|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
240-434 |
1.96e-93 |
|
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: 291.13 E-value: 1.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 240 KYVEMFVVVNNQRFQMWGSNVNETVQRVVDVIALANSFTREINTEVVLAGLEIWTERELIEVAADLQVTLRNFNRWRQEM 319
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 320 LFHRAKHDVAHMIVGHHPGQNT-GQAFLSGACSSSFAAAVESFHHEDVLLFAALMVHELGHNLGIQHDHSA--CFCKDKH 396
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTvGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2632094 397 FCLMHENITKESG--FSNCSSDYFYQFLREHKGTCLFNKP 434
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
526-665 |
4.41e-54 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 183.33 E-value: 4.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 526 QDGTLCDRIH-YCSGGQCKNPDKQCVNIYGYPARSAPEDCYVSMNTRGDRFGNCGRpteDQQKYVTCSNDNVFCGKLVCT 604
Cdd:smart00608 1 QDGTPCDNGQgYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR---ENGTYIPCAPEDVKCGKLQCT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2632094 605 GVESLPRLKAQHTIIQVPHDDDWCWSMDAHNITDiPDDGDVHTGTSCAPNKVCTDYSCVHH 665
Cdd:smart00608 78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
452-524 |
2.62e-33 |
|
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: 122.41 E-value: 2.62e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2632094 452 EDTEQCDCGSACD-LDPRCDP-TCTLKENAECSHGLCCLDCTFRRKGFLCRPTQDECDLPEYCDGSSAECPADSY 524
Cdd:smart00050 1 EEGEECDCGSPKEcTDPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
80-195 |
9.78e-24 |
|
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: 97.38 E-value: 9.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 80 EIITPKRLT-------VQGADSPVKGLSYLLFMEGQKHLVHLKVKRSHFVNNFPVYSY-HNGILRQESPFISHDCHYEGY 151
Cdd:pfam01562 1 EVVIPVRLDpsrrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2632094 152 IEGVSGSFVSVNTCAGLRGILIKEEKSYSIEPMESSRR----FEHVLY 195
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 ... |
240-434 |
1.96e-93 |
|
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: 291.13 E-value: 1.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 240 KYVEMFVVVNNQRFQMWGSNVNETVQRVVDVIALANSFTREINTEVVLAGLEIWTERELIEVAADLQVTLRNFNRWRQEM 319
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 320 LFHRAKHDVAHMIVGHHPGQNT-GQAFLSGACSSSFAAAVESFHHEDVLLFAALMVHELGHNLGIQHDHSA--CFCKDKH 396
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTvGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2632094 397 FCLMHENITKESG--FSNCSSDYFYQFLREHKGTCLFNKP 434
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
240-432 |
1.45e-69 |
|
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: 1.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 240 KYVEMFVVVNNQRFQMWGSNVNETVQRVVDVIALANSFTREINTEVVLAGLEIWTERELIEVAADLQVTLRNFNRWRQEM 319
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 320 LFHRAKHDVAHMIVGHHPGQNT-GQAFLSGACSSSFAAAVESFHHEDVLLFAALMVHELGHNLGIQHDHSACFCKDKhFC 398
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTvGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRS-TC 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2632094 399 LMHENITKES-GFSNCSSDYFYQFLREHKGTCLFN 432
Cdd:cd04269 160 IMAPSPSSLTdAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
526-665 |
4.41e-54 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 183.33 E-value: 4.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 526 QDGTLCDRIH-YCSGGQCKNPDKQCVNIYGYPARSAPEDCYVSMNTRGDRFGNCGRpteDQQKYVTCSNDNVFCGKLVCT 604
Cdd:smart00608 1 QDGTPCDNGQgYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR---ENGTYIPCAPEDVKCGKLQCT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2632094 605 GVESLPRLKAQHTIIQVPHDDDWCWSMDAHNITDiPDDGDVHTGTSCAPNKVCTDYSCVHH 665
Cdd:smart00608 78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
527-632 |
2.23e-40 |
|
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: 143.91 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 527 DGTLCDR-IHYCSGGQCKNPDKQCVNIYGYPARSAPEDCYVSMNTRGDRFGNCGRpteDQQKYVTCSNDNVFCGKLVCTG 605
Cdd:pfam08516 1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR---TNGGYVKCEKRDVLCGKLQCTN 77
|
90 100
....*....|....*....|....*..
gi 2632094 606 VESLPRLKAQHTIIQVPHDDDWCWSMD 632
Cdd:pfam08516 78 VKELPLLGEHATVIYTNINGVTCWGTD 104
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
452-524 |
2.62e-33 |
|
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: 122.41 E-value: 2.62e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2632094 452 EDTEQCDCGSACD-LDPRCDP-TCTLKENAECSHGLCCLDCTFRRKGFLCRPTQDECDLPEYCDGSSAECPADSY 524
Cdd:smart00050 1 EEGEECDCGSPKEcTDPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
452-522 |
1.81e-31 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 117.34 E-value: 1.81e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2632094 452 EDTEQCDCGSA--CDLDPRCDP-TCTLKENAECSHGLCCLDCTFRRKGFLCRPTQDECDLPEYCDGSSAECPAD 522
Cdd:pfam00200 1 EEGEECDCGSLeeCTNDPCCDAkTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
80-195 |
9.78e-24 |
|
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: 97.38 E-value: 9.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 80 EIITPKRLT-------VQGADSPVKGLSYLLFMEGQKHLVHLKVKRSHFVNNFPVYSY-HNGILRQESPFISHDCHYEGY 151
Cdd:pfam01562 1 EVVIPVRLDpsrrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2632094 152 IEGVSGSFVSVNTCAGLRGILIKEEKSYSIEPMESSRR----FEHVLY 195
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
443-481 |
2.48e-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: 38.89 E-value: 2.48e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2632094 443 DSTCGNGMVEDTEQCDCGSACDLDPrCDPTCTLKENAEC 481
Cdd:TIGR02232 1 APTCGDGIIEPGEECDDGNTTSGDG-CSATCRLEEGFAC 38
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
240-434 |
1.96e-93 |
|
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: 291.13 E-value: 1.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 240 KYVEMFVVVNNQRFQMWGSNVNETVQRVVDVIALANSFTREINTEVVLAGLEIWTERELIEVAADLQVTLRNFNRWRQEM 319
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 320 LFHRAKHDVAHMIVGHHPGQNT-GQAFLSGACSSSFAAAVESFHHEDVLLFAALMVHELGHNLGIQHDHSA--CFCKDKH 396
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTvGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2632094 397 FCLMHENITKESG--FSNCSSDYFYQFLREHKGTCLFNKP 434
Cdd:pfam01421 161 GCIMNPSAGSSFPrkFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
240-432 |
1.45e-69 |
|
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: 1.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 240 KYVEMFVVVNNQRFQMWGSNVNETVQRVVDVIALANSFTREINTEVVLAGLEIWTERELIEVAADLQVTLRNFNRWRQEM 319
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 320 LFHRAKHDVAHMIVGHHPGQNT-GQAFLSGACSSSFAAAVESFHHEDVLLFAALMVHELGHNLGIQHDHSACFCKDKhFC 398
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTvGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRS-TC 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2632094 399 LMHENITKES-GFSNCSSDYFYQFLREHKGTCLFN 432
Cdd:cd04269 160 IMAPSPSSLTdAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
526-665 |
4.41e-54 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 183.33 E-value: 4.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 526 QDGTLCDRIH-YCSGGQCKNPDKQCVNIYGYPARSAPEDCYVSMNTRGDRFGNCGRpteDQQKYVTCSNDNVFCGKLVCT 604
Cdd:smart00608 1 QDGTPCDNGQgYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR---ENGTYIPCAPEDVKCGKLQCT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2632094 605 GVESLPRLKAQHTIIQVPHDDDWCWSMDAHNITDiPDDGDVHTGTSCAPNKVCTDYSCVHH 665
Cdd:smart00608 78 NVSELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
527-632 |
2.23e-40 |
|
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: 143.91 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 527 DGTLCDR-IHYCSGGQCKNPDKQCVNIYGYPARSAPEDCYVSMNTRGDRFGNCGRpteDQQKYVTCSNDNVFCGKLVCTG 605
Cdd:pfam08516 1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR---TNGGYVKCEKRDVLCGKLQCTN 77
|
90 100
....*....|....*....|....*..
gi 2632094 606 VESLPRLKAQHTIIQVPHDDDWCWSMD 632
Cdd:pfam08516 78 VKELPLLGEHATVIYTNINGVTCWGTD 104
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
452-524 |
2.62e-33 |
|
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: 122.41 E-value: 2.62e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2632094 452 EDTEQCDCGSACD-LDPRCDP-TCTLKENAECSHGLCCLDCTFRRKGFLCRPTQDECDLPEYCDGSSAECPADSY 524
Cdd:smart00050 1 EEGEECDCGSPKEcTDPCCDPaTCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
452-522 |
1.81e-31 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 117.34 E-value: 1.81e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2632094 452 EDTEQCDCGSA--CDLDPRCDP-TCTLKENAECSHGLCCLDCTFRRKGFLCRPTQDECDLPEYCDGSSAECPAD 522
Cdd:pfam00200 1 EEGEECDCGSLeeCTNDPCCDAkTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
80-195 |
9.78e-24 |
|
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: 97.38 E-value: 9.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 80 EIITPKRLT-------VQGADSPVKGLSYLLFMEGQKHLVHLKVKRSHFVNNFPVYSY-HNGILRQESPFISHDCHYEGY 151
Cdd:pfam01562 1 EVVIPVRLDpsrrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2632094 152 IEGVSGSFVSVNTCAGLRGILIKEEKSYSIEPMESSRR----FEHVLY 195
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
240-431 |
1.62e-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: 84.60 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 240 KYVEMFVVVNNQrfqMWGSNVNETVQRVVdvIALAN---------SFTREINteVVLAGLEIWTERE-LIEVAADLQVTL 309
Cdd:cd04273 1 RYVETLVVADSK---MVEFHHGEDLEHYI--LTLMNivaslykdpSLGNSIN--IVVVRLIVLEDEEsGLLISGNAQKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 310 RNFNRWRQEML----FHRAKHDVAHMI------VGHHPGQNTGQAFLSGACSSSFAAAVesfhHEDVLLFAALMV-HELG 378
Cdd:cd04273 74 KSFCRWQKKLNppndSDPEHHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSI----NEDTGLSSAFTIaHELG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2632094 379 HNLGIQHDHSACFCKD--KHFCLMHENITKESG---FSNCSSDYFYQFLREHKGTCLF 431
Cdd:cd04273 150 HVLGMPHDGDGNSCGPegKDGHIMSPTLGANTGpftWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
240-423 |
2.20e-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: 80.93 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 240 KYVEMFVVVNNQRFQMWGSNVNETVQRVVDVIALANSFTREINT----EVVLAGLEIWTERELIEV-AADLQVTLRNFNR 314
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 315 WRQEmlfHRAKHDVAHMIVGHH-PGQNT-GQAFLSGACSSSFAAAVESfHHEDVLLFAALMVHELGHNLGIQHD---HSA 389
Cdd:cd04267 81 WRAE---GPIRHDNAVLLTAQDfIEGDIlGLAYVGSMCNPYSSVGVVE-DTGFTLLTALTMAHELGHNLGAEHDggdELA 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 2632094 390 CFCKDKHFCLMHENITKESG--FSNCSSDYFYQFLR 423
Cdd:cd04267 157 FECDGGGNYIMAPVDSGLNSyrFSQCSIGSIREFLD 192
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
266-386 |
2.72e-11 |
|
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: 61.62 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 266 RVVDVIALANS-FTREINTEVVLAGLEIWTERELIEVAADLQVTLRNFNRWRQEMLfHRAKHDVAHMIVGHHPGQNTGQA 344
Cdd:pfam13582 2 RIVSLVNRANTiYERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRI-GQYGYDLGHLFTGRDGGGGGGIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2632094 345 FLSGACSSSFAAAVESFHHEDVLLFAALMVHELGHNLGIQHD 386
Cdd:pfam13582 81 YVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
261-387 |
1.42e-08 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 55.50 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 261 NETVQRVVDVIALANS-FTREINTEVVLAGLEIWTERELIEVAADLQVT-------LRNFNRWRqemlfHRAKHDVAHMI 332
Cdd:pfam13688 22 DAAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPACSTGDssdrlseFQDFSAWR-----GTQNDDLAYLF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2632094 333 VgHHPGQNTGQAFLSGACSSSFAAAVESF---------HHEDVLLFAalmvHELGHNLGIQHDH 387
Cdd:pfam13688 97 L-MTNCSGGGLAWLGQLCNSGSAGSVSTRvsgnnvvvsTATEWQVFA----HEIGHNFGAVHDC 155
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
241-430 |
2.97e-07 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 51.97 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 241 YVEMFVVVNnQRFQMWGSNVNETVQRV---VDVIALANSFTREINTEVVLAGLEIWTE-------RELIEVAADLQVTLR 310
Cdd:cd04272 2 YPELFVVVD-YDHQSEFFSNEQLIRYLavmVNAANLRYRDLKSPRIRLLLVGITISKDpdfepyiHPINYGYIDAAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 311 NFN--------RWRQEMLFHRAKHDVAHMIVGHHPGQNTGQAFLSGACSSSFAAAVE----SFhhEDVLLFAalmvHELG 378
Cdd:cd04272 81 NFNeyvkkkrdYFNPDVVFLVTGLDMSTYSGGSLQTGTGGYAYVGGACTENRVAMGEdtpgSY--YGVYTMT----HELA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2632094 379 HNLGIQHDHS-----------ACFCKDKHFCLMH--ENITKESGFSNCSSDYFYQFLREHKGTCL 430
Cdd:cd04272 155 HLLGAPHDGSpppswvkghpgSLDCPWDDGYIMSyvVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
284-400 |
2.09e-05 |
|
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: 45.59 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 284 EVVLAGLEIWTERELIevaadlQVTLRNFNRwrqemlfhrAKHDVAH-MIVGHHPGQNTGQAFLSGACSSSFAAAVESFH 362
Cdd:cd00203 25 SLILIAMQIWRDYLNI------RFVLVGVEI---------DKADIAIlVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDN 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 2632094 363 HEDVLLFAALMVHELGHNLGIQHDHSACfCKDKHFCLM 400
Cdd:cd00203 90 QSGTKEGAQTIAHELGHALGFYHDHDRK-DRDDYPTID 126
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
239-418 |
5.85e-05 |
|
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: 44.92 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 239 PKYVEMFVVVNNQRFQMWGSnVNETVQRVVDVIALANS-FTREINTEVVLAGLE--IWTERELIEVAADLQVT------L 309
Cdd:pfam13583 2 RRVYRVAVATDCTYSASFGS-VDELRANINATVTTANEvYGRDFNVSLALISDRdvIYTDSSTDSFNADCSGGdlgnwrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2632094 310 RNFNRWRQEmlfhrAKHDVAHMIVGHHP-GQNTGQAFLSGACSSS--------FAAAVESFHhedvlLFAalmvHELGHN 380
Cdd:pfam13583 81 ATLTSWRDS-----LNYDLAYLTLMTGPsGQNVGVAWVGALCSSArqnakasgVARSRDEWD-----IFA----HEIGHT 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2632094 381 LGIQHD-------HSACFCKDKHFCLM-HENITKESGFSNCSSDYF 418
Cdd:pfam13583 147 FGAVHDcssqgegLSSSTEDGSGQTIMsYASTASQTAFSPCTIRNI 192
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
443-481 |
2.48e-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: 38.89 E-value: 2.48e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2632094 443 DSTCGNGMVEDTEQCDCGSACDLDPrCDPTCTLKENAEC 481
Cdd:TIGR02232 1 APTCGDGIIEPGEECDDGNTTSGDG-CSATCRLEEGFAC 38
|
|
| ZnMc_MMP_like |
cd04268 |
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
332-389 |
6.41e-03 |
|
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.
Pssm-ID: 239796 [Multi-domain] Cd Length: 165 Bit Score: 38.25 E-value: 6.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2632094 332 IVGHHPGQNTGQAFL-SGACSSSFAAAVESFhhedvllFAALMVHELGHNLGIQHDHSA 389
Cdd:cd04268 63 YGPSQVDPLTGEILLaRVYLYSSFVEYSGAR-------LRNTAEHELGHALGLRHNFAA 114
|
|
| |
