|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
238-437 |
8.09e-86 |
|
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: 8.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 393
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1965410872 394 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 437
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
529-670 |
5.13e-51 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 175.24 E-value: 5.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 529 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 608
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965410872 609 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 670
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
70-187 |
2.87e-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: 118.96 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 70 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 147
Cdd:pfam01562 10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1965410872 148 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 187
Cdd:pfam01562 89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
452-525 |
1.50e-28 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 108.87 E-value: 1.50e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965410872 452 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 525
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 ... |
238-437 |
8.09e-86 |
|
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: 8.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 393
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1965410872 394 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 437
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
238-435 |
7.08e-62 |
|
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: 207.47 E-value: 7.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 393
Cdd:cd04269 80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1965410872 394 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 435
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
529-670 |
5.13e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 175.24 E-value: 5.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 529 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 608
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965410872 609 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 670
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
530-639 |
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 1965410872 530 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 609
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 1965410872 610 IPRLGELdgeitSTLVVQQGRTLNCSGGHV 639
Cdd:pfam08516 81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
70-187 |
2.87e-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: 118.96 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 70 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 147
Cdd:pfam01562 10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1965410872 148 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 187
Cdd:pfam01562 89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
452-525 |
1.50e-28 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 108.87 E-value: 1.50e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965410872 452 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 525
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
452-527 |
2.51e-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: 102.77 E-value: 2.51e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965410872 452 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 527
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 ... |
238-437 |
8.09e-86 |
|
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: 8.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 393
Cdd:pfam01421 80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1965410872 394 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 437
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
238-435 |
7.08e-62 |
|
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: 207.47 E-value: 7.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 393
Cdd:cd04269 80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1965410872 394 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 435
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
529-670 |
5.13e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 175.24 E-value: 5.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 529 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 608
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965410872 609 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 670
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
530-639 |
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 1965410872 530 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 609
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 1965410872 610 IPRLGELdgeitSTLVVQQGRTLNCSGGHV 639
Cdd:pfam08516 81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
70-187 |
2.87e-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: 118.96 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 70 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 147
Cdd:pfam01562 10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1965410872 148 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 187
Cdd:pfam01562 89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
452-525 |
1.50e-28 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 108.87 E-value: 1.50e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965410872 452 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 525
Cdd:pfam00200 1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
452-527 |
2.51e-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: 102.77 E-value: 2.51e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965410872 452 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 527
Cdd:smart00050 1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
238-434 |
3.70e-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: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSvvHTNTYAKSVVNMADLIYKDQL---KTRIVLVAMETWATDNK-FAISENPLITLREFMK 313
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 314 YRR------DFIKEKSDAVHLFSGSQFESSRS-----GAAYIGGICSLLKGGGVNEfgKTDLM-AVTLAQSLAHNIGIIS 381
Cdd:cd04273 79 WQKklnppnDSDPEHHDHAILLTRQDICRSNGncdtlGLAPVGGMCSPSRSCSINE--DTGLSsAFTIAHELGHVLGMPH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1965410872 382 DKrklASGECKcEDTWSGCIMGDTGYYLPKKFT--QCNIEEYHDFLNSGGGACLF 434
Cdd:cd04273 157 DG---DGNSCG-PEGKDGHIMSPTLGANTGPFTwsKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
238-426 |
6.32e-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: 6.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKD---QLKTRIVLVAMETWATdNKFA--ISENPLITLREFM 312
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKG-EQFAppIDSDASNTLNSFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 313 KYRRDFIKeKSDAVHLFSGSQF-ESSRSGAAYIGGICSLLKGGGVNE-FGKTDLMAVTLAQSLAHNIGIISDkrklASGE 390
Cdd:cd04267 80 FWRAEGPI-RHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHD----GGDE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1965410872 391 CKCEDTWSG-CIMGDT-GYYLPKKFTQCNIEEYHDFLN 426
Cdd:cd04267 155 LAFECDGGGnYIMAPVdSGLNSYRFSQCSIGSIREFLD 192
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
267-378 |
8.80e-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: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 267 SVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMkyrrDFIKEKS-----DAVHLFSGSQFESSrSGA 341
Cdd:pfam13582 5 SLVNRANTIYERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQ----EVNDTRIgqygyDLGHLFTGRDGGGG-GGI 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1965410872 342 AYIGGICSLLKGGGVNE--FGKTDLMAVTLAQSLAHNIG 378
Cdd:pfam13582 80 AYVGGVCNSGSKFGVNSgsGPVGDTGADTFAHEIGHNFG 118
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
239-433 |
7.52e-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: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 239 YIELMIVNDHlMFKKHRLSVVHTNTYAKSVVNMADLIYKD--QLKTRIVLVAMETwATDNKFAI-----------SENPL 305
Cdd:cd04272 2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDlkSPRIRLLLVGITI-SKDPDFEPyihpinygyidAAETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 306 ITLREFMKYRRDFikEKSDAVHL--------FSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNI 377
Cdd:cd04272 80 ENFNEYVKKKRDY--FNPDVVFLvtgldmstYSGGSLQTGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965410872 378 GIISD--------KRKLASGECKCEDtwsGCIM----GDTGYYlpkKFTQCNIEEYHDFLNSGGGACL 433
Cdd:cd04272 158 GAPHDgspppswvKGHPGSLDCPWDD---GYIMsyvvNGERQY---RFSQCSQRQIRNVFRRLGASCL 219
|
|
| |
