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Conserved domains on  [gi|157831418|pdb|1IAG|A]
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Chain A, ADAMALYSIN II

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 10136384)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family; M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

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 ...
 6-200 1.67e-94

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: 273.34  E-value: 1.67e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        6 RYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFYRSLNIRVSLTDLEIWSGQDFITIQSSSSNTLNSFGEWRERV 85
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       86 LLIWKRHDNAQLLTAINFEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHDGKDCLRGASLCI 165
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
1IAG_A      166 MRPGLTPGrSYEFSDDSMGYYQKFLNQYKPQCILN 200
Cdd:cd04269 161 MAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 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 ...
 6-200 1.67e-94

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: 273.34  E-value: 1.67e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        6 RYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFYRSLNIRVSLTDLEIWSGQDFITIQSSSSNTLNSFGEWRERV 85
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       86 LLIWKRHDNAQLLTAINFEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHDGKDCLRGASLCI 165
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
1IAG_A      166 MRPGLTPGrSYEFSDDSMGYYQKFLNQYKPQCILN 200
Cdd:cd04269 161 MAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 6-202 5.24e-71

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: 214.09  E-value: 5.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A          6 RYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFYRSLNIRVSLTDLEIWSGQDFITIQSSSSNTLNSFGEWRERV 85
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A         86 LLIWKRHDNAQLLTAINFEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHD---GKDCLRGAS 162
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1IAG_A        163 LCIMRP--GLTPGRsyEFSDDSMGYYQKFLNQYKPQCILNKP 202
Cdd:pfam01421 161 GCIMNPsaGSSFPR--KFSNCSQEDFEQFLTKQKGACLFNKP 200
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 6-200 1.67e-94

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: 273.34  E-value: 1.67e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        6 RYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFYRSLNIRVSLTDLEIWSGQDFITIQSSSSNTLNSFGEWRERV 85
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       86 LLIWKRHDNAQLLTAINFEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHDGKDCLRGASLCI 165
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
1IAG_A      166 MRPGLTPGrSYEFSDDSMGYYQKFLNQYKPQCILN 200
Cdd:cd04269 161 MAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 6-191 7.54e-75

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: 223.45  E-value: 7.54e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        6 RYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFYRS----LNIRVSLTDLEIWSGQDFIT-IQSSSSNTLNSFGE 80
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQILKGEQFAPpIDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       81 WRERVLliwKRHDNAQLLTAINF-EGKIIGKAYTSSMCNPRSSVGIVKDHSPiNLLVAVTMAHELGHNLGMEHDGKDCLR 159
Cdd:cd04267  81 WRAEGP---IRHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGF-TLLTALTMAHELGHNLGAEHDGGDELA 156

                       170       180       190
                ....*....|....*....|....*....|....*.
1IAG_A      160 ----GASLCIMRPGLTPGRSYEFSDDSMGYYQKFLN 191
Cdd:cd04267 157 fecdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 6-202 5.24e-71

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: 214.09  E-value: 5.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A          6 RYIELVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFYRSLNIRVSLTDLEIWSGQDFITIQSSSSNTLNSFGEWRERV 85
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A         86 LLIWKRHDNAQLLTAINFEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHD---GKDCLRGAS 162
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1IAG_A        163 LCIMRP--GLTPGRsyEFSDDSMGYYQKFLNQYKPQCILNKP 202
Cdd:pfam01421 161 GCIMNPsaGSSFPR--KFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 6-190 2.42e-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: 124.94  E-value: 2.42e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        6 RYIELVVVADRRVFmkynsDLNIIRTRVHEIVNIINKFYRS-LNIRVSLTDLEIwsgqdfitiqssssntlnsfgewrer 84
Cdd:cd00203   1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       85 vlliwKRHDNAQLLTAINFEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHDGKDCLR----- 159
Cdd:cd00203  50 -----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRddypt 124

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
1IAG_A      160 ---------GASLCIMRPGLTP---GRSYEFSDDSMGYYQKFL 190
Cdd:cd00203 125 iddtlnaedDDYYSVMSYTKGSfsdGQRKDFSQCDIDQINKLY 167
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 6-199 5.15e-32

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: 114.64  E-value: 5.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        6 RYIELVVVADRRVFMKYNSD--LNIIRTrvheIVNIINKFYR--SL--NIRVSLTDLEIW-SGQDFITIQSSSSNTLNSF 78
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGEdlEHYILT----LMNIVASLYKdpSLgnSINIVVVRLIVLeDEESGLLISGNAQKSLKSF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       79 GEWRERVL----LIWKRHDNAQLLTAINFEGK-----IIGKAYTSSMCNPRSSVGIVKDHspiNLLVAVTMAHELGHNLG 149
Cdd:cd04273  77 CRWQKKLNppndSDPEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDT---GLSSAFTIAHELGHVLG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
1IAG_A      150 MEHDG--KDC-LRGASLCIMRPGLTPG-RSYEFSDDSMGYYQKFLNQYKPQCIL 199
Cdd:cd04273 154 MPHDGdgNSCgPEGKDGHIMSPTLGANtGPFTWSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
5-179 4.12e-15

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 70.14  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A          5 QRYIELVVVADRRVFMKYNSDlnIIRTRVHEIVN-IINKFYRSLNIRVSLTDLEIWSGQD----FITIQSSSSNTLNSF- 78
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGD--AAQANIINMVNtASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFq 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A         79 --GEWRERvlliwKRHDNAQLLTAINFEGKiiGKAYTSSMCNPRSSVGIVKDHSPINLLVAV-----TMAHELGHNLGME 151
Cdd:pfam13688  80 dfSAWRGT-----QNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
1IAG_A        152 HDGKD------CLRGASLC------IMRPGLTPGRSYeFS 179
Cdd:pfam13688 153 HDCDSstssqcCPPSNSTCpaggryIMNPSSSPNSTD-FS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 31-153 8.45e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 67.78  E-value: 8.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A         31 TRVHEIVNIINKFYRS-LNIRVSLTDLEIWSGQDFITIQSSSSNTLNSFGE-WRERvlliwKRHDNAQLLTAINFEGKII 108
Cdd:pfam13582   1 ARIVSLVNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEvNDTR-----IGQYGYDLGHLFTGRDGGG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
1IAG_A        109 --GKAYTSSMCNPRSSVGIVKDHSPINLLVAVTMAHELGHNLGMEHD 153
Cdd:pfam13582  76 ggGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 7-198 2.22e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 66.22  E-value: 2.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        7 YIELVVVADRRVFMKYNSDLNIIRTrVHEIVNIINKFYRSLN---IRVSLTDLEIWSGQDFITIQSSSSN-------TLN 76
Cdd:cd04272   2 YPELFVVVDYDHQSEFFSNEQLIRY-LAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPINYgyidaaeTLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       77 SFGEW--RERVLLiwkRHDNAQLLTAINF----EGKII----GKAYTSSMCNpRSSVGIVKDhSPINLLVAVTMAHELGH 146
Cdd:cd04272  81 NFNEYvkKKRDYF---NPDVVFLVTGLDMstysGGSLQtgtgGYAYVGGACT-ENRVAMGED-TPGSYYGVYTMTHELAH 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1IAG_A      147 NLGMEHDGKD------CLRGASLC------IMRPGLTPGRSYEFSDDSMGYYQKFLNQYKPQCI 198
Cdd:cd04272 156 LLGAPHDGSPppswvkGHPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 35-184 4.73e-10

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: 57.05  E-value: 4.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       35 EIVNIINK----FYRSLNIRVSLTDLEIWSGQDFITIQSSS------------SNTLNSFGEWRERvlliWKRHDNA--Q 96
Cdd:cd04271  26 NILNNVNSasqlYESSFNISLGLRNLTISDASCPSTAVDSApwnlpcnsridiDDRLSIFSQWRGQ----QPDDGNAfwT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       97 LLTAINfEGKIIGKAYTSSMCNPRSSVGIVKDHSPINLLVAVT-----MAHELGHNLGMEHD-------------GKDCL 158
Cdd:cd04271 102 LMTACP-SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHTFGAVHDctsgtcsdgsvgsQQCCP 180

                       170       180       190
                ....*....|....*....|....*....|...
1IAG_A      159 RGASLC------IMRPglTPGRS-YEFSDDSMG 184
Cdd:cd04271 181 LSTSTCdangqyIMNP--SSSSGiTEFSPCTIG 211
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 35-186 2.14e-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: 372637  Cd Length: 193  Bit Score: 51.86  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A         35 EIVNIINKFYRSLNIRVSLtdleIWSGQDFITIQSSSSNTLNSFGE------WRERVLLIW---KRHDNAQLLTAINFEG 105
Cdd:pfam13574   9 NVVNRVNQIYEPDDINING----GLVNPGEIPATTSASDSGNNYCNspttivRRLNFLSQWrgeQDYCLAHLVTMGTFSG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A        106 KIIGKAYTSSMC-----NPRSSVGIVkdhSPINLLVAVT-------MAHELGHNLGMEHDgKDCLRGASLCIMRPGLTPg 173
Cdd:pfam13574  85 GELGLAYVGQICqkgasSPKTNTGLS---TTTNYGSFNYptqewdvVAHEVGHNFGATHD-CDGSQYASSGCERNAATS- 159

                         170
                  ....*....|...
1IAG_A        174 rsyefSDDSMGYY 186
Cdd:pfam13574 160 -----VCSANGSF 167
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 10-176 8.83e-06

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: 44.53  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A         10 LVVVADRRVFMKYNSDLNIIRTRVHEIVNIINKFY-RSLNIRvsltdLEIWSGQD--FITIQSSSSNTLNSFGE---WRE 83
Cdd:pfam13583   6 RVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVS-----LALISDRDviYTDSSTDSFNADCSGGDlgnWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A         84 RVLLIW---KRHDNAQLLT---AINFEGKI--IGKAYTSSMCNPRSSVGIVKDHSPinllvaVTMAHELGHNLGMEHDGK 155
Cdd:pfam13583  81 ATLTSWrdsLNYDLAYLTLmtgPSGQNVGVawVGALCSSARQNAKASGVARSRDEW------DIFAHEIGHTFGAVHDCS 154

                         170       180
                  ....*....|....*....|....*....
1IAG_A        156 DCLRGASL--------CIMRPGLTPGRSY 176
Cdd:pfam13583 155 SQGEGLSSstedgsgqTIMSYASTASQTA 183
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 10-153 1.02e-03

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: 38.89  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       10 LVVVADRRVFMKYNSdlNIIRTRVHEIVNII---NKFYRSLNirvsltdleiWSGQDF---------ITIQSSSSNT--- 74
Cdd:cd04270   5 LLLVADHRFYKYMGR--GEEETTINYLISHIdrvDDIYRNTD----------WDGGGFkgigfqikrIRIHTTPDEVdpg 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAG_A       75 ----LNSFGEW-RERVLLIWKRHDN------AQLLTAINFEGKIIGKAYTSSMcNPRSSVGIVKDH-------------- 129
Cdd:cd04270  73 nkfyNKSFPNWgVEKFLVKLLLEQFsddvclAHLFTYRDFDMGTLGLAYVGSP-RDNSAGGICEKAyyysngkkkylntg 151

                       170       180       190
                ....*....|....*....|....*....|...
1IAG_A      130 --------SPINLLVA-VTMAHELGHNLGMEHD 153
Cdd:cd04270 152 ltttvnygKRVPTKESdLVTAHELGHNFGSPHD 184
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 136-168 1.94e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 37.66  E-value: 1.94e-03
                        10        20        30
                ....*....|....*....|....*....|...
1IAG_A      136 VAVTMAHELGHNLGMEHdgkdCLRGAslCIMRP 168
Cdd:cd11375 123 LLKEAVHELGHLFGLDH----CPYYA--CVMNF 149
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 132-181 8.61e-03

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 35.26  E-value: 8.61e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
1IAG_A      132 INLLVavTMAHELGHNLGMEHDGKdclRGAslcIMRPGLTPG-RSYEFSDD 181
Cdd:cd04278 105 TDLFS--VAAHEIGHALGLGHSSD---PDS---IMYPYYQGPvPKFKLSQD 147
 
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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