|
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
|
|
| |
