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Conserved domains on  [gi|114842412|ref|NP_742123|]
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disintegrin and metalloproteinase domain-containing protein 1b precursor [Mus musculus]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 12023297)

protein containing domains Pep_M12B_propep, ZnMc_adamalysin_II_like, Disintegrin, and ACR

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 ...
 203-397 5.12e-92

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: 286.89  E-value: 5.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  203 KYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEK 282
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  283 LVGRVRHDVAHLIVGHRP-GENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDH--PTCTCGPKH 359
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFgGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 114842412  360 FCLMGEKIGKDSG--FSNCSSDHFLRFLHDHRGVCLLDEP 397
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
489-625 4.66e-39

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 141.34  E-value: 4.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412   489 QDGSKC-HESFLCFNGQCMDPTFQCSRIFGHGSRSASDYCYTSLNSRGDQFGNCGSSSQfpkKYTKCSDKNVMCGKLICT 567
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENG---TYIPCAPEDVKCGKLQCT 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 114842412   568 EVAFLPQIQPNNLLLQVPETEDWCWSVAVFDMRDSlHEEYVKDNTYCGKDKVCKNSIC 625
Cdd:smart00608  78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQC 134
Disintegrin pfam00200
Disintegrin;
415-485 3.17e-28

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 108.10  E-value: 3.17e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114842412  415 EDLEQCDCGS--DCDKSQCCD-ENCKLKGNSVCSTELCCFKCNFKKEGDVCRPADGPCDLEEYCNGTSAACPSD 485
Cdd:pfam00200   1 EEGEECDCGSleECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-159 7.69e-20

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: 86.21  E-value: 7.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412   44 ETVIPERLPGK-------GGKDPGGKVSYMLLMQGQKQLLHLEVKGHYPENNFPVYSY-HNGILRQEMPLLSQDCHYEGY 115
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 114842412  116 MEGVPGSFVSVNICSGLRGVLIKEETSYGIEPML----SSKNFEHVLY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 203-397 5.12e-92

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: 286.89  E-value: 5.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  203 KYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEK 282
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  283 LVGRVRHDVAHLIVGHRP-GENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDH--PTCTCGPKH 359
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFgGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 114842412  360 FCLMGEKIGKDSG--FSNCSSDHFLRFLHDHRGVCLLDEP 397
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 203-395 3.08e-72

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: 234.43  E-value: 3.08e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 203 KYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEK 282
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 283 LVGRVRHDVAHLIVGHRP-GENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDHPTCTCGPKhFC 361
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRS-TC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 114842412 362 LMGEKIGKDS-GFSNCSSDHFLRFLHDHRGVCLLD 395
Cdd:cd04269  160 IMAPSPSSLTdAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
489-625 4.66e-39

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 141.34  E-value: 4.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412   489 QDGSKC-HESFLCFNGQCMDPTFQCSRIFGHGSRSASDYCYTSLNSRGDQFGNCGSSSQfpkKYTKCSDKNVMCGKLICT 567
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENG---TYIPCAPEDVKCGKLQCT 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 114842412   568 EVAFLPQIQPNNLLLQVPETEDWCWSVAVFDMRDSlHEEYVKDNTYCGKDKVCKNSIC 625
Cdd:smart00608  78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQC 134
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 490-596 1.53e-34

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: 127.35  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  490 DGSKCHES-FLCFNGQCMDPTFQCSRIFGHGSRSASDYCYTSLNSRGDQFGNCGSSsqfPKKYTKCSDKNVMCGKLICTE 568
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT---NGGYVKCEKRDVLCGKLQCTN 77

                          90       100
                  ....*....|....*....|....*...
gi 114842412  569 VAFLPQIQPNNLLLQVPETEDWCWSVAV 596
Cdd:pfam08516  78 VKELPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
415-485 3.17e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 108.10  E-value: 3.17e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114842412  415 EDLEQCDCGS--DCDKSQCCD-ENCKLKGNSVCSTELCCFKCNFKKEGDVCRPADGPCDLEEYCNGTSAACPSD 485
Cdd:pfam00200   1 EEGEECDCGSleECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-485 5.26e-25

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: 98.92  E-value: 5.26e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114842412   415 EDLEQCDCGSDCD-KSQCCD-ENCKLKGNSVCSTELCCFKCNFKKEGDVCRPADGPCDLEEYCNGTSAACPSD 485
Cdd:smart00050   1 EEGEECDCGSPKEcTDPCCDpATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-159 7.69e-20

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: 86.21  E-value: 7.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412   44 ETVIPERLPGK-------GGKDPGGKVSYMLLMQGQKQLLHLEVKGHYPENNFPVYSY-HNGILRQEMPLLSQDCHYEGY 115
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 114842412  116 MEGVPGSFVSVNICSGLRGVLIKEETSYGIEPML----SSKNFEHVLY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 203-397 5.12e-92

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: 286.89  E-value: 5.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  203 KYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEK 282
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  283 LVGRVRHDVAHLIVGHRP-GENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDH--PTCTCGPKH 359
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFgGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 114842412  360 FCLMGEKIGKDSG--FSNCSSDHFLRFLHDHRGVCLLDEP 397
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 203-395 3.08e-72

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: 234.43  E-value: 3.08e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 203 KYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEK 282
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 283 LVGRVRHDVAHLIVGHRP-GENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDHPTCTCGPKhFC 361
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRS-TC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 114842412 362 LMGEKIGKDS-GFSNCSSDHFLRFLHDHRGVCLLD 395
Cdd:cd04269  160 IMAPSPSSLTdAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
489-625 4.66e-39

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 141.34  E-value: 4.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412   489 QDGSKC-HESFLCFNGQCMDPTFQCSRIFGHGSRSASDYCYTSLNSRGDQFGNCGSSSQfpkKYTKCSDKNVMCGKLICT 567
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENG---TYIPCAPEDVKCGKLQCT 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 114842412   568 EVAFLPQIQPNNLLLQVPETEDWCWSVAVFDMRDSlHEEYVKDNTYCGKDKVCKNSIC 625
Cdd:smart00608  78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQC 134
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 490-596 1.53e-34

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: 127.35  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  490 DGSKCHES-FLCFNGQCMDPTFQCSRIFGHGSRSASDYCYTSLNSRGDQFGNCGSSsqfPKKYTKCSDKNVMCGKLICTE 568
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT---NGGYVKCEKRDVLCGKLQCTN 77

                          90       100
                  ....*....|....*....|....*...
gi 114842412  569 VAFLPQIQPNNLLLQVPETEDWCWSVAV 596
Cdd:pfam08516  78 VKELPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
415-485 3.17e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 108.10  E-value: 3.17e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114842412  415 EDLEQCDCGS--DCDKSQCCD-ENCKLKGNSVCSTELCCFKCNFKKEGDVCRPADGPCDLEEYCNGTSAACPSD 485
Cdd:pfam00200   1 EEGEECDCGSleECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-485 5.26e-25

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: 98.92  E-value: 5.26e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 114842412   415 EDLEQCDCGSDCD-KSQCCD-ENCKLKGNSVCSTELCCFKCNFKKEGDVCRPADGPCDLEEYCNGTSAACPSD 485
Cdd:smart00050   1 EEGEECDCGSPKEcTDPCCDpATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 203-394 5.48e-21

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: 91.92  E-value: 5.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 203 KYVEMFVVVNHQRFQ-MWGSNINETVQAVMDIIA-LANSFTRGINTEVVLVGLEIWTEGDP-IEVPVDLQTTLRNFNFWr 279
Cdd:cd04273    1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVAsLYKDPSLGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCRW- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 280 QEKLVGR-----VRHDVAHLI------VGHRPGENEGQAFLRGACSGEFAAAVeafhHEDVLLFAAL-MAHELGHNLGIQ 347
Cdd:cd04273   80 QKKLNPPndsdpEHHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSI----NEDTGLSSAFtIAHELGHVLGMP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 114842412 348 HDHPTCTCGP--KHFCLMGEKIGKDSG---FSNCSSDHFLRFLHDHRGVCLL 394
Cdd:cd04273  156 HDGDGNSCGPegKDGHIMSPTLGANTGpftWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-159 7.69e-20

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: 86.21  E-value: 7.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412   44 ETVIPERLPGK-------GGKDPGGKVSYMLLMQGQKQLLHLEVKGHYPENNFPVYSY-HNGILRQEMPLLSQDCHYEGY 115
Cdd:pfam01562   1 EVVIPVRLDPSrrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 114842412  116 MEGVPGSFVSVNICSGLRGVLIKEETSYGIEPML----SSKNFEHVLY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 203-385 6.73e-17

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: 79.77  E-value: 6.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 203 KYVEMFVVVNHQRFQMWGSNINET---VQAVMDIIALANSFTRG-INTEVVLVGLEIWTEGDPIEVP-VDLQTTLRNFNF 277
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILqayITELINIANSIYRSTNLrLGIRISLEGLQILKGEQFAPPIdSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 278 WRQEklvGRVRHDVAHLIVGHRPGENE--GQAFLRGACSGEFAAAVeAFHHEDVLLFAALMAHELGHNLGIQHDHPTCTC 355
Cdd:cd04267   81 WRAE---GPIRHDNAVLLTAQDFIEGDilGLAYVGSMCNPYSSVGV-VEDTGFTLLTALTMAHELGHNLGAEHDGGDELA 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 114842412 356 --GPKHF-CLMGEKIGKDSG--FSNCSSDHFLRFL 385
Cdd:cd04267  157 feCDGGGnYIMAPVDSGLNSyrFSQCSIGSIREFL 191
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
202-363 3.88e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 62.82  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  202 TKYVEMFVVVNHQRFQMWGSN-INETVQAVMDiiALANSFTRGINTEVVLVGLEIWTEGDPIEVP----VDLQTTLRNFN 276
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGDaAQANIINMVN--TASNVYERDFNISLGLVNLTISDSTCPYTPPacstGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  277 FwrQEKLVGRVRHDVAHLIVgHRPGENEGQAFLRGACSGEFAAAVEAF---------HHEDVLLFAalmaHELGHNLGIQ 347
Cdd:pfam13688  80 D--FSAWRGTQNDDLAYLFL-MTNCSGGGLAWLGQLCNSGSAGSVSTRvsgnnvvvsTATEWQVFA----HEIGHNFGAV 152

                         170       180
                  ....*....|....*....|....*..
gi 114842412  348 HDH------PTC-----TCGPKHFCLM 363
Cdd:pfam13688 153 HDCdsstssQCCppsnsTCPAGGRYIM 179
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 233-349 2.85e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 55.45  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  233 IIALANS-FTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFnfwrQEKLVGRVRH---DVAHLIVGHRPGENEGQAF 308
Cdd:pfam13582   6 LVNRANTiYERDLGIRLQLAAIIITTSADTPYTSSDALEILDEL----QEVNDTRIGQygyDLGHLFTGRDGGGGGGIAY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 114842412  309 LRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHD 349
Cdd:pfam13582  82 VGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 204-393 1.60e-06

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 49.66  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 204 YVEMFVVVNhQRFQmwgSNINETVQAVMDIIALANSF------TRGINTEVVLVGLEIWTEGDPIEVPVDLQT------- 270
Cdd:cd04272    2 YPELFVVVD-YDHQ---SEFFSNEQLIRYLAVMVNAAnlryrdLKSPRIRLLLVGITISKDPDFEPYIHPINYgyidaae 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 271 TLRNFN-FWRQEKLvgRVRHDVAHLIV---------GHRPGENEGQAFLRGACSGEFAAAVE--AFHHEDVLLfaalMAH 338
Cdd:cd04272   78 TLENFNeYVKKKRD--YFNPDVVFLVTgldmstysgGSLQTGTGGYAYVGGACTENRVAMGEdtPGSYYGVYT----MTH 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114842412 339 ELGHNLGIQHD----------HPTCT-CGPKHFCLMGEKIGKDSG--FSNCSSDHFLRFLHDHRGVCL 393
Cdd:cd04272  152 ELAHLLGAPHDgspppswvkgHPGSLdCPWDDGYIMSYVVNGERQyrFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 203-375 1.23e-04

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: 43.28  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 203 KYVEMFVVVNHQRFQmwGSNINETVQAVMDIIAlaNSFTRGINTEVVLVGLEIwtegdpievpvdlqttlrnfnfwrqek 282
Cdd:cd00203    1 KVIPYVVVADDRDVE--EENLSAQIQSLILIAM--QIWRDYLNIRFVLVGVEI--------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412 283 lvgrVRHDVAHL-IVGHRPGENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDHPTCtCGPKHFC 361
Cdd:cd00203   50 ----DKADIAILvTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRK-DRDDYPT 124

                        170
                 ....*....|....
gi 114842412 362 LMGEKIGKDSGFSN 375
Cdd:cd00203  125 IDDTLNAEDDDYYS 138
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 191-381 5.07e-04

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: 42.22  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  191 DLLVLTDWwshtKYVEMFVVVNHQRfqmwgSNINETVqavmdiiALANS-FTRGINTEVVLVGLE--IWTEGDPIEVPVD 267
Cdd:pfam13583   6 RVAVATDC----TYSASFGSVDELR-----ANINATV-------TTANEvYGRDFNVSLALISDRdvIYTDSSTDSFNAD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114842412  268 LQTT------LRNFNFWRQEKlvgrvRHDVAHLIVGHRP-GENEGQAFLRGACS--------GEFAAAVEAFhhedvllf 332
Cdd:pfam13583  70 CSGGdlgnwrLATLTSWRDSL-----NYDLAYLTLMTGPsGQNVGVAWVGALCSsarqnakaSGVARSRDEW-------- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 114842412  333 aALMAHELGHNLGIQHDHPTCTCG------PKHFCLMGEKIGKDSG--FSNCSSDHF 381
Cdd:pfam13583 137 -DIFAHEIGHTFGAVHDCSSQGEGlsssteDGSGQTIMSYASTASQtaFSPCTIRNI 192
 
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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