|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
243-442 |
7.07e-91 |
|
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: 283.42 E-value: 7.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 243 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEqLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 322
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 323 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSRGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKHrssAGDCKC 398
Cdd:pfam01421 80 YLKKrkPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHskNLESFAVTMAHELGHNLGMQHDDF---NGGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 160707883 399 PDiWLGCIMED-TGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKP 442
Cdd:pfam01421 157 PP-GGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
534-672 |
7.61e-48 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 165.61 E-value: 7.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 534 LDGYYCDHEQGRCYGGRCKTRDRQCQALWGHAA--ADRFCYEKLNVEGTERGNCGRKGSGWVQCSKQDVLCGFLLCVNIS 611
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAkvAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707883 612 GAPRLGDLGGDISSVTfyhqgKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLP 672
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVD 136
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
70-193 |
1.63e-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: 119.34 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 70 QLDTRVRQDPPRGTPVHLAQVSFVIPAFDSNFTLDLELNHHLLSSQYVERHFSREGTR-QHSTGAGDHCYYHGKLRGNPQ 148
Cdd:pfam01562 7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGvESPPVQTDHCYYQGHVEGHPD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 160707883 149 SFAALSTCQGLHGVFSDGNLTYIVEPKEiagPWGPPQGPLPHLIY 193
Cdd:pfam01562 87 SSVALSTCSGLRGFIRTENEEYLIEPLE---KYSREEGGHPHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
457-530 |
1.90e-29 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 111.56 E-value: 1.90e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707883 457 EAGEECDCGSVQECSRagGNCC--KKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPN 530
Cdd:pfam00200 1 EEGEECDCGSLEECTN--DPCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
243-442 |
7.07e-91 |
|
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: 283.42 E-value: 7.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 243 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEqLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 322
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 323 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSRGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKHrssAGDCKC 398
Cdd:pfam01421 80 YLKKrkPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHskNLESFAVTMAHELGHNLGMQHDDF---NGGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 160707883 399 PDiWLGCIMED-TGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKP 442
Cdd:pfam01421 157 PP-GGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
243-440 |
8.65e-70 |
|
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: 227.50 E-value: 8.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 243 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKeQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 322
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 323 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSRGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKhrssaGDCKC 398
Cdd:cd04269 80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHsrNLLLFAVTMAHELGHNLGMEHDD-----GGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 160707883 399 PDiwLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFN 440
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
534-672 |
7.61e-48 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 165.61 E-value: 7.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 534 LDGYYCDHEQGRCYGGRCKTRDRQCQALWGHAA--ADRFCYEKLNVEGTERGNCGRKGSGWVQCSKQDVLCGFLLCVNIS 611
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAkvAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707883 612 GAPRLGDLGGDISSVTfyhqgKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLP 672
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVD 136
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
70-193 |
1.63e-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: 119.34 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 70 QLDTRVRQDPPRGTPVHLAQVSFVIPAFDSNFTLDLELNHHLLSSQYVERHFSREGTR-QHSTGAGDHCYYHGKLRGNPQ 148
Cdd:pfam01562 7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGvESPPVQTDHCYYQGHVEGHPD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 160707883 149 SFAALSTCQGLHGVFSDGNLTYIVEPKEiagPWGPPQGPLPHLIY 193
Cdd:pfam01562 87 SSVALSTCSGLRGFIRTENEEYLIEPLE---KYSREEGGHPHVVY 128
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
535-642 |
3.54e-31 |
|
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: 117.33 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 535 DGYYCDHEQGRCYGGRCKTRDRQCQALWGHAA--ADRFCYEKLNVEGTERGNCGRKGSGWVQCSKQDVLCGFLLCVNISG 612
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAksAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 160707883 613 APRLGDLggdisSVTFYHQGKELDCRGGHV 642
Cdd:pfam08516 81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
457-530 |
1.90e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 111.56 E-value: 1.90e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707883 457 EAGEECDCGSVQECSRagGNCC--KKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPN 530
Cdd:pfam00200 1 EEGEECDCGSLEECTN--DPCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
457-532 |
2.23e-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: 2.23e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707883 457 EAGEECDCGSVQECsraGGNCCKK--CTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLH 532
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 ... |
243-442 |
7.07e-91 |
|
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: 283.42 E-value: 7.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 243 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEqLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 322
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 323 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSRGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKHrssAGDCKC 398
Cdd:pfam01421 80 YLKKrkPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHskNLESFAVTMAHELGHNLGMQHDDF---NGGCKC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 160707883 399 PDiWLGCIMED-TGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKP 442
Cdd:pfam01421 157 PP-GGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
243-440 |
8.65e-70 |
|
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: 227.50 E-value: 8.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 243 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKeQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 322
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 323 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSRGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKhrssaGDCKC 398
Cdd:cd04269 80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHsrNLLLFAVTMAHELGHNLGMEHDD-----GGCTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 160707883 399 PDiwLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFN 440
Cdd:cd04269 155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
534-672 |
7.61e-48 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 165.61 E-value: 7.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 534 LDGYYCDHEQGRCYGGRCKTRDRQCQALWGHAA--ADRFCYEKLNVEGTERGNCGRKGSGWVQCSKQDVLCGFLLCVNIS 611
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAkvAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707883 612 GAPRLGDLGGDISSVTfyhqgKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLP 672
Cdd:smart00608 81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVD 136
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
70-193 |
1.63e-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: 119.34 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 70 QLDTRVRQDPPRGTPVHLAQVSFVIPAFDSNFTLDLELNHHLLSSQYVERHFSREGTR-QHSTGAGDHCYYHGKLRGNPQ 148
Cdd:pfam01562 7 RLDPSRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGvESPPVQTDHCYYQGHVEGHPD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 160707883 149 SFAALSTCQGLHGVFSDGNLTYIVEPKEiagPWGPPQGPLPHLIY 193
Cdd:pfam01562 87 SSVALSTCSGLRGFIRTENEEYLIEPLE---KYSREEGGHPHVVY 128
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
535-642 |
3.54e-31 |
|
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: 117.33 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 535 DGYYCDHEQGRCYGGRCKTRDRQCQALWGHAA--ADRFCYEKLNVEGTERGNCGRKGSGWVQCSKQDVLCGFLLCVNISG 612
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAksAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 160707883 613 APRLGDLggdisSVTFYHQGKELDCRGGHV 642
Cdd:pfam08516 81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
457-530 |
1.90e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 111.56 E-value: 1.90e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160707883 457 EAGEECDCGSVQECSRagGNCC--KKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPN 530
Cdd:pfam00200 1 EEGEECDCGSLEECTN--DPCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
457-532 |
2.23e-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: 2.23e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160707883 457 EAGEECDCGSVQECsraGGNCCKK--CTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLH 532
Cdd:smart00050 1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
243-430 |
5.64e-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: 77.08 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 243 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKE---QLNTRIVLVAMETWADGDKIQVQD-DLLETLARLMV 318
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 319 YRREGLPEpSDATHLFSGRTFQSTSS-GAAYVGGICSLSRGGGVNE-YGNMGAMAVTLAQTLGQNLGMMwnkHrSSAGDC 396
Cdd:cd04267 81 WRAEGPIR-HDNAVLLTAQDFIEGDIlGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAE---H-DGGDEL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 160707883 397 KCPDIWLG-CIMEDT-GFYLPRKFSRCSIDEYNQFL 430
Cdd:cd04267 156 AFECDGGGnYIMAPVdSGLNSYRFSQCSIGSIREFL 191
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
243-439 |
9.10e-15 |
|
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: 73.81 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 243 KYVELIVINDHQLFEQMRQSVVLTsnFAKSVVNLADVIYKEQL---NTRIVLVAMETWADGDK-IQVQDDLLETLARLMV 318
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGEDLEH--YILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 319 Y-RREGLPEPSDATH-----LFSGRTFQSTSS-----GAAYVGGICSLSRGGGVNEYGNMGAmAVTLAQTLGQNLGMMwn 387
Cdd:cd04273 79 WqKKLNPPNDSDPEHhdhaiLLTRQDICRSNGncdtlGLAPVGGMCSPSRSCSINEDTGLSS-AFTIAHELGHVLGMP-- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 160707883 388 kHRSSAGDCKcPDIWLGCIMEDTGFYLPRKF--SRCSIDEYNQFLQEGGGSCLF 439
Cdd:cd04273 156 -HDGDGNSCG-PEGKDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
272-383 |
2.83e-09 |
|
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: 55.45 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 272 SVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRREGLPEPS-DATHLFSGRTFqSTSSGAAYVG 350
Cdd:pfam13582 5 SLVNRANTIYERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGyDLGHLFTGRDG-GGGGGIAYVG 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 160707883 351 GICSLSRGGGVNeYGNMGA---MAVTLAQTLGQNLG 383
Cdd:pfam13582 84 GVCNSGSKFGVN-SGSGPVgdtGADTFAHEIGHNFG 118
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
244-438 |
3.52e-07 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 51.58 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 244 YVELIVIND---HQLFEQMRQsvvLTSNFAkSVVNLADVIYKEQLNTRI--VLVAMETWADGDKIQVQDDLL-------E 311
Cdd:cd04272 2 YPELFVVVDydhQSEFFSNEQ---LIRYLA-VMVNAANLRYRDLKSPRIrlLLVGITISKDPDFEPYIHPINygyidaaE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 312 TLARLMVY-RREGLPEPSDATHLFSGRTFQSTSSGA--------AYVGGICSLSRGGGVNE----YGNMGAMAVTLAQTL 378
Cdd:cd04272 78 TLENFNEYvKKKRDYFNPDVVFLVTGLDMSTYSGGSlqtgtggyAYVGGACTENRVAMGEDtpgsYYGVYTMTHELAHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707883 379 G----QNLGMMWNKHRSSAGDCKcpdiW-LGCIMEdTGFYLPR--KFSRCSIDEYNQFLQEGGGSCL 438
Cdd:cd04272 158 GaphdGSPPPSWVKGHPGSLDCP----WdDGYIMS-YVVNGERqyRFSQCSQRQIRNVFRRLGASCL 219
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
242-419 |
7.80e-06 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 47.41 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 242 TKYVELIVINDHQLFEQMRQSVVLTsnFAKSVVNLADVIYKEQLNTRIVLVAMETWADGD----KIQVQDDLLETLARLM 317
Cdd:pfam13688 2 TRTVALLVAADCSYVAAFGGDAAQA--NIINMVNTASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707883 318 VYRREGLPEPSDATHLFSGRTFQSTssGAAYVGGICSLSRGGGVNEYGNMGAMAV-------TLAQTLGQNLG------M 384
Cdd:pfam13688 80 DFSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVstatewqVFAHEIGHNFGavhdcdS 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 160707883 385 MWNKHRSSAGDCKCPDIWlGCIM-EDTGFYLpRKFS 419
Cdd:pfam13688 158 STSSQCCPPSNSTCPAGG-RYIMnPSSSPNS-TDFS 191
|
|
| |
