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Conserved domains on  [gi|9966766|ref|NP_065063|]
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disintegrin and metalloproteinase domain-containing protein 21 preproprotein [Mus musculus]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10480592)

disintegrin and metalloproteinase domain-containing protein also contains an ADAM domain and belongs to the ADAM family of membrane-anchored metalloproteases; ADAMs (A Disintegrin And Metalloprotease) are glycoproteins that play roles in cell signaling, cell fusion, and cell-cell interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-400 3.06e-62

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: 206.31  E-value: 3.06e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  212 WFLELAVVVDYGFFTNAQQNLSKVRGDVVLVVNMVDSMYKPLDTYVTLVGIEIWNRGNVLPME-NIHQVLEDFSHWKQIS 290
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  291 LS-QVHHDAAHIFI-RSSLISVLGIAYIAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHDEESCSCGKSGCV 368
Cdd:cd04269  81 LLpRKPHDNAQLLTgRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 9966766  369 MSTFRV-PAERFTNCSYSDFMKTTLNQ-GTCLYN 400
Cdd:cd04269 161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
495-631 4.86e-50

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 171.39  E-value: 4.86e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766     495 QDGVPCGAG-AYCYQKQCNNHDQQCREIFGKGARSASHNCYKEINLQGNRFGHCGTDGTVFLKCRMSDVFCGKVHCENVE 573
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 9966766     574 DIHHPQAPYVLQNIYANGITCWSTGHCLGMGvPDVGEVKDGTTCGVGKICLHKKCVSL 631
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
419-491 1.96e-33

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 122.73  E-value: 1.96e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9966766    419 ESEEECDCGSVQECEQDPCCF-LNCTLRPAAACSFGLCCKDCKFMLLGELCRPKINECDLPEWCNGTSHQCPED 491
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-164 2.15e-25

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: 101.62  E-value: 2.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766     46 EVVIPLKVT------SRARGAKNSEWLSYSLVFGGRRHVVHMRVKKLLVSTHIPVLTYTEEHTPLSDYPFVPSDCYYHGY 119
Cdd:pfam01562   1 EVVIPVRLDpsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 9966766    120 VEGALESLVAFSACNgGLQGVLQMNGFSYEIEPIKH----SSTFEHLVY 164
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-400 3.06e-62

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: 206.31  E-value: 3.06e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  212 WFLELAVVVDYGFFTNAQQNLSKVRGDVVLVVNMVDSMYKPLDTYVTLVGIEIWNRGNVLPME-NIHQVLEDFSHWKQIS 290
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  291 LS-QVHHDAAHIFI-RSSLISVLGIAYIAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHDEESCSCGKSGCV 368
Cdd:cd04269  81 LLpRKPHDNAQLLTgRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 9966766  369 MSTFRV-PAERFTNCSYSDFMKTTLNQ-GTCLYN 400
Cdd:cd04269 161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
495-631 4.86e-50

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 171.39  E-value: 4.86e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766     495 QDGVPCGAG-AYCYQKQCNNHDQQCREIFGKGARSASHNCYKEINLQGNRFGHCGTDGTVFLKCRMSDVFCGKVHCENVE 573
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 9966766     574 DIHHPQAPYVLQNIYANGITCWSTGHCLGMGvPDVGEVKDGTTCGVGKICLHKKCVSL 631
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 213-402 4.44e-44

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: 157.08  E-value: 4.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    213 FLELAVVVDYGFFTNAQQNLSKVRGDVVLVVNMVDSMYKPLDTYVTLVGIEIWNRGNVLPM-ENIHQVLEDFSHWKQISL 291
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVsGDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    292 SQVH-HDAAHIFIRSSLI-SVLGIAYIAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHDEES--CSCG-KSG 366
Cdd:pfam01421  82 KKRKpHDVAQLLSGVEFGgTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPpGGG 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 9966766    367 CVM--STFRVPAERFTNCSYSDFMKTTLNQ-GTCLYNHP 402
Cdd:pfam01421 162 CIMnpSAGSSFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 496-597 1.16e-38

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: 138.52  E-value: 1.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    496 DGVPCGAG-AYCYQKQCNNHDQQCREIFGKGARSASHNCYKEINLQGNRFGHCGTDGTVFLKCRMSDVFCGKVHCENVED 574
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|...
gi 9966766    575 IHHPQAPYVLQNIYANGITCWST 597
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGT 103
Disintegrin pfam00200
Disintegrin;
419-491 1.96e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 122.73  E-value: 1.96e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9966766    419 ESEEECDCGSVQECEQDPCCF-LNCTLRPAAACSFGLCCKDCKFMLLGELCRPKINECDLPEWCNGTSHQCPED 491
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 419-493 1.30e-30

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: 114.71  E-value: 1.30e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9966766     419 ESEEECDCGSVQECeQDPCCF-LNCTLRPAAACSFGLCCKDCKFMLLGELCRPKINECDLPEWCNGTSHQCPEDGY 493
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDpATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-164 2.15e-25

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: 101.62  E-value: 2.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766     46 EVVIPLKVT------SRARGAKNSEWLSYSLVFGGRRHVVHMRVKKLLVSTHIPVLTYTEEHTPLSDYPFVPSDCYYHGY 119
Cdd:pfam01562   1 EVVIPVRLDpsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 9966766    120 VEGALESLVAFSACNgGLQGVLQMNGFSYEIEPIKH----SSTFEHLVY 164
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 315-394 7.35e-04

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 42.46  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766   315 YIAGICRPPLDCGVENFQGDAWSLFAN-TVAHELGHTFGMKH---DEESCSCGKSGcVMSTfrVPAERFTNCSYSDFMKT 390
Cdd:NF038115 149 NANGVAQVGMDLQVKGYNVTLDLYVATqTLAHELGHLFGLYNghaESAECSEGGYR-LMCG--SLAENFENLFGSSELQR 225


                 ....
gi 9966766   391 TLNQ 394
Cdd:NF038115 226 FYNN 229
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
343-370 7.66e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 7.66e-04
                        10        20
                ....*....|....*....|....*...
gi 9966766  343 VAHELGHTFGMKHdeescsCGKSGCVMS 370
Cdd:COG1913 127 AVHELGHLFGLGH------CPNPRCVMH 148
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
343-370 2.14e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.52  E-value: 2.14e-03
                         10        20
                 ....*....|....*....|....*...
gi 9966766   343 VAHELGHTFGMKHdeescsCGKSGCVMS 370
Cdd:NF033823 126 AVHELGHLLGLGH------CPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 343-370 6.93e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.08  E-value: 6.93e-03
                         10        20
                 ....*....|....*....|....*...
gi 9966766   343 VAHELGHTFGMKHdeescsCGKSGCVMS 370
Cdd:PRK13267 129 VTHELGHTLGLEH------CDNPRCVMN 150
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-400 3.06e-62

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: 206.31  E-value: 3.06e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  212 WFLELAVVVDYGFFTNAQQNLSKVRGDVVLVVNMVDSMYKPLDTYVTLVGIEIWNRGNVLPME-NIHQVLEDFSHWKQIS 290
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  291 LS-QVHHDAAHIFI-RSSLISVLGIAYIAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHDEESCSCGKSGCV 368
Cdd:cd04269  81 LLpRKPHDNAQLLTgRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 9966766  369 MSTFRV-PAERFTNCSYSDFMKTTLNQ-GTCLYN 400
Cdd:cd04269 161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
495-631 4.86e-50

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 171.39  E-value: 4.86e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766     495 QDGVPCGAG-AYCYQKQCNNHDQQCREIFGKGARSASHNCYKEINLQGNRFGHCGTDGTVFLKCRMSDVFCGKVHCENVE 573
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 9966766     574 DIHHPQAPYVLQNIYANGITCWSTGHCLGMGvPDVGEVKDGTTCGVGKICLHKKCVSL 631
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 213-402 4.44e-44

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: 157.08  E-value: 4.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    213 FLELAVVVDYGFFTNAQQNLSKVRGDVVLVVNMVDSMYKPLDTYVTLVGIEIWNRGNVLPM-ENIHQVLEDFSHWKQISL 291
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVsGDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    292 SQVH-HDAAHIFIRSSLI-SVLGIAYIAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHDEES--CSCG-KSG 366
Cdd:pfam01421  82 KKRKpHDVAQLLSGVEFGgTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPpGGG 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 9966766    367 CVM--STFRVPAERFTNCSYSDFMKTTLNQ-GTCLYNHP 402
Cdd:pfam01421 162 CIMnpSAGSSFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 496-597 1.16e-38

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: 138.52  E-value: 1.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    496 DGVPCGAG-AYCYQKQCNNHDQQCREIFGKGARSASHNCYKEINLQGNRFGHCGTDGTVFLKCRMSDVFCGKVHCENVED 574
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|...
gi 9966766    575 IHHPQAPYVLQNIYANGITCWST 597
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGT 103
Disintegrin pfam00200
Disintegrin;
419-491 1.96e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 122.73  E-value: 1.96e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9966766    419 ESEEECDCGSVQECEQDPCCF-LNCTLRPAAACSFGLCCKDCKFMLLGELCRPKINECDLPEWCNGTSHQCPED 491
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 419-493 1.30e-30

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: 114.71  E-value: 1.30e-30
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9966766     419 ESEEECDCGSVQECeQDPCCF-LNCTLRPAAACSFGLCCKDCKFMLLGELCRPKINECDLPEWCNGTSHQCPEDGY 493
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDpATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-164 2.15e-25

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: 101.62  E-value: 2.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766     46 EVVIPLKVT------SRARGAKNSEWLSYSLVFGGRRHVVHMRVKKLLVSTHIPVLTYTEEHTPLSDYPFVPSDCYYHGY 119
Cdd:pfam01562   1 EVVIPVRLDpsrrrrSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 9966766    120 VEGALESLVAFSACNgGLQGVLQMNGFSYEIEPIKH----SSTFEHLVY 164
Cdd:pfam01562  81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 213-384 3.02e-22

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: 94.79  E-value: 3.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  213 FLELAVVVDYGFFTNAQQNLSKVRGDVVLVVNMVDSMYKPLDTY----VTLVGIEIWNrGNVL---PMENIHQVLEDFSH 285
Cdd:cd04267   2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLRlgirISLEGLQILK-GEQFappIDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  286 WKQISLSqvHHDAAHIFIRSSLIS--VLGIAYIAGICRPPLDCGV---ENFQGDAWslfaNTVAHELGHTFGMKHDEESC 360
Cdd:cd04267  81 WRAEGPI--RHDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVvedTGFTLLTA----LTMAHELGHNLGAEHDGGDE 154

                       170       180       190
                ....*....|....*....|....*....|
gi 9966766  361 SC----GKSGCVMSTFRVPA--ERFTNCSY 384
Cdd:cd04267 155 LAfecdGGGNYIMAPVDSGLnsYRFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 213-398 2.06e-18

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: 84.21  E-value: 2.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  213 FLELAVVVDYGFFtnAQQNLSKVRGDVVLVVNMVDSMYK------PLDtyVTLVGIEIWNRGNVLPME--NIHQVLEDFS 284
Cdd:cd04273   2 YVETLVVADSKMV--EFHHGEDLEHYILTLMNIVASLYKdpslgnSIN--IVVVRLIVLEDEESGLLIsgNAQKSLKSFC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  285 HWKQ-----ISLSQVHHDAAHIFIRSSLIS------VLGIAYIAGICRPPLDCGVEnfQGDAWSLfANTVAHELGHTFGM 353
Cdd:cd04273  78 RWQKklnppNDSDPEHHDHAILLTRQDICRsngncdTLGLAPVGGMCSPSRSCSIN--EDTGLSS-AFTIAHELGHVLGM 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 9966766  354 KHDEESCSCGKS---GCVMS-TFRVPAERFT--NCS---YSDFMKTtlNQGTCL 398
Cdd:cd04273 155 PHDGDGNSCGPEgkdGHIMSpTLGANTGPFTwsKCSrryLTSFLDT--GDGNCL 206
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 238-356 8.97e-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: 62.77  E-value: 8.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    238 DVVLVVNMVDSMYKP-LDTYVTLVGIEIWNRGN-VLPMENIHQVLEDFSHWKQISLSQVHHDAAHIFIRSSLISVLGIAY 315
Cdd:pfam13582   2 RIVSLVNRANTIYERdLGIRLQLAAIIITTSADtPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGGGIAY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 9966766    316 IAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHD 356
Cdd:pfam13582  82 VGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
216-376 8.78e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 58.97  E-value: 8.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    216 LAVVVDYGFFTNAQQNlsKVRGDVVLVVNMVDS-MYKPLDTYVTLVGIEIWNRGNVLPM-----ENIHQVLEDFshwkQI 289
Cdd:pfam13688   7 LLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPpacstGDSSDRLSEF----QD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    290 SLSQVH---HDAAHIFIRSSLISVlGIAYIAGICrPPLDCGVENFQGD------AWSLFANTVAHELGHTFGMKHDEESc 360
Cdd:pfam13688  81 FSAWRGtqnDDLAYLFLMTNCSGG-GLAWLGQLC-NSGSAGSVSTRVSgnnvvvSTATEWQVFAHEIGHNFGAVHDCDS- 157

                         170
                  ....*....|....*.
gi 9966766    361 SCGKSGCVMSTFRVPA 376
Cdd:pfam13688 158 STSSQCCPPSNSTCPA 173
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 288-371 3.87e-08

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: 53.29  E-value: 3.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  288 QISLSQV---HHDAAHIFIRSSL-ISVLGIAYIAGICRPPLDCGVENFQGDAWSLFANTVAHELGHTFGMKHDEESCSCG 363
Cdd:cd00203  41 RFVLVGVeidKADIAILVTRQDFdGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRD 120


                ....*...
gi 9966766  364 KSGCVMST 371
Cdd:cd00203 121 DYPTIDDT 128
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 215-357 3.34e-07

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 51.58  E-value: 3.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  215 ELAVVVDYGFFTNAQQNlSKVRGDVVLVVNMVDSMYKPL---DTYVTLVGIEI--------WNRGNVLPMENIHQVLEDF 283
Cdd:cd04272   4 ELFVVVDYDHQSEFFSN-EQLIRYLAVMVNAANLRYRDLkspRIRLLLVGITIskdpdfepYIHPINYGYIDAAETLENF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  284 SHWKQISLSQVHHDAAHIFIRSSLI---------SVLGIAYIAGICrppldcgVENFQG---DAWSLF--ANTVAHELGH 349
Cdd:cd04272  83 NEYVKKKRDYFNPDVVFLVTGLDMStysggslqtGTGGYAYVGGAC-------TENRVAmgeDTPGSYygVYTMTHELAH 155


                ....*...
gi 9966766  350 TFGMKHDE 357
Cdd:cd04272 156 LLGAPHDG 163
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 265-371 3.33e-06

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: 48.96  E-value: 3.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766  265 WNRGNVLPMeNIHQVLEDFSHWKQislSQVHHDAAHIFIRSSLIS--VLGIAYIAGICRPPldcgvENFQGDAWSLFANT 342
Cdd:cd04271  68 WNLPCNSRI-DIDDRLSIFSQWRG---QQPDDGNAFWTLMTACPSgsEVGVAWLGQLCRTG-----ASDQGNETVAGTNV 138

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 9966766  343 V----------AHELGHTFGMKHDEESCSCGKSG------CVMST 371
Cdd:cd04271 139 VvrtsnewqvfAHEIGHTFGAVHDCTSGTCSDGSvgsqqcCPLST 183
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 235-367 5.38e-05

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 44.93  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    235 VRGDVVLVVNMVDSMYKPLDTYVTLVGIEI------------WN-RGNVLPMENIHQVLedFSHWKqislSQVHHDAAHI 301
Cdd:pfam13574   3 VTENLVNVVNRVNQIYEPDDININGGLVNPgeipattsasdsGNnYCNSPTTIVRRLNF--LSQWR----GEQDYCLAHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766    302 FIRSSL-ISVLGIAYIAGICRPPLDC-------------GVENFQGDAWSLFAntvaHELGHTFGMKHDEESCSCGKSGC 367
Cdd:pfam13574  77 VTMGTFsGGELGLAYVGQICQKGASSpktntglstttnyGSFNYPTQEWDVVA----HEVGHNFGATHDCDGSQYASSGC 152
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 315-394 7.35e-04

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 42.46  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966766   315 YIAGICRPPLDCGVENFQGDAWSLFAN-TVAHELGHTFGMKH---DEESCSCGKSGcVMSTfrVPAERFTNCSYSDFMKT 390
Cdd:NF038115 149 NANGVAQVGMDLQVKGYNVTLDLYVATqTLAHELGHLFGLYNghaESAECSEGGYR-LMCG--SLAENFENLFGSSELQR 225


                 ....
gi 9966766   391 TLNQ 394
Cdd:NF038115 226 FYNN 229
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
343-370 7.66e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 7.66e-04
                        10        20
                ....*....|....*....|....*...
gi 9966766  343 VAHELGHTFGMKHdeescsCGKSGCVMS 370
Cdd:COG1913 127 AVHELGHLFGLGH------CPNPRCVMH 148
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 342-370 9.50e-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: 40.74  E-value: 9.50e-04
                        10        20
                ....*....|....*....|....*....
gi 9966766  342 TVAHELGHTFGMKHdeescsCGKSGCVMS 370
Cdd:cd11375 126 EAVHELGHLFGLDH------CPYYACVMN 148
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
343-370 2.14e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.52  E-value: 2.14e-03
                         10        20
                 ....*....|....*....|....*...
gi 9966766   343 VAHELGHTFGMKHdeescsCGKSGCVMS 370
Cdd:NF033823 126 AVHELGHLLGLGH------CPNPRCVMH 147
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 312-365 2.38e-03

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: 39.91  E-value: 2.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966766    312 GIAYIAGICRPPLD---CGVENFQGDAWSLFAntvaHELGHTFGMKHDEESCSCGKS 365
Cdd:pfam13583 109 GVAWVGALCSSARQnakASGVARSRDEWDIFA----HEIGHTFGAVHDCSSQGEGLS 161
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 343-370 6.93e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.08  E-value: 6.93e-03
                         10        20
                 ....*....|....*....|....*...
gi 9966766   343 VAHELGHTFGMKHdeescsCGKSGCVMS 370
Cdd:PRK13267 129 VTHELGHTLGLEH------CDNPRCVMN 150
 
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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