|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
410-677 |
8.86e-116 |
|
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: 359.77 E-value: 8.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 410 NTCSLYIQTDPLIWRHIREGIadhdrgrkyevdektREEITSLIAHHVTAVNYIYRNTKFDGRtEHRNIRFEVQRIKIDD 489
Cdd:cd04270 1 NTCKLLLVADHRFYKYMGRGE---------------EETTINYLISHIDRVDDIYRNTDWDGG-GFKGIGFQIKRIRIHT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 490 DSACRNSYNGPHNaFCNEHMDVSNFLNLHSLEDHSDF-CLAYVFTYRDFTGGTLGLAWVASAS-GASGGICEKYKTYTet 567
Cdd:cd04270 65 TPDEVDPGNKFYN-KSFPNWGVEKFLVKLLLEQFSDDvCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYS-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 568 vggqyQSTKRSLNTGIITFVNYNSRVPPKVSQLTLAHEIGHNFGSPHDYP-QECRPGGL-NGNYIMFASATSGDRPNNSK 645
Cdd:cd04270 142 -----NGKKKYLNTGLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDiAECAPGESqGGNYIMYARATSGDKENNKK 216
|
250 260 270
....*....|....*....|....*....|..
gi 281364977 646 FSPCSIRNISNVLDVLvgntKRDCFKASEGAF 677
Cdd:cd04270 217 FSPCSKKSISKVLEVK----SNSCFVERSQSF 244
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
445-658 |
3.19e-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: 372637 Cd Length: 193 Bit Score: 124.28 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 445 TREEITSLIAHhvtaVNYIYRNTKFDGRTEHRNIrfevqrIKIDDDSacrnSYNGPHNAFCNEHMDVSNFLN-LHSLEDH 523
Cdd:pfam13574 3 VTENLVNVVNR----VNQIYEPDDININGGLVNP------GEIPATT----SASDSGNNYCNSPTTIVRRLNfLSQWRGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 524 SDFCLAYVFTYRDFTGGTLGLAWVasasgasGGICEKyktytetvggqyQSTKRSLNTGIITFVNYNSRVPPKVSQLTLA 603
Cdd:pfam13574 69 QDYCLAHLVTMGTFSGGELGLAYV-------GQICQK------------GASSPKTNTGLSTTTNYGSFNYPTQEWDVVA 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281364977 604 HEIGHNFGSPHDYP--QECRPGGL----------NGNYIMFASATSgdrpNNSKFSPCSIRNISNVL 658
Cdd:pfam13574 130 HEVGHNFGATHDCDgsQYASSGCErnaatsvcsaNGSFIMNPASKS----NNDLFSPCSISLICDVL 192
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
684-776 |
1.74e-18 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 80.75 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 684 ESGEECDCGFNEEECKDKCCYPrliseydqslnssaKGCTRRAKTQCspSQGPCClsNSCTFVPTSYhqKCKEET-ECSW 762
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDA--------------KTCKLKPGAQC--SSGPCC--TNCQFKPAGT--VCRPSKdECDL 60
|
90
....*....|....
gi 281364977 763 SSTCNGTTAECPEP 776
Cdd:pfam00200 61 PEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
684-778 |
3.53e-16 |
|
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: 74.26 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 684 ESGEECDCGFnEEECKDKCCYPrliseydqslnssaKGCTRRAKTQCspSQGPCClsNSCTFVPTSYhqKCKE-ETECSW 762
Cdd:smart00050 1 EEGEECDCGS-PKECTDPCCDP--------------ATCKLKPGAQC--ASGPCC--DNCKFKPAGT--LCRPsVDECDL 59
|
90
....*....|....*.
gi 281364977 763 SSTCNGTTAECPEPRH 778
Cdd:smart00050 60 PEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
54-149 |
1.76e-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: 39.60 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 54 IRASHNRARRSVTKDQY----VHLKFASHGRDFHLRLKRDLNTFSNklDF----YDSKGPIDVSTDHI-----YEGEVIG 120
Cdd:pfam01562 6 VRLDPSRRRRSLASESTyldtLSYRLAAFGKKFHLHLTPNRLLLAP--GFtvtyYLDGGTGVESPPVQtdhcyYQGHVEG 83
|
90 100
....*....|....*....|....*....
gi 281364977 121 DRNSYVFGSIHNGvFEGKIITERDAYYVE 149
Cdd:pfam01562 84 HPDSSVALSTCSG-LRGFIRTENEEYLIE 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
410-677 |
8.86e-116 |
|
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: 359.77 E-value: 8.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 410 NTCSLYIQTDPLIWRHIREGIadhdrgrkyevdektREEITSLIAHHVTAVNYIYRNTKFDGRtEHRNIRFEVQRIKIDD 489
Cdd:cd04270 1 NTCKLLLVADHRFYKYMGRGE---------------EETTINYLISHIDRVDDIYRNTDWDGG-GFKGIGFQIKRIRIHT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 490 DSACRNSYNGPHNaFCNEHMDVSNFLNLHSLEDHSDF-CLAYVFTYRDFTGGTLGLAWVASAS-GASGGICEKYKTYTet 567
Cdd:cd04270 65 TPDEVDPGNKFYN-KSFPNWGVEKFLVKLLLEQFSDDvCLAHLFTYRDFDMGTLGLAYVGSPRdNSAGGICEKAYYYS-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 568 vggqyQSTKRSLNTGIITFVNYNSRVPPKVSQLTLAHEIGHNFGSPHDYP-QECRPGGL-NGNYIMFASATSGDRPNNSK 645
Cdd:cd04270 142 -----NGKKKYLNTGLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDiAECAPGESqGGNYIMYARATSGDKENNKK 216
|
250 260 270
....*....|....*....|....*....|..
gi 281364977 646 FSPCSIRNISNVLDVLvgntKRDCFKASEGAF 677
Cdd:cd04270 217 FSPCSKKSISKVLEVK----SNSCFVERSQSF 244
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
445-658 |
3.19e-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: 372637 Cd Length: 193 Bit Score: 124.28 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 445 TREEITSLIAHhvtaVNYIYRNTKFDGRTEHRNIrfevqrIKIDDDSacrnSYNGPHNAFCNEHMDVSNFLN-LHSLEDH 523
Cdd:pfam13574 3 VTENLVNVVNR----VNQIYEPDDININGGLVNP------GEIPATT----SASDSGNNYCNSPTTIVRRLNfLSQWRGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 524 SDFCLAYVFTYRDFTGGTLGLAWVasasgasGGICEKyktytetvggqyQSTKRSLNTGIITFVNYNSRVPPKVSQLTLA 603
Cdd:pfam13574 69 QDYCLAHLVTMGTFSGGELGLAYV-------GQICQK------------GASSPKTNTGLSTTTNYGSFNYPTQEWDVVA 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281364977 604 HEIGHNFGSPHDYP--QECRPGGL----------NGNYIMFASATSgdrpNNSKFSPCSIRNISNVL 658
Cdd:pfam13574 130 HEVGHNFGATHDCDgsQYASSGCErnaatsvcsaNGSFIMNPASKS----NNDLFSPCSISLICDVL 192
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
408-647 |
2.36e-20 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 90.17 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 408 NKNTCSLYIQTDpliwrhiregiadhDRGRKYEVDEKTREEITSLIAhhvTAVNYIYRNTkfdgrtehrNIRFEVQRIKI 487
Cdd:pfam13688 1 STRTVALLVAAD--------------CSYVAAFGGDAAQANIINMVN---TASNVYERDF---------NISLGLVNLTI 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 488 DDdsacrnsYNGPHNAFCNEHMDVSNFLN----LHSLEDHSDFCLAYVFTYRDFTGGtlGLAWVAS--ASGASGGICEKY 561
Cdd:pfam13688 55 SD-------STCPYTPPACSTGDSSDRLSefqdFSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQlcNSGSAGSVSTRV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 562 ktytetvggqyqstkrslntgiitfVNYNSRVPPKVSQLTLAHEIGHNFGSPHD-----YPQECRPGGL----NGNYIMF 632
Cdd:pfam13688 126 -------------------------SGNNVVVSTATEWQVFAHEIGHNFGAVHDcdsstSSQCCPPSNStcpaGGRYIMN 180
|
250
....*....|....*
gi 281364977 633 ASATsgdrPNNSKFS 647
Cdd:pfam13688 181 PSSS----PNSTDFS 191
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
684-776 |
1.74e-18 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 80.75 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 684 ESGEECDCGFNEEECKDKCCYPrliseydqslnssaKGCTRRAKTQCspSQGPCClsNSCTFVPTSYhqKCKEET-ECSW 762
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDA--------------KTCKLKPGAQC--SSGPCC--TNCQFKPAGT--VCRPSKdECDL 60
|
90
....*....|....
gi 281364977 763 SSTCNGTTAECPEP 776
Cdd:pfam00200 61 PEYCNGTSAECPPD 74
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
430-659 |
3.46e-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: 84.01 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 430 IADHDRGRKYEVDEktrEEITSLIAHHVTAVNYIYRNTKFDgrtehRNIRF---EVQRIKIDDDsacrnsynGPHNAFcn 506
Cdd:cd04267 8 VADHRMVSYFNSDE---NILQAYITELINIANSIYRSTNLR-----LGIRIsleGLQILKGEQF--------APPIDS-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 507 ehmDVSNFLNLHSLEDH---SDFCLAYVFTYRDFT-GGTLGLAWVasasgasGGICEKYktytetvggqyqstkrsLNTG 582
Cdd:cd04267 70 ---DASNTLNSFSFWRAegpIRHDNAVLLTAQDFIeGDILGLAYV-------GSMCNPY-----------------SSVG 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281364977 583 IITFVNYNsrvppKVSQLTLAHEIGHNFGSPHDYPQECR-PGGLNGNYIMfasATSGDRPNNSKFSPCSIRNISNVLD 659
Cdd:cd04267 123 VVEDTGFT-----LLTALTMAHELGHNLGAEHDGGDELAfECDGGGNYIM---APVDSGLNSYRFSQCSIGSIREFLD 192
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
453-615 |
1.65e-16 |
|
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: 77.03 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 453 IAHHVTAVNYIYRntkfdgrTEHrNIRFEVQRIKIDDDsACRNSYNGPHNAFCNEHMDvsnflNLHSLEDHSDFCLAYVF 532
Cdd:pfam13582 3 IVSLVNRANTIYE-------RDL-GIRLQLAAIIITTS-ADTPYTSSDALEILDELQE-----VNDTRIGQYGYDLGHLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 533 TYRDFtGGTLGLAWVasasgasGGICekyktytetvggqyQSTKRSLntgiitfVNYNSRVPPKVSQLTLAHEIGHNFGS 612
Cdd:pfam13582 69 TGRDG-GGGGGIAYV-------GGVC--------------NSGSKFG-------VNSGSGPVGDTGADTFAHEIGHNFGL 119
|
...
gi 281364977 613 PHD 615
Cdd:pfam13582 120 NHT 122
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
684-778 |
3.53e-16 |
|
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: 74.26 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 684 ESGEECDCGFnEEECKDKCCYPrliseydqslnssaKGCTRRAKTQCspSQGPCClsNSCTFVPTSYhqKCKE-ETECSW 762
Cdd:smart00050 1 EEGEECDCGS-PKECTDPCCDP--------------ATCKLKPGAQC--ASGPCC--DNCKFKPAGT--LCRPsVDECDL 59
|
90
....*....|....*.
gi 281364977 763 SSTCNGTTAECPEPRH 778
Cdd:smart00050 60 PEYCNGTSADCPPDPY 75
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
529-658 |
3.34e-11 |
|
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: 63.79 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 529 AYVFTYRDFTGGTLGLAWVasasgasGGICekyktytetvggqyqSTKRSLntGIITFVNYNsrvPPKVSqLTLAHEIGH 608
Cdd:cd04269 90 AQLLTGRDFDGNTVGLAYV-------GGMC---------------SPKYSG--GVVQDHSRN---LLLFA-VTMAHELGH 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 281364977 609 NFGSPHDyPQECRPGGlnGNYIMFASATSGdrpnNSKFSPCSIRNISNVL 658
Cdd:cd04269 142 NLGMEHD-DGGCTCGR--STCIMAPSPSSL----TDAFSNCSYEDYQKFL 184
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
488-651 |
5.04e-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: 62.54 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 488 DDDSACRNSYNGPHNAFCNEHMDV-SNFLNLH---SLEDHSDFCLAYVFTYRDFTGGTLGLAWVASASGASGGicekykt 563
Cdd:cd00203 10 DDRDVEEENLSAQIQSLILIAMQIwRDYLNIRfvlVGVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRG------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 564 ytetvggqyqstkrslnTGIITFVNYNsrvpPKVSQLTLAHEIGHNFGSPHDYPQECRPGGLN-----------GNYIMF 632
Cdd:cd00203 83 -----------------VGVLQDNQSG----TKEGAQTIAHELGHALGFYHDHDRKDRDDYPTiddtlnaedddYYSVMS 141
|
170
....*....|....*....
gi 281364977 633 ASATSGDRPNNSKFSPCSI 651
Cdd:cd00203 142 YTKGSFSDGQRKDFSQCDI 160
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
445-654 |
5.20e-10 |
|
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: 60.90 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 445 TREEITSLIAHHVTAVNYIYRNTkFdgrtehrNIRFEVQRIKIDDDSACR-NSYNGPHNAFCNEHMDVSNFLNLHS--LE 521
Cdd:cd04271 19 SVEEARRNILNNVNSASQLYESS-F-------NISLGLRNLTISDASCPStAVDSAPWNLPCNSRIDIDDRLSIFSqwRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 522 DHSDFCLAYVFTYRDF-TGGTLGLAWVasasgasGGICekyKTYTETVGGQYQSTkrslnTGIITfVNYNSRvppkvsqL 600
Cdd:cd04271 91 QQPDDGNAFWTLMTACpSGSEVGVAWL-------GQLC---RTGASDQGNETVAG-----TNVVV-RTSNEW-------Q 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 601 TLAHEIGHNFGSPHD-YPQECRPGGL---------------NGNYIMFASATSGdrpnNSKFSPCSIRNI 654
Cdd:cd04271 148 VFAHEIGHTFGAVHDcTSGTCSDGSVgsqqccplststcdaNGQYIMNPSSSSG----ITEFSPCTIGNI 213
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
439-654 |
3.00e-08 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 404471 Cd Length: 203 Bit Score: 55.32 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 439 YEVDEKTREEITSLIAHHVTAVNYIYRNTKfdgrtehrNIRFEVQRikiDDDSACRNSYNGPHNAFCNEHMDVSNFLN-L 517
Cdd:pfam13583 15 YSASFGSVDELRANINATVTTANEVYGRDF--------NVSLALIS---DRDVIYTDSSTDSFNADCSGGDLGNWRLAtL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 518 HSLEDHSDFCLAYVFTYRDFTGGTLGLAWVasasgasGGICEKYKtytETVGGQYQSTKRSlntgiitfvNYNsrvppkv 597
Cdd:pfam13583 84 TSWRDSLNYDLAYLTLMTGPSGQNVGVAWV-------GALCSSAR---QNAKASGVARSRD---------EWD------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281364977 598 sqlTLAHEIGHNFGSPHDYPQECRPGGL-----NGNYIM-FASATSGDrpnnsKFSPCSIRNI 654
Cdd:pfam13583 138 ---IFAHEIGHTFGAVHDCSSQGEGLSSstedgSGQTIMsYASTASQT-----AFSPCTIRNI 192
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
477-664 |
3.10e-08 |
|
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: 55.32 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 477 NIRFEVQRIKI--DDDSACRNSYNGPH--NAFCNehmdVSNFLNLHSLEDHSDFCLAYVFTYRDF-----TGGTLGLAWV 547
Cdd:cd04273 45 SINIVVVRLIVleDEESGLLISGNAQKslKSFCR----WQKKLNPPNDSDPEHHDHAILLTRQDIcrsngNCDTLGLAPV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 548 asasgasGGICEKYK--TYTETVGgqyqstkrsLNTGIitfvnynsrvppkvsqlTLAHEIGHNFGSPHD-YPQECRPGG 624
Cdd:cd04273 121 -------GGMCSPSRscSINEDTG---------LSSAF-----------------TIAHELGHVLGMPHDgDGNSCGPEG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 281364977 625 LNGNyIMfaSATSGDRPNNSKFSPCSIRNISNVLDVLVGN 664
Cdd:cd04273 168 KDGH-IM--SPTLGANTGPFTWSKCSRRYLTSFLDTGDGN 204
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
447-658 |
4.37e-06 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 49.27 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 447 EEITSLIAHHVTAVNYIYRNTKfdgrteHRNIRFEVQRIKIDDDSACRNSYNGPHNAFCNEHMDVSNFlNLHSLEDHSDF 526
Cdd:cd04272 21 EQLIRYLAVMVNAANLRYRDLK------SPRIRLLLVGITISKDPDFEPYIHPINYGYIDAAETLENF-NEYVKKKRDYF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 527 CLAYVF--TYRD---FTGG-----TLGLAWVASASGASG-GICEkyktytETvGGQYqstkrslnTGIITFvnynsrvpp 595
Cdd:cd04272 94 NPDVVFlvTGLDmstYSGGslqtgTGGYAYVGGACTENRvAMGE------DT-PGSY--------YGVYTM--------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281364977 596 kvsqltlAHEIGHNFGSPHDYPQEC-RPGGLNGN--------YIMfaSATSGDrPNNSKFSPCSIRNISNVL 658
Cdd:cd04272 150 -------THELAHLLGAPHDGSPPPsWVKGHPGSldcpwddgYIM--SYVVNG-ERQYRFSQCSQRQIRNVF 211
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
430-651 |
7.23e-06 |
|
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: 48.07 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 430 IADHDRGRKYEVD-EKTREEITSLIAHhvtaVNYIYRNTkfdgrtehrNIRFEVQRIKI--DDDSacrnsyngphnafCN 506
Cdd:pfam01421 8 VVDKQLFQKMGSDtTVVRQRVFQVVNL----VNSIYKEL---------NIRVVLVGLEIwtDEDK-------------ID 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 507 EHMDVS----NFLNLHS--LEDHSDFCLAYVFTYRDFTGGTLGLAWVasasgasGGICEKYKtytetvggqyqstkrslN 580
Cdd:pfam01421 62 VSGDANdtlrNFLKWRQeyLKKRKPHDVAQLLSGVEFGGTTVGAAYV-------GGMCSLEY-----------------S 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281364977 581 TGIITFvnynsrvpPKVSQL----TLAHEIGHNFGSPHD---YPQECRPGGLngnYIMFASATSgdrPNNSKFSPCSI 651
Cdd:pfam01421 118 GGVNED--------HSKNLEsfavTMAHELGHNLGMQHDdfnGGCKCPPGGG---CIMNPSAGS---SFPRKFSNCSQ 181
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
54-149 |
1.76e-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: 39.60 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281364977 54 IRASHNRARRSVTKDQY----VHLKFASHGRDFHLRLKRDLNTFSNklDF----YDSKGPIDVSTDHI-----YEGEVIG 120
Cdd:pfam01562 6 VRLDPSRRRRSLASESTyldtLSYRLAAFGKKFHLHLTPNRLLLAP--GFtvtyYLDGGTGVESPPVQtdhcyYQGHVEG 83
|
90 100
....*....|....*....|....*....
gi 281364977 121 DRNSYVFGSIHNGvFEGKIITERDAYYVE 149
Cdd:pfam01562 84 HPDSSVALSTCSG-LRGFIRTENEEYLIE 111
|
|
| |
