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Conserved domains on  [gi|2172664032|ref|NP_001386057|]
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disintegrin and metalloproteinase domain-containing protein 15 isoform 1 precursor [Rattus norvegicus]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 10259595)

protein containing domains Pep_M12B_propep, ZnMc_adamalysin_II_like, DISIN, and ACR

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 ...
 215-413 9.45e-79

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: 252.92  E-value: 9.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 215 KIVELVIVADNSEVRKY-PDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTD 293
Cdd:cd04269     1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 294 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGnsCPCPGpa 373
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2172664032 374 paKSCIMEASTDFLPgLNFSNCSRWALEKALLDGMGSCLF 413
Cdd:cd04269   157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
510-651 4.66e-44

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 155.60  E-value: 4.66e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032  510 DGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRsPSGSYMPCNLRDAICGQLQCQWGR 589
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR-ENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2172664032  590 NQPLLGSVQDqlseVLEANGTQLNCSWVDLDLGNDVaQPLLALPGTACGPGLVCIGHRCQPV 651
Cdd:smart00608  81 ELPLLGEHAT----VIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 432-505 1.64e-33

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


:

Pssm-ID: 214490  Cd Length: 75  Bit Score: 123.18  E-value: 1.64e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172664032  432 DPGEQCDCGFPDECTDPCCDYFTCQLRPGAQCASdGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPD 505
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 67-147 9.69e-14

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.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 68.88  E-value: 9.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032  67 PETLRIGLELDGENHILELQQNRDLVPGRPTLVWYQPDGTRMVSEGHSLENCCYRGRVQGRPSSWVSLCACSGIRGLVVL 146
Cdd:pfam01562  24 LDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRT 103


                  .
gi 2172664032 147 S 147
Cdd:pfam01562 104 E 104
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 215-413 9.45e-79

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: 252.92  E-value: 9.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 215 KIVELVIVADNSEVRKY-PDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTD 293
Cdd:cd04269     1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 294 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGnsCPCPGpa 373
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2172664032 374 paKSCIMEASTDFLPgLNFSNCSRWALEKALLDGMGSCLF 413
Cdd:cd04269   157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 215-416 7.83e-69

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: 226.41  E-value: 7.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 215 KIVELVIVADNSEVRKY-PDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTD 293
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 294 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGNSCPCPgpa 373
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2172664032 374 PAKSCIMEASTDFLPGLNFSNCSRWALEKALLDGMGSCLFEWP 416
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
510-651 4.66e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 155.60  E-value: 4.66e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032  510 DGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRsPSGSYMPCNLRDAICGQLQCQWGR 589
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR-ENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2172664032  590 NQPLLGSVQDqlseVLEANGTQLNCSWVDLDLGNDVaQPLLALPGTACGPGLVCIGHRCQPV 651
Cdd:smart00608  81 ELPLLGEHAT----VIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 432-505 1.64e-33

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 123.18  E-value: 1.64e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172664032  432 DPGEQCDCGFPDECTDPCCDYFTCQLRPGAQCASdGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPD 505
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 510-619 3.62e-33

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: 123.49  E-value: 3.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 510 DGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPsGSYMPCNLRDAICGQLQCQWGR 589
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2172664032 590 NQPLLGSvqdqLSEVLEANGTQLNCSWVDL 619
Cdd:pfam08516  80 ELPLLGE----HATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
432-505 1.01e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 120.81  E-value: 1.01e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2172664032 432 DPGEQCDCGFPDECT-DPCCDYFTCQLRPGAQCASdGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPD 505
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 67-147 9.69e-14

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: 68.88  E-value: 9.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032  67 PETLRIGLELDGENHILELQQNRDLVPGRPTLVWYQPDGTRMVSEGHSLENCCYRGRVQGRPSSWVSLCACSGIRGLVVL 146
Cdd:pfam01562  24 LDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRT 103


                  .
gi 2172664032 147 S 147
Cdd:pfam01562 104 E 104
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
348-394 9.76e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 9.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2172664032 348 IAHELGHSLGLDHdspgnsCPCPGpapaksCIMeastdflpglNFSN 394
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPR------CVM----------HFSN 151
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 215-413 9.45e-79

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: 252.92  E-value: 9.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 215 KIVELVIVADNSEVRKY-PDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTD 293
Cdd:cd04269     1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 294 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGnsCPCPGpa 373
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2172664032 374 paKSCIMEASTDFLPgLNFSNCSRWALEKALLDGMGSCLF 413
Cdd:cd04269   157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 215-416 7.83e-69

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: 226.41  E-value: 7.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 215 KIVELVIVADNSEVRKY-PDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTD 293
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 294 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGNSCPCPgpa 373
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2172664032 374 PAKSCIMEASTDFLPGLNFSNCSRWALEKALLDGMGSCLFEWP 416
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
510-651 4.66e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 155.60  E-value: 4.66e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032  510 DGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRsPSGSYMPCNLRDAICGQLQCQWGR 589
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR-ENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2172664032  590 NQPLLGSVQDqlseVLEANGTQLNCSWVDLDLGNDVaQPLLALPGTACGPGLVCIGHRCQPV 651
Cdd:smart00608  81 ELPLLGEHAT----VIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 432-505 1.64e-33

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


Pssm-ID: 214490  Cd Length: 75  Bit Score: 123.18  E-value: 1.64e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2172664032  432 DPGEQCDCGFPDECTDPCCDYFTCQLRPGAQCASdGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPD 505
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 510-619 3.62e-33

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: 123.49  E-value: 3.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 510 DGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPsGSYMPCNLRDAICGQLQCQWGR 589
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 2172664032 590 NQPLLGSvqdqLSEVLEANGTQLNCSWVDL 619
Cdd:pfam08516  80 ELPLLGE----HATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
432-505 1.01e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 120.81  E-value: 1.01e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2172664032 432 DPGEQCDCGFPDECT-DPCCDYFTCQLRPGAQCASdGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPD 505
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 217-397 3.84e-26

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: 106.35  E-value: 3.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 217 VELVIVADNSEVRKYP-DFQQLLNRTLEVALLLDTFFQ----PLNVRVALVGLEAWTQRDLI-EMSSNPAVLLDNFLRWR 290
Cdd:cd04267     3 IELVVVADHRMVSYFNsDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSFWR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 291 RTDLlPRlpHDSAQLVTVTSF-SGPMVGMAIQNSICSPDFSGGVNMDHSTSILgVASSIAHELGHSLGLDHDsPGNSCPC 369
Cdd:cd04267    83 AEGP-IR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHD-GGDELAF 157

                         170       180
                  ....*....|....*....|....*...
gi 2172664032 370 PGPApAKSCIMEASTDFLPGLNFSNCSR 397
Cdd:cd04267   158 ECDG-GGNYIMAPVDSGLNSYRFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 215-413 7.14e-24

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: 100.39  E-value: 7.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 215 KIVELVIVADNSEVRKY--PDFQQ----LLNrtlEVALLldtFFQPL---NVRVALVGLEAWTQR-DLIEMSSNPAVLLD 284
Cdd:cd04273     1 RYVETLVVADSKMVEFHhgEDLEHyiltLMN---IVASL---YKDPSlgnSINIVVVRLIVLEDEeSGLLISGNAQKSLK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 285 NFLRWRRTdLLPRLP-----HDSAQLVTVTSFSGP-----MVGMAIQNSICSPDFSGGVNMDHStsiLGVASSIAHELGH 354
Cdd:cd04273    75 SFCRWQKK-LNPPNDsdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELGH 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 355 SLGLDHDSPGNSCpcpGPAPAKSCIMEASTDFLPG-LNFSNCSRWALEKALLDGMGSCLF 413
Cdd:cd04273   151 VLGMPHDGDGNSC---GPEGKDGHIMSPTLGANTGpFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 67-147 9.69e-14

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: 68.88  E-value: 9.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032  67 PETLRIGLELDGENHILELQQNRDLVPGRPTLVWYQPDGTRMVSEGHSLENCCYRGRVQGRPSSWVSLCACSGIRGLVVL 146
Cdd:pfam01562  24 LDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRT 103


                  .
gi 2172664032 147 S 147
Cdd:pfam01562 104 E 104
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 255-361 2.06e-12

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: 64.70  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 255 LNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTdllpRLPHDSAQLVTV--TSFSGPMVGMAIQNSICSPDFSGG 332
Cdd:pfam13582  18 LGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYDLGHLftGRDGGGGGGIAYVGGVCNSGSKFG 93

                          90       100
                  ....*....|....*....|....*....
gi 2172664032 333 VNMDHSTSILGVASSIAHELGHSLGLDHD 361
Cdd:pfam13582  94 VNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
214-380 4.45e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 65.90  E-value: 4.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 214 TKIVELVIVADNSEVRKYP-DF-----QQLLNRTLEVallldtFFQPLNVRVALVGLEAWTQRDLI----EMSSNPAVLL 283
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGgDAaqaniINMVNTASNV------YERDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 284 DNFLR---WRRTDllprlPHDSAQLVTVTSFSGPmvGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHS 355
Cdd:pfam13688  76 SEFQDfsaWRGTQ-----NDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHN 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2172664032 356 LGLDHD---SPGNSCpCPGPAPAK----SCIM 380
Cdd:pfam13688 149 FGAVHDcdsSTSSQC-CPPSNSTCpaggRYIM 179
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 299-404 8.84e-09

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: 55.61  E-value: 8.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 299 PHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGN--------SCPCP 370
Cdd:cd00203    51 KADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKdrddyptiDDTLN 130

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2172664032 371 GPAPAKSCIMEASTDFLPGLN---FSNCSRWALEKAL 404
Cdd:cd00203   131 AEDDDYYSVMSYTKGSFSDGQrkdFSQCDIDQINKLY 167
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 301-397 1.34e-07

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 52.63  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 301 DSAQLVTVTSFSGPMVGMAIQNSIC-------------SPDFSGGVNMDHSTSILgvasSIAHELGHSLGLDHDSPGNSC 367
Cdd:pfam13574  72 CLAHLVTMGTFSGGELGLAYVGQICqkgasspktntglSTTTNYGSFNYPTQEWD----VVAHEVGHNFGATHDCDGSQY 147

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2172664032 368 PCPG-PAPAKSCIMEASTDFL-----PGLN--FSNCSR 397
Cdd:pfam13574 148 ASSGcERNAATSVCSANGSFImnpasKSNNdlFSPCSI 185
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 303-414 1.48e-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: 47.37  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 303 AQLVTVTSFSGPMVGMAIQNS--------ICSPD--FSGGVN----------MDHSTSILGVASSI--AHELGHSLGLDH 360
Cdd:cd04270   104 AHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAyyYSNGKKkylntgltttVNYGKRVPTKESDLvtAHELGHNFGSPH 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2172664032 361 DSPGNSCpCPGPAPAKSCIMEA---STDFLPGLNFSNCSRWALEKALLDGMGSCLFE 414
Cdd:cd04270   184 DPDIAEC-APGESQGGNYIMYAratSGDKENNKKFSPCSKKSISKVLEVKSNSCFVE 239
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 283-384 6.45e-05

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 45.10  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 283 LDNFLRWRRtdllpRLPHDSAQLVTV-TSF-SGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHS 355
Cdd:cd04271    82 LSIFSQWRG-----QQPDDGNAFWTLmTACpSGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHT 156

                          90       100
                  ....*....|....*....|....*....
gi 2172664032 356 LGLDHDSPGNSCPCPGPAPAKSCIMEAST 384
Cdd:cd04271   157 FGAVHDCTSGTCSDGSVGSQQCCPLSTST 185
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 217-397 1.69e-04

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 43.88  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 217 VELVIVADNsevrkypDFQQLLNRTLEVALLLDTFFQPLN----------VRVALVGleawtqrdlIEMSSNPAVLLDNF 286
Cdd:cd04272     3 PELFVVVDY-------DHQSEFFSNEQLIRYLAVMVNAANlryrdlksprIRLLLVG---------ITISKDPDFEPYIH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 287 LRWRRTDL----LPRL-----------PHDSAQLVT----VTSFSGPM----VGMAIQNSICSpDFSGGVNMDHSTSILG 343
Cdd:cd04272    67 PINYGYIDaaetLENFneyvkkkrdyfNPDVVFLVTgldmSTYSGGSLqtgtGGYAYVGGACT-ENRVAMGEDTPGSYYG 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2172664032 344 VaSSIAHELGHSLGLDHD-SPGNSCPCPGPApAKSC------IMeaSTDF--LPGLNFSNCSR 397
Cdd:cd04272   146 V-YTMTHELAHLLGAPHDgSPPPSWVKGHPG-SLDCpwddgyIM--SYVVngERQYRFSQCSQ 204
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 215-396 2.60e-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: 42.99  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 215 KIVELVIVADNSEVRKYPDFQQLLNRTLE-VALLLDTFFQPLNVRVALVGleawtQRDLIEMSSNPAVL----------- 282
Cdd:pfam13583   3 RVYRVAVATDCTYSASFGSVDELRANINAtVTTANEVYGRDFNVSLALIS-----DRDVIYTDSSTDSFnadcsggdlgn 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 283 --LDNFLRWRRTdllprLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSggvNMDHStsilGVASS------IAHELGH 354
Cdd:pfam13583  78 wrLATLTSWRDS-----LNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQ---NAKAS----GVARSrdewdiFAHEIGH 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2172664032 355 SLGLDHDSPGNSCP-----CPGPApakSCIME-ASTDFLPglNFSNCS 396
Cdd:pfam13583 146 TFGAVHDCSSQGEGlssstEDGSG---QTIMSyASTASQT--AFSPCT 188
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 332-362 4.29e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 38.75  E-value: 4.29e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2172664032 332 GVNMDHSTSILGVAssiAHELGHSLGLDHDS 362
Cdd:pfam00413  99 GSDPPHGINLFLVA---AHEIGHALGLGHSS 126
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 281-394 4.59e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 38.82  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172664032 281 VLLDNFLRWrrtdLLPRLPHDSAQLVTVTSFSGPM------VGMAIQNS---ICS-----PDFSGGVNmDHSTSILGVAS 346
Cdd:cd11375    51 YLADDILDA----LLKLKPPDADCVLGVTDVDLYEpglnfvFGLADGGSgvaVVStarlrPEFYGLPP-DEGLFLERLLK 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2172664032 347 SIAHELGHSLGLDHdspgnscpCPGPApaksCIMeastdflpglNFSN 394
Cdd:cd11375   126 EAVHELGHLFGLDH--------CPYYA----CVM----------NFSN 151
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
348-394 9.76e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 9.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2172664032 348 IAHELGHSLGLDHdspgnsCPCPGpapaksCIMeastdflpglNFSN 394
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPR------CVM----------HFSN 151
 
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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