|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
238-432 |
1.94e-95 |
|
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: 295.75 E-value: 1.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 238 KYVEMFVVVNHQRFQMWGSDVNTTVQAVVDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFNLWRQEK 317
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 318 LMGRVRHDVAHLIVGHRPGA-NEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDR--PGCTCGPKH 394
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9910118 395 LCLMHETISKTSG--FSNCSSDHFLRFLHDHRGACLLDRP 432
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
524-660 |
7.24e-48 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 166.00 E-value: 7.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 524 QDGTQCDRI-YYCSGGLCKNPDKQCARIYGYPARSAPEECYISVNTKANRFGNCGHPTSAnlkYEACSNEDIFCGKLVCT 602
Cdd:smart00608 1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGT---YIPCAPEDVKCGKLQCT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 9910118 603 DVRYLPQVKPLHSLLQIPYGDDWCWSMDAYNVTDiPDYGDVQGGTYCAPKKVCMESIC 660
Cdd:smart00608 78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQC 134
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
450-522 |
1.59e-34 |
|
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: 125.88 E-value: 1.59e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9910118 450 EESEECDCGNACDSH-PCCEP-TCTLKVGAQCSEGLCCYKCTFKKKGTLCRPAEDVCDLPEYCNGITGECPANSY 522
Cdd:smart00050 1 EEGEECDCGSPKECTdPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
79-194 |
6.03e-23 |
|
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: 95.07 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 79 ETVIPERLPG-------QGSDDPGGKVSYVLLMQGQKQLLHLEVKGHYSERNFPVYSY-HHGILGQEVPLLSQACHYEGH 150
Cdd:pfam01562 1 EVVIPVRLDPsrrrrslASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 9910118 151 IEGVPGSFVSVSICSGLRGVLIKEETAYGIEPLLFSTD----FEHILY 194
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
238-432 |
1.94e-95 |
|
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: 295.75 E-value: 1.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 238 KYVEMFVVVNHQRFQMWGSDVNTTVQAVVDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFNLWRQEK 317
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 318 LMGRVRHDVAHLIVGHRPGA-NEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDR--PGCTCGPKH 394
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9910118 395 LCLMHETISKTSG--FSNCSSDHFLRFLHDHRGACLLDRP 432
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
238-430 |
1.16e-74 |
|
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: 240.60 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 238 KYVEMFVVVNHQRFQMWGSDVNTTVQAVVDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFNLWRQEK 317
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 318 LMGRVRHDVAHLIVGHRP-GANEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDRPGCTCGPKhLC 396
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRS-TC 159
|
170 180 190
....*....|....*....|....*....|....*
gi 9910118 397 LMHETISK-TSGFSNCSSDHFLRFLHDHRGACLLD 430
Cdd:cd04269 160 IMAPSPSSlTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
524-660 |
7.24e-48 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 166.00 E-value: 7.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 524 QDGTQCDRI-YYCSGGLCKNPDKQCARIYGYPARSAPEECYISVNTKANRFGNCGHPTSAnlkYEACSNEDIFCGKLVCT 602
Cdd:smart00608 1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGT---YIPCAPEDVKCGKLQCT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 9910118 603 DVRYLPQVKPLHSLLQIPYGDDWCWSMDAYNVTDiPDYGDVQGGTYCAPKKVCMESIC 660
Cdd:smart00608 78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQC 134
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
525-630 |
2.86e-36 |
|
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: 131.97 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 525 DGTQCDR-IYYCSGGLCKNPDKQCARIYGYPARSAPEECYISVNTKANRFGNCGHPTSanlKYEACSNEDIFCGKLVCTD 603
Cdd:pfam08516 1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNG---GYVKCEKRDVLCGKLQCTN 77
|
90 100
....*....|....*....|....*..
gi 9910118 604 VRYLPQVKPLHSLLQIPYGDDWCWSMD 630
Cdd:pfam08516 78 VKELPLLGEHATVIYTNINGVTCWGTD 104
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
450-522 |
1.59e-34 |
|
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: 125.88 E-value: 1.59e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9910118 450 EESEECDCGNACDSH-PCCEP-TCTLKVGAQCSEGLCCYKCTFKKKGTLCRPAEDVCDLPEYCNGITGECPANSY 522
Cdd:smart00050 1 EEGEECDCGSPKECTdPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
450-520 |
1.79e-30 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 114.26 E-value: 1.79e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910118 450 EESEECDCGNA--CDSHPCCEP-TCTLKVGAQCSEGLCCYKCTFKKKGTLCRPAEDVCDLPEYCNGITGECPAN 520
Cdd:pfam00200 1 EEGEECDCGSLeeCTNDPCCDAkTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
79-194 |
6.03e-23 |
|
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: 95.07 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 79 ETVIPERLPG-------QGSDDPGGKVSYVLLMQGQKQLLHLEVKGHYSERNFPVYSY-HHGILGQEVPLLSQACHYEGH 150
Cdd:pfam01562 1 EVVIPVRLDPsrrrrslASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 9910118 151 IEGVPGSFVSVSICSGLRGVLIKEETAYGIEPLLFSTD----FEHILY 194
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
444-479 |
5.29e-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: 38.12 E-value: 5.29e-04
10 20 30
....*....|....*....|....*....|....*.
gi 9910118 444 CGNGVVEESEECDCGNACDSHPcCEPTCTLKVGAQC 479
Cdd:TIGR02232 4 CGDGIIEPGEECDDGNTTSGDG-CSATCRLEEGFAC 38
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
238-432 |
1.94e-95 |
|
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: 295.75 E-value: 1.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 238 KYVEMFVVVNHQRFQMWGSDVNTTVQAVVDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFNLWRQEK 317
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 318 LMGRVRHDVAHLIVGHRPGA-NEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDR--PGCTCGPKH 394
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9910118 395 LCLMHETISKTSG--FSNCSSDHFLRFLHDHRGACLLDRP 432
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
238-430 |
1.16e-74 |
|
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: 240.60 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 238 KYVEMFVVVNHQRFQMWGSDVNTTVQAVVDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFNLWRQEK 317
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 318 LMGRVRHDVAHLIVGHRP-GANEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDRPGCTCGPKhLC 396
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRS-TC 159
|
170 180 190
....*....|....*....|....*....|....*
gi 9910118 397 LMHETISK-TSGFSNCSSDHFLRFLHDHRGACLLD 430
Cdd:cd04269 160 IMAPSPSSlTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
524-660 |
7.24e-48 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 166.00 E-value: 7.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 524 QDGTQCDRI-YYCSGGLCKNPDKQCARIYGYPARSAPEECYISVNTKANRFGNCGHPTSAnlkYEACSNEDIFCGKLVCT 602
Cdd:smart00608 1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGT---YIPCAPEDVKCGKLQCT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 9910118 603 DVRYLPQVKPLHSLLQIPYGDDWCWSMDAYNVTDiPDYGDVQGGTYCAPKKVCMESIC 660
Cdd:smart00608 78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQC 134
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
525-630 |
2.86e-36 |
|
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: 131.97 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 525 DGTQCDR-IYYCSGGLCKNPDKQCARIYGYPARSAPEECYISVNTKANRFGNCGHPTSanlKYEACSNEDIFCGKLVCTD 603
Cdd:pfam08516 1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNG---GYVKCEKRDVLCGKLQCTN 77
|
90 100
....*....|....*....|....*..
gi 9910118 604 VRYLPQVKPLHSLLQIPYGDDWCWSMD 630
Cdd:pfam08516 78 VKELPLLGEHATVIYTNINGVTCWGTD 104
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
450-522 |
1.59e-34 |
|
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: 125.88 E-value: 1.59e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9910118 450 EESEECDCGNACDSH-PCCEP-TCTLKVGAQCSEGLCCYKCTFKKKGTLCRPAEDVCDLPEYCNGITGECPANSY 522
Cdd:smart00050 1 EEGEECDCGSPKECTdPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
450-520 |
1.79e-30 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 114.26 E-value: 1.79e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910118 450 EESEECDCGNA--CDSHPCCEP-TCTLKVGAQCSEGLCCYKCTFKKKGTLCRPAEDVCDLPEYCNGITGECPAN 520
Cdd:pfam00200 1 EEGEECDCGSLeeCTNDPCCDAkTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
79-194 |
6.03e-23 |
|
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: 95.07 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 79 ETVIPERLPG-------QGSDDPGGKVSYVLLMQGQKQLLHLEVKGHYSERNFPVYSY-HHGILGQEVPLLSQACHYEGH 150
Cdd:pfam01562 1 EVVIPVRLDPsrrrrslASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 9910118 151 IEGVPGSFVSVSICSGLRGVLIKEETAYGIEPLLFSTD----FEHILY 194
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
238-429 |
9.95e-21 |
|
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: 91.15 E-value: 9.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 238 KYVEMFVVVNHQRFQ-MWGSDVNTTVQAVVDIIA-LANSFTRGINTEVVLVGLEIWTEGDP-IEVPVDLQATLRNFNLWR 314
Cdd:cd04273 1 RYVETLVVADSKMVEfHHGEDLEHYILTLMNIVAsLYKDPSLGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCRWQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 315 QEKLMGRV----RHDVAHLI------VGHRPGANEGQAFLDGACSGGFAAAVeafhHEDVLLFAAL-MAHELGHNLGIRH 383
Cdd:cd04273 81 KKLNPPNDsdpeHHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSI----NEDTGLSSAFtIAHELGHVLGMPH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9910118 384 DRPGCTCGP--KHLCLMHETISKTSG---FSNCSSDHFLRFLHDHRGACLL 429
Cdd:cd04273 157 DGDGNSCGPegKDGHIMSPTLGANTGpftWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
238-420 |
2.45e-19 |
|
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: 86.71 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 238 KYVEMFVVVNHQRFQMWGSDVNTT---VQAVVDIIALANSFTRG-INTEVVLVGLEIWTEGDPIEVP-VDLQATLRNFNL 312
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILqayITELINIANSIYRSTNLrLGIRISLEGLQILKGEQFAPPIdSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 313 WRQEklmGRVRHDVAHLIVGH--RPGANEGQAFLDGACSGGFAAAVeAFHHEDVLLFAALMAHELGHNLGIRHDRPGCTC 390
Cdd:cd04267 81 WRAE---GPIRHDNAVLLTAQdfIEGDILGLAYVGSMCNPYSSVGV-VEDTGFTLLTALTMAHELGHNLGAEHDGGDELA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 9910118 391 GPK---HLCLMHETISKTSG--FSNCSSDHFLRFL 420
Cdd:cd04267 157 FECdggGNYIMAPVDSGLNSyrFSQCSIGSIREFL 191
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
264-384 |
2.52e-12 |
|
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: 64.31 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 264 AVVDIIALANS-FTRGINTEVVLVGLEIWTEGDPIEVPVDLQATLRNFnlwrQEKLMGRVRH---DVAHLIVGHRPGANE 339
Cdd:pfam13582 2 RIVSLVNRANTiYERDLGIRLQLAAIIITTSADTPYTSSDALEILDEL----QEVNDTRIGQygyDLGHLFTGRDGGGGG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 9910118 340 GQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHD 384
Cdd:pfam13582 78 GIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
240-384 |
3.66e-10 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 60.13 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 240 VEMFVVVNHQRFQMWGSD-VNTTVQAVVDiiALANSFTRGINTEVVLVGLEIWTEGDPIEVP----VDLQATLRNFNLwr 314
Cdd:pfam13688 5 VALLVAADCSYVAAFGGDaAQANIINMVN--TASNVYERDFNISLGLVNLTISDSTCPYTPPacstGDSSDRLSEFQD-- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9910118 315 QEKLMGRVRHDVAHLIVgHRPGANEGQAFLDGACSGGFAAAVEAF---------HHEDVLLFAalmaHELGHNLGIRHD 384
Cdd:pfam13688 81 FSAWRGTQNDDLAYLFL-MTNCSGGGLAWLGQLCNSGSAGSVSTRvsgnnvvvsTATEWQVFA----HEIGHNFGAVHD 154
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
239-384 |
9.89e-05 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 44.26 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 239 YVEMFVVVNhQRFQMWGSDVNttvQAVVDIIALANSF------TRGINTEVVLVGLEIWTEGDPIEVPVDLQ-------A 305
Cdd:cd04272 2 YPELFVVVD-YDHQSEFFSNE---QLIRYLAVMVNAAnlryrdLKSPRIRLLLVGITISKDPDFEPYIHPINygyidaaE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 306 TLRNFNLWRQEKlMGRVRHDVAHLIV---------GHRPGANEGQAFLDGACSGGFAAAVE--AFHHEDVLLfaalMAHE 374
Cdd:cd04272 78 TLENFNEYVKKK-RDYFNPDVVFLVTgldmstysgGSLQTGTGGYAYVGGACTENRVAMGEdtPGSYYGVYT----MTHE 152
|
170
....*....|
gi 9910118 375 LGHNLGIRHD 384
Cdd:cd04272 153 LAHLLGAPHD 162
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
257-391 |
1.30e-04 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 404471 Cd Length: 203 Bit Score: 43.76 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 257 DVNTTVQAVVDIIALANS-FTRGINTEVVLVGLE--IWTEGDPIEVPVDLQAT-LRNFNLWRQEKLMGRVRHDVAHLIVG 332
Cdd:pfam13583 21 SVDELRANINATVTTANEvYGRDFNVSLALISDRdvIYTDSSTDSFNADCSGGdLGNWRLATLTSWRDSLNYDLAYLTLM 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9910118 333 HRPGANE-GQAFLDGACS--------GGFAAAVEAFhhedvllfaALMAHELGHNLGIRHDRPGCTCG 391
Cdd:pfam13583 101 TGPSGQNvGVAWVGALCSsarqnakaSGVARSRDEW---------DIFAHEIGHTFGAVHDCSSQGEG 159
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
444-479 |
5.29e-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: 38.12 E-value: 5.29e-04
10 20 30
....*....|....*....|....*....|....*.
gi 9910118 444 CGNGVVEESEECDCGNACDSHPcCEPTCTLKVGAQC 479
Cdd:TIGR02232 4 CGDGIIEPGEECDDGNTTSGDG-CSATCRLEEGFAC 38
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
320-410 |
4.66e-03 |
|
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: 38.66 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910118 320 GRVRHDVAHL-IVGHRPGANEGQAFLDGACSGGFAAAVEAFHHEDVLLFAALMAHELGHNLGIRHDRPGCtCGPKHLCLM 398
Cdd:cd00203 48 EIDKADIAILvTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRK-DRDDYPTID 126
|
90
....*....|..
gi 9910118 399 HETISKTSGFSN 410
Cdd:cd00203 127 DTLNAEDDDYYS 138
|
|
| |
