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Conserved domains on  [gi|572882555|ref|NP_001275904|]
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disintegrin and metalloproteinase domain-containing protein 12 isoform 5 preproprotein [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 ...
 211-413 1.79e-105

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: 320.40  E-value: 1.79e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  211 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 290
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  291 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 370
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 572882555  371 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 413
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
507-649 1.52e-53

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 181.02  E-value: 1.52e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555   507 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 586
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882555   587 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 649
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-156 5.21e-33

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: 123.58  E-value: 5.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555   60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTGHCYYHGHVRGYSDSAVSLSTCSGLR 139
Cdd:pfam01562  19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLR 98

                          90
                  ....*....|....*..
gi 572882555  140 GLIVFENESYVLEPMKS 156
Cdd:pfam01562  99 GFIRTENEEYLIEPLEK 115
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 436-504 1.95e-28

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: 108.55  E-value: 1.95e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882555   436 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 504
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 211-413 1.79e-105

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: 320.40  E-value: 1.79e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  211 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 290
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  291 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 370
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 572882555  371 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 413
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 211-411 1.58e-97

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: 299.53  E-value: 1.58e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 211 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 291 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDtlDRGCSCQMav 370
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 572882555 371 ekGGCIMNASTGYPfPMVFSSCSRKDLETSLEKGMGVCLFN 411
Cdd:cd04269  157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
507-649 1.52e-53

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 181.02  E-value: 1.52e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555   507 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 586
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882555   587 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 649
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 507-617 1.52e-40

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: 143.91  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  507 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKvSKSSFAKCEMRDAKCGKIQCQGGA 586
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 572882555  587 SRPVIGTNAVSIETNIPLQQggrilCRGTHV 617
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGVT-----CWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-156 5.21e-33

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: 123.58  E-value: 5.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555   60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTGHCYYHGHVRGYSDSAVSLSTCSGLR 139
Cdd:pfam01562  19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLR 98

                          90
                  ....*....|....*..
gi 572882555  140 GLIVFENESYVLEPMKS 156
Cdd:pfam01562  99 GFIRTENEEYLIEPLEK 115
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 436-504 1.95e-28

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: 108.55  E-value: 1.95e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882555   436 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 504
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
440-502 5.81e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 104.25  E-value: 5.81e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882555  440 PEEC-MNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPAN 502
Cdd:pfam00200  11 LEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 285-397 2.36e-04

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 44.00  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 285 DWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMApimSMCTADQSGGIVMDHSDNPlgAAVTLAHELGHNFGMNHDTLDRG- 363
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197

                         90       100       110
                 ....*....|....*....|....*....|....
gi 572882555 364 CScqmavEKGGCIMNASTGYPFPMVFSSCSRKDL 397
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 211-413 1.79e-105

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: 320.40  E-value: 1.79e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  211 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 290
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  291 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQmav 370
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 572882555  371 EKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLP 413
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 211-411 1.58e-97

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: 299.53  E-value: 1.58e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 211 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMK 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 291 LLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDtlDRGCSCQMav 370
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 572882555 371 ekGGCIMNASTGYPfPMVFSSCSRKDLETSLEKGMGVCLFN 411
Cdd:cd04269  157 --STCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
507-649 1.52e-53

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 181.02  E-value: 1.52e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555   507 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSkSSFAKCEMRDAKCGKIQCQGGA 586
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 572882555   587 SRPVIGTNAVSIETNIplqqgGRILCRGTHVYLGDDmPDPGLVLAGTKCADGKICLNRQCQNI 649
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 507-617 1.52e-40

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: 143.91  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  507 DGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKvSKSSFAKCEMRDAKCGKIQCQGGA 586
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 572882555  587 SRPVIGTNAVSIETNIPLQQggrilCRGTHV 617
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGVT-----CWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 211-402 1.59e-33

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: 127.15  E-value: 1.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 211 KYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYR----PLNIRIVLVGVEVWN--DMDKcSVSQDPFTSLHEFL 284
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKgeQFAP-PIDSDASNTLNSFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 285 DWRKMKllpRKSHDNAQLVSGVYF-QGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAaVTLAHELGHNFGMNHDtlDRG 363
Cdd:cd04267   80 FWRAEG---PIRHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLTA-LTMAHELGHNLGAEHD--GGD 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 572882555 364 CSCQMAVEKGGCIMNASTGYPFPMVFSSCSRKDLETSLE 402
Cdd:cd04267  154 ELAFECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 60-156 5.21e-33

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: 123.58  E-value: 5.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555   60 DSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTGHCYYHGHVRGYSDSAVSLSTCSGLR 139
Cdd:pfam01562  19 SESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLR 98

                          90
                  ....*....|....*..
gi 572882555  140 GLIVFENESYVLEPMKS 156
Cdd:pfam01562  99 GFIRTENEEYLIEPLEK 115
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 211-410 2.08e-32

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: 124.66  E-value: 2.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 211 KYVELVIVADNREFQRQGKdlEKVKQRLIEIANHVDKFYR-PL---NIRIVLVGVEVWNDMDK-CSVSQDPFTSLHEFLD 285
Cdd:cd04273    1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 286 WRKmKLLPR-----KSHDNAQLVSGVYFQG-----TTIGMAPIMSMCTADQSGGIVmdhSDNPLGAAVTLAHELGHNFGM 355
Cdd:cd04273   79 WQK-KLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELGHVLGM 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 572882555 356 NHDTLDRGCScqmAVEKGGCIMNASTGYPF-PMVFSSCSRKDLETSLEKGMGVCLF 410
Cdd:cd04273  155 PHDGDGNSCG---PEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 436-504 1.95e-28

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: 108.55  E-value: 1.95e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 572882555   436 DCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVY 504
Cdd:smart00050   7 DCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
440-502 5.81e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 104.25  E-value: 5.81e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 572882555  440 PEEC-MNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPAN 502
Cdd:pfam00200  11 LEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
209-382 2.54e-18

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 83.62  E-value: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  209 ATKYVELVIVADNrEFqRQGKDLEKVKQRLIEIANHVD-KFYRPLNIRIVLVGVEVWNDMD----KCSVSQDPFTSLHEF 283
Cdd:pfam13688   1 STRTVALLVAADC-SY-VAAFGGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  284 LD---WRKmkllpRKSHDNAQLVSGVYFQGTtiGMAPIMSMCTADQSGGIVMDHSDN-----PLGAAVTLAHELGHNFGM 355
Cdd:pfam13688  79 QDfsaWRG-----TQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNnvvvsTATEWQVFAHEIGHNFGA 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 572882555  356 NHD----TLDRGCSCQMAVEKGG--CIMNASTG 382
Cdd:pfam13688 152 VHDcdssTSSQCCPPSNSTCPAGgrYIMNPSSS 184
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 211-395 7.73e-18

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: 81.41  E-value: 7.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 211 KYVELVIVADNREFqrqgkDLEKVKQRLIEIANHVDKFYR-PLNIRIVLVGVEVwndmdkcsvsqdpftslhefldwrkm 289
Cdd:cd00203    1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI-------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 290 kllprKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTlDRGCSCQMA 369
Cdd:cd00203   50 -----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDH-DRKDRDDYP 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 572882555 370 VEK---------GGCIMNA-----STGYPFPmvFSSCSRK 395
Cdd:cd00203  124 TIDdtlnaedddYYSVMSYtkgsfSDGQRKD--FSQCDID 161
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 238-358 1.78e-13

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: 67.40  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  238 LIEIANHVdkFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMkllpRKSHDNA---QLVSGVYFQGTTiG 314
Cdd:pfam13582   6 LVNRANTI--YERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYdlgHLFTGRDGGGGG-G 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 572882555  315 MAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHD 358
Cdd:pfam13582  79 IAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 215-408 4.91e-10

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: 60.47  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 215 LVIVADNREFQRQGKDLEK-VKQRLIEIANHVDKFYRPL--------NIRIVLVGVEVwNDMDKCSVSQDPFTSlHEFLD 285
Cdd:cd04270    5 LLLVADHRFYKYMGRGEEEtTINYLISHIDRVDDIYRNTdwdgggfkGIGFQIKRIRI-HTTPDEVDPGNKFYN-KSFPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 286 WRKMKLLPRKSHDN-------AQLVSGVYFQGTTIGMAPIMSMcTADQSGGIVMDHSDNPLG------------------ 340
Cdd:cd04270   83 WGVEKFLVKLLLEQfsddvclAHLFTYRDFDMGTLGLAYVGSP-RDNSAGGICEKAYYYSNGkkkylntgltttvnygkr 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 572882555 341 -----AAVTLAHELGHNFGMNHDTldRGCSCQMAVEKGG-CIMNAS--TGY-PFPMVFSSCSRKDLETSLEKGMGVC 408
Cdd:cd04270  162 vptkeSDLVTAHELGHNFGSPHDP--DIAECAPGESQGGnYIMYARatSGDkENNKKFSPCSKKSISKVLEVKSNSC 236
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 212-396 6.80e-10

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 59.67  E-value: 6.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 212 YVELVIVADnREFQRQGKDLEKVKQRLIEIANHVDKFYRPLN---IRIVLVGVEVWNDMDKCSVSQ-------DPFTSLH 281
Cdd:cd04272    2 YPELFVVVD-YDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHpinygyiDAAETLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 282 EFLDWRKMKLLPRKsHDNAQLVSG----VYFQGT----TIGMAPIMSMCTADqsgGIVMDHsDNP--LGAAVTLAHELGH 351
Cdd:cd04272   81 NFNEYVKKKRDYFN-PDVVFLVTGldmsTYSGGSlqtgTGGYAYVGGACTEN---RVAMGE-DTPgsYYGVYTMTHELAH 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 572882555 352 NFGMNHDTLDRGCSCQMAVEKGGC------IMNASTGYPFPMVFSSCSRKD 396
Cdd:cd04272  156 LLGAPHDGSPPPSWVKGHPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQ 206
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 210-393 2.20e-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: 404471  Cd Length: 203  Bit Score: 54.93  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  210 TKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFY-RPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRK 288
Cdd:pfam13583   1 TRRVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRDVIYTDSSTDSFNADCSGGDLGNWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  289 MKL---LPRKSHDNAQLVSGVYFQGTTIGMAPIMSMC-TADQS--GGIVMDHSDNPlgaaVTLAHELGHNFGMNHDTLDR 362
Cdd:pfam13583  81 ATLtswRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNakASGVARSRDEW----DIFAHEIGHTFGAVHDCSSQ 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 572882555  363 GCSCQMAVE--KGGCIMNASTGYPFPMvFSSCS 393
Cdd:pfam13583 157 GEGLSSSTEdgSGQTIMSYASTASQTA-FSPCT 188
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 234-402 1.19e-06

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 49.55  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  234 VKQRLIEIANHVDKFYRP--LNIRIVLVGV----------EVWNDmdKCSVSQDPFTSLHEFLDWRKmkllpRKSHDNAQ 301
Cdd:pfam13574   3 VTENLVNVVNRVNQIYEPddININGGLVNPgeipattsasDSGNN--YCNSPTTIVRRLNFLSQWRG-----EQDYCLAH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555  302 LVSGVYFQGTTIGMAPIMSMCTADQS---------GGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTlDRGCSCQMAVEK 372
Cdd:pfam13574  76 LVTMGTFSGGELGLAYVGQICQKGASspktntglsTTTNYGSFNYPTQEWDVVAHEVGHNFGATHDC-DGSQYASSGCER 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 572882555  373 GGCIMNASTGYPFPM---------VFSSCSRKDLETSLE 402
Cdd:pfam13574 155 NAATSVCSANGSFIMnpasksnndLFSPCSISLICDVLG 193
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 232-409 8.88e-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: 44.72  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 232 EKVKQRLIEIANHVDKFYR-PLNIRIVLVGVEVwNDMDKCS--VSQDPFTS-----------LHEFLDWRKmkllPRKSH 297
Cdd:cd04271   21 EEARRNILNNVNSASQLYEsSFNISLGLRNLTI-SDASCPStaVDSAPWNLpcnsrididdrLSIFSQWRG----QQPDD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 298 DNA--QLVSGVYfQGTTIGMAPIMSMCTADQSGGIVMDHSdNPLGAAVT------LAHELGHNFGMNHDTlDRGCSCQMA 369
Cdd:cd04271   96 GNAfwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGHTFGAVHDC-TSGTCSDGS 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 572882555 370 VEKGGC--------------IMNASTGYPFpMVFSSCSRKDLETSLEKG--MGVCL 409
Cdd:cd04271  173 VGSQQCcplststcdangqyIMNPSSSSGI-TEFSPCTIGNICSLLGRNpvRTSCL 227
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 285-397 2.36e-04

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 44.00  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 572882555 285 DWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMApimSMCTADQSGGIVMDHSDNPlgAAVTLAHELGHNFGMNHDTLDRG- 363
Cdd:NF038115 123 DNDRVGNAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVTLDLYV--ATQTLAHELGHLFGLYNGHAESAe 197

                         90       100       110
                 ....*....|....*....|....*....|....
gi 572882555 364 CScqmavEKGGCIMNASTGYPFPMVFSSCSRKDL 397
Cdd:NF038115 198 CS-----EGGYRLMCGSLAENFENLFGSSELQRF 226
 
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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