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Conserved domains on  [gi|150378458|ref|NP_031425|]
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disintegrin and metalloproteinase domain-containing protein 10 preproprotein [Mus musculus]

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 10259607)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family; M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 221-460 1.77e-138

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: 407.53  E-value: 1.77e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 221 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTSDEKDPTNPF---RF 293
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 294 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 371
Cdd:cd04270   81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 372 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 450
Cdd:cd04270  161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234

                        250
                 ....*....|
gi 150378458 451 NCFVESGQPI 460
Cdd:cd04270  235 SCFVERSQSF 244
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 467-546 9.96e-24

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: 95.06  E-value: 9.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458   467 EQGEECDCGYSDQCKDDCCFDANqpegkkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAKEGICNGFTALCP 545
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71


                   .
gi 150378458   546 A 546
Cdd:smart00050  72 P 72
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-156 9.88e-09

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 54.24  E-value: 9.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458   46 HQRAKRAVSHEDQF---LLLDFHAHGRQFNLRMKRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFS 115
Cdd:pfam01562  10 PSRRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 150378458  116 HGSVIDGrFEGFIKTRGGTFYIEPAERYIKDRIlPFHSVIY 156
Cdd:pfam01562  90 ALSTCSG-LRGFIRTENEEYLIEPLEKYSREEG-GHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 221-460 1.77e-138

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: 407.53  E-value: 1.77e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 221 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTSDEKDPTNPF---RF 293
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 294 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 371
Cdd:cd04270   81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 372 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 450
Cdd:cd04270  161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234

                        250
                 ....*....|
gi 150378458 451 NCFVESGQPI 460
Cdd:cd04270  235 SCFVERSQSF 244
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 245-395 4.17e-32

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: 120.94  E-value: 4.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  245 AQISSHVKAIDTIYQTtDFSgirnISFMVKRIRINTTSDEKDPTNPfrfPNIGVEKFLELNSEQ-NHDDYCLAYVFTDRD 323
Cdd:pfam13582   1 ARIVSLVNRANTIYER-DLG----IRLQLAAIIITTSADTPYTSSD---ALEILDELQEVNDTRiGQYGYDLGHLFTGRD 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150378458  324 FDdGVLGLAWVGapsgssgGICeksklySDGKKKSLNtgiitvqnYGSHVPPKVSHITFAHEVGHNFGSPHD 395
Cdd:pfam13582  73 GG-GGGGIAYVG-------GVC------NSGSKFGVN--------SGSGPVGDTGADTFAHEIGHNFGLNHT 122
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 467-546 9.96e-24

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: 95.06  E-value: 9.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458   467 EQGEECDCGYSDQCKDDCCFDANqpegkkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAKEGICNGFTALCP 545
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71


                   .
gi 150378458   546 A 546
Cdd:smart00050  72 P 72
Disintegrin pfam00200
Disintegrin;
467-546 2.70e-21

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 88.07  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  467 EQGEECDCGYSDQCKDD-CCfdanqpEGKKCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRD-DSDCAKEGICNGFTALC 544
Cdd:pfam00200   1 EEGEECDCGSLEECTNDpCC------DAKTCKLKPGAQC--SSGPCCT-NCQFKPAGTVCRPsKDECDLPEYCNGTSAEC 71


                  ..
gi 150378458  545 PA 546
Cdd:pfam00200  72 PP 73
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-156 9.88e-09

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: 54.24  E-value: 9.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458   46 HQRAKRAVSHEDQF---LLLDFHAHGRQFNLRMKRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFS 115
Cdd:pfam01562  10 PSRRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 150378458  116 HGSVIDGrFEGFIKTRGGTFYIEPAERYIKDRIlPFHSVIY 156
Cdd:pfam01562  90 ALSTCSG-LRGFIRTENEEYLIEPLEKYSREEG-GHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 221-460 1.77e-138

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: 407.53  E-value: 1.77e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 221 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTSDEKDPTNPF---RF 293
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 294 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 371
Cdd:cd04270   81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 372 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 450
Cdd:cd04270  161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234

                        250
                 ....*....|
gi 150378458 451 NCFVESGQPI 460
Cdd:cd04270  235 SCFVERSQSF 244
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 245-395 4.17e-32

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: 120.94  E-value: 4.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  245 AQISSHVKAIDTIYQTtDFSgirnISFMVKRIRINTTSDEKDPTNPfrfPNIGVEKFLELNSEQ-NHDDYCLAYVFTDRD 323
Cdd:pfam13582   1 ARIVSLVNRANTIYER-DLG----IRLQLAAIIITTSADTPYTSSD---ALEILDELQEVNDTRiGQYGYDLGHLFTGRD 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150378458  324 FDdGVLGLAWVGapsgssgGICeksklySDGKKKSLNtgiitvqnYGSHVPPKVSHITFAHEVGHNFGSPHD 395
Cdd:pfam13582  73 GG-GGGGIAYVG-------GVC------NSGSKFGVN--------SGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 242-446 1.11e-30

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: 119.27  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  242 AVIAQISSHVKAIDTIYQTTDFSGirNISFmVKRIRINTTSDEKDPTNPFRF-PNIGVEKFLELNSEQNHDDYCLAYVFT 320
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPDDINI--NGGL-VNPGEIPATTSASDSGNNYCNsPTTIVRRLNFLSQWRGEQDYCLAHLVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  321 DRDFDDGVLGLAWVGapsgssgGICEKSklYSdgkKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHD----- 395
Cdd:pfam13574  79 MGTFSGGELGLAYVG-------QICQKG--AS---SPKTNTGLSTTTNYGSFNYPTQEWDVVAHEVGHNFGATHDcdgsq 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150378458  396 SGTECTPGESKNLGQKENGNYIMYARATSgdklNNNKFSLCSIRNISQVLE 446
Cdd:pfam13574 147 YASSGCERNAATSVCSANGSFIMNPASKS----NNDLFSPCSISLICDVLG 193
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
221-434 2.50e-26

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 106.73  E-value: 2.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  221 NTCQLYIQTDHLFFKYYGtREAVIAQISSHVKAIDTIYQTtDFsgirNISFMVKRIRINTTSDEKDPtNPFRFPNIG--V 298
Cdd:pfam13688   3 RTVALLVAADCSYVAAFG-GDAAQANIINMVNTASNVYER-DF----NISLGLVNLTISDSTCPYTP-PACSTGDSSdrL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  299 EKFLELNSEQNHDDYCLAYVFTDRDFDDGvlGLAWVG--APSGSSGGICEKsklysdgkkkslntgiitVQNYGSHVPPK 376
Cdd:pfam13688  76 SEFQDFSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGqlCNSGSAGSVSTR------------------VSGNNVVVSTA 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150378458  377 VSHITFAHEVGHNFGSPHD----SGTECTPGESKNLGQkeNGNYIMYARATSgdklNNNKFS 434
Cdd:pfam13688 136 TEWQVFAHEIGHNFGAVHDcdssTSSQCCPPSNSTCPA--GGRYIMNPSSSP----NSTDFS 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 467-546 9.96e-24

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: 95.06  E-value: 9.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458   467 EQGEECDCGYSDQCKDDCCFDANqpegkkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAKEGICNGFTALCP 545
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71


                   .
gi 150378458   546 A 546
Cdd:smart00050  72 P 72
Disintegrin pfam00200
Disintegrin;
467-546 2.70e-21

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 88.07  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  467 EQGEECDCGYSDQCKDD-CCfdanqpEGKKCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRD-DSDCAKEGICNGFTALC 544
Cdd:pfam00200   1 EEGEECDCGSLEECTNDpCC------DAKTCKLKPGAQC--SSGPCCT-NCQFKPAGTVCRPsKDECDLPEYCNGTSAEC 71


                  ..
gi 150378458  545 PA 546
Cdd:pfam00200  72 PP 73
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 221-446 2.51e-19

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: 86.71  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 221 NTCQLYIQTDHLFFKYY-GTREAVIAQISSHVKAIDTIYQTTDfsGIRNISFMVKRIRINTTSDEKDPTNPfrfpNIGVE 299
Cdd:cd04267    1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTN--LRLGIRISLEGLQILKGEQFAPPIDS----DASNT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 300 KFL-ELNSEQNHDDYCLAYVFTDRDFDDG-VLGLAWVGA--PSGSSGGICEksklysdgkkkslntgiitvqnygSHVPP 375
Cdd:cd04267   75 LNSfSFWRAEGPIRHDNAVLLTAQDFIEGdILGLAYVGSmcNPYSSVGVVE------------------------DTGFT 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150378458 376 KVSHITFAHEVGHNFGSPHDSGTECTPGESKnlgqkeNGNYIMyarATSGDKLNNNKFSLCSIRNISQVLE 446
Cdd:cd04267  131 LLTALTMAHELGHNLGAEHDGGDELAFECDG------GGNYIM---APVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 225-452 2.79e-15

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: 74.96  E-value: 2.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 225 LYIQTDHLFFKYYG-----TREAVIaQISSHVkaiDTIYQTTdfsgirNISFMVKRI-------RINTTSDEKDPTNPFr 292
Cdd:cd04269    5 LVVVVDNSLYKKYGsnlskVRQRVI-EIVNIV---DSIYRPL------NIRVVLVGLeiwtdkdKISVSGDAGETLNRF- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 293 fpniGVEKFLELNSEQNHDDyclAYVFTDRDFDDGVLGLAWVGapsgssgGICekSKLYSdgkkkslnTGIITvqnYGSH 372
Cdd:cd04269   74 ----LDWKRSNLLPRKPHDN---AQLLTGRDFDGNTVGLAYVG-------GMC--SPKYS--------GGVVQ---DHSR 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 373 VPPKVShITFAHEVGHNFGSPHDsGTECTPGESknlgqkengNYIMYARATSGDKlnnnKFSLCSIRNISQVLEKKRNNC 452
Cdd:cd04269  127 NLLLFA-VTMAHELGHNLGMEHD-DGGCTCGRS---------TCIMAPSPSSLTD----AFSNCSYEDYQKFLSRGGGQC 191
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 220-441 2.52e-13

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: 69.57  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  220 RNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTdfsgiRNISF-MVKRIRINTTSDEKDPTNPFRFPN-IG 297
Cdd:pfam13583   2 RRVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYGRD-----FNVSLaLISDRDVIYTDSSTDSFNADCSGGdLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  298 VEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGApSGSSGGICEKSKLYSDGKKkslntgiitvqNYGshvppkv 377
Cdd:pfam13583  77 NWRLATLTSWRDSLNYDLAYLTLMTGPSGQNVGVAWVGA-LCSSARQNAKASGVARSRD-----------EWD------- 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150378458  378 shiTFAHEVGHNFGSPHDSGTECTPGESKNlgQKENGNYIM-YARATSGDklnnnKFSLCSIRNI 441
Cdd:pfam13583 138 ---IFAHEIGHTFGAVHDCSSQGEGLSSST--EDGSGQTIMsYASTASQT-----AFSPCTIRNI 192
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 227-454 1.77e-11

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: 64.75  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 227 IQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTdFsgirNISFMVKRIRINTTSDEKDPT--NPFRFP---NIGVEKF 301
Cdd:cd04271    7 VAADCSYTKSFGSVEEARRNILNNVNSASQLYESS-F----NISLGLRNLTISDASCPSTAVdsAPWNLPcnsRIDIDDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 302 LELNS----EQNHDDYCLAYVFTDRDFDDGVlGLAWVGApsgssggICEKSKlysdgkkkslntgiiTVQNYGSHVPPKV 377
Cdd:cd04271   82 LSIFSqwrgQQPDDGNAFWTLMTACPSGSEV-GVAWLGQ-------LCRTGA---------------SDQGNETVAGTNV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 378 SHIT------FAHEVGHNFGSPHDsgteCTPGESKNLGQKE-------------NGNYIMYARATSGdklnNNKFSLCSI 438
Cdd:cd04271  139 VVRTsnewqvFAHEIGHTFGAVHD----CTSGTCSDGSVGSqqccplststcdaNGQYIMNPSSSSG----ITEFSPCTI 210

                        250
                 ....*....|....*...
gi 150378458 439 RNISQVLEKK--RNNCFV 454
Cdd:cd04271  211 GNICSLLGRNpvRTSCLS 228
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 305-438 4.72e-11

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: 61.77  E-value: 4.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 305 NSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGiceksklysdgkkkslnTGIITVQNYGshvpPKVSHITFAH 384
Cdd:cd00203   44 LVGVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRG-----------------VGVLQDNQSG----TKEGAQTIAH 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 150378458 385 EVGHNFGSPHDSGTECTPGESKNLGQKEN----GNYIMYARATSGDKLNNNKFSLCSI 438
Cdd:cd00203  103 ELGHALGFYHDHDRKDRDDYPTIDDTLNAedddYYSVMSYTKGSFSDGQRKDFSQCDI 160
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-156 9.88e-09

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: 54.24  E-value: 9.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458   46 HQRAKRAVSHEDQF---LLLDFHAHGRQFNLRMKRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFS 115
Cdd:pfam01562  10 PSRRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 150378458  116 HGSVIDGrFEGFIKTRGGTFYIEPAERYIKDRIlPFHSVIY 156
Cdd:pfam01562  90 ALSTCSG-LRGFIRTENEEYLIEPLEKYSREEG-GHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 225-452 2.14e-08

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: 55.00  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  225 LYIQTDHLFFKYYGTREAVIAQ-ISSHVKAIDTIYQTTDFSGIRN-ISFMVKRIRINTTSDekdptnpfrfPNIGVEKFL 302
Cdd:pfam01421   5 LFIVVDKQLFQKMGSDTTVVRQrVFQVVNLVNSIYKELNIRVVLVgLEIWTDEDKIDVSGD----------ANDTLRNFL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458  303 E-----LNSEQNHDdycLAYVFTDRDFDDGVLGLAWVGapsgssgGICekSKLYSDG--KKKSLNTGIITVqnygshvpp 375
Cdd:pfam01421  75 KwrqeyLKKRKPHD---VAQLLSGVEFGGTTVGAAYVG-------GMC--SLEYSGGvnEDHSKNLESFAV--------- 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150378458  376 kvshiTFAHEVGHNFGSPHD-SGTECTPGESknlgqkenGNYIMYARATSGDKLnnnKFSLCSIRNISQVLEKKRNNC 452
Cdd:pfam01421 134 -----TMAHELGHNLGMQHDdFNGGCKCPPG--------GGCIMNPSAGSSFPR---KFSNCSQEDFEQFLTKQKGAC 195
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 225-445 7.24e-08

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 53.89  E-value: 7.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 225 LYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRnisFMVKRIRINTTSDEKDPTNPFRFPNIGVEKFLE- 303
Cdd:cd04272    5 LFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKSPRIR---LLLVGITISKDPDFEPYIHPINYGYIDAAETLEn 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 304 ----LNSEQNHDDYCLAYVFTDRD---FDDG-----VLGLAWVG-APSGSSGGICEKS-KLYsdgkkkslntgiitvqnY 369
Cdd:cd04272   82 fneyVKKKRDYFNPDVVFLVTGLDmstYSGGslqtgTGGYAYVGgACTENRVAMGEDTpGSY-----------------Y 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150378458 370 GSHvppkvshiTFAHEVGHNFGSPHDSGTECT--PGESKNLGQKENGNYIM-YARATsgdkLNNNKFSLCSIRNISQVL 445
Cdd:cd04272  145 GVY--------TMTHELAHLLGAPHDGSPPPSwvKGHPGSLDCPWDDGYIMsYVVNG----ERQYRFSQCSQRQIRNVF 211
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 268-452 1.39e-05

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: 46.85  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 268 NISFMVKRIRINttsdEKDPTNPFRFPNIGV--EKFLELNSEQNHDD------YCLAYVFTDRDFD-----DGVLGLAWV 334
Cdd:cd04273   45 SINIVVVRLIVL----EDEESGLLISGNAQKslKSFCRWQKKLNPPNdsdpehHDHAILLTRQDICrsngnCDTLGLAPV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150378458 335 GapsgssgGICEKSKlysdgkKKSLN--TGIITVqnygshvppkvshITFAHEVGHNFGSPHDsgtectpGESKNLGQKE 412
Cdd:cd04273  121 G-------GMCSPSR------SCSINedTGLSSA-------------FTIAHELGHVLGMPHD-------GDGNSCGPEG 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 150378458 413 NGNYIMyarATSGDKlNNNKF--SLCSIRNISQVLEKKRNNC 452
Cdd:cd04273  168 KDGHIM---SPTLGA-NTGPFtwSKCSRRYLTSFLDTGDGNC 205
 
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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