|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
205-391 |
2.29e-67 |
|
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: 220.95 E-value: 2.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDHYG-NYTVMLSDLYSVINIVDTIYEVIGIKILLVGVEVWNKKNLIVI-DDVSKSLRLYCRWKASN 282
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 283 FLHRLKHDVSHLFIYRHLRG-LSGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDICKCSYSKCI 361
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
|
170 180 190
....*....|....*....|....*....|..
gi 283436121 362 MHMDSPPIPK-FSNCSYNYFWSYTVK-NTRCL 391
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRgGGQCL 192
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
489-624 |
2.12e-50 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 172.54 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 489 DGIPC-GVSAYCYEKQCNDRNEHCRQIFGQNAKTASVHCYREINTKGDRFGHCGLQGPTYIKCKSNDALCGRIQCDNVVQ 567
Cdd:smart00608 2 DGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 283436121 568 IPNMKDHSTIHFALVKNVSCWGTDYHTGTSlTDIGDVKDGTECEQNHICINRHCVHI 624
Cdd:smart00608 82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
412-484 |
1.68e-33 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 123.12 E-value: 1.68e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436121 412 EDKEQCDCGSLRNCTNDLCC-MSNCTLSTGSSCAFGLCCKNCQFLPSGTLCRKRDNICDLPEWCNGTSHECPDD 484
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
41-159 |
1.45e-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: 96.61 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 41 EVVIPMKVTEKTRGMNL------PNWISYSLKLGGQRYIIHMKIKNLFLTRHLPVFTYSDQDSLLEDYPFVQDDCYYQGY 114
Cdd:pfam01562 1 EVVIPVRLDPSRRRRSLasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 283436121 115 VEGDSESLVSLSSCfGGFHGLLEINNIVYEIMPKKF----SRKFEHLVY 159
Cdd:pfam01562 81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
205-391 |
2.29e-67 |
|
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: 220.95 E-value: 2.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDHYG-NYTVMLSDLYSVINIVDTIYEVIGIKILLVGVEVWNKKNLIVI-DDVSKSLRLYCRWKASN 282
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 283 FLHRLKHDVSHLFIYRHLRG-LSGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDICKCSYSKCI 361
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
|
170 180 190
....*....|....*....|....*....|..
gi 283436121 362 MHMDSPPIPK-FSNCSYNYFWSYTVK-NTRCL 391
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRgGGQCL 192
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
489-624 |
2.12e-50 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 172.54 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 489 DGIPC-GVSAYCYEKQCNDRNEHCRQIFGQNAKTASVHCYREINTKGDRFGHCGLQGPTYIKCKSNDALCGRIQCDNVVQ 567
Cdd:smart00608 2 DGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 283436121 568 IPNMKDHSTIHFALVKNVSCWGTDYHTGTSlTDIGDVKDGTECEQNHICINRHCVHI 624
Cdd:smart00608 82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
205-391 |
1.69e-44 |
|
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: 158.62 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDHYG-NYTVMLSDLYSVINIVDTIYEVIGIKILLVGVEVWNKKNLI-VIDDVSKSLRLYCRWKASN 282
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGsDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIdVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 283 FLHRLKHDVSHLFIYRHLRGL-SGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDI--CKC-SYS 358
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 283436121 359 KCIMHMD--SPPIPKFSNCSYNYFWSYTVK-NTRCL 391
Cdd:pfam01421 161 GCIMNPSagSSFPRKFSNCSQEDFEQFLTKqKGACL 196
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
489-592 |
1.95e-43 |
|
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: 152.00 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 489 DGIPCGVS-AYCYEKQCNDRNEHCRQIFGQNAKTASVHCYREINTKGDRFGHCGLQGPTYIKCKSNDALCGRIQCDNVVQ 567
Cdd:pfam08516 1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*
gi 283436121 568 IPNMKDHSTIHFALVKNVSCWGTDY 592
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
412-484 |
1.68e-33 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 123.12 E-value: 1.68e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436121 412 EDKEQCDCGSLRNCTNDLCC-MSNCTLSTGSSCAFGLCCKNCQFLPSGTLCRKRDNICDLPEWCNGTSHECPDD 484
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
412-486 |
1.25e-29 |
|
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: 112.01 E-value: 1.25e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436121 412 EDKEQCDCGSLRNCTNDLCCMSNCTLSTGSSCAFGLCCKNCQFLPSGTLCRKRDNICDLPEWCNGTSHECPDDAY 486
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
41-159 |
1.45e-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: 96.61 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 41 EVVIPMKVTEKTRGMNL------PNWISYSLKLGGQRYIIHMKIKNLFLTRHLPVFTYSDQDSLLEDYPFVQDDCYYQGY 114
Cdd:pfam01562 1 EVVIPVRLDPSRRRRSLasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 283436121 115 VEGDSESLVSLSSCfGGFHGLLEINNIVYEIMPKKF----SRKFEHLVY 159
Cdd:pfam01562 81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
403-443 |
8.39e-03 |
|
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: 34.66 E-value: 8.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 283436121 403 RTRCGNGVVEDKEQCDCGslrNCTNDLCCMSNCTLSTGSSC 443
Cdd:TIGR02232 1 APTCGDGIIEPGEECDDG---NTTSGDGCSATCRLEEGFAC 38
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
205-391 |
2.29e-67 |
|
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: 220.95 E-value: 2.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDHYG-NYTVMLSDLYSVINIVDTIYEVIGIKILLVGVEVWNKKNLIVI-DDVSKSLRLYCRWKASN 282
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVsGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 283 FLHRLKHDVSHLFIYRHLRG-LSGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDICKCSYSKCI 361
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
|
170 180 190
....*....|....*....|....*....|..
gi 283436121 362 MHMDSPPIPK-FSNCSYNYFWSYTVK-NTRCL 391
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRgGGQCL 192
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
489-624 |
2.12e-50 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 172.54 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 489 DGIPC-GVSAYCYEKQCNDRNEHCRQIFGQNAKTASVHCYREINTKGDRFGHCGLQGPTYIKCKSNDALCGRIQCDNVVQ 567
Cdd:smart00608 2 DGTPCdNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 283436121 568 IPNMKDHSTIHFALVKNVSCWGTDYHTGTSlTDIGDVKDGTECEQNHICINRHCVHI 624
Cdd:smart00608 82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
205-391 |
1.69e-44 |
|
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: 158.62 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDHYG-NYTVMLSDLYSVINIVDTIYEVIGIKILLVGVEVWNKKNLI-VIDDVSKSLRLYCRWKASN 282
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGsDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIdVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 283 FLHRLKHDVSHLFIYRHLRGL-SGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDI--CKC-SYS 358
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 283436121 359 KCIMHMD--SPPIPKFSNCSYNYFWSYTVK-NTRCL 391
Cdd:pfam01421 161 GCIMNPSagSSFPRKFSNCSQEDFEQFLTKqKGACL 196
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
489-592 |
1.95e-43 |
|
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: 152.00 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 489 DGIPCGVS-AYCYEKQCNDRNEHCRQIFGQNAKTASVHCYREINTKGDRFGHCGLQGPTYIKCKSNDALCGRIQCDNVVQ 567
Cdd:pfam08516 1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*
gi 283436121 568 IPNMKDHSTIHFALVKNVSCWGTDY 592
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
412-484 |
1.68e-33 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 123.12 E-value: 1.68e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 283436121 412 EDKEQCDCGSLRNCTNDLCC-MSNCTLSTGSSCAFGLCCKNCQFLPSGTLCRKRDNICDLPEWCNGTSHECPDD 484
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
412-486 |
1.25e-29 |
|
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: 112.01 E-value: 1.25e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 283436121 412 EDKEQCDCGSLRNCTNDLCCMSNCTLSTGSSCAFGLCCKNCQFLPSGTLCRKRDNICDLPEWCNGTSHECPDDAY 486
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
205-383 |
1.78e-24 |
|
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: 101.93 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDHYGNytvmlSDL--Y--SVINIVDTIY--EVIG--IKILLVGVEVWN--KKNLIVIDDVSKSLRL 274
Cdd:cd04273 1 RYVETLVVADSKMVEFHHG-----EDLehYilTLMNIVASLYkdPSLGnsINIVVVRLIVLEdeESGLLISGNAQKSLKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 275 YCRWKAS----NFLHRLKHDVSHLF----IYRHLR--GLSGIGSTGGICDPKRSCAVVTfiDRTLNLrAIGVAHHLGHNL 344
Cdd:cd04273 76 FCRWQKKlnppNDSDPEHHDHAILLtrqdICRSNGncDTLGLAPVGGMCSPSRSCSINE--DTGLSS-AFTIAHELGHVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 283436121 345 GMKHDEDICKC---SYSKCIM--HMDSPPIPKF-SNCSYNYFWSY 383
Cdd:cd04273 153 GMPHDGDGNSCgpeGKDGHIMspTLGANTGPFTwSKCSRRYLTSF 197
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
41-159 |
1.45e-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: 96.61 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 41 EVVIPMKVTEKTRGMNL------PNWISYSLKLGGQRYIIHMKIKNLFLTRHLPVFTYSDQDSLLEDYPFVQDDCYYQGY 114
Cdd:pfam01562 1 EVVIPVRLDPSRRRRSLasestyLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 283436121 115 VEGDSESLVSLSSCfGGFHGLLEINNIVYEIMPKKF----SRKFEHLVY 159
Cdd:pfam01562 81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
207-379 |
4.45e-21 |
|
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: 91.71 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 207 VELVVVVDKTLYDHY-GNYTVMLSDLYSVINIVDTIYEVI----GIKILLVGVEVWNKKNLIVIDDVSKSLRL--YCRWK 279
Cdd:cd04267 3 IELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTnlrlGIRISLEGLQILKGEQFAPPIDSDASNTLnsFSFWR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 280 ASNflhRLKHDVSHLFIYRHLRGLSGIG--STGGICDPKRSCAVVTFIDRTLnLRAIGVAHHLGHNLGMKHDEDIC---- 353
Cdd:cd04267 83 AEG---PIRHDNAVLLTAQDFIEGDILGlaYVGSMCNPYSSVGVVEDTGFTL-LTALTMAHELGHNLGAEHDGGDElafe 158
|
170 180
....*....|....*....|....*...
gi 283436121 354 KCSYSKCIMH-MDSPPIPK-FSNCSYNY 379
Cdd:cd04267 159 CDGGGNYIMApVDSGLNSYrFSQCSIGS 186
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
204-373 |
4.84e-11 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 62.44 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 204 TKIVELVVVVDKTLYD-HYGNYTVmlSDLYSVINIVDTIYEV-IGIKILLVGVEVWNKKNLIVIDDVSK---SLRLYCRW 278
Cdd:pfam13688 2 TRTVALLVAADCSYVAaFGGDAAQ--ANIINMVNTASNVYERdFNISLGLVNLTISDSTCPYTPPACSTgdsSDRLSEFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 279 KASNFLHRLKHDVSHLFIYRHLRGlSGIGSTGGICDPKRSCAVVTFIDRTLNLRAIG-----VAHHLGHNLGMKHDEDIC 353
Cdd:pfam13688 80 DFSAWRGTQNDDLAYLFLMTNCSG-GGLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHNFGAVHDCDSS 158
|
170 180 190
....*....|....*....|....*....|...
gi 283436121 354 K----CSYS--------KCIMHMDSPP-IPKFS 373
Cdd:pfam13688 159 TssqcCPPSnstcpaggRYIMNPSSSPnSTDFS 191
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
233-349 |
1.99e-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: 55.84 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 233 SVINIVDTIYEV-IGIKILLVGVEVW--------NKKNLIVIDDVSKSLRLycRWKASNFlhrlkhDVSHLFIYRHLRGL 303
Cdd:pfam13582 5 SLVNRANTIYERdLGIRLQLAAIIITtsadtpytSSDALEILDELQEVNDT--RIGQYGY------DLGHLFTGRDGGGG 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 283436121 304 SGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHD 349
Cdd:pfam13582 77 GGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
209-376 |
6.14e-07 |
|
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.
Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 51.22 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 209 LVVVVDKTLYDHYG--NYTVMLSDLYSVINIVDTIYEVI---GIKILLVGVEVwnkKNLIVIDDVSKS-------LRLYC 276
Cdd:cd04270 5 LLLVADHRFYKYMGrgEEETTINYLISHIDRVDDIYRNTdwdGGGFKGIGFQI---KRIRIHTTPDEVdpgnkfyNKSFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 277 RWKASNFLHRLKHDVS-------HLFIYRHLR----GLSGIGS-----TGGICDP------KRSCAVVTFIDRTLNLRA- 333
Cdd:cd04270 82 NWGVEKFLVKLLLEQFsddvclaHLFTYRDFDmgtlGLAYVGSprdnsAGGICEKayyysnGKKKYLNTGLTTTVNYGKr 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 334 -------IGVAHHLGHNLGMKHDEDICKCSYS-----KCIMHM-----DSPPIPKFSNCS 376
Cdd:cd04270 162 vptkesdLVTAHELGHNFGSPHDPDIAECAPGesqggNYIMYAratsgDKENNKKFSPCS 221
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
205-381 |
1.57e-06 |
|
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: 48.67 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDhygnYTVMLSDLYSVINIVDTIYE-VIGIKILLVGVEVwnkknlividdvskslrlycrwkasnf 283
Cdd:cd00203 1 KVIPYVVVADDRDVE----EENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI--------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 284 lhrLKHDVSHLFIYRHLRGLSGIGS-TGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDICKCSYSKCIM 362
Cdd:cd00203 50 ---DKADIAILVTRQDFDGGTGGWAyLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTID 126
|
170
....*....|....*....
gi 283436121 363 hMDSPPIPKFSNCSYNYFW 381
Cdd:cd00203 127 -DTLNAEDDDYYSVMSYTK 144
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
205-380 |
6.69e-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: 41.84 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 205 KIVELVVVVDKTLYDHYGNYTVMLSDLYSVINIVDTIYE-VIGIKILLVGvevwnKKNLIVIDDVSKSLRLYCRWKAS-- 281
Cdd:pfam13583 3 RVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYGrDFNVSLALIS-----DRDVIYTDSSTDSFNADCSGGDLgn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283436121 282 ---NFLHR----LKHDVSHLFI-YRHLRGLSGIGSTGGICDPKRSCAVVTFIDRTLNLRAIgVAHHLGHNLGMKHD--ED 351
Cdd:pfam13583 78 wrlATLTSwrdsLNYDLAYLTLmTGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDI-FAHEIGHTFGAVHDcsSQ 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 283436121 352 ICKCSYSKC------IM---HMDSPpiPKFSNCSYNYF 380
Cdd:pfam13583 157 GEGLSSSTEdgsgqtIMsyaSTASQ--TAFSPCTIRNI 192
|
|
| myxo_disulf_rpt |
TIGR02232 |
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ... |
403-443 |
8.39e-03 |
|
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: 34.66 E-value: 8.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 283436121 403 RTRCGNGVVEDKEQCDCGslrNCTNDLCCMSNCTLSTGSSC 443
Cdd:TIGR02232 1 APTCGDGIIEPGEECDDG---NTTSGDGCSATCRLEEGFAC 38
|
|
| |
