|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
239-438 |
2.82e-85 |
|
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: 271.87 E-value: 2.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 319 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 394
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025608636 395 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 438
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
530-671 |
6.09e-51 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 175.24 E-value: 6.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 530 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 609
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025608636 610 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 671
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
71-188 |
4.44e-31 |
|
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: 118.19 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 71 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 148
Cdd:pfam01562 10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1025608636 149 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 188
Cdd:pfam01562 89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
453-526 |
1.01e-28 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 109.64 E-value: 1.01e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025608636 453 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 526
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
239-438 |
2.82e-85 |
|
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: 271.87 E-value: 2.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 319 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 394
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025608636 395 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 438
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
239-436 |
1.82e-61 |
|
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: 207.08 E-value: 1.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 319 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 394
Cdd:cd04269 80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025608636 395 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 436
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
530-671 |
6.09e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 175.24 E-value: 6.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 530 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 609
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025608636 610 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 671
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
531-640 |
1.06e-34 |
|
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: 127.73 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 531 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 610
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 1025608636 611 IPRLGELdgeitSTLVVQQGRTLNCSGGHV 640
Cdd:pfam08516 81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
71-188 |
4.44e-31 |
|
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: 118.19 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 71 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 148
Cdd:pfam01562 10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1025608636 149 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 188
Cdd:pfam01562 89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
453-526 |
1.01e-28 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 109.64 E-value: 1.01e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025608636 453 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 526
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
453-528 |
1.61e-26 |
|
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: 103.54 E-value: 1.61e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025608636 453 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 528
Cdd:smart00050 1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
239-438 |
2.82e-85 |
|
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: 271.87 E-value: 2.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 319 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 394
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1025608636 395 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 438
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
239-436 |
1.82e-61 |
|
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: 207.08 E-value: 1.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 319 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 394
Cdd:cd04269 80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1025608636 395 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 436
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
530-671 |
6.09e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 175.24 E-value: 6.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 530 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 609
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025608636 610 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 671
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
531-640 |
1.06e-34 |
|
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: 127.73 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 531 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 610
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 1025608636 611 IPRLGELdgeitSTLVVQQGRTLNCSGGHV 640
Cdd:pfam08516 81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
71-188 |
4.44e-31 |
|
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: 118.19 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 71 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 148
Cdd:pfam01562 10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1025608636 149 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 188
Cdd:pfam01562 89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
453-526 |
1.01e-28 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 109.64 E-value: 1.01e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025608636 453 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 526
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
453-528 |
1.61e-26 |
|
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: 103.54 E-value: 1.61e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025608636 453 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 528
Cdd:smart00050 1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
239-435 |
4.03e-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: 83.83 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 239 KYIELMIVNDHLMFKKHRLSvvHTNTYAKSVVNMADLIYKDQL---KTRIVLVAMETWATDNK-FAISENPLITLREFMK 314
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 315 YRR------DFIKEKSDAVHLFSGSQFESSRS-----GAAYIGGICSLLKGGGVNEfgKTDLM-AVTLAQSLAHNIGIIS 382
Cdd:cd04273 79 WQKklnppnDSDPEHHDHAILLTRQDICRSNGncdtlGLAPVGGMCSPSRSCSINE--DTGLSsAFTIAHELGHVLGMPH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1025608636 383 DKrklASGECKcEDTWSGCIMGDTGYYLPKKFT--QCNIEEYHDFLNSGGGACLF 435
Cdd:cd04273 157 DG---DGNSCG-PEGKDGHIMSPTLGANTGPFTwsKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
239-427 |
7.86e-17 |
|
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: 79.77 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKD---QLKTRIVLVAMETWATdNKFA--ISENPLITLREFM 313
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKG-EQFAppIDSDASNTLNSFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 314 KYRRDFIKeKSDAVHLFSGSQF-ESSRSGAAYIGGICSLLKGGGVNE-FGKTDLMAVTLAQSLAHNIGIISDkrklASGE 391
Cdd:cd04267 80 FWRAEGPI-RHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHD----GGDE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1025608636 392 CKCEDTWSG-CIMGDT-GYYLPKKFTQCNIEEYHDFLN 427
Cdd:cd04267 155 LAFECDGGGnYIMAPVdSGLNSYRFSQCSIGSIREFLD 192
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
268-379 |
9.59e-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: 463926 [Multi-domain] Cd Length: 122 Bit Score: 57.38 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 268 SVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMkyrrDFIKEKS-----DAVHLFSGSQFESSrSGA 342
Cdd:pfam13582 5 SLVNRANTIYERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQ----EVNDTRIgqygyDLGHLFTGRDGGGG-GGI 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1025608636 343 AYIGGICSLLKGGGVNE--FGKTDLMAVTLAQSLAHNIG 379
Cdd:pfam13582 80 AYVGGVCNSGSKFGVNSgsGPVGDTGADTFAHEIGHNFG 118
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
240-434 |
8.83e-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: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 240 YIELMIVNDHlMFKKHRLSVVHTNTYAKSVVNMADLIYKD--QLKTRIVLVAMETwATDNKFAI-----------SENPL 306
Cdd:cd04272 2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDlkSPRIRLLLVGITI-SKDPDFEPyihpinygyidAAETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025608636 307 ITLREFMKYRRDFikEKSDAVHL--------FSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNI 378
Cdd:cd04272 80 ENFNEYVKKKRDY--FNPDVVFLvtgldmstYSGGSLQTGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025608636 379 GIISD--------KRKLASGECKCEDtwsGCIM----GDTGYYlpkKFTQCNIEEYHDFLNSGGGACL 434
Cdd:cd04272 158 GAPHDgspppswvKGHPGSLDCPWDD---GYIMsyvvNGERQY---RFSQCSQRQIRNVFRRLGASCL 219
|
|
| |
