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Conserved domains on  [gi|568954889|ref|XP_006509516|]
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testase-8 isoform X1 [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 ...
 222-408 3.86e-60

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: 201.30  E-value: 3.86e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 222 FLDLALVVDCERIRYHNNNKSHVLVEVFLIISLINKIYFALDIEVVLIGLELWNEGNLVPV-DRMQILLEEFCVWKTLSL 300
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 301 NIRIPNDIAHLFVNHSF-GKFLGLAYVGTVCLPSHNCGVDRLLGPNLFQFAHIIAHEIGHNLGMEHDSSSCTCGGiNYCL 379
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGR-STCI 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568954889 380 M-SSTYSFNPEFSNCSYSNFWTTYATTN--CL 408
Cdd:cd04269  161 MaPSPSSLTDAFSNCSYEDYQKFLSRGGgqCL 192
ACR smart00608
ADAM Cysteine-Rich Domain;
505-641 4.29e-59

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 196.43  E-value: 4.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889   505 LDGSPCRDG-GYCYEKRCNNRDEQCKQIFGKEARSADHSCYRELNTQGDRFGNCGMIRDAYLRCHDSDILCGRVQCENVT 583
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568954889   584 RIPFLRDHSTVHWTHLNGVTCWGTDYHFGMTiPDIGIVKDGTDCGPEHVCINKKCVSK 641
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
429-501 3.97e-32

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.88  E-value: 3.97e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954889  429 DDGEQCDCGDRHMCERDQCCNSR-CALNDGAACAFGLCCLYCQIMPAGTVCREEVNECDLPEWCNGHSHKCPND 501
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKtCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 57-173 8.22e-26

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: 103.16  E-value: 8.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889   57 EVVIPLRVTGNR-------PMWAMGWLTYSLHFGGQKHFIHIKAKKFLVSRLFSVFTYTKQGALHKDQPYVQNDCYYHGH 129
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568954889  130 MDGDPESMVAITTCyGGFQGILQINGTVYEIKP----KNLSSTFEHLV 173
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPlekySREEGGHPHVV 127
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 222-408 3.86e-60

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: 201.30  E-value: 3.86e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 222 FLDLALVVDCERIRYHNNNKSHVLVEVFLIISLINKIYFALDIEVVLIGLELWNEGNLVPV-DRMQILLEEFCVWKTLSL 300
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 301 NIRIPNDIAHLFVNHSF-GKFLGLAYVGTVCLPSHNCGVDRLLGPNLFQFAHIIAHEIGHNLGMEHDSSSCTCGGiNYCL 379
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGR-STCI 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568954889 380 M-SSTYSFNPEFSNCSYSNFWTTYATTN--CL 408
Cdd:cd04269  161 MaPSPSSLTDAFSNCSYEDYQKFLSRGGgqCL 192
ACR smart00608
ADAM Cysteine-Rich Domain;
505-641 4.29e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 196.43  E-value: 4.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889   505 LDGSPCRDG-GYCYEKRCNNRDEQCKQIFGKEARSADHSCYRELNTQGDRFGNCGMIRDAYLRCHDSDILCGRVQCENVT 583
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568954889   584 RIPFLRDHSTVHWTHLNGVTCWGTDYHFGMTiPDIGIVKDGTDCGPEHVCINKKCVSK 641
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 506-609 6.76e-52

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: 175.50  E-value: 6.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  506 DGSPCRDG-GYCYEKRCNNRDEQCKQIFGKEARSADHSCYRELNTQGDRFGNCGMIRDAYLRCHDSDILCGRVQCENVTR 584
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 568954889  585 IPFLRDHSTVHWTHLNGVTCWGTDY 609
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 222-398 8.47e-43

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: 154.00  E-value: 8.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  222 FLDLALVVDCERIRYHNNNKSHVLVEVFLIISLINKIYFALDIEVVLIGLELWNEGNLVPV-DRMQILLEEFCVWKTLSL 300
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVsGDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  301 NIRIPNDIAHLFVNHSF-GKFLGLAYVGTVCLPSHNCGVDRLLGPNLFQFAHIIAHEIGHNLGMEHDSSS--CTCGGINY 377
Cdd:pfam01421  82 KKRKPHDVAQLLSGVEFgGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGGG 161

                         170       180
                  ....*....|....*....|...
gi 568954889  378 CLM--SSTYSFNPEFSNCSYSNF 398
Cdd:pfam01421 162 CIMnpSAGSSFPRKFSNCSQEDF 184
Disintegrin pfam00200
Disintegrin;
429-501 3.97e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.88  E-value: 3.97e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954889  429 DDGEQCDCGDRHMCERDQCCNSR-CALNDGAACAFGLCCLYCQIMPAGTVCREEVNECDLPEWCNGHSHKCPND 501
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKtCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 429-503 2.43e-26

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: 102.77  E-value: 2.43e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954889   429 DDGEQCDCGDRHMCeRDQCCNS-RCALNDGAACAFGLCCLYCQIMPAGTVCREEVNECDLPEWCNGHSHKCPNDVY 503
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 57-173 8.22e-26

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: 103.16  E-value: 8.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889   57 EVVIPLRVTGNR-------PMWAMGWLTYSLHFGGQKHFIHIKAKKFLVSRLFSVFTYTKQGALHKDQPYVQNDCYYHGH 129
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568954889  130 MDGDPESMVAITTCyGGFQGILQINGTVYEIKP----KNLSSTFEHLV 173
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPlekySREEGGHPHVV 127
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 423-460 3.99e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 35.43  E-value: 3.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568954889  423 CGNGVVDDGEQCDCGDRHMCERdqcCNSRCALNDGAAC 460
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTTSGDG---CSATCRLEEGFAC 38
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 222-408 3.86e-60

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: 201.30  E-value: 3.86e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 222 FLDLALVVDCERIRYHNNNKSHVLVEVFLIISLINKIYFALDIEVVLIGLELWNEGNLVPV-DRMQILLEEFCVWKTLSL 300
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 301 NIRIPNDIAHLFVNHSF-GKFLGLAYVGTVCLPSHNCGVDRLLGPNLFQFAHIIAHEIGHNLGMEHDSSSCTCGGiNYCL 379
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGR-STCI 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568954889 380 M-SSTYSFNPEFSNCSYSNFWTTYATTN--CL 408
Cdd:cd04269  161 MaPSPSSLTDAFSNCSYEDYQKFLSRGGgqCL 192
ACR smart00608
ADAM Cysteine-Rich Domain;
505-641 4.29e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 196.43  E-value: 4.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889   505 LDGSPCRDG-GYCYEKRCNNRDEQCKQIFGKEARSADHSCYRELNTQGDRFGNCGMIRDAYLRCHDSDILCGRVQCENVT 583
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568954889   584 RIPFLRDHSTVHWTHLNGVTCWGTDYHFGMTiPDIGIVKDGTDCGPEHVCINKKCVSK 641
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 506-609 6.76e-52

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: 175.50  E-value: 6.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  506 DGSPCRDG-GYCYEKRCNNRDEQCKQIFGKEARSADHSCYRELNTQGDRFGNCGMIRDAYLRCHDSDILCGRVQCENVTR 584
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 568954889  585 IPFLRDHSTVHWTHLNGVTCWGTDY 609
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 222-398 8.47e-43

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: 154.00  E-value: 8.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  222 FLDLALVVDCERIRYHNNNKSHVLVEVFLIISLINKIYFALDIEVVLIGLELWNEGNLVPV-DRMQILLEEFCVWKTLSL 300
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVsGDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  301 NIRIPNDIAHLFVNHSF-GKFLGLAYVGTVCLPSHNCGVDRLLGPNLFQFAHIIAHEIGHNLGMEHDSSS--CTCGGINY 377
Cdd:pfam01421  82 KKRKPHDVAQLLSGVEFgGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGGG 161

                         170       180
                  ....*....|....*....|...
gi 568954889  378 CLM--SSTYSFNPEFSNCSYSNF 398
Cdd:pfam01421 162 CIMnpSAGSSFPRKFSNCSQEDF 184
Disintegrin pfam00200
Disintegrin;
429-501 3.97e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.88  E-value: 3.97e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954889  429 DDGEQCDCGDRHMCERDQCCNSR-CALNDGAACAFGLCCLYCQIMPAGTVCREEVNECDLPEWCNGHSHKCPND 501
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKtCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 429-503 2.43e-26

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: 102.77  E-value: 2.43e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954889   429 DDGEQCDCGDRHMCeRDQCCNS-RCALNDGAACAFGLCCLYCQIMPAGTVCREEVNECDLPEWCNGHSHKCPNDVY 503
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 57-173 8.22e-26

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: 103.16  E-value: 8.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889   57 EVVIPLRVTGNR-------PMWAMGWLTYSLHFGGQKHFIHIKAKKFLVSRLFSVFTYTKQGALHKDQPYVQNDCYYHGH 129
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568954889  130 MDGDPESMVAITTCyGGFQGILQINGTVYEIKP----KNLSSTFEHLV 173
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPlekySREEGGHPHVV 127
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 222-395 1.16e-23

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: 99.03  E-value: 1.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 222 FLDLALVVDCERIRYHNNNKSHVLVEVFLIISLINKIY----FALDIEVVLIGLELWNEGNLVPVD--RMQILLEEFCVW 295
Cdd:cd04267    2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIdsDASNTLNSFSFW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 296 KTlslNIRIPNDIAHLFVNHSF--GKFLGLAYVGTVCLPSHNCGVDRLLGPNlFQFAHIIAHEIGHNLGMEHDSSSCT-- 371
Cdd:cd04267   82 RA---EGPIRHDNAVLLTAQDFieGDILGLAYVGSMCNPYSSVGVVEDTGFT-LLTALTMAHELGHNLGAEHDGGDELaf 157

                        170       180
                 ....*....|....*....|....*..
gi 568954889 372 -CGGINYCLMSSTYSF--NPEFSNCSY 395
Cdd:cd04267  158 eCDGGGNYIMAPVDSGlnSYRFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 222-409 6.87e-22

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: 94.23  E-value: 6.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 222 FLDLALVVDCERIRYHNnnKSHVLVEVFLIISLINKIY----FALDIEVVLIGLELWN--EGNLVPVDRMQILLEEFCVW 295
Cdd:cd04273    2 YVETLVVADSKMVEFHH--GEDLEHYILTLMNIVASLYkdpsLGNSINIVVVRLIVLEdeESGLLISGNAQKSLKSFCRW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 296 KTlSLNIRIPNDIAH-----------LFVNHSFGKFLGLAYVGTVCLPSHNCGVDRLLGpnlFQFAHIIAHEIGHNLGME 364
Cdd:cd04273   80 QK-KLNPPNDSDPEHhdhailltrqdICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELGHVLGMP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568954889 365 HDSSSCTCG--GINYCLMSSTYSFNPE---FSNCS---YSNFWTTYaTTNCLR 409
Cdd:cd04273  156 HDGDGNSCGpeGKDGHIMSPTLGANTGpftWSKCSrryLTSFLDTG-DGNCLL 207
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 285-395 1.55e-14

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: 72.17  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 285 MQILLEEFCVWKTLSLNIRIPNDIAHLFVNHSF-GKFLGLAYVGTVCLPSHNCGVDRLLGPNLFQFAHIIAHEIGHNLGM 363
Cdd:cd00203   31 MQIWRDYLNIRFVLVGVEIDKADIAILVTRQDFdGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGF 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568954889 364 EHDSSSCTCGGIN-------------YCLMSSTYSF-----NPEFSNCSY 395
Cdd:cd00203  111 YHDHDRKDRDDYPtiddtlnaedddyYSVMSYTKGSfsdgqRKDFSQCDI 160
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
224-391 8.19e-14

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 70.53  E-value: 8.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  224 DLALVVDCERIRYHNNNKSHVLVeVFLIISLINKIYFALDIEVVLIGLELWNEGNLVP-----VDRMQILLEEFCVWKtl 298
Cdd:pfam13688   6 ALLVAADCSYVAAFGGDAAQANI-INMVNTASNVYERDFNISLGLVNLTISDSTCPYTppacsTGDSSDRLSEFQDFS-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  299 SLNIRIPNDIAHLFVNHSFGKfLGLAYVGTVC------LPSHNCGVDRLLGPNlFQFAHIIAHEIGHNLGMEHD------ 366
Cdd:pfam13688  83 AWRGTQNDDLAYLFLMTNCSG-GGLAWLGQLCnsgsagSVSTRVSGNNVVVST-ATEWQVFAHEIGHNFGAVHDcdssts 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568954889  367 SSSC-----TCGGINYCLMSSTYSFN-PEFS 391
Cdd:pfam13688 161 SQCCppsnsTCPAGGRYIMNPSSSPNsTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 251-366 7.74e-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: 7.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  251 IISLINKIY-FALDIEVVLIGLELWNEGNLVPV--DRMQILLEEFCVWktlSLNIRIPN-DIAHLFVNHSFGKFLGLAYV 326
Cdd:pfam13582   6 LVNRANTIYeRDLGIRLQLAAIIITTSADTPYTssDALEILDELQEVN---DTRIGQYGyDLGHLFTGRDGGGGGGIAYV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568954889  327 GTVCLPSHNCGVDRLLGPNLFQFAHIIAHEIGHNLGMEHD 366
Cdd:pfam13582  83 GGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 224-398 2.92e-08

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: 54.55  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  224 DLALVVDCERIRYHNNnKSHVLVEVFLIISLINKIYfALDIEVvliGLELWNEGNLVPVD------RMQILLEEFCVWKT 297
Cdd:pfam13583   6 RVAVATDCTYSASFGS-VDELRANINATVTTANEVY-GRDFNV---SLALISDRDVIYTDsstdsfNADCSGGDLGNWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  298 LSLNIRIPN---DIAHLFvnHSFGKF---LGLAYVGTVCLPS---HNCGVDRLLGPNlFQfahIIAHEIGHNLGMEHDSS 368
Cdd:pfam13583  81 ATLTSWRDSlnyDLAYLT--LMTGPSgqnVGVAWVGALCSSArqnAKASGVARSRDE-WD---IFAHEIGHTFGAVHDCS 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 568954889  369 SCTCG-GINYC------LMS--STYSfNPEFSNCSYSNF 398
Cdd:pfam13583 155 SQGEGlSSSTEdgsgqtIMSyaSTAS-QTAFSPCTIRNI 192
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 307-397 2.19e-07

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 51.86  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889  307 DIAHLFVNHSF-GKFLGLAYVGTVCL-----PSHNCGVDRLLGPNLF----QFAHIIAHEIGHNLGMEHD-------SSS 369
Cdd:pfam13574  72 CLAHLVTMGTFsGGELGLAYVGQICQkgassPKTNTGLSTTTNYGSFnyptQEWDVVAHEVGHNFGATHDcdgsqyaSSG 151

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568954889  370 C-------TCGGINYCLMS-STYSFNPEFSNCSYSN 397
Cdd:pfam13574 152 CernaatsVCSANGSFIMNpASKSNNDLFSPCSISL 187
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 289-408 4.11e-07

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: 51.65  E-value: 4.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 289 LEEFCVWKTLSLNiripNDIA--HLFVNHSFGKFLGLAYVGTVCLPSH-NCGVDRLLGPNLFQFA----HIIAHEIGHNL 361
Cdd:cd04271   82 LSIFSQWRGQQPD----DGNAfwTLMTACPSGSEVGVAWLGQLCRTGAsDQGNETVAGTNVVVRTsnewQVFAHEIGHTF 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 362 GMEHDSSSCTCGGINY-----CLMSST-------YSFNP-------EFSNCSYSNFWT----TYATTNCL 408
Cdd:cd04271  158 GAVHDCTSGTCSDGSVgsqqcCPLSTStcdangqYIMNPssssgitEFSPCTIGNICSllgrNPVRTSCL 227
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 308-394 4.17e-06

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: 48.91  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954889 308 IAHLFVNHSF-GKFLGLAYVGTVCLPSH----------NCGVDRLLGPNLFQF-----------AHII-AHEIGHNLGME 364
Cdd:cd04270  103 LAHLFTYRDFdMGTLGLAYVGSPRDNSAggicekayyySNGKKKYLNTGLTTTvnygkrvptkeSDLVtAHELGHNFGSP 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568954889 365 HDSSSCTC------GGiNYcLM-----SSTYSFNPEFSNCS 394
Cdd:cd04270  183 HDPDIAECapgesqGG-NY-IMyaratSGDKENNKKFSPCS 221
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 321-368 9.37e-05

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 44.26  E-value: 9.37e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568954889 321 LGLAYVGTVClpSHN---CGVDRllgPNLFQFAHIIAHEIGHNLGMEHDSS 368
Cdd:cd04272  119 GGYAYVGGAC--TENrvaMGEDT---PGSYYGVYTMTHELAHLLGAPHDGS 164
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 325-369 2.81e-04

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 42.75  E-value: 2.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568954889 325 YVGTVCL------PSHNCGVDRLLGPNLFqFAHIIAHEIGHNLGMEHDSSS 369
Cdd:cd04327   63 YVGTDALligadaPTMNLGWFTDDTPDPE-FSRVVLHEFGHALGFIHEHQS 112
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 423-460 3.99e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 35.43  E-value: 3.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568954889  423 CGNGVVDDGEQCDCGDRHMCERdqcCNSRCALNDGAAC 460
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTTSGDG---CSATCRLEEGFAC 38
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 337-389 4.79e-03

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


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 38.37  E-value: 4.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568954889  337 GVDRLLGPNLFQFAhiiAHEIGHNLGMEH--DSSSctcgginycLMSSTYSFNPE 389
Cdd:pfam00413  99 GSDPPHGINLFLVA---AHEIGHALGLGHssDPGA---------IMYPTYSPLDS 141
 
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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