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Conserved domains on  [gi|162329887]
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Chain A, Coagulation factor X-activating enzyme heavy chain

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 10136411)

protein containing domains ZnMc_adamalysin_II_like, DISIN, and ACR

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 12-203 5.78e-85

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: 257.93  E-value: 5.78e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  12 FIELVIIVDHSMAKKCNS--TATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDL 89
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  90 MTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVGIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVM 169
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIM 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 162329887 170 SPVLSDqPSKLFSNCSIHDYQRYLTRYKPKCIFN 203
Cdd:cd04269  162 APSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
298-418 4.37e-45

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 152.90  E-value: 4.37e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   298 QNGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQE-NLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNN- 375
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVs 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 162329887   376 -------------SPRNKNPCNMHYSC--MDQHKGMVDPGTKCEDGKVCNNkRQCVDV 418
Cdd:smart00608  81 elpllgehatviySNIGGLVCWSLDYHlgTDPDIGMVKDGTKCGPGKVCIN-GQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 222-294 6.58e-36

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: 126.65  E-value: 6.58e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162329887   222 EEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRD 294
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 12-203 5.78e-85

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: 257.93  E-value: 5.78e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  12 FIELVIIVDHSMAKKCNS--TATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDL 89
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  90 MTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVGIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVM 169
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIM 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 162329887 170 SPVLSDqPSKLFSNCSIHDYQRYLTRYKPKCIFN 203
Cdd:cd04269  162 APSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 12-205 4.66e-65

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: 207.15  E-value: 4.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   12 FIELVIIVDHSMAKKCNS--TATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDL 89
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   90 MTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVGIVQEQGNRNFKTAVIMAHELSHNLGMYHD--GKNCICNDS-S 166
Cdd:pfam01421  82 KKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPGgG 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 162329887  167 CVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCIFNPP 205
Cdd:pfam01421 162 CIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
298-418 4.37e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 152.90  E-value: 4.37e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   298 QNGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQE-NLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNN- 375
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVs 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 162329887   376 -------------SPRNKNPCNMHYSC--MDQHKGMVDPGTKCEDGKVCNNkRQCVDV 418
Cdd:smart00608  81 elpllgehatviySNIGGLVCWSLDYHlgTDPDIGMVKDGTKCGPGKVCIN-GQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 222-294 6.58e-36

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: 126.65  E-value: 6.58e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162329887   222 EEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRD 294
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
Disintegrin pfam00200
Disintegrin;
222-294 9.73e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.11  E-value: 9.73e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162329887  222 EEGEECDCGSPANCQ-NPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRD 294
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 299-374 2.02e-21

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: 88.44  E-value: 2.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162329887  299 NGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQE-NLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLN 374
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTN 77
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 12-203 5.78e-85

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: 257.93  E-value: 5.78e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  12 FIELVIIVDHSMAKKCNS--TATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDL 89
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  90 MTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVGIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICNDSSCVM 169
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIM 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 162329887 170 SPVLSDqPSKLFSNCSIHDYQRYLTRYKPKCIFN 203
Cdd:cd04269  162 APSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 12-205 4.66e-65

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: 207.15  E-value: 4.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   12 FIELVIIVDHSMAKKCNS--TATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDL 89
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   90 MTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVGIVQEQGNRNFKTAVIMAHELSHNLGMYHD--GKNCICNDS-S 166
Cdd:pfam01421  82 KKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPGgG 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 162329887  167 CVMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCIFNPP 205
Cdd:pfam01421 162 CIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
298-418 4.37e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 152.90  E-value: 4.37e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   298 QNGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQE-NLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLNN- 375
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVs 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 162329887   376 -------------SPRNKNPCNMHYSC--MDQHKGMVDPGTKCEDGKVCNNkRQCVDV 418
Cdd:smart00608  81 elpllgehatviySNIGGLVCWSLDYHlgTDPDIGMVKDGTKCGPGKVCIN-GQCVDV 137
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 12-193 7.40e-43

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: 149.11  E-value: 7.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  12 FIELVIIVDHSMAKKCNSTATNTK--IYEIVNSANEIFN----PLNIHVTLIGVEFWCDRDLINV-TSSADETLNSFGEW 84
Cdd:cd04267    2 EIELVVVADHRMVSYFNSDENILQayITELINIANSIYRstnlRLGIRISLEGLQILKGEQFAPPiDSDASNTLNSFSFW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  85 RASDlmtRKSHDNALLFTdmRFDLN---TLGITFLAGMCQAYRSVGIVQEQGNrNFKTAVIMAHELSHNLGMYHDGKNCI 161
Cdd:cd04267   82 RAEG---PIRHDNAVLLT--AQDFIegdILGLAYVGSMCNPYSSVGVVEDTGF-TLLTALTMAHELGHNLGAEHDGGDEL 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 162329887 162 CN----DSSCVMSPVLSDQPSKLFSNCSIHDYQRYL 193
Cdd:cd04267  156 AFecdgGGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 222-294 6.58e-36

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: 126.65  E-value: 6.58e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162329887   222 EEGEECDCGSPANCQNPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRD 294
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 12-200 1.15e-33

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: 125.04  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  12 FIELVIIVDHSMAKKCNSTATNTKIYEIVNSANEIF------NPLNIHVTLIgvEFWCDR-DLINVTSSADETLNSFGEW 84
Cdd:cd04273    2 YVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYkdpslgNSINIVVVRL--IVLEDEeSGLLISGNAQKSLKSFCRW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  85 RASDLMTRKS----HDNALLFTdmRFDL-------NTLGITFLAGMCQAYRSVGIVQEQGnrnFKTAVIMAHELSHNLGM 153
Cdd:cd04273   80 QKKLNPPNDSdpehHDHAILLT--RQDIcrsngncDTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELGHVLGM 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162329887 154 YHDGKNCICNDSS---CVMSPVLSDQPSKLF-SNCSIHDYQRYLTRYKPKC 200
Cdd:cd04273  155 PHDGDGNSCGPEGkdgHIMSPTLGANTGPFTwSKCSRRYLTSFLDTGDGNC 205
Disintegrin pfam00200
Disintegrin;
222-294 9.73e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.11  E-value: 9.73e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162329887  222 EEGEECDCGSPANCQ-NPCCDAATCKLKPGAECGNGLCCYQCKIKTAGTVCRRARDECDVPEHCTGQSAECPRD 294
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 12-193 6.09e-23

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: 94.90  E-value: 6.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  12 FIELVIIVDHSMAKKCNSTATntkIYEIVNSANEIFN-PLNIHVTLIGVEfwcdrdlinvtssadetlnsfgewrasdlm 90
Cdd:cd00203    2 VIPYVVVADDRDVEEENLSAQ---IQSLILIAMQIWRdYLNIRFVLVGVE------------------------------ 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  91 tRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVGIVQEQGNRNFKTAVIMAHELSHNLGMYHDGKNCICN------- 163
Cdd:cd00203   49 -IDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDdyptidd 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 162329887 164 -------DSSCVMSPVL---SDQPSKLFSNCSIHDYQRYL 193
Cdd:cd00203  128 tlnaeddDYYSVMSYTKgsfSDGQRKDFSQCDIDQINKLY 167
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 299-374 2.02e-21

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: 88.44  E-value: 2.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162329887  299 NGKPCQNNRGYCYNGDCPIMRNQCISLFGSRANVAKDSCFQE-NLKGSYYGYCRKENGRKIPCAPQDVKCGRLFCLN 374
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTN 77
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
15-182 3.16e-15

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 73.61  E-value: 3.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   15 LVIIVDHSMAKKCNSTATNTKIYEIVNSANEIF-NPLNIHVTLIGVEFW----CDRDLINVTSSADETLNSFGEwrASDL 89
Cdd:pfam13688   7 LLVAADCSYVAAFGGDAAQANIINMVNTASNVYeRDFNISLGLVNLTISdstcPYTPPACSTGDSSDRLSEFQD--FSAW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   90 MTRKSHDNALLFTDmrFDLNTLGITFLAGMCQAYrSVGIVQEQGNRNFK------TAVIMAHELSHNLGMYHD------- 156
Cdd:pfam13688  85 RGTQNDDLAYLFLM--TNCSGGGLAWLGQLCNSG-SAGSVSTRVSGNNVvvstatEWQVFAHEIGHNFGAVHDcdsstss 161

                         170       180       190
                  ....*....|....*....|....*....|.
gi 162329887  157 ----GKNCICNDS-SCVMSPVlSDQPSKLFS 182
Cdd:pfam13688 162 qccpPSNSTCPAGgRYIMNPS-SSPNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 39-156 2.98e-13

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: 66.24  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   39 IVNSANEIFNP-LNIHVTLIGVEFWCDRDLINVTSSADETLNSFgewrASDLMTRKSHDNA---LLFTDmRFDLNTLGIT 114
Cdd:pfam13582   6 LVNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDEL----QEVNDTRIGQYGYdlgHLFTG-RDGGGGGGIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 162329887  115 FLAGMCQAYRSVGIVQEQGNRNFKTAVIMAHELSHNLGMYHD 156
Cdd:pfam13582  81 YVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 24-186 4.76e-13

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: 67.64  E-value: 4.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   24 AKKCNSTATNTKIYEIVNSANEIF-NPLNIHVTLIGvefwcDRDLINVTSSAD-------------ETLNSFGEWRASdl 89
Cdd:pfam13583  17 ASFGSVDELRANINATVTTANEVYgRDFNVSLALIS-----DRDVIYTDSSTDsfnadcsggdlgnWRLATLTSWRDS-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887   90 mtrKSHDNALLFTDMRFDLNTLGITFLAGMC-QAYRSvgivqEQGN---RNFKTAVIMAHELSHNLGMYHDGKN--CICN 163
Cdd:pfam13583  90 ---LNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQN-----AKASgvaRSRDEWDIFAHEIGHTFGAVHDCSSqgEGLS 161

                         170       180
                  ....*....|....*....|....*....
gi 162329887  164 DSSC------VMSPVlSDQPSKLFSNCSI 186
Cdd:pfam13583 162 SSTEdgsgqtIMSYA-STASQTAFSPCTI 189
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 11-201 4.24e-12

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 65.45  E-value: 4.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  11 IFIELVIIVDHSMAKKCNSTaTNTKIYEIV--NSAN----EIFNPlNIHVTLIGVEF----WCDRDLINVTSSAD---ET 77
Cdd:cd04272    1 VYPELFVVVDYDHQSEFFSN-EQLIRYLAVmvNAANlryrDLKSP-RIRLLLVGITIskdpDFEPYIHPINYGYIdaaET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  78 LNSFGEWrasdlMTRKSH----DNALLFT--DMRFDLN------TLGITFLAGMCQAYRsVGIVQEQGNrNFKTAVIMAH 145
Cdd:cd04272   79 LENFNEY-----VKKKRDyfnpDVVFLVTglDMSTYSGgslqtgTGGYAYVGGACTENR-VAMGEDTPG-SYYGVYTMTH 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162329887 146 ELSHNLGMYHDG----KNCICNDSS--C------VMSPVLSDQPSKLFSNCSIHDYQRYLTRYKPKCI 201
Cdd:cd04272  152 ELAHLLGAPHDGspppSWVKGHPGSldCpwddgyIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 15-200 2.20e-08

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: 54.69  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  15 LVIIVDHS----MAKKCNSTATNtKIYEIVNSANEIFNPLNIHVTLI-GVEFWCDRDLINVTSSADETLN-----SFGEW 84
Cdd:cd04270    5 LLLVADHRfykyMGRGEEETTIN-YLISHIDRVDDIYRNTDWDGGGFkGIGFQIKRIRIHTTPDEVDPGNkfynkSFPNW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162329887  85 RASDLMTRKSHDN-------ALLFTDMRFDLNTLGITFLA--------GMCQ----------AYRSVGIVQEQGN-RNFK 138
Cdd:cd04270   84 GVEKFLVKLLLEQfsddvclAHLFTYRDFDMGTLGLAYVGsprdnsagGICEkayyysngkkKYLNTGLTTTVNYgKRVP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162329887 139 TAVI---MAHELSHNLGMYHDGKNCIC-----NDSSCVMSP--VLSDQP-SKLFSNCSIHDYQRYLTRYKPKC 200
Cdd:cd04270  164 TKESdlvTAHELGHNFGSPHDPDIAECapgesQGGNYIMYAraTSGDKEnNKKFSPCSKKSISKVLEVKSNSC 236
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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