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Conserved domains on  [gi|152148996|pdb|2DW0|A]
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Chain A, Catrocollastatin

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 10136411)

protein containing domains 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 ...
 8-201 2.86e-93

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: 278.73  E-value: 2.86e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        8 RFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTD 87
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       88 LLTRKKHDNAQLLTAIDLD-RVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSCGDYACI 166
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
2DW0_A      167 MRPEISPePSTFFSNCSYFECWDFIMNHNPECILN 201
Cdd:cd04269 161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
297-415 2.79e-47

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 158.68  E-value: 2.79e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         297 NGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFER-NQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDN-- 373
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVse 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
2DW0_A         374 ------------SPGQNNPCKM--FYSNEDEHKGMVLPGTKCADGKVCSNGHCVDV 415
Cdd:smart00608  82 lpllgehatviySNIGGLVCWSldYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 220-294 6.73e-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: 123.95  E-value: 6.73e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2DW0_A         220 EVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVF 294
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 8-201 2.86e-93

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: 278.73  E-value: 2.86e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        8 RFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTD 87
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       88 LLTRKKHDNAQLLTAIDLD-RVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSCGDYACI 166
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
2DW0_A      167 MRPEISPePSTFFSNCSYFECWDFIMNHNPECILN 201
Cdd:cd04269 161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 8-203 9.54e-64

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: 203.30  E-value: 9.54e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A          8 RFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTD 87
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         88 LLTRKKHDNAQLLTAIDL-DRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHD--SGYCSCGDYA 164
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFgGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
2DW0_A        165 -CIMRPEISPEPSTFFSNCSYFECWDFIMNHNPECILNEP 203
Cdd:pfam01421 161 gCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
297-415 2.79e-47

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 158.68  E-value: 2.79e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         297 NGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFER-NQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDN-- 373
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVse 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
2DW0_A         374 ------------SPGQNNPCKM--FYSNEDEHKGMVLPGTKCADGKVCSNGHCVDV 415
Cdd:smart00608  82 lpllgehatviySNIGGLVCWSldYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 220-294 6.73e-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: 123.95  E-value: 6.73e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2DW0_A         220 EVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVF 294
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
220-292 1.19e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 115.03  E-value: 1.19e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DW0_A        220 EVGEECDCGTPENCQ-NECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPAD 292
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 297-370 1.01e-20

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: 86.52  E-value: 1.01e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2DW0_A        297 NGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFER-NQKGNYYGYCRKENGNKIPCAPEDVKCGRLYC 370
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQC 75
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
87-169 9.73e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 9.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       87 DLLTRKKHDNAQL---LTAIDL-----DRVIGLAYvgsmchPKRSTGII-------QDYSE---INLV---VAVIMAHEM 145
Cdd:COG1913  58 DFLSRLKEEDGDKvlgVTDVDLyapglNFVFGLAY------LGGRVAVVstarlrpEFYGLppdEELFlerVLKEAVHEL 131

                        90       100
                ....*....|....*....|....
2DW0_A      146 GHNLGINHdsgycsCGDYACIMRP 169
Cdd:COG1913 132 GHLFGLGH------CPNPRCVMHF 149
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 8-201 2.86e-93

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: 278.73  E-value: 2.86e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        8 RFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTD 87
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       88 LLTRKKHDNAQLLTAIDLD-RVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSCGDYACI 166
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
2DW0_A      167 MRPEISPePSTFFSNCSYFECWDFIMNHNPECILN 201
Cdd:cd04269 161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 8-203 9.54e-64

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: 203.30  E-value: 9.54e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A          8 RFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTD 87
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         88 LLTRKKHDNAQLLTAIDL-DRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHD--SGYCSCGDYA 164
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFgGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
2DW0_A        165 -CIMRPEISPEPSTFFSNCSYFECWDFIMNHNPECILNEP 203
Cdd:pfam01421 161 gCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 8-191 2.86e-49

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: 165.67  E-value: 2.86e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        8 RFVELVLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYM----YIHVALVGLEIWSNEDKITV-KPEAGYTLNAFGE 82
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTnlrlGIRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       83 WRKTDlltRKKHDNAQLLTAIDLDR--VIGLAYVGSMCHPKRSTGIIQDYSEiNLVVAVIMAHEMGHNLGINHDSGYCSC 160
Cdd:cd04267  81 WRAEG---PIRHDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVVEDTGF-TLLTALTMAHELGHNLGAEHDGGDELA 156

                       170       180       190
                ....*....|....*....|....*....|....*
2DW0_A      161 ----GDYACIMRPEISPEPSTFFSNCSYFECWDFI 191
Cdd:cd04267 157 fecdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
ACR smart00608
ADAM Cysteine-Rich Domain;
297-415 2.79e-47

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 158.68  E-value: 2.79e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         297 NGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFER-NQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDN-- 373
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVse 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
2DW0_A         374 ------------SPGQNNPCKM--FYSNEDEHKGMVLPGTKCADGKVCSNGHCVDV 415
Cdd:smart00608  82 lpllgehatviySNIGGLVCWSldYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 220-294 6.73e-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: 123.95  E-value: 6.73e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2DW0_A         220 EVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVF 294
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 8-200 5.67e-33

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 123.12  E-value: 5.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        8 RFVELVLVVDKAMVTKNNGDldKIKTRMYEIVNTVNEIYRY----MYIHVALVGLEIWSNEDK-ITVKPEAGYTLNAFGE 82
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKDpslgNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       83 WRKT----DLLTRKKHDNAQLLTAIDLDR------VIGLAYVGSMCHPKRSTGIIQDyseINLVVAVIMAHEMGHNLGIN 152
Cdd:cd04273  79 WQKKlnppNDSDPEHHDHAILLTRQDICRsngncdTLGLAPVGGMCSPSRSCSINED---TGLSSAFTIAHELGHVLGMP 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
2DW0_A      153 HDSGYCSCGDYA---CIMRPEISPEPSTFF-SNCS--YFEcwDFIMNHNPECIL 200
Cdd:cd04273 156 HDGDGNSCGPEGkdgHIMSPTLGANTGPFTwSKCSrrYLT--SFLDTGDGNCLL 207
Disintegrin pfam00200
Disintegrin;
220-292 1.19e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 115.03  E-value: 1.19e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DW0_A        220 EVGEECDCGTPENCQ-NECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPAD 292
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 8-167 1.40e-22

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: 93.74  E-value: 1.40e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        8 RFVELVLVVDKAMVtknngDLDKIKTRMYEIVNTVNEIYR-YMYIHVALVGLEIwsnedkitvkpeagytlnafgewrkt 86
Cdd:cd00203   1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       87 dlltrKKHDNAQLLTAIDLDRVI-GLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSCGDYAC 165
Cdd:cd00203  50 -----DKADIAILVTRQDFDGGTgGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPT 124


                ..
2DW0_A      166 IM 167
Cdd:cd00203 125 ID 126
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 297-370 1.01e-20

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: 86.52  E-value: 1.01e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2DW0_A        297 NGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFER-NQKGNYYGYCRKENGNKIPCAPEDVKCGRLYC 370
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQC 75
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
8-180 7.67e-19

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 84.01  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A          8 RFVELVLVVDKAMVTKNNGDldKIKTRMYEIVNTV-NEIYRYMYIHVALVGLEIWSNED----KITVKPEAGYTLNAF-- 80
Cdd:pfam13688   3 RTVALLVAADCSYVAAFGGD--AAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFqd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         81 -GEWRKTDlltrkKHDNAQLLTAIDLDRViGLAYVGSMCHPKRSTGIIQDYSEINLVVAV-----IMAHEMGHNLGINHD 154
Cdd:pfam13688  81 fSAWRGTQ-----NDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHD 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
2DW0_A        155 ------SGYCSCGDYAC------IMRPEISPEpSTFFS 180
Cdd:pfam13688 155 cdsstsSQCCPPSNSTCpaggryIMNPSSSPN-STDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 33-154 1.02e-16

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: 75.87  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         33 TRMYEIVNTVNEIY-RYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWrktdLLTRKKHDNA---QLLTAIDLDRV 108
Cdd:pfam13582   1 ARIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEV----NDTRIGQYGYdlgHLFTGRDGGGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
2DW0_A        109 IGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHD 154
Cdd:pfam13582  77 GGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 37-211 2.71e-11

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 62.26  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         37 EIVNTVNEIYRYMYIHVALvgleIWSNEDKITVKPEA--------------GYTLNAFGEWRktdllTRKKHDNAQLLTA 102
Cdd:pfam13574   9 NVVNRVNQIYEPDDINING----GLVNPGEIPATTSAsdsgnnycnspttiVRRLNFLSQWR-----GEQDYCLAHLVTM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        103 IDL-DRVIGLAYVGSMCH-----PKRSTGIIQDYSEINLVVAV----IMAHEMGHNLGINHDsgyCSCGDYACIMRPEIS 172
Cdd:pfam13574  80 GTFsGGELGLAYVGQICQkgassPKTNTGLSTTTNYGSFNYPTqewdVVAHEVGHNFGATHD---CDGSQYASSGCERNA 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
2DW0_A        173 PEpstffSNCSyfECWDFIMNHNPECilneplGTDIISP 211
Cdd:pfam13574 157 AT-----SVCS--ANGSFIMNPASKS------NNDLFSP 182
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 26-183 4.54e-10

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: 59.17  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A         26 GDLDKIKTRMYEIVNTVNEIY-RYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTDLLT---RKKHDNAQLLT 101
Cdd:pfam13583  20 GSVDELRANINATVTTANEVYgRDFNVSLALISDRDVIYTDSSTDSFNADCSGGDLGNWRLATLTSwrdSLNYDLAYLTL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        102 AIDLDR-VIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVImAHEMGHNLGINHDSGYCSC--------GDYACIMRPeIS 172
Cdd:pfam13583 100 MTGPSGqNVGVAWVGALCSSARQNAKASGVARSRDEWDIF-AHEIGHTFGAVHDCSSQGEglssstedGSGQTIMSY-AS 177

                         170
                  ....*....|.
2DW0_A        173 PEPSTFFSNCS 183
Cdd:pfam13583 178 TASQTAFSPCT 188
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 38-183 5.40e-09

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: 56.28  E-value: 5.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       38 IVNTVNEIYRYMY-IHVALVGLEIWSNEDKITVKPEAGYT------------LNAFGEWRKTdlltRKKHDNA--QLLTA 102
Cdd:cd04271  30 NVNSASQLYESSFnISLGLRNLTISDASCPSTAVDSAPWNlpcnsrididdrLSIFSQWRGQ----QPDDGNAfwTLMTA 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A      103 IDLDRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAV-----IMAHEMGHNLGINHD--SGYCSCGDYA---C------- 165
Cdd:cd04271 106 CPSGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTsnewqVFAHEIGHTFGAVHDctSGTCSDGSVGsqqCcplstst 185

                       170       180
                ....*....|....*....|....*
2DW0_A      166 -------IMRPEISpEPSTFFSNCS 183
Cdd:cd04271 186 cdangqyIMNPSSS-SGITEFSPCT 209
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 9-154 7.97e-09

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 55.44  E-value: 7.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        9 FVELVLVVDKAMVtKNNGDLDKIKTRMYEIVNTVNEIYRYMY---IHVALVGLEIWSNED-KITVKP------EAGYTLN 78
Cdd:cd04272   2 YPELFVVVDYDHQ-SEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDfEPYIHPinygyiDAAETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       79 AFGEW--RKTDLLTrkkHDNAQLLTAIDLD---------RVIGLAYVGSMCHpKRSTGIIQD----YSEINLvvaviMAH 143
Cdd:cd04272  81 NFNEYvkKKRDYFN---PDVVFLVTGLDMStysggslqtGTGGYAYVGGACT-ENRVAMGEDtpgsYYGVYT-----MTH 151

                       170
                ....*....|.
2DW0_A      144 EMGHNLGINHD 154
Cdd:cd04272 152 ELAHLLGAPHD 162
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 88-169 1.18e-04

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: 42.67  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       88 LLTRKKHDNAQLL--TAIDL-----DRVIGLAY------VGSMC--HPkRSTGIIQDYSEINLVVAVIMAHEMGHNLGIN 152
Cdd:cd11375  60 LLKLKPPDADCVLgvTDVDLyepglNFVFGLADggsgvaVVSTArlRP-EFYGLPPDEGLFLERLLKEAVHELGHLFGLD 138

                        90
                ....*....|....*..
2DW0_A      153 HdsgycsCGDYACIMRP 169
Cdd:cd11375 139 H------CPYYACVMNF 149
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 35-183 1.47e-04

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: 43.13  E-value: 1.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       35 MYEIVNTVNEIYR--------YMYIHVALVGLEIWSNEDKitVKPEAGYTLNAFGEWRKTDLLTRKKHDN-------AQL 99
Cdd:cd04270  29 LISHIDRVDDIYRntdwdgggFKGIGFQIKRIRIHTTPDE--VDPGNKFYNKSFPNWGVEKFLVKLLLEQfsddvclAHL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A      100 LTAIDLDR-VIGLAYVGS--------MCHP--------KRS--TGII--QDYSE--INLVVAVIMAHEMGHNLGINHDSG 156
Cdd:cd04270 107 FTYRDFDMgTLGLAYVGSprdnsaggICEKayyysngkKKYlnTGLTttVNYGKrvPTKESDLVTAHELGHNFGSPHDPD 186

                       170       180       190
                ....*....|....*....|....*....|....*..
2DW0_A      157 YCSC-------GDYacIMRPEI---SPEPSTFFSNCS 183
Cdd:cd04270 187 IAECapgesqgGNY--IMYARAtsgDKENNKKFSPCS 221
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 328-413 4.12e-04

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 38.48  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A        328 VYEAEDSCfeRNQKGNYYGYCRKENgnkipcapEDVkCGRLYCKDnspGQNNPCKMfysnedeHKGMVLPGTKCADGKVC 407
Cdd:pfam17771   4 LYSADEQC--RLIFGPGSTFCPNGD--------EDV-CSKLWCSN---PGGSTCTT-------KNLPAADGTPCGNKKWC 62


                  ....*.
2DW0_A        408 SNGHCV 413
Cdd:pfam17771  63 LNGKCV 68
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
87-169 9.73e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 9.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DW0_A       87 DLLTRKKHDNAQL---LTAIDL-----DRVIGLAYvgsmchPKRSTGII-------QDYSE---INLV---VAVIMAHEM 145
Cdd:COG1913  58 DFLSRLKEEDGDKvlgVTDVDLyapglNFVFGLAY------LGGRVAVVstarlrpEFYGLppdEELFlerVLKEAVHEL 131

                        90       100
                ....*....|....*....|....
2DW0_A      146 GHNLGINHdsgycsCGDYACIMRP 169
Cdd:COG1913 132 GHLFGLGH------CPNPRCVMHF 149
 
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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