|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
196-395 |
1.13e-100 |
|
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: 309.62 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 352
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039776955 353 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
45-152 |
7.77e-36 |
|
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: 131.67 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 45 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 124
Cdd:pfam01562 17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96
|
90 100 110
....*....|....*....|....*....|..
gi 1039776955 125 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 152
Cdd:pfam01562 97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
412-486 |
1.63e-33 |
|
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: 123.18 E-value: 1.63e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039776955 412 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 486
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
488-607 |
9.00e-32 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 120.54 E-value: 9.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 488 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 555
Cdd:smart00608 1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039776955 556 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 607
Cdd:smart00608 81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
196-395 |
1.13e-100 |
|
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: 309.62 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 352
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039776955 353 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
196-393 |
5.63e-78 |
|
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: 249.84 E-value: 5.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEdiPGCYCPepr 352
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039776955 353 eGGGCIMTESIGSkFPRIFSRCSKIDLESFVTKPQTGCLTN 393
Cdd:cd04269 156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
45-152 |
7.77e-36 |
|
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: 131.67 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 45 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 124
Cdd:pfam01562 17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96
|
90 100 110
....*....|....*....|....*....|..
gi 1039776955 125 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 152
Cdd:pfam01562 97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
412-486 |
1.63e-33 |
|
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: 123.18 E-value: 1.63e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039776955 412 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 486
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
412-484 |
1.78e-32 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 120.04 E-value: 1.78e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039776955 412 EHGEQCDCGTPQDCQ-NPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPED 484
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
488-607 |
9.00e-32 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 120.54 E-value: 9.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 488 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 555
Cdd:smart00608 1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039776955 556 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 607
Cdd:smart00608 81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
489-527 |
1.32e-12 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 64.56 E-value: 1.32e-12
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1039776955 489 NGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYT 527
Cdd:pfam08516 1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYE 41
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
196-395 |
1.13e-100 |
|
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: 309.62 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEDIPGCYCPepr 352
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039776955 353 EGGGCIMTESIGSKFPRIFSRCSKIDLESFVTKPQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
196-393 |
5.63e-78 |
|
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: 249.84 E-value: 5.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKLGS-REAVRQRVLEVVNHVDKLYQELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 274 LQGQHPHDNVQLITGVDFIGSTVGLAKVSALCSR-HSGAVNQDHSKNSIGVASTMAHELGHNLGMSHDEdiPGCYCPepr 352
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039776955 353 eGGGCIMTESIGSkFPRIFSRCSKIDLESFVTKPQTGCLTN 393
Cdd:cd04269 156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
196-391 |
1.32e-37 |
|
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: 139.68 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKLGsREAVRQRVLEVVNHVDKLYQELS----FRVVLVGLEIWNKDKF--YISRYANVTLENFLSW 269
Cdd:cd04273 1 RYVETLVVADSKMVEFHH-GEDLEHYILTLMNIVASLYKDPSlgnsINIVVVRLIVLEDEESglLISGNAQKSLKSFCRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 270 --REQNLQGQHP--HDNVQLITGVDFIGS-----TVGLAKVSALCSRH-SGAVNQDhskNSIGVASTMAHELGHNLGMSH 339
Cdd:cd04273 80 qkKLNPPNDSDPehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSrSCSINED---TGLSSAFTIAHELGHVLGMPH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039776955 340 DEDIPGCycpEPREGGGCIMTESIGSKF-PRIFSRCSKIDLESFVTKPQTGCL 391
Cdd:cd04273 157 DGDGNSC---GPEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCL 206
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
45-152 |
7.77e-36 |
|
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: 131.67 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 45 PSHWGQYPESLSYALGTSGHVFTLHLRKNRDLLGSSYTETYSAANGSEVTEQLQEQDHCLYQGHVEGYEGSAASISTCAG 124
Cdd:pfam01562 17 LASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSG 96
|
90 100 110
....*....|....*....|....*....|..
gi 1039776955 125 LRGFFRVGSTVHLIEPL---DADEEGQ-HAMY 152
Cdd:pfam01562 97 LRGFIRTENEEYLIEPLekySREEGGHpHVVY 128
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
196-377 |
2.04e-34 |
|
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: 129.85 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKL-GSREAVRQRVLEVVNHVDKLYQELSF----RVVLVGLEIWNKDKFY--ISRYANVTLENFLS 268
Cdd:cd04267 1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAppIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 269 WREQNLQGqhpHDNVQLITGVDFI-GSTVGLAKVSALC-SRHSGAVNQDHSKNSIgVASTMAHELGHNLGMSHDEDipGC 346
Cdd:cd04267 81 WRAEGPIR---HDNAVLLTAQDFIeGDILGLAYVGSMCnPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGG--DE 154
|
170 180 190
....*....|....*....|....*....|.
gi 1039776955 347 YCPEPREGGGCIMTESIGSKFPRIFSRCSKI 377
Cdd:cd04267 155 LAFECDGGGNYIMAPVDSGLNSYRFSQCSIG 185
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
412-486 |
1.63e-33 |
|
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: 123.18 E-value: 1.63e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039776955 412 EHGEQCDCGTPQDCQNPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPEDAF 486
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
412-484 |
1.78e-32 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 120.04 E-value: 1.78e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039776955 412 EHGEQCDCGTPQDCQ-NPCCNATTCQLVKGAECASGTCCHECKVKPAGEVCRLSKDKCDLEEFCDGRKPTCPED 484
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
488-607 |
9.00e-32 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 120.54 E-value: 9.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 488 QNGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYTFSIPPG-----C---NGRMY--SGRINRCGALYCEGGQ 555
Cdd:smart00608 1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIpcAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039776955 556 KP--LERSFCTFSSNHG--VCHALGTGSNIDT-FELVLQGTKCEEGKVCMDGSCQDL 607
Cdd:smart00608 81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
197-392 |
9.27e-19 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 85.87 E-value: 9.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 197 YVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLYQELS---FRVVLVGLEIwNKDKFYISRYAN---------VTLE 264
Cdd:cd04272 2 YPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITI-SKDPDFEPYIHPinygyidaaETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 265 NFlswREQNLQGQHP--HDNVQLITGVDF--------IGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVaSTMAHELGHN 334
Cdd:cd04272 81 NF---NEYVKKKRDYfnPDVVFLVTGLDMstysggslQTGTGGYAYVGGACTENRVAMGEDTPGSYYGV-YTMTHELAHL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039776955 335 LGMSHDEDIPGCYCPEPREGGGC------IMteSIGSKFPRI--FSRCSKIDLESFVTKPQTGCLT 392
Cdd:cd04272 157 LGAPHDGSPPPSWVKGHPGSLDCpwddgyIM--SYVVNGERQyrFSQCSQRQIRNVFRRLGASCLH 220
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
195-365 |
1.93e-17 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 81.31 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 195 TRYVELYVVADsQEFQKLGSREAVRQRVLEVVNHVDKL-YQELSFRVVLVGLEIWNKDKFYISRYANV-----TLENFLS 268
Cdd:pfam13688 2 TRTVALLVAAD-CSYVAAFGGDAAQANIINMVNTASNVyERDFNISLGLVNLTISDSTCPYTPPACSTgdssdRLSEFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 269 WREQNlqGQHPHDNVQLITGVDFigSTVGLAKVSALCSRHS-GAVNQDHSKNSIGVAS-----TMAHELGHNLGMSHDED 342
Cdd:pfam13688 81 FSAWR--GTQNDDLAYLFLMTNC--SGGGLAWLGQLCNSGSaGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCD 156
|
170 180
....*....|....*....|....*....
gi 1039776955 343 I--PGCYCPEPRE----GGGCIMTESIGS 365
Cdd:pfam13688 157 SstSSQCCPPSNStcpaGGRYIMNPSSSP 185
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
221-340 |
2.29e-14 |
|
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: 70.09 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 221 RVLEVVNHVDKLYQ-ELSFRVVLVGLEIWNKDKF-YISRYANVTLENFLswreQNLQGQHPHDN---VQLITGVDFIGsT 295
Cdd:pfam13582 2 RIVSLVNRANTIYErDLGIRLQLAAIIITTSADTpYTSSDALEILDELQ----EVNDTRIGQYGydlGHLFTGRDGGG-G 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1039776955 296 VGLAKVSALC-SRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHD 340
Cdd:pfam13582 77 GGIAYVGGVCnSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
221-382 |
8.05e-14 |
|
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: 69.86 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 221 RVLEVVNHVDKLYQELSFR------VVLVGLEIWNKdkfyisrYANVTLenFLSwreqnLQGQHPHDNVQLITGVDFIGS 294
Cdd:cd00203 1 KVIPYVVVADDRDVEEENLsaqiqsLILIAMQIWRD-------YLNIRF--VLV-----GVEIDKADIAILVTRQDFDGG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 295 TVGLAKVSALC-SRHSGAVNQDHSKNSIGVASTMAHELGHNLGMSHD------EDIPGCYCPEPRE--GGGCIM-----T 360
Cdd:cd00203 67 TGGWAYLGRVCdSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDhdrkdrDDYPTIDDTLNAEddDYYSVMsytkgS 146
|
170 180
....*....|....*....|..
gi 1039776955 361 ESIGSKFPriFSRCSKIDLESF 382
Cdd:cd00203 147 FSDGQRKD--FSQCDIDQINKL 166
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
200-376 |
2.91e-13 |
|
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: 70.10 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 200 LYVVADSQEFQKLGS--REAVRQRVLEVVNHVDKLYQELSFRVVL---VGLEIW----NKD--------KFYISRYANVT 262
Cdd:cd04270 5 LLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGGGfkgIGFQIKririHTTpdevdpgnKFYNKSFPNWG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 263 LENFLswrEQNLQGQHPHDN--VQLITGVDFIGSTVGLAKVSALCSRHSGAVNQDHSKNSIGVAS--------------- 325
Cdd:cd04270 85 VEKFL---VKLLLEQFSDDVclAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKKKylntgltttvnygkr 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039776955 326 --------TMAHELGHNLGMSHDEDIPGCyCPEPREGGGCIMTESIGS---KFPRIFSRCSK 376
Cdd:cd04270 162 vptkesdlVTAHELGHNFGSPHDPDIAEC-APGESQGGNYIMYARATSgdkENNKKFSPCSK 222
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
489-527 |
1.32e-12 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 64.56 E-value: 1.32e-12
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1039776955 489 NGTPCPG--GYCFDGSCPTLAQQCRDLWGPGARVAADSCYT 527
Cdd:pfam08516 1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYE 41
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
217-376 |
2.58e-10 |
|
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: 60.72 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 217 AVRQRVLEVVNHVDKLY--QELSFRVVLVG---LEI-------WNKDKFyiSRYANVTLENFLSwreqNLQGQHPHDNVQ 284
Cdd:pfam13574 2 NVTENLVNVVNRVNQIYepDDININGGLVNpgeIPAttsasdsGNNYCN--SPTTIVRRLNFLS----QWRGEQDYCLAH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 285 LITGVDFIGSTVGLAKVSALCSRHSGAVnqdhsKNSIGVAST---------------MAHELGHNLGMSHDEDI-----P 344
Cdd:pfam13574 76 LVTMGTFSGGELGLAYVGQICQKGASSP-----KTNTGLSTTtnygsfnyptqewdvVAHEVGHNFGATHDCDGsqyasS 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039776955 345 GCYCPEPR----EGGGCIMTESIGSKfPRIFSRCSK 376
Cdd:pfam13574 151 GCERNAATsvcsANGSFIMNPASKSN-NDLFSPCSI 185
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
202-392 |
1.61e-09 |
|
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: 58.97 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 202 VVADSQEFQKLGSREAVRQRVLEVVNHVDKLYqELSFRVVL--VGLEI--------------WN---KDKFYISRyanvT 262
Cdd:cd04271 7 VAADCSYTKSFGSVEEARRNILNNVNSASQLY-ESSFNISLglRNLTIsdascpstavdsapWNlpcNSRIDIDD----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 263 LENFLSWReqnlqGQHPHDNV---QLITGVDfIGSTVGLAKVSALC-SRHSGAVNQDH-SKNSIGVAST----MAHELGH 333
Cdd:cd04271 82 LSIFSQWR-----GQQPDDGNafwTLMTACP-SGSEVGVAWLGQLCrTGASDQGNETVaGTNVVVRTSNewqvFAHEIGH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039776955 334 NLGMSHDEDIPGCY---------CPEPRE----GGGCIMTESIGSKFPRiFSRCSKIDLESFVTK--PQTGCLT 392
Cdd:cd04271 156 TFGAVHDCTSGTCSdgsvgsqqcCPLSTStcdaNGQYIMNPSSSSGITE-FSPCTIGNICSLLGRnpVRTSCLS 228
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
196-346 |
7.65e-06 |
|
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: 47.61 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 196 RYVELYVVADSQEFQKLGSREAVRQRVLEVVNHVDKLY-QELSFRVVLVG----------LEIWNKDKFyISRYANVTLE 264
Cdd:pfam13583 3 RVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISdrdviytdssTDSFNADCS-GGDLGNWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039776955 265 NFLSWReqnlqGQHPHDNVQLITGVDFIGSTVGLAKVSALCSrhsgAVNQDHSKNsiGVA------STMAHELGHNLGMS 338
Cdd:pfam13583 82 TLTSWR-----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCS----SARQNAKAS--GVArsrdewDIFAHEIGHTFGAV 150
|
....*...
gi 1039776955 339 HDEDIPGC 346
Cdd:pfam13583 151 HDCSSQGE 158
|
|
| |
