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Conserved domains on  [gi|2044188123|ref|XP_041613650|]
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LOW QUALITY PROTEIN: disintegrin and metalloproteinase domain-containing protein 21 [Vulpes lagopus]

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 ...
 207-395 5.04e-63

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: 208.24  E-value: 5.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 207 WFLELVVVVDHNFLIYSQSNFSMVQEDVFIVVNIVDSIYQQLGTYVILIGIEIWNQGNVFPMI-SIEQVLEDFSKWKQIS 285
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 286 LS-QLQYDAAHFFIRNSLI-SVLGIAYVAGICRPPIDCGVNNFQGDSWSLFALTVAHELGHTLGMWHDEEFCLCEQSGCI 363
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2044188123 364 MNAMRV-PAEKFTNCSYIDFTKTTLNQ-GSCLHN 395
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
490-626 2.72e-62

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 204.13  E-value: 2.72e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123  490 QDGIPC-GDNAYCYEGRCNNHDKQCREIFGEGAKSAYQSCYQEINSLGNRFGHCGISGTTYLKCNISDIFCGRVQCDNVT 568
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2044188123  569 DIPHLRDHSTLQQTHINGVTCWSIDYHLGMDtPDVGEVKDGTMCGPGKICIRKKCVSL 626
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
414-486 4.91e-34

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 124.28  E-value: 4.91e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044188123 414 EGEEECDCGSIKQCEQDPCCL-LNCTLRPKAACAFGLCCKDCKFMPSGKLCRHQVNKCDLPEWCNGTSHQCPED 486
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-158 1.16e-32

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: 122.42  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123  40 EVVTPLKVTD--RGRSAKSPG----WLSYSLKFRGQRHIIHMRVKKLLVSKHFPVFTYTDQHALLQDQPFVPDDCYYHGY 113
Cdd:pfam01562   1 EVVIPVRLDPsrRRRSLASEStyldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2044188123 114 VEGISESLVALSTCSGsFRGMLQINDLAYEIEPI----RHSTKFEHLVY 158
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPLekysREEGGHPHVVY 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 ...
 207-395 5.04e-63

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: 208.24  E-value: 5.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 207 WFLELVVVVDHNFLIYSQSNFSMVQEDVFIVVNIVDSIYQQLGTYVILIGIEIWNQGNVFPMI-SIEQVLEDFSKWKQIS 285
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 286 LS-QLQYDAAHFFIRNSLI-SVLGIAYVAGICRPPIDCGVNNFQGDSWSLFALTVAHELGHTLGMWHDEEFCLCEQSGCI 363
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2044188123 364 MNAMRV-PAEKFTNCSYIDFTKTTLNQ-GSCLHN 395
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
490-626 2.72e-62

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 204.13  E-value: 2.72e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123  490 QDGIPC-GDNAYCYEGRCNNHDKQCREIFGEGAKSAYQSCYQEINSLGNRFGHCGISGTTYLKCNISDIFCGRVQCDNVT 568
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2044188123  569 DIPHLRDHSTLQQTHINGVTCWSIDYHLGMDtPDVGEVKDGTMCGPGKICIRKKCVSL 626
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 491-594 3.62e-50

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: 170.49  E-value: 3.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 491 DGIPCGDN-AYCYEGRCNNHDKQCREIFGEGAKSAYQSCYQEINSLGNRFGHCGISGTTYLKCNISDIFCGRVQCDNVTD 569
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 2044188123 570 IPHLRDHSTLQQTHINGVTCWSIDY 594
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 208-397 6.16e-42

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: 151.30  E-value: 6.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 208 FLELVVVVDHNFLIYSQSNFSMVQEDVFIVVNIVDSIYQQLGTYVILIGIEIWNQGNVFPMIS-IEQVLEDFSKWKQISL 286
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGdANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 287 SQL-QYDAAHFFIRNSLI-SVLGIAYVAGICRPPIDCGVNNFQGDSWSLFALTVAHELGHTLGMWHDEEF--CLC-EQSG 361
Cdd:pfam01421  82 KKRkPHDVAQLLSGVEFGgTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGGG 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2044188123 362 CIMNAMRV--PAEKFTNCSYIDFTKTTLNQ-GSCLHNIP 397
Cdd:pfam01421 162 CIMNPSAGssFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
Disintegrin pfam00200
Disintegrin;
414-486 4.91e-34

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 124.28  E-value: 4.91e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044188123 414 EGEEECDCGSIKQCEQDPCCL-LNCTLRPKAACAFGLCCKDCKFMPSGKLCRHQVNKCDLPEWCNGTSHQCPED 486
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-158 1.16e-32

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: 122.42  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123  40 EVVTPLKVTD--RGRSAKSPG----WLSYSLKFRGQRHIIHMRVKKLLVSKHFPVFTYTDQHALLQDQPFVPDDCYYHGY 113
Cdd:pfam01562   1 EVVIPVRLDPsrRRRSLASEStyldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2044188123 114 VEGISESLVALSTCSGsFRGMLQINDLAYEIEPI----RHSTKFEHLVY 158
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPLekysREEGGHPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 414-488 7.97e-32

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: 118.18  E-value: 7.97e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044188123  414 EGEEECDCGSIKQCeQDPCC-LLNCTLRPKAACAFGLCCKDCKFMPSGKLCRHQVNKCDLPEWCNGTSHQCPEDVY 488
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
338-365 9.20e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.63  E-value: 9.20e-03
                          10        20
                  ....*....|....*....|....*...
gi 2044188123 338 VAHELGHTLGMWHdeefclCEQSGCIMN 365
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMH 148
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 207-395 5.04e-63

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: 208.24  E-value: 5.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 207 WFLELVVVVDHNFLIYSQSNFSMVQEDVFIVVNIVDSIYQQLGTYVILIGIEIWNQGNVFPMI-SIEQVLEDFSKWKQIS 285
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 286 LS-QLQYDAAHFFIRNSLI-SVLGIAYVAGICRPPIDCGVNNFQGDSWSLFALTVAHELGHTLGMWHDEEFCLCEQSGCI 363
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2044188123 364 MNAMRV-PAEKFTNCSYIDFTKTTLNQ-GSCLHN 395
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
490-626 2.72e-62

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 204.13  E-value: 2.72e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123  490 QDGIPC-GDNAYCYEGRCNNHDKQCREIFGEGAKSAYQSCYQEINSLGNRFGHCGISGTTYLKCNISDIFCGRVQCDNVT 568
Cdd:smart00608   1 QDGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2044188123  569 DIPHLRDHSTLQQTHINGVTCWSIDYHLGMDtPDVGEVKDGTMCGPGKICIRKKCVSL 626
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 491-594 3.62e-50

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: 170.49  E-value: 3.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 491 DGIPCGDN-AYCYEGRCNNHDKQCREIFGEGAKSAYQSCYQEINSLGNRFGHCGISGTTYLKCNISDIFCGRVQCDNVTD 569
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 2044188123 570 IPHLRDHSTLQQTHINGVTCWSIDY 594
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 208-397 6.16e-42

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: 151.30  E-value: 6.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 208 FLELVVVVDHNFLIYSQSNFSMVQEDVFIVVNIVDSIYQQLGTYVILIGIEIWNQGNVFPMIS-IEQVLEDFSKWKQISL 286
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGdANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 287 SQL-QYDAAHFFIRNSLI-SVLGIAYVAGICRPPIDCGVNNFQGDSWSLFALTVAHELGHTLGMWHDEEF--CLC-EQSG 361
Cdd:pfam01421  82 KKRkPHDVAQLLSGVEFGgTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGGG 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2044188123 362 CIMNAMRV--PAEKFTNCSYIDFTKTTLNQ-GSCLHNIP 397
Cdd:pfam01421 162 CIMNPSAGssFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
Disintegrin pfam00200
Disintegrin;
414-486 4.91e-34

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 124.28  E-value: 4.91e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044188123 414 EGEEECDCGSIKQCEQDPCCL-LNCTLRPKAACAFGLCCKDCKFMPSGKLCRHQVNKCDLPEWCNGTSHQCPED 486
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-158 1.16e-32

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: 122.42  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123  40 EVVTPLKVTD--RGRSAKSPG----WLSYSLKFRGQRHIIHMRVKKLLVSKHFPVFTYTDQHALLQDQPFVPDDCYYHGY 113
Cdd:pfam01562   1 EVVIPVRLDPsrRRRSLASEStyldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2044188123 114 VEGISESLVALSTCSGsFRGMLQINDLAYEIEPI----RHSTKFEHLVY 158
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPLekysREEGGHPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 414-488 7.97e-32

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: 118.18  E-value: 7.97e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044188123  414 EGEEECDCGSIKQCeQDPCC-LLNCTLRPKAACAFGLCCKDCKFMPSGKLCRHQVNKCDLPEWCNGTSHQCPEDVY 488
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 208-385 1.84e-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: 95.56  E-value: 1.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 208 FLELVVVVDHNFLIYSQSNFSMVQEDVFIVVNIVDSIYQ----QLGTYVILIGIEIWNqGNVF---PMISIEQVLEDFSK 280
Cdd:cd04267     2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILK-GEQFappIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 281 WKQISLSQlqYDAAHFFIRNSLIS--VLGIAYVAGICRPPIDCGV---NNFQGDSWslfaLTVAHELGHTLGMWHDEEFC 355
Cdd:cd04267    81 WRAEGPIR--HDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVvedTGFTLLTA----LTMAHELGHNLGAEHDGGDE 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2044188123 356 LCEQ----SGCIMNAMRVPAEK--FTNCSYIDFTKT 385
Cdd:cd04267   155 LAFEcdggGNYIMAPVDSGLNSyrFSQCSIGSIREF 190
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 208-394 2.14e-20

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: 89.99  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 208 FLELVVVVDHNFL-IYSQSNfsmVQEDVFIVVNIVDSIYQQ--LGTY--VILIGIEIWNQGNVFPMIS--IEQVLEDFSK 280
Cdd:cd04273     2 YVETLVVADSKMVeFHHGED---LEHYILTLMNIVASLYKDpsLGNSinIVVVRLIVLEDEESGLLISgnAQKSLKSFCR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 281 WKQISLSQLQYDAAHFFIR-----------NSLISVLGIAYVAGICRPPIDCGVNnfQGDSWSLfALTVAHELGHTLGMW 349
Cdd:cd04273    79 WQKKLNPPNDSDPEHHDHAilltrqdicrsNGNCDTLGLAPVGGMCSPSRSCSIN--EDTGLSS-AFTIAHELGHVLGMP 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2044188123 350 HDEEFCLCE---QSGCIMNAMRVP-AEKFT--NCS--YI-DFTKTtlNQGSCLH 394
Cdd:cd04273   156 HDGDGNSCGpegKDGHIMSPTLGAnTGPFTwsKCSrrYLtSFLDT--GDGNCLL 207
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 237-351 5.34e-15

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: 72.02  E-value: 5.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 237 VVNIVDSIYQ-QLGTYVILIGIEIWNQGN-VFPMISIEQVLEDFSKWKQISLSQLQYDAAHFFIRNSLISVLGIAYVAGI 314
Cdd:pfam13582   6 LVNRANTIYErDLGIRLQLAAIIITTSADtPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGGGIAYVGGV 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2044188123 315 CRPPIDCGVNNFQGDSWSLFALTVAHELGHTLGMWHD 351
Cdd:pfam13582  86 CNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-365 3.41e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 57.04  E-value: 3.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 211 LVVVVDHNFLIYSQSNFsmVQEDVFIVVNIVDSIYQQ-LGTYVILIGIEIWNQGNVFPMI-----SIEQVLEDF---SKW 281
Cdd:pfam13688   7 LLVAADCSYVAAFGGDA--AQANIINMVNTASNVYERdFNISLGLVNLTISDSTCPYTPPacstgDSSDRLSEFqdfSAW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 282 KqislSQLQYDAAHFFiRNSLISVLGIAYVAGICRPPIDCGVNNFQGD-----SWSLFALTVAHELGHTLGMWHDeeFCL 356
Cdd:pfam13688  85 R----GTQNDDLAYLF-LMTNCSGGGLAWLGQLCNSGSAGSVSTRVSGnnvvvSTATEWQVFAHEIGHNFGAVHD--CDS 157

                         170       180
                  ....*....|....*....|...
gi 2044188123 357 -------------CEQSG-CIMN 365
Cdd:pfam13688 158 stssqccppsnstCPAGGrYIMN 180
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 271-364 5.70e-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: 55.99  E-value: 5.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 271 IEQVLEDFSKWKQI--SLSQLQY---DAAHFFIRNSL-ISVLGIAYVAGICRPPIDCGVNNFQGDSWSLFALTVAHELGH 344
Cdd:cd00203    27 ILIAMQIWRDYLNIrfVLVGVEIdkaDIAILVTRQDFdGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGH 106

                          90       100
                  ....*....|....*....|
gi 2044188123 345 TLGMWHDEEFCLCEQSGCIM 364
Cdd:cd00203   107 ALGFYHDHDRKDRDDYPTID 126
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 210-352 1.64e-06

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 49.66  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 210 ELVVVVDHNFliysQSNFSMVQEDV--FIV-VNIVDSIYQQL---GTYVILIGIEI--------WNQGNVFPMISIEQVL 275
Cdd:cd04272     4 ELFVVVDYDH----QSEFFSNEQLIryLAVmVNAANLRYRDLkspRIRLLLVGITIskdpdfepYIHPINYGYIDAAETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 276 EDFSKWKQISLSQLQYDAAHFFIRNSLI---------SVLGIAYVAGICrppidcgVNNFQG---DSWSLF--ALTVAHE 341
Cdd:cd04272    80 ENFNEYVKKKRDYFNPDVVFLVTGLDMStysggslqtGTGGYAYVGGAC-------TENRVAmgeDTPGSYygVYTMTHE 152

                         170
                  ....*....|.
gi 2044188123 342 LGHTLGMWHDE 352
Cdd:cd04272   153 LAHLLGAPHDG 163
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 230-362 1.68e-06

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: 49.16  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 230 VQEDVFIVVNIVDSIY--QQLGTYVILIGI-------EIWNQGNVFPMISIEQV--LEDFSKWKqislSQLQYDAAHF-F 297
Cdd:pfam13574   3 VTENLVNVVNRVNQIYepDDININGGLVNPgeipattSASDSGNNYCNSPTTIVrrLNFLSQWR----GEQDYCLAHLvT 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044188123 298 IRNSLISVLGIAYVAGICR-------------PPIDCGVNNFQGDSWslfaLTVAHELGHTLGMWHDeefCLCEQSGC 362
Cdd:pfam13574  79 MGTFSGGELGLAYVGQICQkgasspktntglsTTTNYGSFNYPTQEW----DVVAHEVGHNFGATHD---CDGSQYAS 149
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 230-362 2.21e-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: 46.26  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 230 VQEDVFIVVNIVDSIYQQlgTYVILIGI-----------------EIWNQGnVFPMISIEQVLEDFSKWKqislSQLQ-Y 291
Cdd:cd04271    23 ARRNILNNVNSASQLYES--SFNISLGLrnltisdascpstavdsAPWNLP-CNSRIDIDDRLSIFSQWR----GQQPdD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044188123 292 DAAHFFIRNSLIS--VLGIAYVAGICRPPIDCGVNNFQ---------GDSWSLFAltvaHELGHTLGMWHDeefclCEQS 360
Cdd:cd04271    96 GNAFWTLMTACPSgsEVGVAWLGQLCRTGASDQGNETVagtnvvvrtSNEWQVFA----HEIGHTFGAVHD-----CTSG 166


                  ..
gi 2044188123 361 GC 362
Cdd:cd04271   167 TC 168
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 324-350 2.06e-03

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 39.40  E-value: 2.06e-03
                          10        20
                  ....*....|....*....|....*..
gi 2044188123 324 NNFQGDSWSLFALTVAHELGHTLGMWH 350
Cdd:cd04268    84 SSFVEYSGARLRNTAEHELGHALGLRH 110
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 337-365 6.59e-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: 38.05  E-value: 6.59e-03
                          10        20
                  ....*....|....*....|....*....
gi 2044188123 337 TVAHELGHTLGMWHdeefclCEQSGCIMN 365
Cdd:cd11375   126 EAVHELGHLFGLDH------CPYYACVMN 148
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
338-365 9.20e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.63  E-value: 9.20e-03
                          10        20
                  ....*....|....*....|....*...
gi 2044188123 338 VAHELGHTLGMWHdeefclCEQSGCIMN 365
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMH 148
 
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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