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Conserved domains on  [gi|114326453|ref|NP_003808|]
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disintegrin and metalloproteinase domain-containing protein 7 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 ...
 199-394 8.15e-97

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: 298.45  E-value: 8.15e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  199 KYVELFIVADDTVYRRNGHPHNKLRNRIWGMVNFVNMIYKTLNIHVTLVGIEIWTHEDKIELYSNIETTLLRFSFWQEKI 278
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  279 LKTRKDFDHVVLLSGKWLYSHVQGISYPGGMCLPYYSTSIIKDLLPDTNIIANRMAHQLGHNLGMQHDEF--PCTC-PSG 355
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 114326453  356 KCVM-DSDGSIPALKFSKCSQNQYHQYLKDYKPTCMLNIP 394
Cdd:pfam01421 161 GCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
488-624 9.89e-47

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 162.53  E-value: 9.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453   488 NGFPCKNSEGYCFMGKCPTREDQCSELFDDEAIESHDICY-KMNTKGNKFGYCKNKENRFLPCEEKDVRCGKIYCTGGEL 566
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 114326453   567 SSLLGEDKTYHLKDPQKnatVKCKTIFLYHDS-TDIGLVASGTKCGEGMVCNNGECLNM 624
Cdd:smart00608  82 LPLLGEHATVIYSNIGG---LVCWSLDYHLGTdPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 28-153 1.98e-37

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: 135.90  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453   28 QLVRPKKL-PLIQKRDTGHTHDddilktYEEELLYEIKLNRKTLVLHLLRSREFLGSNYSETFYSMKGEAFTRHPQIMDH 106
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSLASEST------YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 114326453  107 CFYQGSIVHEYDSAASISTCNGLRGFFRINDQRYLIEPVKYSDEGEH 153
Cdd:pfam01562  75 CYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEG 121
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 411-485 8.31e-36

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: 129.35  E-value: 8.31e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114326453   411 DEGEECDCGPAQECTNPCCDAHTCVLKPGFTCAEGECCESCQIKKAGSICRPAKDECDFPEMCTGHSPACPKDQF 485
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 199-394 8.15e-97

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: 298.45  E-value: 8.15e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  199 KYVELFIVADDTVYRRNGHPHNKLRNRIWGMVNFVNMIYKTLNIHVTLVGIEIWTHEDKIELYSNIETTLLRFSFWQEKI 278
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  279 LKTRKDFDHVVLLSGKWLYSHVQGISYPGGMCLPYYSTSIIKDLLPDTNIIANRMAHQLGHNLGMQHDEF--PCTC-PSG 355
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 114326453  356 KCVM-DSDGSIPALKFSKCSQNQYHQYLKDYKPTCMLNIP 394
Cdd:pfam01421 161 GCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 199-392 5.76e-76

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: 243.29  E-value: 5.76e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 199 KYVELFIVADDTVYRRNGHPHNKLRNRIWGMVNFVNMIYKTLNIHVTLVGIEIWTHEDKIELYSNIETTLLRFSFWQEKI 278
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 279 LKTRKDFDHVVLLSGKWLYSHVQGISYPGGMCLPYYSTSIIKDLLPDTNIIANRMAHQLGHNLGMQHDEFPCTCPSGKCV 358
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 114326453 359 MDSDGSIPALKFSKCSQNQYHQYLKDYKPTCMLN 392
Cdd:cd04269  161 MAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
488-624 9.89e-47

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 162.53  E-value: 9.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453   488 NGFPCKNSEGYCFMGKCPTREDQCSELFDDEAIESHDICY-KMNTKGNKFGYCKNKENRFLPCEEKDVRCGKIYCTGGEL 566
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 114326453   567 SSLLGEDKTYHLKDPQKnatVKCKTIFLYHDS-TDIGLVASGTKCGEGMVCNNGECLNM 624
Cdd:smart00608  82 LPLLGEHATVIYSNIGG---LVCWSLDYHLGTdPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 28-153 1.98e-37

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: 135.90  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453   28 QLVRPKKL-PLIQKRDTGHTHDddilktYEEELLYEIKLNRKTLVLHLLRSREFLGSNYSETFYSMKGEAFTRHPQIMDH 106
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSLASEST------YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 114326453  107 CFYQGSIVHEYDSAASISTCNGLRGFFRINDQRYLIEPVKYSDEGEH 153
Cdd:pfam01562  75 CYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEG 121
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 411-485 8.31e-36

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: 129.35  E-value: 8.31e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114326453   411 DEGEECDCGPAQECTNPCCDAHTCVLKPGFTCAEGECCESCQIKKAGSICRPAKDECDFPEMCTGHSPACPKDQF 485
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
411-483 9.83e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 9.83e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114326453  411 DEGEECDCGPAQECT-NPCCDAHTCVLKPGFTCAEGECCESCQIKKAGSICRPAKDECDFPEMCTGHSPACPKD 483
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 488-594 1.64e-32

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: 121.18  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  488 NGFPCKNSEGYCFMGKCPTREDQCSELFDDEAIESHDICY-KMNTKGNKFGYCKNKENRFLPCEEKDVRCGKIYCTGGEL 566
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYeEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*...
gi 114326453  567 SSLLGEDKTYHLKDPQKnatVKCKTIFL 594
Cdd:pfam08516  81 LPLLGEHATVIYTNING---VTCWGTDY 105
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 199-394 8.15e-97

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: 298.45  E-value: 8.15e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  199 KYVELFIVADDTVYRRNGHPHNKLRNRIWGMVNFVNMIYKTLNIHVTLVGIEIWTHEDKIELYSNIETTLLRFSFWQEKI 278
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  279 LKTRKDFDHVVLLSGKWLYSHVQGISYPGGMCLPYYSTSIIKDLLPDTNIIANRMAHQLGHNLGMQHDEF--PCTC-PSG 355
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 114326453  356 KCVM-DSDGSIPALKFSKCSQNQYHQYLKDYKPTCMLNIP 394
Cdd:pfam01421 161 GCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 199-392 5.76e-76

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: 243.29  E-value: 5.76e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 199 KYVELFIVADDTVYRRNGHPHNKLRNRIWGMVNFVNMIYKTLNIHVTLVGIEIWTHEDKIELYSNIETTLLRFSFWQEKI 278
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 279 LKTRKDFDHVVLLSGKWLYSHVQGISYPGGMCLPYYSTSIIKDLLPDTNIIANRMAHQLGHNLGMQHDEFPCTCPSGKCV 358
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 114326453 359 MDSDGSIPALKFSKCSQNQYHQYLKDYKPTCMLN 392
Cdd:cd04269  161 MAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
488-624 9.89e-47

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 162.53  E-value: 9.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453   488 NGFPCKNSEGYCFMGKCPTREDQCSELFDDEAIESHDICY-KMNTKGNKFGYCKNKENRFLPCEEKDVRCGKIYCTGGEL 566
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 114326453   567 SSLLGEDKTYHLKDPQKnatVKCKTIFLYHDS-TDIGLVASGTKCGEGMVCNNGECLNM 624
Cdd:smart00608  82 LPLLGEHATVIYSNIGG---LVCWSLDYHLGTdPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 28-153 1.98e-37

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: 135.90  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453   28 QLVRPKKL-PLIQKRDTGHTHDddilktYEEELLYEIKLNRKTLVLHLLRSREFLGSNYSETFYSMKGEAFTRHPQIMDH 106
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSLASEST------YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 114326453  107 CFYQGSIVHEYDSAASISTCNGLRGFFRINDQRYLIEPVKYSDEGEH 153
Cdd:pfam01562  75 CYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEG 121
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 411-485 8.31e-36

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: 129.35  E-value: 8.31e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 114326453   411 DEGEECDCGPAQECTNPCCDAHTCVLKPGFTCAEGECCESCQIKKAGSICRPAKDECDFPEMCTGHSPACPKDQF 485
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
411-483 9.83e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 9.83e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114326453  411 DEGEECDCGPAQECT-NPCCDAHTCVLKPGFTCAEGECCESCQIKKAGSICRPAKDECDFPEMCTGHSPACPKD 483
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 199-391 8.25e-33

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: 125.81  E-value: 8.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 199 KYVELFIVADDTVYRrnGHPHNKLRNRIWGMVNFVNMIYK--TL--NIHVTLVGIEIWTHEDK-IELYSNIETTLLRFSF 273
Cdd:cd04273    1 RYVETLVVADSKMVE--FHHGEDLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 274 WQEKILKTRKD----FDHVVLLSGKWLYSH-----VQGISYPGGMCLPYYSTSIIKDLLPDTNIIanrMAHQLGHNLGMQ 344
Cdd:cd04273   79 WQKKLNPPNDSdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTGLSSAFT---IAHELGHVLGMP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 114326453 345 HDEFPCTCPS---GKCVMDSDGSIPALKF--SKCSQNQYHQYLKDYKPTCML 391
Cdd:cd04273  156 HDGDGNSCGPegkDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 488-594 1.64e-32

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: 121.18  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  488 NGFPCKNSEGYCFMGKCPTREDQCSELFDDEAIESHDICY-KMNTKGNKFGYCKNKENRFLPCEEKDVRCGKIYCTGGEL 566
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYeEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*...
gi 114326453  567 SSLLGEDKTYHLKDPQKnatVKCKTIFL 594
Cdd:pfam08516  81 LPLLGEHATVIYTNING---VTCWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 199-383 1.46e-27

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: 110.20  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 199 KYVELFIVADDTVYRRNGHPHNKLRNRIWGMVNFVNMIYK----TLNIHVTLVGIEIWTHEDKI-ELYSNIETTLLRFSF 273
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 274 WQEKilkTRKDFDHVVLLSGKWLYSH-VQGISYPGGMCLPYYSTSIIKDLLPdTNIIANRMAHQLGHNLGMQHDEFPCTC 352
Cdd:cd04267   81 WRAE---GPIRHDNAVLLTAQDFIEGdILGLAYVGSMCNPYSSVGVVEDTGF-TLLTALTMAHELGHNLGAEHDGGDELA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 114326453 353 PS----GKCVMD-SDGSIPALKFSKCSQNQYHQYLK 383
Cdd:cd04267  157 FEcdggGNYIMApVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 200-389 1.16e-17

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 82.40  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 200 YVELFIVADDTVYRRNGHPHNKLRNRIwGMVNFVNMIYKTLN---IHVTLVGIEIWTHED-----KIELYSNIET--TLL 269
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNEQLIRYLA-VMVNAANLRYRDLKsprIRLLLVGITISKDPDfepyiHPINYGYIDAaeTLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 270 RFSfwqeKILKTRKDF---DHVVLLSGK----WLYSH----VQGISYPGGMClPYYSTSIIKDLlPDTNIIANRMAHQLG 338
Cdd:cd04272   81 NFN----EYVKKKRDYfnpDVVFLVTGLdmstYSGGSlqtgTGGYAYVGGAC-TENRVAMGEDT-PGSYYGVYTMTHELA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 114326453 339 HNLGMQHDEFPctcPSGKCVMD--------SDGSIPA--------LKFSKCSQNQYHQYLKDYKPTC 389
Cdd:cd04272  155 HLLGAPHDGSP---PPSWVKGHpgsldcpwDDGYIMSyvvngerqYRFSQCSQRQIRNVFRRLGASC 218
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
201-371 9.55e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 64.75  E-value: 9.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  201 VELFIVADDTVYRRngHPHNKLRNRIWGMVNFV-NMIYKTLNIHVTLVGIEIWTHED----KIELYSNIETTLLRFSFWQ 275
Cdd:pfam13688   5 VALLVAADCSYVAA--FGGDAAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQDFS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  276 EkiLKTRKDFDHVVLLSGKwlYSHVQGISYPGGMCLPYYSTSIikdllpDTNIIANRM-----------AHQLGHNLGMQ 344
Cdd:pfam13688  83 A--WRGTQNDDLAYLFLMT--NCSGGGLAWLGQLCNSGSAGSV------STRVSGNNVvvstatewqvfAHEIGHNFGAV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 114326453  345 HD-----EFPC------TCP-SGKCVMDSDGSIPALKFS 371
Cdd:pfam13688 153 HDcdsstSSQCcppsnsTCPaGGRYIMNPSSSPNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 230-346 2.06e-11

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 61.62  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  230 VNFVNMIYKT-LNIHVTLVGIEIWTHEDKIELYSNIETTLLRFS-FWQEKILKTRKDFDHVVLLSGkwlYSHVQGISYPG 307
Cdd:pfam13582   7 VNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQeVNDTRIGQYGYDLGHLFTGRD---GGGGGGIAYVG 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 114326453  308 GMCLPYYSTSIIKDLLPDTNIIANRMAHQLGHNLGMQHD 346
Cdd:pfam13582  84 GVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 199-378 6.04e-11

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 61.77  E-value: 6.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 199 KYVELFIVADDTVYRRNGHPHNklrnrIWGMVNFVNMIY-KTLNIHVTLVGIEIWTHedkielysniettllrfsfwQEK 277
Cdd:cd00203    1 KVIPYVVVADDRDVEEENLSAQ-----IQSLILIAMQIWrDYLNIRFVLVGVEIDKA--------------------DIA 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453 278 ILKTRKDFDHVVLlsgkwlyshvqGISYPGGMCLPYYSTSIIKDLLPDTNIIANRMAHQLGHNLGMQHDEFPCTCPSGKC 357
Cdd:cd00203   56 ILVTRQDFDGGTG-----------GWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPT 124

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 114326453 358 VMDSDGSIPA------------------LKFSKCSQNQY 378
Cdd:cd00203  125 IDDTLNAEDDdyysvmsytkgsfsdgqrKDFSQCDIDQI 163
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 199-374 4.20e-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: 45.30  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  199 KYVELFIVADDTVYRRNGHPhNKLRNRIWGMVNFVNMIY-KTLNIHVTLVGIE--IWTHEDKIELYSNIETT------LL 269
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSV-DELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSSTDSFNADCSGGdlgnwrLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114326453  270 RFSFWQEKilktrKDFDHVVLLSGKWLYSHVQGISYPGGMCLPYYST---SIIKDLLPDTNIIAnrmaHQLGHNLGMQHD 346
Cdd:pfam13583  82 TLTSWRDS-----LNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQNakaSGVARSRDEWDIFA----HEIGHTFGAVHD 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 114326453  347 -EFPC------TCP-SGKCVMDSDGSIPALKFSKCS 374
Cdd:pfam13583 153 cSSQGeglsssTEDgSGQTIMSYASTASQTAFSPCT 188
 
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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