|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
147-386 |
6.28e-139 |
|
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: 406.37 E-value: 6.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 147 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTSDEKDPTNPF---RF 219
Cdd:cd04270 1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 220 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 297
Cdd:cd04270 81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 298 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 376
Cdd:cd04270 161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234
|
250
....*....|
gi 1720430081 377 NCFVESGQPI 386
Cdd:cd04270 235 SCFVERSQSF 244
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
171-321 |
1.32e-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: 122.09 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 171 AQISSHVKAIDTIYQTtDFSgirnISFMVKRIRINTTSDEKDPTNPfrfPNIGVEKFLELNSEQ-NHDDYCLAYVFTDRD 249
Cdd:pfam13582 1 ARIVSLVNRANTIYER-DLG----IRLQLAAIIITTSADTPYTSSD---ALEILDELQEVNDTRiGQYGYDLGHLFTGRD 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430081 250 FDdGVLGLAWVGapsgssgGICeksklySDGKKKSLNtgiitvqnYGSHVPPKVSHITFAHEVGHNFGSPHD 321
Cdd:pfam13582 73 GG-GGGGIAYVG-------GVC------NSGSKFGVN--------SGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
393-472 |
1.26e-22 |
|
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: 91.98 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 393 EQGEECDCGYSDQCKDDCCFDANqpegkkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAKEGICNGFTALCP 471
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71
|
.
gi 1720430081 472 A 472
Cdd:smart00050 72 P 72
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
393-472 |
3.02e-20 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 84.99 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 393 EQGEECDCGYSDQCKDD-CCfdanqpEGKKCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRD-DSDCAKEGICNGFTALC 470
Cdd:pfam00200 1 EEGEECDCGSLEECTNDpCC------DAKTCKLKPGAQC--SSGPCCT-NCQFKPAGTVCRPsKDECDLPEYCNGTSAEC 71
|
..
gi 1720430081 471 PA 472
Cdd:pfam00200 72 PP 73
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
2-82 |
1.41e-03 |
|
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: 39.22 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 2 KRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFSHGSVIDGrFEGFIKTRGGTFYIEPAERYIKDRI 74
Cdd:pfam01562 43 TPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPLEKYSREEG 121
|
....*...
gi 1720430081 75 lPFHSVIY 82
Cdd:pfam01562 122 -GHPHVVY 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
147-386 |
6.28e-139 |
|
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: 406.37 E-value: 6.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 147 NTCQLYIQTDHLFFKYYGT--REAVIAQISSHVKAIDTIYQTTDFSG--IRNISFMVKRIRINTTSDEKDPTNPF---RF 219
Cdd:cd04270 1 NTCKLLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGggFKGIGFQIKRIRIHTTPDEVDPGNKFynkSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 220 PNIGVEKFLELNS-EQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPS-GSSGGICEKSKLYSDGKKKSLNTGIITVQNYGS 297
Cdd:cd04270 81 PNWGVEKFLVKLLlEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYSNGKKKYLNTGLTTTVNYGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 298 HVPPKVSHITFAHEVGHNFGSPHDSG-TECTPGESknlgqkENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRN 376
Cdd:cd04270 161 RVPTKESDLVTAHELGHNFGSPHDPDiAECAPGES------QGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSN 234
|
250
....*....|
gi 1720430081 377 NCFVESGQPI 386
Cdd:cd04270 235 SCFVERSQSF 244
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
171-321 |
1.32e-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: 122.09 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 171 AQISSHVKAIDTIYQTtDFSgirnISFMVKRIRINTTSDEKDPTNPfrfPNIGVEKFLELNSEQ-NHDDYCLAYVFTDRD 249
Cdd:pfam13582 1 ARIVSLVNRANTIYER-DLG----IRLQLAAIIITTSADTPYTSSD---ALEILDELQEVNDTRiGQYGYDLGHLFTGRD 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430081 250 FDdGVLGLAWVGapsgssgGICeksklySDGKKKSLNtgiitvqnYGSHVPPKVSHITFAHEVGHNFGSPHD 321
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 ... |
168-372 |
1.01e-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: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 168 AVIAQISSHVKAIDTIYQTTDFSGirNISFmVKRIRINTTSDEKDPTNPFRF-PNIGVEKFLELNSEQNHDDYCLAYVFT 246
Cdd:pfam13574 2 NVTENLVNVVNRVNQIYEPDDINI--NGGL-VNPGEIPATTSASDSGNNYCNsPTTIVRRLNFLSQWRGEQDYCLAHLVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 247 DRDFDDGVLGLAWVGapsgssgGICEKSklYSdgkKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHD----- 321
Cdd:pfam13574 79 MGTFSGGELGLAYVG-------QICQKG--AS---SPKTNTGLSTTTNYGSFNYPTQEWDVVAHEVGHNFGATHDcdgsq 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720430081 322 SGTECTPGESKNLGQKENGNYIMYARATSgdklNNNKFSLCSIRNISQVLE 372
Cdd:pfam13574 147 YASSGCERNAATSVCSANGSFIMNPASKS----NNDLFSPCSISLICDVLG 193
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
147-360 |
3.11e-26 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 106.35 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 147 NTCQLYIQTDHLFFKYYGtREAVIAQISSHVKAIDTIYQTtDFsgirNISFMVKRIRINTTSDEKDPtNPFRFPNIG--V 224
Cdd:pfam13688 3 RTVALLVAADCSYVAAFG-GDAAQANIINMVNTASNVYER-DF----NISLGLVNLTISDSTCPYTP-PACSTGDSSdrL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 225 EKFLELNSEQNHDDYCLAYVFTDRDFDDGvlGLAWVG--APSGSSGGICEKsklysdgkkkslntgiitVQNYGSHVPPK 302
Cdd:pfam13688 76 SEFQDFSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGqlCNSGSAGSVSTR------------------VSGNNVVVSTA 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430081 303 VSHITFAHEVGHNFGSPHD----SGTECTPGESKNLGQkeNGNYIMYARATSgdklNNNKFS 360
Cdd:pfam13688 136 TEWQVFAHEIGHNFGAVHDcdssTSSQCCPPSNSTCPA--GGRYIMNPSSSP----NSTDFS 191
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
393-472 |
1.26e-22 |
|
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: 91.98 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 393 EQGEECDCGYSDQCKDDCCFDANqpegkkCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRDDSD-CAKEGICNGFTALCP 471
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPAT------CKLKPGAQC--ASGPCCD-NCKFKPAGTLCRPSVDeCDLPEYCNGTSADCP 71
|
.
gi 1720430081 472 A 472
Cdd:smart00050 72 P 72
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
393-472 |
3.02e-20 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 84.99 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 393 EQGEECDCGYSDQCKDD-CCfdanqpEGKKCKLKPGKQCspSQGPCCTaQCAFKSKSEKCRD-DSDCAKEGICNGFTALC 470
Cdd:pfam00200 1 EEGEECDCGSLEECTNDpCC------DAKTCKLKPGAQC--SSGPCCT-NCQFKPAGTVCRPsKDECDLPEYCNGTSAEC 71
|
..
gi 1720430081 471 PA 472
Cdd:pfam00200 72 PP 73
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
147-372 |
3.18e-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: 85.93 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 147 NTCQLYIQTDHLFFKYY-GTREAVIAQISSHVKAIDTIYQTTDfsGIRNISFMVKRIRINTTSDEKDPTNPfrfpNIGVE 225
Cdd:cd04267 1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTN--LRLGIRISLEGLQILKGEQFAPPIDS----DASNT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 226 KFL-ELNSEQNHDDYCLAYVFTDRDFDDG-VLGLAWVGA--PSGSSGGICEksklysdgkkkslntgiitvqnygSHVPP 301
Cdd:cd04267 75 LNSfSFWRAEGPIRHDNAVLLTAQDFIEGdILGLAYVGSmcNPYSSVGVVE------------------------DTGFT 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720430081 302 KVSHITFAHEVGHNFGSPHDSGTECTPGESKnlgqkeNGNYIMyarATSGDKLNNNKFSLCSIRNISQVLE 372
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 ... |
151-378 |
2.17e-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: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 151 LYIQTDHLFFKYYG-----TREAVIaQISSHVkaiDTIYQTTdfsgirNISFMVKRI-------RINTTSDEKDPTNPFr 218
Cdd:cd04269 5 LVVVVDNSLYKKYGsnlskVRQRVI-EIVNIV---DSIYRPL------NIRVVLVGLeiwtdkdKISVSGDAGETLNRF- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 219 fpniGVEKFLELNSEQNHDDyclAYVFTDRDFDDGVLGLAWVGapsgssgGICekSKLYSdgkkkslnTGIITvqnYGSH 298
Cdd:cd04269 74 ----LDWKRSNLLPRKPHDN---AQLLTGRDFDGNTVGLAYVG-------GMC--SPKYS--------GGVVQ---DHSR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 299 VPPKVShITFAHEVGHNFGSPHDsGTECTPGESknlgqkengNYIMYARATSGDKlnnnKFSLCSIRNISQVLEKKRNNC 378
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 ... |
146-367 |
2.24e-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: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 146 RNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTdfsgiRNISF-MVKRIRINTTSDEKDPTNPFRFPN-IG 223
Cdd:pfam13583 2 RRVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYGRD-----FNVSLaLISDRDVIYTDSSTDSFNADCSGGdLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 224 VEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGApSGSSGGICEKSKLYSDGKKkslntgiitvqNYGshvppkv 303
Cdd:pfam13583 77 NWRLATLTSWRDSLNYDLAYLTLMTGPSGQNVGVAWVGA-LCSSARQNAKASGVARSRD-----------EWD------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430081 304 shiTFAHEVGHNFGSPHDSGTECTPGESKNlgQKENGNYIM-YARATSGDklnnnKFSLCSIRNI 367
Cdd:pfam13583 138 ---IFAHEIGHTFGAVHDCSSQGEGLSSST--EDGSGQTIMsYASTASQT-----AFSPCTIRNI 192
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
231-364 |
3.62e-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: 62.15 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 231 NSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGiceksklysdgkkkslnTGIITVQNYGshvpPKVSHITFAH 310
Cdd:cd00203 44 LVGVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRG-----------------VGVLQDNQSG----TKEGAQTIAH 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430081 311 EVGHNFGSPHDSGTECTPGESKNLGQKEN----GNYIMYARATSGDKLNNNKFSLCSI 364
Cdd:cd00203 103 ELGHALGFYHDHDRKDRDDYPTIDDTLNAedddYYSVMSYTKGSFSDGQRKDFSQCDI 160
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
153-380 |
5.27e-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: 63.21 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 153 IQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTdFsgirNISFMVKRIRINTTSDEKDPT--NPFRFP---NIGVEKF 227
Cdd:cd04271 7 VAADCSYTKSFGSVEEARRNILNNVNSASQLYESS-F----NISLGLRNLTISDASCPSTAVdsAPWNLPcnsRIDIDDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 228 LELNS----EQNHDDYCLAYVFTDRDFDDGVlGLAWVGApsgssggICEKSKlysdgkkkslntgiiTVQNYGSHVPPKV 303
Cdd:cd04271 82 LSIFSqwrgQQPDDGNAFWTLMTACPSGSEV-GVAWLGQ-------LCRTGA---------------SDQGNETVAGTNV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 304 SHIT------FAHEVGHNFGSPHDsgteCTPGESKNLGQKE-------------NGNYIMYARATSGdklnNNKFSLCSI 364
Cdd:cd04271 139 VVRTsnewqvFAHEIGHTFGAVHD----CTSGTCSDGSVGSqqccplststcdaNGQYIMNPSSSSG----ITEFSPCTI 210
|
250
....*....|....*...
gi 1720430081 365 RNISQVLEKK--RNNCFV 380
Cdd:cd04271 211 GNICSLLGRNpvRTSCLS 228
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
151-378 |
1.56e-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: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 151 LYIQTDHLFFKYYGTREAVIAQ-ISSHVKAIDTIYQTTDFSGIRN-ISFMVKRIRINTTSDekdptnpfrfPNIGVEKFL 228
Cdd:pfam01421 5 LFIVVDKQLFQKMGSDTTVVRQrVFQVVNLVNSIYKELNIRVVLVgLEIWTDEDKIDVSGD----------ANDTLRNFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 229 E-----LNSEQNHDdycLAYVFTDRDFDDGVLGLAWVGapsgssgGICekSKLYSDG--KKKSLNTGIITVqnygshvpp 301
Cdd:pfam01421 75 KwrqeyLKKRKPHD---VAQLLSGVEFGGTTVGAAYVG-------GMC--SLEYSGGvnEDHSKNLESFAV--------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430081 302 kvshiTFAHEVGHNFGSPHD-SGTECTPGESknlgqkenGNYIMYARATSGDKLnnnKFSLCSIRNISQVLEKKRNNC 378
Cdd:pfam01421 134 -----TMAHELGHNLGMQHDdFNGGCKCPPG--------GGCIMNPSAGSSFPR---KFSNCSQEDFEQFLTKQKGAC 195
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
151-371 |
5.81e-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: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 151 LYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRnisFMVKRIRINTTSDEKDPTNPFRFPNIGVEKFLE- 229
Cdd:cd04272 5 LFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKSPRIR---LLLVGITISKDPDFEPYIHPINYGYIDAAETLEn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 230 ----LNSEQNHDDYCLAYVFTDRD---FDDG-----VLGLAWVG-APSGSSGGICEKS-KLYsdgkkkslntgiitvqnY 295
Cdd:cd04272 82 fneyVKKKRDYFNPDVVFLVTGLDmstYSGGslqtgTGGYAYVGgACTENRVAMGEDTpGSY-----------------Y 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720430081 296 GSHvppkvshiTFAHEVGHNFGSPHDSGTECT--PGESKNLGQKENGNYIM-YARATsgdkLNNNKFSLCSIRNISQVL 371
Cdd:cd04272 145 GVY--------TMTHELAHLLGAPHDGSPPPSwvKGHPGSLDCPWDDGYIMsYVVNG----ERQYRFSQCSQRQIRNVF 211
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
194-378 |
1.18e-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: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 194 NISFMVKRIRINttsdEKDPTNPFRFPNIGV--EKFLELNSEQNHDD------YCLAYVFTDRDFD-----DGVLGLAWV 260
Cdd:cd04273 45 SINIVVVRLIVL----EDEESGLLISGNAQKslKSFCRWQKKLNPPNdsdpehHDHAILLTRQDICrsngnCDTLGLAPV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 261 GapsgssgGICEKSKlysdgkKKSLN--TGIITVqnygshvppkvshITFAHEVGHNFGSPHDsgtectpGESKNLGQKE 338
Cdd:cd04273 121 G-------GMCSPSR------SCSINedTGLSSA-------------FTIAHELGHVLGMPHD-------GDGNSCGPEG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720430081 339 NGNYIMyarATSGDKlNNNKF--SLCSIRNISQVLEKKRNNC 378
Cdd:cd04273 168 KDGHIM---SPTLGA-NTGPFtwSKCSRRYLTSFLDTGDGNC 205
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
2-82 |
1.41e-03 |
|
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: 39.22 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430081 2 KRDTSLFSDEFKVET------SNKVLDYDTSH-IYTGHIYGEEGSFSHGSVIDGrFEGFIKTRGGTFYIEPAERYIKDRI 74
Cdd:pfam01562 43 TPNRLLLAPGFTVTYyldggtGVESPPVQTDHcYYQGHVEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPLEKYSREEG 121
|
....*...
gi 1720430081 75 lPFHSVIY 82
Cdd:pfam01562 122 -GHPHVVY 128
|
|
| |
