187954921  362 SCIMAPYKSNSP--KFSNCSYEEMFSVVTKR--SCLYDIP 397
Cdd:pfam01421 161 GCIMNPSAGSSFprKFSNCSQEDFEQFLTKQkgACLFNKP 200
Disintegrin pfam00200
Disintegrin;
416-488 4.57e-37

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.75  E-value: 4.57e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187954921  416 EEGEECDCGSTESCLQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKTGTVCREEKNECDLPEWCNGTSAECPGD 488
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 416-490 1.19e-33

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 123.18  E-value: 1.19e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187954921   416 EEGEECDCGSTESClQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKTGTVCREEKNECDLPEWCNGTSAECPGDVY 490
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 6.51e-24

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: 97.38  E-value: 6.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921   41 EVVTPLRVTVTR------GNNISPGWLSYSLNIEGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEEQPFVQNDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 187954921  115 VDEDPESLVIVNTCFGsLQGTLEINGTTYEIMP----KSTTSTFEHLAY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 410-447 5.04e-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: 35.04  E-value: 5.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 187954921  410 CGNNLVEEGEECDCGSTESclqDPCCSSDCVLKPGAQC 447
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 ...
 207-395 2.03e-66

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: 217.48  E-value: 2.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 207 RFIDYFVVIDHNRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEIRKVLGAFCNWKINA 286
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 287 IGNRVRHDIIHLFVRRSY-GTYLGLANVGTVClTLNCA--VNSFLSDSLSDMAFIIAHEMGHNLGMMHDGSSCTCGLSSC 363
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMC-SPKYSggVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187954921 364 IMAPYKSNSPK-FSNCSYEEMFSVVTKR--SCLYD 395
Cdd:cd04269  160 IMAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
492-628 2.04e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 174.86  E-value: 2.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921   492 ADGIPCSGE-GYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSMYRRCNLADVLCGRIQCENVI 570
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 187954921   571 QLPQRRNHETVHYTHFSNVTCWTTDYHFGITiDDVGAVSDGTTCGPDYLCVHRKCVSK 628
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 493-596 2.39e-45

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 157.01  E-value: 2.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  493 DGIPCS-GEGYCYKMECHQRDEQCRKIFGNGSRSADEICYMEMNRRGDRFGNCGNDSSMYRRCNLADVLCGRIQCENVIQ 571
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 187954921  572 LPQRRNHETVHYTHFSNVTCWTTDY 596
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 207-397 1.35e-43

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: 155.92  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  207 RFIDYFVVIDHNRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEIRKVLGAFCNWKINA 286
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  287 IGNRVRHDIIHLFVRRS-YGTYLGLANVGTVCLTL-NCAVNSFLSDSLSDMAFIIAHEMGHNLGMMHDGSS--CTCG-LS 361
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEfGGTTVGAAYVGGMCSLEySGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 187954921  362 SCIMAPYKSNSP--KFSNCSYEEMFSVVTKR--SCLYDIP 397
Cdd:pfam01421 161 GCIMNPSAGSSFprKFSNCSQEDFEQFLTKQkgACLFNKP 200
Disintegrin pfam00200
Disintegrin;
416-488 4.57e-37

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.75  E-value: 4.57e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187954921  416 EEGEECDCGSTESCLQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKTGTVCREEKNECDLPEWCNGTSAECPGD 488
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 416-490 1.19e-33

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 123.18  E-value: 1.19e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187954921   416 EEGEECDCGSTESClQDPCC-SSDCVLKPGAQCAFGLCCKNCQFLKTGTVCREEKNECDLPEWCNGTSAECPGDVY 490
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 6.51e-24

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: 97.38  E-value: 6.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921   41 EVVTPLRVTVTR------GNNISPGWLSYSLNIEGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEEQPFVQNDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 187954921  115 VDEDPESLVIVNTCFGsLQGTLEINGTTYEIMP----KSTTSTFEHLAY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 207-383 8.24e-22

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: 94.23  E-value: 8.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 207 RFIDYFVVIDHN--RYVHRNNntttcIQDM-LQVVNGINGYY----LQIQTDVVLTKLEVW-SQNNLINVEQEIRKVLGA 278
Cdd:cd04273    1 RYVETLVVADSKmvEFHHGED-----LEHYiLTLMNIVASLYkdpsLGNSINIVVVRLIVLeDEESGLLISGNAQKSLKS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 279 FCNW--KIN--AIGNRVRHDIIHLFVRRSYGTY------LGLANVGTVC-LTLNCAVNSflsDSLSDMAFIIAHEMGHNL 347
Cdd:cd04273   76 FCRWqkKLNppNDSDPEHHDHAILLTRQDICRSngncdtLGLAPVGGMCsPSRSCSINE---DTGLSSAFTIAHELGHVL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 187954921 348 GMMHDGSSCTCG---LSSCIMAPY-KSNSPKF--SNCSYEEM 383
Cdd:cd04273  153 GMPHDGDGNSCGpegKDGHIMSPTlGANTGPFtwSKCSRRYL 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 207-380 3.58e-18

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: 83.24  E-value: 3.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 207 RFIDYFVVIDHNRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQT----DVVLTKLEVWSQNNLINVEQ-EIRKVLGAFCN 281
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 282 WKInaiGNRVRHDIIHLFVRRSY--GTYLGLANVGTVCltlncavNSFLSDSLS-------DMAFIIAHEMGHNLGMMHD 352
Cdd:cd04267   81 WRA---EGPIRHDNAVLLTAQDFieGDILGLAYVGSMC-------NPYSSVGVVedtgftlLTALTMAHELGHNLGAEHD 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 187954921 353 GSSCTC----GLSSCIMAPY--KSNSPKFSNCSY 380
Cdd:cd04267  151 GGDELAfecdGGGNYIMAPVdsGLNSYRFSQCSI 184
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
206-376 7.05e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 64.75  E-value: 7.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  206 HRFIDYFVVIDHnRYV--HRNNNTTTCIQDMLQVVNgiNGYYLQIQTDVVLTKLEVWSQNNLI----NVEQEIRKVLGAF 279
Cdd:pfam13688   2 TRTVALLVAADC-SYVaaFGGDAAQANIINMVNTAS--NVYERDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  280 CNwkINAIGNRVRHDIIHLFVRRSYGTYlGLANVGTVC-------LTLNCAVNSFLSDSLSDmAFIIAHEMGHNLGMMHD 352
Cdd:pfam13688  79 QD--FSAWRGTQNDDLAYLFLMTNCSGG-GLAWLGQLCnsgsagsVSTRVSGNNVVVSTATE-WQVFAHEIGHNFGAVHD 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 187954921  353 ----GSSCTCGLSS--------CIMAPY-KSNSPKFS 376
Cdd:pfam13688 155 cdssTSSQCCPPSNstcpaggrYIMNPSsSPNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 237-352 9.48e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 56.99  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  237 VVNGINGYY-LQIQTDVVLTKLEVWSQNNLINVEQEIRKVLGAFCNWKINAIGNRVrHDIIHLFVRRSYGTYLGLANVGT 315
Cdd:pfam13582   6 LVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYG-YDLGHLFTGRDGGGGGGIAYVGG 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 187954921  316 VCL-TLNCAVNSFLSDSLSDMAFIIAHEMGHNLGMMHD 352
Cdd:pfam13582  85 VCNsGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 288-380 3.74e-08

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: 53.29  E-value: 3.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 288 GNRVRHDIIHLFVR--RSYGTyLGLANVGTVCLTLNcAVNSFLSDSL--SDMAFIIAHEMGHNLGMMHDGSSC------- 356
Cdd:cd00203   47 VEIDKADIAILVTRqdFDGGT-GGWAYLGRVCDSLR-GVGVLQDNQSgtKEGAQTIAHELGHALGFYHDHDRKdrddypt 124

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 187954921 357 -------TCGLSSCIMAPYKS-----NSPKFSNCSY 380
Cdd:cd00203  125 iddtlnaEDDDYYSVMSYTKGsfsdgQRKDFSQCDI 160
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 226-387 1.20e-07

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: 52.63  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  226 NTTTCIqdmLQVVNGINGYYLQ--IQTDVVLTK---LEVW-----SQNNLINVEQEIRKVLGAFCNWkinaIGNRvRHDI 295
Cdd:pfam13574   2 NVTENL---VNVVNRVNQIYEPddININGGLVNpgeIPATtsasdSGNNYCNSPTTIVRRLNFLSQW----RGEQ-DYCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  296 IHLFVRRSY-GTYLGLANVGTVCLT--LNCAVNSFLSDSLSDMAF--------IIAHEMGHNLGMMHD-------GSSC- 356
Cdd:pfam13574  74 AHLVTMGTFsGGELGLAYVGQICQKgaSSPKTNTGLSTTTNYGSFnyptqewdVVAHEVGHNFGATHDcdgsqyaSSGCe 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 187954921  357 -TCGLSSC------IMAPY-KSNSPKFSNCSYEEMFSVV 387
Cdd:pfam13574 154 rNAATSVCsangsfIMNPAsKSNNDLFSPCSISLICDVL 192
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 294-379 1.18e-05

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: 46.84  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921  294 DIIHLFVR-RSYGTYLGLANVGTVCLTLNCAVNSFLSDSLSDMAFIIAHEMGHNLGMMHDGSSCTCGLS--------SCI 364
Cdd:pfam13583  93 DLAYLTLMtGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDIFAHEIGHTFGAVHDCSSQGEGLSsstedgsgQTI 172

                          90
                  ....*....|....*.
gi 187954921  365 MAPYKSNS-PKFSNCS 379
Cdd:pfam13583 173 MSYASTASqTAFSPCT 188
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 289-393 2.61e-05

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 46.19  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 289 NRVRHDIIHLFVRRSYGTY---------LGLANVGTVCLTLNCAVNSFLSDSLSDMaFIIAHEMGHNLGMMHDGS----S 355
Cdd:cd04272   91 DYFNPDVVFLVTGLDMSTYsggslqtgtGGYAYVGGACTENRVAMGEDTPGSYYGV-YTMTHELAHLLGAPHDGSpppsW 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 187954921 356 CTCGLSS--C------IMApYKSNSP---KFSNCSYEEMFSVV--TKRSCL 393
Cdd:cd04272  170 VKGHPGSldCpwddgyIMS-YVVNGErqyRFSQCSQRQIRNVFrrLGASCL 219
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 212-392 8.38e-05

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: 44.67  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 212 FVVIDHNRYVH-RNNNTTTCIQ---DMLQVVN-----------GINGYYLQIQTDVVLTK-LEVWSQNNLINVEQEIRKV 275
Cdd:cd04270    6 LLVADHRFYKYmGRGEEETTINyliSHIDRVDdiyrntdwdggGFKGIGFQIKRIRIHTTpDEVDPGNKFYNKSFPNWGV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 276 lGAFCNwKINAIGNRVRHDIIHLFVRRSY--GTyLGLANVGT--------VC-----------LTLNCAVNSFLSDS--- 331
Cdd:cd04270   86 -EKFLV-KLLLEQFSDDVCLAHLFTYRDFdmGT-LGLAYVGSprdnsaggICekayyysngkkKYLNTGLTTTVNYGkrv 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187954921 332 ---LSDMAFiiAHEMGHNLGMMHD--GSSCTCGLS---SCIMAPY-----KSNSPKFSNCSYEEMFSV--VTKRSC 392
Cdd:cd04270  163 ptkESDLVT--AHELGHNFGSPHDpdIAECAPGESqggNYIMYARatsgdKENNKKFSPCSKKSISKVleVKSNSC 236
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 276-393 3.53e-04

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: 42.79  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 276 LGAFCNWKinaiGNRVRHDII--HLFVRRSYGTYLGLANVGTVCLTL------NCAVNSFLSDSLSDMAFIIAHEMGHNL 347
Cdd:cd04271   82 LSIFSQWR----GQQPDDGNAfwTLMTACPSGSEVGVAWLGQLCRTGasdqgnETVAGTNVVVRTSNEWQVFAHEIGHTF 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187954921 348 GMMHDGSSCTCGL-------------SSC------IMAPYKSNS-PKFSNCSYEEMFSVVTKR----SCL 393
Cdd:cd04271  158 GAVHDCTSGTCSDgsvgsqqccplstSTCdangqyIMNPSSSSGiTEFSPCTIGNICSLLGRNpvrtSCL 227
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 410-447 5.04e-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: 35.04  E-value: 5.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 187954921  410 CGNNLVEEGEECDCGSTESclqDPCCSSDCVLKPGAQC 447
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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