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Conserved domains on  [gi|4557251|ref|NP_001101|]
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disintegrin and metalloproteinase domain-containing protein 10 isoform 1 preproprotein [Homo sapiens]

Protein Classification

ZnMc_TACE_like and DISIN domain-containing protein( domain architecture ID 10259607)

protein containing domains Pep_M12B_propep, ZnMc_TACE_like, and DISIN

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 ...
 220-459 2.28e-137

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: 404.45  E-value: 2.28e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  220 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTADEKDPTNPF---RF 292
Cdd:cd04270   1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  293 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 370
Cdd:cd04270  81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  371 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 449
Cdd:cd04270 161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234

                       250
                ....*....|
gi 4557251  450 NCFVESGQPI 459
Cdd:cd04270 235 SCFVERSQSF 244
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 466-545 6.67e-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: 95.84  E-value: 6.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251     466 EQGEECDCGYSDQCKDECCFDANqpegrkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAREGICNGFTALCP 544
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71


                   .
gi 4557251     545 A 545
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 6.02e-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: 54.63  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251     46 HQRAKRAVSHEDQF---LRLDFHAHGRHFNLRMKRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFS 115
Cdd:pfam01562  10 PSRRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4557251    116 HGSVIDGrFEGFIQTRGGTFYVEPAERYIKDRTlPFHSVIY 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 ...
 220-459 2.28e-137

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: 404.45  E-value: 2.28e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  220 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTADEKDPTNPF---RF 292
Cdd:cd04270   1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  293 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 370
Cdd:cd04270  81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  371 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 449
Cdd:cd04270 161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234

                       250
                ....*....|
gi 4557251  450 NCFVESGQPI 459
Cdd:cd04270 235 SCFVERSQSF 244
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 244-394 2.58e-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: 121.32  E-value: 2.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    244 AQISSHVKAIDTIYQTtDFSgirnISFMVKRIRINTTADEKDPTNPfrfPNIGVEKFLELNSEQ-NHDDYCLAYVFTDRD 322
Cdd:pfam13582   1 ARIVSLVNRANTIYER-DLG----IRLQLAAIIITTSADTPYTSSD---ALEILDELQEVNDTRiGQYGYDLGHLFTGRD 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557251    323 FDdGVLGLAWVGapsgssgGICeksklySDGKKKSLNtgiitvqnYGSHVPPKVSHITFAHEVGHNFGSPHD 394
Cdd:pfam13582  73 GG-GGGGIAYVG-------GVC------NSGSKFGVN--------SGSGPVGDTGADTFAHEIGHNFGLNHT 122
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 466-545 6.67e-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: 95.84  E-value: 6.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251     466 EQGEECDCGYSDQCKDECCFDANqpegrkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAREGICNGFTALCP 544
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71


                   .
gi 4557251     545 A 545
Cdd:smart00050  72 P 72
Disintegrin pfam00200
Disintegrin;
466-545 1.38e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 86.14  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    466 EQGEECDCGYSDQC-KDECCfdanqpEGRKCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRD-DSDCAREGICNGFTALC 543
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCC------DAKTCKLKPGAQC--SSGPCCT-NCQFKPAGTVCRPsKDECDLPEYCNGTSAEC 71


                  ..
gi 4557251    544 PA 545
Cdd:pfam00200  72 PP 73
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-156 6.02e-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: 54.63  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251     46 HQRAKRAVSHEDQF---LRLDFHAHGRHFNLRMKRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFS 115
Cdd:pfam01562  10 PSRRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4557251    116 HGSVIDGrFEGFIQTRGGTFYVEPAERYIKDRTlPFHSVIY 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 ...
 220-459 2.28e-137

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: 404.45  E-value: 2.28e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  220 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTADEKDPTNPF---RF 292
Cdd:cd04270   1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  293 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 370
Cdd:cd04270  81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  371 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 449
Cdd:cd04270 161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234

                       250
                ....*....|
gi 4557251  450 NCFVESGQPI 459
Cdd:cd04270 235 SCFVERSQSF 244
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 244-394 2.58e-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: 121.32  E-value: 2.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    244 AQISSHVKAIDTIYQTtDFSgirnISFMVKRIRINTTADEKDPTNPfrfPNIGVEKFLELNSEQ-NHDDYCLAYVFTDRD 322
Cdd:pfam13582   1 ARIVSLVNRANTIYER-DLG----IRLQLAAIIITTSADTPYTSSD---ALEILDELQEVNDTRiGQYGYDLGHLFTGRD 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557251    323 FDdGVLGLAWVGapsgssgGICeksklySDGKKKSLNtgiitvqnYGSHVPPKVSHITFAHEVGHNFGSPHD 394
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 ...
 241-445 7.22e-31

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: 119.66  E-value: 7.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    241 AVIAQISSHVKAIDTIYQTTDFSGirNISFmVKRIRINTTADEKDPTNPFRF-PNIGVEKFLELNSEQNHDDYCLAYVFT 319
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPDDINI--NGGL-VNPGEIPATTSASDSGNNYCNsPTTIVRRLNFLSQWRGEQDYCLAHLVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    320 DRDFDDGVLGLAWVGapsgssgGICEKSklYSdgkKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHD----- 394
Cdd:pfam13574  79 MGTFSGGELGLAYVG-------QICQKG--AS---SPKTNTGLSTTTNYGSFNYPTQEWDVVAHEVGHNFGATHDcdgsq 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 4557251    395 SGTECTPGESKNLGQKENGNYIMYARATSgdklNNNKFSLCSIRNISQVLE 445
Cdd:pfam13574 147 YASSGCERNAATSVCSANGSFIMNPASKS----NNDLFSPCSISLICDVLG 193
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
220-433 1.39e-25

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 104.42  E-value: 1.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    220 NTCQLYIQTDHLFFKYYGtREAVIAQISSHVKAIDTIYQTtDFsgirNISFMVKRIRINTTADEKDPtNPFRFPNIG--V 297
Cdd:pfam13688   3 RTVALLVAADCSYVAAFG-GDAAQANIINMVNTASNVYER-DF----NISLGLVNLTISDSTCPYTP-PACSTGDSSdrL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    298 EKFLELNSEQNHDDYCLAYVFTDRDFDDGvlGLAWVG--APSGSSGGICEKsklysdgkkkslntgiitVQNYGSHVPPK 375
Cdd:pfam13688  76 SEFQDFSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGqlCNSGSAGSVSTR------------------VSGNNVVVSTA 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557251    376 VSHITFAHEVGHNFGSPHD----SGTECTPGESKNLGQkeNGNYIMYARATSgdklNNNKFS 433
Cdd:pfam13688 136 TEWQVFAHEIGHNFGAVHDcdssTSSQCCPPSNSTCPA--GGRYIMNPSSSP----NSTDFS 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 466-545 6.67e-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: 95.84  E-value: 6.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251     466 EQGEECDCGYSDQCKDECCFDANqpegrkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAREGICNGFTALCP 544
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71


                   .
gi 4557251     545 A 545
Cdd:smart00050  72 P 72
Disintegrin pfam00200
Disintegrin;
466-545 1.38e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 86.14  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    466 EQGEECDCGYSDQC-KDECCfdanqpEGRKCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRD-DSDCAREGICNGFTALC 543
Cdd:pfam00200   1 EEGEECDCGSLEECtNDPCC------DAKTCKLKPGAQC--SSGPCCT-NCQFKPAGTVCRPsKDECDLPEYCNGTSAEC 71


                  ..
gi 4557251    544 PA 545
Cdd:pfam00200  72 PP 73
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 220-445 1.26e-18

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: 84.39  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  220 NTCQLYIQTDHLFFKYY-GTREAVIAQISSHVKAIDTIYQTTDfsGIRNISFMVKRIRINTTADEKDPTNPfrfpNIGVE 298
Cdd:cd04267   1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTN--LRLGIRISLEGLQILKGEQFAPPIDS----DASNT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  299 KFL-ELNSEQNHDDYCLAYVFTDRDFDDG-VLGLAWVGA--PSGSSGGICEksklysdgkkkslntgiitvqnygSHVPP 374
Cdd:cd04267  75 LNSfSFWRAEGPIRHDNAVLLTAQDFIEGdILGLAYVGSmcNPYSSVGVVE------------------------DTGFT 130

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557251  375 KVSHITFAHEVGHNFGSPHDSGTECTPGESKnlgqkeNGNYIMyarATSGDKLNNNKFSLCSIRNISQVLE 445
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 ...
 224-451 1.15e-14

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: 73.03  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  224 LYIQTDHLFFKYYG-----TREAVIaQISSHVkaiDTIYQTTdfsgirNISFMVKRI-------RINTTADEKDPTNPFr 291
Cdd:cd04269   5 LVVVVDNSLYKKYGsnlskVRQRVI-EIVNIV---DSIYRPL------NIRVVLVGLeiwtdkdKISVSGDAGETLNRF- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  292 fpniGVEKFLELNSEQNHDDyclAYVFTDRDFDDGVLGLAWVGapsgssgGICekSKLYSdgkkkslnTGIITvqnYGSH 371
Cdd:cd04269  74 ----LDWKRSNLLPRKPHDN---AQLLTGRDFDGNTVGLAYVG-------GMC--SPKYS--------GGVVQ---DHSR 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  372 VPPKVShITFAHEVGHNFGSPHDsGTECTPGESknlgqkengNYIMYARATSGDKlnnnKFSLCSIRNISQVLEKKRNNC 451
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 ...
 224-440 8.49e-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: 68.03  E-value: 8.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    224 LYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTdfsgiRNISF-MVKRIRINTTADEKDPTNPFRFPN-IGVEKFL 301
Cdd:pfam13583   7 VAVATDCTYSASFGSVDELRANINATVTTANEVYGRD-----FNVSLaLISDRDVIYTDSSTDSFNADCSGGdLGNWRLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    302 ELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGApSGSSGGICEKSKLYSDGKKkslntgiitvqNYGshvppkvshiTF 381
Cdd:pfam13583  82 TLTSWRDSLNYDLAYLTLMTGPSGQNVGVAWVGA-LCSSARQNAKASGVARSRD-----------EWD----------IF 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    382 AHEVGHNFGSPHDSGTECTPGESKNlgQKENGNYIM-YARATSGDklnnnKFSLCSIRNI 440
Cdd:pfam13583 140 AHEIGHTFGAVHDCSSQGEGLSSST--EDGSGQTIMsYASTASQT-----AFSPCTIRNI 192
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 226-453 3.93e-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: 63.59  E-value: 3.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  226 IQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTdFsgirNISFMVKRIRIN-----TTADEKDPTNPFRFPNIGVEKF 300
Cdd:cd04271   7 VAADCSYTKSFGSVEEARRNILNNVNSASQLYESS-F----NISLGLRNLTISdascpSTAVDSAPWNLPCNSRIDIDDR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  301 LELNS----EQNHDDYCLAYVFTDRDFDDGVlGLAWVGApsgssggICEKSKlysdgkkkslntgiiTVQNYGSHVPPKV 376
Cdd:cd04271  82 LSIFSqwrgQQPDDGNAFWTLMTACPSGSEV-GVAWLGQ-------LCRTGA---------------SDQGNETVAGTNV 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  377 SHIT------FAHEVGHNFGSPHDsgteCTPGESKNLGQKE-------------NGNYIMYARATSGdklnNNKFSLCSI 437
Cdd:cd04271 139 VVRTsnewqvFAHEIGHTFGAVHD----CTSGTCSDGSVGSqqccplststcdaNGQYIMNPSSSSG----ITEFSPCTI 210

                       250
                ....*....|....*...
gi 4557251  438 RNISQVLEKK--RNNCFV 453
Cdd:cd04271 211 GNICSLLGRNpvRTSCLS 228
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 304-437 6.85e-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: 61.38  E-value: 6.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  304 NSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGiceksklysdgkkkslnTGIITVQNYGshvpPKVSHITFAH 383
Cdd:cd00203  44 LVGVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRG-----------------VGVLQDNQSG----TKEGAQTIAH 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557251  384 EVGHNFGSPHDSGTECTPGESKNLGQKEN----GNYIMYARATSGDKLNNNKFSLCSI 437
Cdd:cd00203 103 ELGHALGFYHDHDRKDRDDYPTIDDTLNAedddYYSVMSYTKGSFSDGQRKDFSQCDI 160
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-156 6.02e-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: 54.63  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251     46 HQRAKRAVSHEDQF---LRLDFHAHGRHFNLRMKRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFS 115
Cdd:pfam01562  10 PSRRRRSLASESTYldtLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 4557251    116 HGSVIDGrFEGFIQTRGGTFYVEPAERYIKDRTlPFHSVIY 156
Cdd:pfam01562  90 ALSTCSG-LRGFIRTENEEYLIEPLEKYSREEG-GHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 224-451 6.59e-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: 53.46  E-value: 6.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    224 LYIQTDHLFFKYYGTREAVIAQ-ISSHVKAIDTIYQTTDFSGIRN-ISFMVKRIRINTTADekdptnpfrfPNIGVEKFL 301
Cdd:pfam01421   5 LFIVVDKQLFQKMGSDTTVVRQrVFQVVNLVNSIYKELNIRVVLVgLEIWTDEDKIDVSGD----------ANDTLRNFL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251    302 E-----LNSEQNHDdycLAYVFTDRDFDDGVLGLAWVGapsgssgGICekSKLYSDG--KKKSLNTGIITVqnygshvpp 374
Cdd:pfam01421  75 KwrqeyLKKRKPHD---VAQLLSGVEFGGTTVGAAYVG-------GMC--SLEYSGGvnEDHSKNLESFAV--------- 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557251    375 kvshiTFAHEVGHNFGSPHD-SGTECTPGESknlgqkenGNYIMYARATSGDKLnnnKFSLCSIRNISQVLEKKRNNC 451
Cdd:pfam01421 134 -----TMAHELGHNLGMQHDdFNGGCKCPPG--------GGCIMNPSAGSSFPR---KFSNCSQEDFEQFLTKQKGAC 195
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 224-444 7.17e-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: 7.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  224 LYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRnisFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLE- 302
Cdd:cd04272   5 LFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKSPRIR---LLLVGITISKDPDFEPYIHPINYGYIDAAETLEn 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  303 ----LNSEQNHDDYCLAYVFTDRD---FDDG-----VLGLAWVG-APSGSSGGICEKS-KLYsdgkkkslntgiitvqnY 368
Cdd:cd04272  82 fneyVKKKRDYFNPDVVFLVTGLDmstYSGGslqtgTGGYAYVGgACTENRVAMGEDTpGSY-----------------Y 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557251  369 GSHvppkvshiTFAHEVGHNFGSPHDSGTECT--PGESKNLGQKENGNYIM-YARATsgdkLNNNKFSLCSIRNISQVL 444
Cdd:cd04272 145 GVY--------TMTHELAHLLGAPHDGSPPPSwvKGHPGSLDCPWDDGYIMsYVVNG----ERQYRFSQCSQRQIRNVF 211
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 267-451 1.76e-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: 46.46  E-value: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  267 NISFMVKRIRINttadEKDPTNPFRFPNIGV--EKFLELNSEQNHDD------YCLAYVFTDRDFD-----DGVLGLAWV 333
Cdd:cd04273  45 SINIVVVRLIVL----EDEESGLLISGNAQKslKSFCRWQKKLNPPNdsdpehHDHAILLTRQDICrsngnCDTLGLAPV 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557251  334 GapsgssgGICEKSKlysdgkKKSLN--TGIITVqnygshvppkvshITFAHEVGHNFGSPHDsgtectpGESKNLGQKE 411
Cdd:cd04273 121 G-------GMCSPSR------SCSINedTGLSSA-------------FTIAHELGHVLGMPHD-------GDGNSCGPEG 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4557251  412 NGNYIMyarATSGDKlNNNKF--SLCSIRNISQVLEKKRNNC 451
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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