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Conserved domains on  [gi|530404800|ref|XP_005268208|]
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disintegrin and metalloproteinase domain-containing protein 20 isoform X1 [Homo sapiens]

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 ...
 257-446 7.26e-73

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: 235.59  E-value: 7.26e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 257 RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYN 336
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 337 LNNRLQHDVAHLFIKDT-QGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCI 415
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDfDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530404800 416 MHAYR-KVTTKFSNCSYAQYWDSTISS-GLCIQ 446
Cdd:cd04269  161 MAPSPsSLTDAFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
542-678 8.21e-57

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 190.26  E-value: 8.21e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800   542 QDGISC-NVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVG 620
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530404800   621 VIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAiPDIGEVKDGTVCGPEKICIRKKCASM 678
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
466-538 3.47e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 130.44  E-value: 3.47e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530404800  466 EEGEECDCGTIRQCAKDPCCL-LNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDD 538
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 91-209 3.55e-29

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: 112.79  E-value: 3.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800   91 EVVIPLKVISRGR------GAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGY 164
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 530404800  165 VEGVPESLVALSTCSgGFLGMLQINDLVYEIKPISV----SATFEHLVY 209
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 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 ...
 257-446 7.26e-73

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: 235.59  E-value: 7.26e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 257 RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYN 336
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 337 LNNRLQHDVAHLFIKDT-QGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCI 415
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDfDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530404800 416 MHAYR-KVTTKFSNCSYAQYWDSTISS-GLCIQ 446
Cdd:cd04269  161 MAPSPsSLTDAFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
542-678 8.21e-57

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 190.26  E-value: 8.21e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800   542 QDGISC-NVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVG 620
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530404800   621 VIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAiPDIGEVKDGTVCGPEKICIRKKCASM 678
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 257-449 4.86e-46

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: 163.24  E-value: 4.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  257 RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYN 336
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  337 LNNRLQHDVAHLFI-KDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDT--QWCVC-ELQ 412
Cdd:pfam01421  81 LKKRKPHDVAQLLSgVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 530404800  413 WCIMHAY--RKVTTKFSNCSYAQYWDSTIS-SGLCIQPPP 449
Cdd:pfam01421 161 GCIMNPSagSSFPRKFSNCSQEDFEQFLTKqKGACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 543-646 2.44e-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: 157.39  E-value: 2.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  543 DGISCNVN-AFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVGV 621
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 530404800  622 IPNLIEHSTVQQFHLNDTTCWGTDY 646
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
466-538 3.47e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 130.44  E-value: 3.47e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530404800  466 EEGEECDCGTIRQCAKDPCCL-LNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDD 538
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 466-540 5.86e-35

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 127.04  E-value: 5.86e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530404800   466 EEGEECDCGTIRQCaKDPCC-LLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVY 540
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 91-209 3.55e-29

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: 112.79  E-value: 3.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800   91 EVVIPLKVISRGR------GAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGY 164
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 530404800  165 VEGVPESLVALSTCSgGFLGMLQINDLVYEIKPISV----SATFEHLVY 209
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 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 ...
 257-446 7.26e-73

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: 235.59  E-value: 7.26e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 257 RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYN 336
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 337 LNNRLQHDVAHLFIKDT-QGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCI 415
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDfDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 530404800 416 MHAYR-KVTTKFSNCSYAQYWDSTISS-GLCIQ 446
Cdd:cd04269  161 MAPSPsSLTDAFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
542-678 8.21e-57

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 190.26  E-value: 8.21e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800   542 QDGISC-NVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVG 620
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530404800   621 VIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAiPDIGEVKDGTVCGPEKICIRKKCASM 678
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 257-449 4.86e-46

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: 163.24  E-value: 4.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  257 RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYN 336
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  337 LNNRLQHDVAHLFI-KDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDT--QWCVC-ELQ 412
Cdd:pfam01421  81 LKKRKPHDVAQLLSgVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 530404800  413 WCIMHAY--RKVTTKFSNCSYAQYWDSTIS-SGLCIQPPP 449
Cdd:pfam01421 161 GCIMNPSagSSFPRKFSNCSQEDFEQFLTKqKGACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 543-646 2.44e-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: 157.39  E-value: 2.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  543 DGISCNVN-AFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVGV 621
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 530404800  622 IPNLIEHSTVQQFHLNDTTCWGTDY 646
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
466-538 3.47e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 130.44  E-value: 3.47e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530404800  466 EEGEECDCGTIRQCAKDPCCL-LNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDD 538
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 466-540 5.86e-35

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 127.04  E-value: 5.86e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530404800   466 EEGEECDCGTIRQCaKDPCC-LLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVY 540
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 91-209 3.55e-29

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: 112.79  E-value: 3.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800   91 EVVIPLKVISRGR------GAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGY 164
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 530404800  165 VEGVPESLVALSTCSgGFLGMLQINDLVYEIKPISV----SATFEHLVY 209
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 257-436 8.32e-23

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: 96.72  E-value: 8.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 257 RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLE----VDVILTGIDIWTASNP-LPTSGDLDNVLEDFSI 331
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILKGEQFaPPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 332 WKNYNLNNrlqHDVAHLFIK-DTQGMK-LGVAYVKGICQNPFNTGvdVFED---NRLVvfAITLGHELGHNLGMQHDTQW 406
Cdd:cd04267   81 WRAEGPIR---HDNAVLLTAqDFIEGDiLGLAYVGSMCNPYSSVG--VVEDtgfTLLT--ALTMAHELGHNLGAEHDGGD 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530404800 407 CVCELQ----WCIMH--AYRKVTTKFSNCSYAQYWD 436
Cdd:cd04267  154 ELAFECdgggNYIMApvDSGLNSYRFSQCSIGSIRE 189
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 257-430 7.46e-16

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: 76.89  E-value: 7.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 257 RFVELVVVVDN--IRYlFSQSNattVQHEVFNVVNIVDS-FYHPL---EVDVILTGIDIWTASNPLPT-SGDLDNVLEDF 329
Cdd:cd04273    1 RYVETLVVADSkmVEF-HHGED---LEHYILTLMNIVASlYKDPSlgnSINIVVVRLIVLEDEESGLLiSGNAQKSLKSF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 330 SIWKN----YNLNNRLQHDVAHLF------IKDTQGMKLGVAYVKGICqNPFNTGVdVFEDNRLVVfAITLGHELGHNLG 399
Cdd:cd04273   77 CRWQKklnpPNDSDPEHHDHAILLtrqdicRSNGNCDTLGLAPVGGMC-SPSRSCS-INEDTGLSS-AFTIAHELGHVLG 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530404800 400 MQHDTQWCVCELQW---CIMHAYR-KVTTKF--SNCS 430
Cdd:cd04273  154 MPHDGDGNSCGPEGkdgHIMSPTLgANTGPFtwSKCS 190
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
256-405 4.06e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 59.74  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  256 QRFVELVVVVDNIRYLFSQSNAttVQHEVFNVVNIVDS-FYHPLEVDVILTGIDIWTASNPLPTS----GDLDNVLEDFS 330
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGDA--AQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPacstGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  331 IWKNynLNNRLQHDVAHLFI-KDTQGMklGVAYVKGIC---------QNPFNTGVDVFEDNRLVVFAitlgHELGHNLGM 400
Cdd:pfam13688  80 DFSA--WRGTQNDDLAYLFLmTNCSGG--GLAWLGQLCnsgsagsvsTRVSGNNVVVSTATEWQVFA----HEIGHNFGA 151


                  ....*
gi 530404800  401 QHDTQ 405
Cdd:pfam13688 152 VHDCD 156
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 279-403 1.58e-09

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 58.02  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  279 TVQHEVFNVVNIVDSFYHP--LEVDVILTGIDiwtASNPLPTSGDLDNVLEDFSIWKNYNLN------NRLQHDVAHL-F 349
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPddININGGLVNPG---EIPATTSASDSGNNYCNSPTTIVRRLNflsqwrGEQDYCLAHLvT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530404800  350 IKDTQGMKLGVAYVKGICQN-------------PFNTGVDVFEDNRLVVFAitlgHELGHNLGMQHD 403
Cdd:pfam13574  79 MGTFSGGELGLAYVGQICQKgasspktntglstTTNYGSFNYPTQEWDVVA----HEVGHNFGATHD 141
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 286-403 1.25e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 53.91  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800  286 NVVNIVDSFY-HPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWkNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVK 364
Cdd:pfam13582   5 SLVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEV-NDTRIGQYGYDLGHLFTGRDGGGGGGIAYVG 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530404800  365 GICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHD 403
Cdd:pfam13582  84 GVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 325-442 1.12e-07

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: 52.14  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 325 VLEDFSIWKNYNLNNRL----QHDVAHLFIKDTQGMK-LGVAYVKGICQNpfNTGVDVFEDNRLV--VFAITLGHELGHN 397
Cdd:cd00203   30 AMQIWRDYLNIRFVLVGveidKADIAILVTRQDFDGGtGGWAYLGRVCDS--LRGVGVLQDNQSGtkEGAQTIAHELGHA 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530404800 398 LGMQHDTQWCVCELQWCIMHAYRKVTTKFSncSYAQYWDSTISSG 442
Cdd:cd00203  108 LGFYHDHDRKDRDDYPTIDDTLNAEDDDYY--SVMSYTKGSFSDG 150
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 261-430 1.98e-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: 46.60  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 261 LVVVVDnirYLFSQSNATTVQHEVFN-VVNIVDSfyhpleVDVILTGID---------------IWTASNPLPTSGDLDN 324
Cdd:cd04270    5 LLLVAD---HRFYKYMGRGEEETTINyLISHIDR------VDDIYRNTDwdgggfkgigfqikrIRIHTTPDEVDPGNKF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 325 VLEDFSIWKNYNLNNRL---QHD----VAHLFI-KDTQGMKLGVAYVK--------GICQNPF----------NTG-VDV 377
Cdd:cd04270   76 YNKSFPNWGVEKFLVKLlleQFSddvcLAHLFTyRDFDMGTLGLAYVGsprdnsagGICEKAYyysngkkkylNTGlTTT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530404800 378 FEDNRLV---VFAITLGHELGHNLGMQHDTQWCVC---ELQW--CIMHAY-----RKVTTKFSNCS 430
Cdd:cd04270  156 VNYGKRVptkESDLVTAHELGHNFGSPHDPDIAECapgESQGgnYIMYARatsgdKENNKKFSPCS 221
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 258-433 5.49e-05

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 45.04  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 258 FVELVVVVDNIRY-LFSQSNATTVQHEVFnvVNIVDSFYHPLE---VDVILTGIDIWTASNPLPTSGDLDN-------VL 326
Cdd:cd04272    2 YPELFVVVDYDHQsEFFSNEQLIRYLAVM--VNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPINYgyidaaeTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 327 EDFSIWKnYNLNNRLQHDVAHL-----FIKDTQGMK----LGVAYVKGICQNpfnTGVDVFEDNRLVVF-AITLGHELGH 396
Cdd:cd04272   80 ENFNEYV-KKKRDYFNPDVVFLvtgldMSTYSGGSLqtgtGGYAYVGGACTE---NRVAMGEDTPGSYYgVYTMTHELAH 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530404800 397 NLGMQHDTQ----WCVCEL--QWC------IMHAYRKVTT--KFSNCSYAQ 433
Cdd:cd04272  156 LLGAPHDGSpppsWVKGHPgsLDCpwddgyIMSYVVNGERqyRFSQCSQRQ 206
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 321-403 7.36e-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: 42.02  E-value: 7.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530404800 321 DLDNVLEDFSIWKnYNLNNrlqHDVA--HLFIKDTQGMKLGVAYVKGICQNPFN---------TGVDVFEDNRLVVFAit 389
Cdd:cd04271   77 DIDDRLSIFSQWR-GQQPD---DGNAfwTLMTACPSGSEVGVAWLGQLCRTGASdqgnetvagTNVVVRTSNEWQVFA-- 150

                         90
                 ....*....|....
gi 530404800 390 lgHELGHNLGMQHD 403
Cdd:cd04271  151 --HEIGHTFGAVHD 162
 
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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