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Conserved domains on  [gi|6137610|pdb|1BUD|A]
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Chain A, PROTEIN (ACUTOLYSIN A)

Protein Classification

ZnMc_adamalysin_II_like domain-containing protein( domain architecture ID 10136384)

ZnMc_adamalysin_II_like domain-containing protein

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 ...
 3-197 1.76e-92

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: 267.94  E-value: 1.76e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        3 RYMEIVIVVDHSMVKKYNGDSDSIKAWVYEMINTITESYSYLKIDISLSGLEIWSGKDLIDVEASAGNTLKSFGEWRAKD 82
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       83 LIHRISHDNAQLLTATDFDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAITLAHEMAHNLGVSHDEGSCSCGGKSCI 162
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
1BUD_A      163 MSPSISDETiKYFSDCSYIQCRDYISKENPPCILN 197
Cdd:cd04269 161 MAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLLN 194
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 3-197 1.76e-92

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: 267.94  E-value: 1.76e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        3 RYMEIVIVVDHSMVKKYNGDSDSIKAWVYEMINTITESYSYLKIDISLSGLEIWSGKDLIDVEASAGNTLKSFGEWRAKD 82
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       83 LIHRISHDNAQLLTATDFDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAITLAHEMAHNLGVSHDEGSCSCGGKSCI 162
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
1BUD_A      163 MSPSISDETiKYFSDCSYIQCRDYISKENPPCILN 197
Cdd:cd04269 161 MAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 3-197 8.88e-61

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: 187.89  E-value: 8.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A          3 RYMEIVIVVDHSMVKKYNGDSDSIKAWVYEMINTITESYSYLKIDISLSGLEIWSGKDLIDVEASAGNTLKSFGEWRAKD 82
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A         83 LIHRISHDNAQLLTATDFDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAITLAHEMAHNLGVSHDEGS--CSCG-GK 159
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPpGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
1BUD_A        160 SCIMSPSISDETIKYFSDCSYIQCRDYISKENPPCILN 197
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 3-197 1.76e-92

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: 267.94  E-value: 1.76e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        3 RYMEIVIVVDHSMVKKYNGDSDSIKAWVYEMINTITESYSYLKIDISLSGLEIWSGKDLIDVEASAGNTLKSFGEWRAKD 82
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       83 LIHRISHDNAQLLTATDFDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAITLAHEMAHNLGVSHDEGSCSCGGKSCI 162
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
1BUD_A      163 MSPSISDETiKYFSDCSYIQCRDYISKENPPCILN 197
Cdd:cd04269 161 MAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLLN 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 3-188 2.27e-71

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: 214.59  E-value: 2.27e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        3 RYMEIVIVVDHSMVKKYNGDSDSIKAWVYEMINTITESYSY----LKIDISLSGLEIWSGKDLIDV-EASAGNTLKSFGE 77
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       78 WRAKDLIHrisHDNAQLLTATDF-DGATIGLAYVASMCNPKRSVGVIQDHSSvNRLVAITLAHEMAHNLGVSHDEGSCSC 156
Cdd:cd04267  81 WRAEGPIR---HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGF-TLLTALTMAHELGHNLGAEHDGGDELA 156

                       170       180       190
                ....*....|....*....|....*....|....*.
1BUD_A      157 ----GGKSCIMSPSISDETIKYFSDCSYIQCRDYIS 188
Cdd:cd04267 157 fecdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 3-197 8.88e-61

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: 187.89  E-value: 8.88e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A          3 RYMEIVIVVDHSMVKKYNGDSDSIKAWVYEMINTITESYSYLKIDISLSGLEIWSGKDLIDVEASAGNTLKSFGEWRAKD 82
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A         83 LIHRISHDNAQLLTATDFDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAITLAHEMAHNLGVSHDEGS--CSCG-GK 159
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPpGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
1BUD_A        160 SCIMSPSISDETIKYFSDCSYIQCRDYISKENPPCILN 197
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 3-187 2.45e-36

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: 124.56  E-value: 2.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        3 RYMEIVIVVDHSMVkkyngDSDSIKAWVYEMINTITESYS-YLKIDISLSGLEIwsgkdlidveasagntlksfgewrak 81
Cdd:cd00203   1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       82 dlihrISHDNAQLLTATDFDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAITLAHEMAHNLGVSHDEGSCSC----- 156
Cdd:cd00203  50 -----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRddypt 124

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
1BUD_A      157 ---------GGKSCIMSP---SISDETIKYFSDCSYIQCRDYI 187
Cdd:cd00203 125 iddtlnaedDDYYSVMSYtkgSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 3-189 5.73e-31

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: 111.95  E-value: 5.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        3 RYMEIVIVVDHSMVKKYNGDSdsIKAWVYEMINTITESYSY----LKIDISLSGLEIW-SGKDLIDVEASAGNTLKSFGE 77
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGED--LEHYILTLMNIVASLYKDpslgNSINIVVVRLIVLeDEESGLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       78 WRAK----DLIHRISHDNAQLLTATDFDGA-----TIGLAYVASMCNPKRSVGVIQDH--SSvnrlvAITLAHEMAHNLG 146
Cdd:cd04273  79 WQKKlnppNDSDPEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTglSS-----AFTIAHELGHVLG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
1BUD_A      147 VSHDEGSCSCG---GKSCIMSPSISDETIKYF-SDCSyiqcRDYISK 189
Cdd:cd04273 154 MPHDGDGNSCGpegKDGHIMSPTLGANTGPFTwSKCS----RRYLTS 196
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
7-176 2.59e-23

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 91.71  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A          7 IVIVVDHSMVKKYNGDSdsIKAWVYEMINTITE-SYSYLKIDISLSGLEIWSGKDLIDVEA----SAGNTLKSFGEWRAk 81
Cdd:pfam13688   7 LLVAADCSYVAAFGGDA--AQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPAcstgDSSDRLSEFQDFSA- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A         82 dLIHRISHDNAQLLTATDFDGAtiGLAYVASMCNPKRSVGVIQDHSSVNRLV-----AITLAHEMAHNLGVSHD------ 150
Cdd:pfam13688  84 -WRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVstateWQVFAHEIGHNFGAVHDcdssts 160

                         170       180       190
                  ....*....|....*....|....*....|..
1BUD_A        151 EGSCSCGGKSC------IMSPSiSDETIKYFS 176
Cdd:pfam13688 161 SQCCPPSNSTCpaggryIMNPS-SSPNSTDFS 191
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 32-185 4.10e-15

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: 372637  Cd Length: 193  Bit Score: 70.35  E-value: 4.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A         32 EMINTITESYSYlkIDISLSGLEIWSGKDLIDVEASA-GNTLKSFGEW--RAKDLIHRIS----HDNAQLLTATDFDGAT 104
Cdd:pfam13574   9 NVVNRVNQIYEP--DDININGGLVNPGEIPATTSASDsGNNYCNSPTTivRRLNFLSQWRgeqdYCLAHLVTMGTFSGGE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        105 IGLAYVASMC-----NPKRSVGV---IQDHSSVNRLVAI-TLAHEMAHNLGVSHD---EGSCSCGGKSC----------- 161
Cdd:pfam13574  87 LGLAYVGQICqkgasSPKTNTGLsttTNYGSFNYPTQEWdVVAHEVGHNFGATHDcdgSQYASSGCERNaatsvcsangs 166

                         170       180
                  ....*....|....*....|....*
1BUD_A        162 -IMSPSiSDETIKYFSDCSYIQCRD 185
Cdd:pfam13574 167 fIMNPA-SKSNNDLFSPCSISLICD 190
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 34-150 1.11e-14

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: 67.40  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A         34 INTITESYsyLKIDISLSGLEIWSGKDLIDVEASAGNTLKSFGEWRAKdlihRISHDNA---QLLTATDFDGATiGLAYV 110
Cdd:pfam13582  10 ANTIYERD--LGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYdlgHLFTGRDGGGGG-GIAYV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
1BUD_A        111 ASMCNPKRSVGVIQDHSSVNRLVAITLAHEMAHNLGVSHD 150
Cdd:pfam13582  83 GGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 4-195 3.18e-13

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: 3.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        4 YMEIVIVVDhSMVKKYNGDSDSIKAWVYEMINTITESYSYL---KIDISLSGLEIWSGKD-------LIDVEASAGNTLK 73
Cdd:cd04272   2 YPELFVVVD-YDHQSEFFSNEQLIRYLAVMVNAANLRYRDLkspRIRLLLVGITISKDPDfepyihpINYGYIDAAETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       74 SFGEW-RAKDliHRISHDNAQLLTATDF----DGA----TIGLAYVASMCNpKRSVGVIQDHSSVNRLVaITLAHEMAHN 144
Cdd:cd04272  81 NFNEYvKKKR--DYFNPDVVFLVTGLDMstysGGSlqtgTGGYAYVGGACT-ENRVAMGEDTPGSYYGV-YTMTHELAHL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1BUD_A      145 LGVSHDE-GSCS-----CGGKSC------IMSPSISDETIKYFSDCSYIQCRDYISKENPPCI 195
Cdd:cd04272 157 LGAPHDGsPPPSwvkghPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 7-179 7.80e-12

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 61.67  E-value: 7.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        7 IVIVVDHSMVKKYNGDsDSIKAWVYEMINTITESY-SYLKIDISLSGLEIWSGKDLIDVEASA------------GNTLK 73
Cdd:cd04271   5 IGVAADCSYTKSFGSV-EEARRNILNNVNSASQLYeSSFNISLGLRNLTISDASCPSTAVDSApwnlpcnsridiDDRLS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       74 SFGEWRAKdlihRISHDNA--QLLTATDfDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAITL-----AHEMAHNLG 146
Cdd:cd04271  84 IFSQWRGQ----QPDDGNAfwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSNewqvfAHEIGHTFG 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
1BUD_A      147 VSHDEGSCSC-----GGKSC--------------IMSPSiSDETIKYFSDCS 179
Cdd:cd04271 159 AVHDCTSGTCsdgsvGSQQCcplststcdangqyIMNPS-SSSGITEFSPCT 209
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 7-194 7.83e-11

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: 59.31  E-value: 7.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A        7 IVIVVDHSMVKKYNGDSDSIK-AWVYEMINTITESYSYLKID------ISLSGLEIWSGKDLIDVEASAGNTLKSFGEWR 79
Cdd:cd04270   5 LLLVADHRFYKYMGRGEEETTiNYLISHIDRVDDIYRNTDWDgggfkgIGFQIKRIRIHTTPDEVDPGNKFYNKSFPNWG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A       80 AKDLIHRISHDN-------AQLLTATDFDGATIGLAYVAS--------MCNP--------KRS--VGVIqdhSSVN---- 130
Cdd:cd04270  85 VEKFLVKLLLEQfsddvclAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKayyysngkKKYlnTGLT---TTVNygkr 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1BUD_A      131 ---RLVAITLAHEMAHNLGVSHDEGSCSC------GGKScIMSP---SISDETIKYFSDCSYIQCRDYISKENPPC 194
Cdd:cd04270 162 vptKESDLVTAHELGHNFGSPHDPDIAECapgesqGGNY-IMYAratSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 3-179 8.32e-08

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: 50.31  E-value: 8.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A          3 RYMEIVIVVDHSMVKkYNGDSDSIKAWVYEMINTITESYSYlkiDISLSgLEIWSGKDLI--DVEASAGNTLKSFGEWRA 80
Cdd:pfam13583   3 RVYRVAVATDCTYSA-SFGSVDELRANINATVTTANEVYGR---DFNVS-LALISDRDVIytDSSTDSFNADCSGGDLGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUD_A         81 KDLIHRISH------DNAQLLTATDFDGATIGLAYVASMCNPKRSVGVIQDHSSVNRLVAItLAHEMAHNLGVSHDEGSC 154
Cdd:pfam13583  78 WRLATLTSWrdslnyDLAYLTLMTGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDI-FAHEIGHTFGAVHDCSSQ 156

                         170       180       190
                  ....*....|....*....|....*....|...
1BUD_A        155 SCGGK--------SCIMSPSiSDETIKYFSDCS 179
Cdd:pfam13583 157 GEGLSsstedgsgQTIMSYA-STASQTAFSPCT 188
 
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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