|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
237-436 |
1.51e-83 |
|
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: 266.86 E-value: 1.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSVGHTNSYAKSVVNVADLIYKEqLNTRIVLVAMETWATDNKFTISENPLVTLREFMKYRRD 316
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 317 FIREKS--DAVHLFSGSQFQSSRSGAAYIGGICSLLKGGGVNEFGKPDL--LAVTLAQSLGHNLGIFSDKRKlltGECKC 392
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1702262856 393 EdTWSGCIMGD-TGYYLPSKFSKCDIEEYHEFLNNGGGACLFNKP 436
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
528-668 |
1.16e-50 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 174.47 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 528 MDGYSCDNKQGICFGGRCKTRDRQCKYIWGEKVTAADRYCYEKLNIEGTEKGNCGRGKDTWIQCNKQDVLCGYLLCSNIS 607
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1702262856 608 NVPRLGELDGEITSSViqlgKSYNCSGGHVKLDEETDLGYVEDGTPCGPEMICFERRCLPT 668
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
451-524 |
1.29e-30 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 115.03 E-value: 1.29e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1702262856 451 EDGEECDCGTTAECAIEggDCC--HTCTLTAGSECSNGLCCRKCQFESKGVVCRDAVNDCDIPENCTGNSSQCSPN 524
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
67-186 |
1.90e-27 |
|
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: 107.79 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 67 VLNTRVSSRSDRKQSTHVARASFQVDAFGSSFILDVMLNHDLLSSEY-LERHIEHGGKTVEVKGG-EHCYYQGQIRGNSE 144
Cdd:pfam01562 7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGVESPPVQtDHCYYQGHVEGHPD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1702262856 145 SFVALSTCHGLHGMFYDGNHTYLIEPEESYTSHEDFYFHSVY 186
Cdd:pfam01562 87 SSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
237-436 |
1.51e-83 |
|
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: 266.86 E-value: 1.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSVGHTNSYAKSVVNVADLIYKEqLNTRIVLVAMETWATDNKFTISENPLVTLREFMKYRRD 316
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 317 FIREKS--DAVHLFSGSQFQSSRSGAAYIGGICSLLKGGGVNEFGKPDL--LAVTLAQSLGHNLGIFSDKRKlltGECKC 392
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1702262856 393 EdTWSGCIMGD-TGYYLPSKFSKCDIEEYHEFLNNGGGACLFNKP 436
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
237-434 |
4.84e-66 |
|
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: 219.41 E-value: 4.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSVGHTNSYAKSVVNVADLIYKeQLNTRIVLVAMETWATDNKFTISENPLVTLREFMKYRRD 316
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 317 FI--REKSDAVHLFSGSQFQSSRSGAAYIGGICSLLKGGGVNEFGKPDLL--AVTLAQSLGHNLGIFSDkrkllTGECKC 392
Cdd:cd04269 80 NLlpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLlfAVTMAHELGHNLGMEHD-----DGGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1702262856 393 EDtwSGCIMGDTGYYLPSKFSKCDIEEYHEFLNNGGGACLFN 434
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
528-668 |
1.16e-50 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 174.47 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 528 MDGYSCDNKQGICFGGRCKTRDRQCKYIWGEKVTAADRYCYEKLNIEGTEKGNCGRGKDTWIQCNKQDVLCGYLLCSNIS 607
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1702262856 608 NVPRLGELDGEITSSViqlgKSYNCSGGHVKLDEETDLGYVEDGTPCGPEMICFERRCLPT 668
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
529-637 |
4.76e-35 |
|
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: 128.89 E-value: 4.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 529 DGYSCDNKQGICFGGRCKTRDRQCKYIWGEKVTAADRYCYEKLNIEGTEKGNCGRGKDTWIQCNKQDVLCGYLLCSNISN 608
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*....
gi 1702262856 609 VPRLGELDGEITSSViqlgKSYNCSGGHV 637
Cdd:pfam08516 81 LPLLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
451-524 |
1.29e-30 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 115.03 E-value: 1.29e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1702262856 451 EDGEECDCGTTAECAIEggDCC--HTCTLTAGSECSNGLCCRKCQFESKGVVCRDAVNDCDIPENCTGNSSQCSPN 524
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
451-526 |
2.60e-28 |
|
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: 108.55 E-value: 2.60e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1702262856 451 EDGEECDCGTTAECAIEggdCC--HTCTLTAGSECSNGLCCRKCQFESKGVVCRDAVNDCDIPENCTGNSSQCSPNIH 526
Cdd:smart00050 1 EEGEECDCGSPKECTDP---CCdpATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
67-186 |
1.90e-27 |
|
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: 107.79 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 67 VLNTRVSSRSDRKQSTHVARASFQVDAFGSSFILDVMLNHDLLSSEY-LERHIEHGGKTVEVKGG-EHCYYQGQIRGNSE 144
Cdd:pfam01562 7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGVESPPVQtDHCYYQGHVEGHPD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1702262856 145 SFVALSTCHGLHGMFYDGNHTYLIEPEESYTSHEDFYFHSVY 186
Cdd:pfam01562 87 SSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
443-483 |
8.05e-04 |
|
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.
Pssm-ID: 200169 [Multi-domain] Cd Length: 38 Bit Score: 37.74 E-value: 8.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1702262856 443 PECGNGFVEDGEECDCGTTaecaIEGGDCCHTCTLTAGSEC 483
Cdd:TIGR02232 2 PTCGDGIIEPGEECDDGNT----TSGDGCSATCRLEEGFAC 38
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
237-436 |
1.51e-83 |
|
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: 266.86 E-value: 1.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSVGHTNSYAKSVVNVADLIYKEqLNTRIVLVAMETWATDNKFTISENPLVTLREFMKYRRD 316
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 317 FIREKS--DAVHLFSGSQFQSSRSGAAYIGGICSLLKGGGVNEFGKPDL--LAVTLAQSLGHNLGIFSDKRKlltGECKC 392
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1702262856 393 EdTWSGCIMGD-TGYYLPSKFSKCDIEEYHEFLNNGGGACLFNKP 436
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
237-434 |
4.84e-66 |
|
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: 219.41 E-value: 4.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSVGHTNSYAKSVVNVADLIYKeQLNTRIVLVAMETWATDNKFTISENPLVTLREFMKYRRD 316
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 317 FI--REKSDAVHLFSGSQFQSSRSGAAYIGGICSLLKGGGVNEFGKPDLL--AVTLAQSLGHNLGIFSDkrkllTGECKC 392
Cdd:cd04269 80 NLlpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLlfAVTMAHELGHNLGMEHD-----DGGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1702262856 393 EDtwSGCIMGDTGYYLPSKFSKCDIEEYHEFLNNGGGACLFN 434
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
528-668 |
1.16e-50 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 174.47 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 528 MDGYSCDNKQGICFGGRCKTRDRQCKYIWGEKVTAADRYCYEKLNIEGTEKGNCGRGKDTWIQCNKQDVLCGYLLCSNIS 607
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1702262856 608 NVPRLGELDGEITSSViqlgKSYNCSGGHVKLDEETDLGYVEDGTPCGPEMICFERRCLPT 668
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
529-637 |
4.76e-35 |
|
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: 128.89 E-value: 4.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 529 DGYSCDNKQGICFGGRCKTRDRQCKYIWGEKVTAADRYCYEKLNIEGTEKGNCGRGKDTWIQCNKQDVLCGYLLCSNISN 608
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*....
gi 1702262856 609 VPRLGELDGEITSSViqlgKSYNCSGGHV 637
Cdd:pfam08516 81 LPLLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
451-524 |
1.29e-30 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 115.03 E-value: 1.29e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1702262856 451 EDGEECDCGTTAECAIEggDCC--HTCTLTAGSECSNGLCCRKCQFESKGVVCRDAVNDCDIPENCTGNSSQCSPN 524
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
451-526 |
2.60e-28 |
|
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: 108.55 E-value: 2.60e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1702262856 451 EDGEECDCGTTAECAIEggdCC--HTCTLTAGSECSNGLCCRKCQFESKGVVCRDAVNDCDIPENCTGNSSQCSPNIH 526
Cdd:smart00050 1 EEGEECDCGSPKECTDP---CCdpATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
67-186 |
1.90e-27 |
|
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: 107.79 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 67 VLNTRVSSRSDRKQSTHVARASFQVDAFGSSFILDVMLNHDLLSSEY-LERHIEHGGKTVEVKGG-EHCYYQGQIRGNSE 144
Cdd:pfam01562 7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGVESPPVQtDHCYYQGHVEGHPD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1702262856 145 SFVALSTCHGLHGMFYDGNHTYLIEPEESYTSHEDFYFHSVY 186
Cdd:pfam01562 87 SSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
237-433 |
8.32e-18 |
|
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: 82.67 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSvgHTNSYAKSVVNVADLIYKEQL---NTRIVLVAMETWATDNK-FTISENPLVTLREFMK 312
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 313 YRR------DFIREKSDAVHLFSGSQFQSSRS-----GAAYIGGICSLLKGGGVNE---FGkpdlLAVTLAQSLGHNLGI 378
Cdd:cd04273 79 WQKklnppnDSDPEHHDHAILLTRQDICRSNGncdtlGLAPVGGMCSPSRSCSINEdtgLS----SAFTIAHELGHVLGM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1702262856 379 FSDkrklltGECK-CEDTW-SGCIMGDTGYYLPSKF--SKCDIEEYHEFLNNGGGACLF 433
Cdd:cd04273 155 PHD------GDGNsCGPEGkDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
237-425 |
3.77e-16 |
|
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: 77.46 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSVGHTNSYAKSVVNVADLIYKE---QLNTRIVLVAMETW-ATDNKFTISENPLVTLREFMK 312
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 313 YRRDfIREKSDAVHLFSGSQFQSSRS-GAAYIGGICSLLKGGGVNE-FGKPDLLAVTLAQSLGHNLGIFSDKrkllTGEC 390
Cdd:cd04267 81 WRAE-GPIRHDNAVLLTAQDFIEGDIlGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHDG----GDEL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1702262856 391 KCEDTWSG-CIMGDTGYYLPSK-FSKCDIEEYHEFLN 425
Cdd:cd04267 156 AFECDGGGnYIMAPVDSGLNSYrFSQCSIGSIREFLD 192
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
266-377 |
3.69e-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: 463926 [Multi-domain] Cd Length: 122 Bit Score: 67.01 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 266 SVVNVADLIYKEQLNTRIVLVAMETWATDNKFTISENPLVTLREFMkyrrDFIREKS-----DAVHLFSGSQFQSSrSGA 340
Cdd:pfam13582 5 SLVNRANTIYERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQ----EVNDTRIgqygyDLGHLFTGRDGGGG-GGI 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1702262856 341 AYIGGICSLLKGGGVNEFGKP--DLLAVTLAQSLGHNLG 377
Cdd:pfam13582 80 AYVGGVCNSGSKFGVNSGSGPvgDTGADTFAHEIGHNFG 118
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
238-432 |
7.51e-09 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 56.98 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 238 YIELMIVNDHLMCKkHRLSVGHTNSYAKSVVNVADLIYKEQLNTRI--VLVAMETwATDNKFTI-----------SENPL 304
Cdd:cd04272 2 YPELFVVVDYDHQS-EFFSNEQLIRYLAVMVNAANLRYRDLKSPRIrlLLVGITI-SKDPDFEPyihpinygyidAAETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 305 VTLREFMKYRRDFirEKSDAVHL--------FSGSQFQSSRSGAAYIGGICSLLKGGGVNEFGKPDLLAVTLAQSLGHNL 376
Cdd:cd04272 80 ENFNEYVKKKRDY--FNPDVVFLvtgldmstYSGGSLQTGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1702262856 377 GIFSD------KRKLLTGECKCedTWS-GCIM----GDTGYYlpsKFSKCDIEEYHEFLNNGGGACL 432
Cdd:cd04272 158 GAPHDgspppsWVKGHPGSLDC--PWDdGYIMsyvvNGERQY---RFSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
237-424 |
3.21e-06 |
|
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: 48.29 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 237 KYIELMIVNDHLMCKKHRLSvghtnSYAKSVVNVADLIYKEQLNTRIVLVAMETWATDNKFtisenplvtlrefmkyrrd 316
Cdd:cd00203 1 KVIPYVVVADDRDVEEENLS-----AQIQSLILIAMQIWRDYLNIRFVLVGVEIDKADIAI------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702262856 317 fireksdavhLFSGSQFQSSRSGAAYIGGICSLLKGGGV---NEFGkPDLLAVTLAQSLGHNLGIFSDKRKLLTGECKC- 392
Cdd:cd00203 57 ----------LVTRQDFDGGTGGWAYLGRVCDSLRGVGVlqdNQSG-TKEGAQTIAHELGHALGFYHDHDRKDRDDYPTi 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1702262856 393 ------EDTWSGCIM----GDTGYYLPSKFSKCDIEEYHEFL 424
Cdd:cd00203 126 ddtlnaEDDDYYSVMsytkGSFSDGQRKDFSQCDIDQINKLY 167
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
443-483 |
8.05e-04 |
|
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.
Pssm-ID: 200169 [Multi-domain] Cd Length: 38 Bit Score: 37.74 E-value: 8.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1702262856 443 PECGNGFVEDGEECDCGTTaecaIEGGDCCHTCTLTAGSEC 483
Cdd:TIGR02232 2 PTCGDGIIEPGEECDDGNT----TSGDGCSATCRLEEGFAC 38
|
|
| |
