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Conserved domains on  [gi|7657319|ref|NP_055294|]
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ADAM DEC1 isoform 1 precursor [Homo sapiens]

Protein Classification

Pep_M12B_propep and ZnMc_adamalysin_II_like domain-containing protein( domain architecture ID 12023285)

protein containing domains Pep_M12B_propep, ZnMc_adamalysin_II_like, and Disintegrin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 218-412 3.68e-89

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: 270.33  E-value: 3.68e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    218 KYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSN 297
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    298 LGKKI-HDHAQLLSGISFNNRRVGLAASNSLCSPS-SVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKC---PSG 372
Cdd:pfam01421  81 LKKRKpHDVAQLLSGVEFGGTTVGAAYVGGMCSLEySGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCkcpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 7657319    373 SCVMNQYLSSKFPKDFSTSCRAHFERYLLSQKPKCLLQAP 412
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-171 1.37e-31

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: 117.80  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319     43 EIVCPKKL-HILHKREIknnqtekhGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENM 121
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSL--------ASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 7657319    122 EHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHA 171
Cdd:pfam01562  73 DHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG 122
Disintegrin super family cl10507
Disintegrin;
429-461 1.72e-12

Disintegrin;


The actual alignment was detected with superfamily member smart00050:

Pssm-ID: 471982  Cd Length: 75  Bit Score: 62.71  E-value: 1.72e-12
                           10        20        30
                   ....*....|....*....|....*....|...
gi 7657319     429 EVGEDCDCGSPKECTNLCCEALTCKLKPGTDCG 461
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCA 33
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 218-412 3.68e-89

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: 270.33  E-value: 3.68e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    218 KYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSN 297
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    298 LGKKI-HDHAQLLSGISFNNRRVGLAASNSLCSPS-SVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKC---PSG 372
Cdd:pfam01421  81 LKKRKpHDVAQLLSGVEFGGTTVGAAYVGGMCSLEySGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCkcpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 7657319    373 SCVMNQYLSSKFPKDFSTSCRAHFERYLLSQKPKCLLQAP 412
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 218-409 2.27e-71

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: 224.42  E-value: 2.27e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  218 KYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSN 297
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  298 LGKKI-HDHAQLLSGISFNNRRVGLAASNSLCSPS-SVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKCPSGSCV 375
Cdd:cd04269  81 LLPRKpHDNAQLLTGRDFDGNTVGLAYVGGMCSPKySGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 7657319  376 MNQYLSSkFPKDFSTSCRAHFERYLLSQKPKCLL 409
Cdd:cd04269 161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLL 193
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-171 1.37e-31

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: 117.80  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319     43 EIVCPKKL-HILHKREIknnqtekhGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENM 121
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSL--------ASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 7657319    122 EHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHA 171
Cdd:pfam01562  73 DHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG 122
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 429-461 1.72e-12

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: 62.71  E-value: 1.72e-12
                           10        20        30
                   ....*....|....*....|....*....|...
gi 7657319     429 EVGEDCDCGSPKECTNLCCEALTCKLKPGTDCG 461
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCA 33
Disintegrin pfam00200
Disintegrin;
429-461 4.66e-12

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 61.49  E-value: 4.66e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 7657319    429 EVGEDCDCGSPKECT-NLCCEALTCKLKPGTDCG 461
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCS 34
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 218-412 3.68e-89

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: 270.33  E-value: 3.68e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    218 KYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSN 297
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    298 LGKKI-HDHAQLLSGISFNNRRVGLAASNSLCSPS-SVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKC---PSG 372
Cdd:pfam01421  81 LKKRKpHDVAQLLSGVEFGGTTVGAAYVGGMCSLEySGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCkcpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 7657319    373 SCVMNQYLSSKFPKDFSTSCRAHFERYLLSQKPKCLLQAP 412
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 218-409 2.27e-71

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: 224.42  E-value: 2.27e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  218 KYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSN 297
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  298 LGKKI-HDHAQLLSGISFNNRRVGLAASNSLCSPS-SVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKCPSGSCV 375
Cdd:cd04269  81 LLPRKpHDNAQLLTGRDFDGNTVGLAYVGGMCSPKySGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 7657319  376 MNQYLSSkFPKDFSTSCRAHFERYLLSQKPKCLL 409
Cdd:cd04269 161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLL 193
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 43-171 1.37e-31

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: 117.80  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319     43 EIVCPKKL-HILHKREIknnqtekhGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENM 121
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSL--------ASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQT 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 7657319    122 EHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHA 171
Cdd:pfam01562  73 DHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG 122
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 218-389 1.32e-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: 92.10  E-value: 1.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  218 KYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTID----VQVALVGMEIWSDGDKIKVV-PSASTTFDNFLR 292
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILKGEQFAPPIdSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  293 WHSSNLGKkiHDHAQLLSGISFNNRR-VGLAASNSLCSP-SSVAVIEAKKKNNVALVgVMSHELGHVLGMP-DVPFNTKC 369
Cdd:cd04267  81 WRAEGPIR--HDNAVLLTAQDFIEGDiLGLAYVGSMCNPySSVGVVEDTGFTLLTAL-TMAHELGHNLGAEhDGGDELAF 157

                       170       180
                ....*....|....*....|...
gi 7657319  370 P---SGSCVMNQYLSSKFPKDFS 389
Cdd:cd04267 158 EcdgGGNYIMAPVDSGLNSYRFS 180
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 218-409 7.25e-18

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 81.90  E-value: 7.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  218 KYIDLYLVLDNAFYKNYN-ENLTlirSFVFDVMNLLNVIY------NTIDVQValVGMEIWSDGDK-IKVVPSASTTFDN 289
Cdd:cd04273   1 RYVETLVVADSKMVEFHHgEDLE---HYILTLMNIVASLYkdpslgNSINIVV--VRLIVLEDEESgLLISGNAQKSLKS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  290 FLRWHSSNLGK-----KIHDHAQLLSG----ISFNNRRV-GLAASNSLCSPS-SVAVIEAkkkNNVALVGVMSHELGHVL 358
Cdd:cd04273  76 FCRWQKKLNPPndsdpEHHDHAILLTRqdicRSNGNCDTlGLAPVGGMCSPSrSCSINED---TGLSSAFTIAHELGHVL 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657319  359 GMP-DVPFNtKCPS---GSCVMNQYLSSKFPKDFSTSC-RAHFERYLLSQKPKCLL 409
Cdd:cd04273 153 GMPhDGDGN-SCGPegkDGHIMSPTLGANTGPFTWSKCsRRYLTSFLDTGDGNCLL 207
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
220-389 4.39e-14

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 70.53  E-value: 4.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    220 IDLYLVLDNAFYKNYNENLTliRSFVFDVMN-LLNVIYNTIDVQVALVGMEIWSDGD----KIKVVPSASTTFDNFlRWH 294
Cdd:pfam13688   5 VALLVAADCSYVAAFGGDAA--QANIINMVNtASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEF-QDF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    295 SSNLGKKIHDHAQLLSGISFNNRrvGLAASNSLCSPSSVAVIEAKKKNNVALVG------VMSHELGHVLGMP-D----- 362
Cdd:pfam13688  82 SAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVStatewqVFAHEIGHNFGAVhDcdsst 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 7657319    363 -----VPFNTKCP-SGSCVMNqYLSSKFPKDFS 389
Cdd:pfam13688 160 ssqccPPSNSTCPaGGRYIMN-PSSSPNSTDFS 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 429-461 1.72e-12

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: 62.71  E-value: 1.72e-12
                           10        20        30
                   ....*....|....*....|....*....|...
gi 7657319     429 EVGEDCDCGSPKECTNLCCEALTCKLKPGTDCG 461
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCA 33
Disintegrin pfam00200
Disintegrin;
429-461 4.66e-12

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 61.49  E-value: 4.66e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 7657319    429 EVGEDCDCGSPKECT-NLCCEALTCKLKPGTDCG 461
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCS 34
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 219-408 1.66e-08

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 54.67  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  219 YIDLYLVLDNAFYKNYNENLTLIRSF-VFdvMNLLNVIYNTI---DVQVALVGMEI--------WSDGDKIKVVPSAST- 285
Cdd:cd04272   2 YPELFVVVDYDHQSEFFSNEQLIRYLaVM--VNAANLRYRDLkspRIRLLLVGITIskdpdfepYIHPINYGYIDAAETl 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  286 -TFDNFLRwhssnlGKKI---HDHAQLLSGI--------SFNNRRVGLAASNSLCSPSSVAVIEAKKKNNVALVgVMSHE 353
Cdd:cd04272  80 eNFNEYVK------KKRDyfnPDVVFLVTGLdmstysggSLQTGTGGYAYVGGACTENRVAMGEDTPGSYYGVY-TMTHE 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7657319  354 LGHVLGMP----DVPFNTKCPSGS--CVMNQ-YLSSKFPKD-----FSTSCRAHFERYLLSQKPKCL 408
Cdd:cd04272 153 LAHLLGAPhdgsPPPSWVKGHPGSldCPWDDgYIMSYVVNGerqyrFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 248-359 4.97e-07

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: 48.52  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    248 VMNLLNVIYNT-IDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLlsgisFNNRRV----GLA 322
Cdd:pfam13582   6 LVNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHL-----FTGRDGggggGIA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 7657319    323 ASNSLCSPSS-VAVIEAKKKNNVALVGVMSHELGHVLG 359
Cdd:pfam13582  81 YVGGVCNSGSkFGVNSGSGPVGDTGADTFAHEIGHNFG 118
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 261-361 7.09e-07

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: 49.06  E-value: 7.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319  261 VQVALVGMEIWSDGDKIKVVPSasttfdnflrwhssNLGKKIHDHAQLLSGISFNNRRVGLA-ASNSLCSPSSVAVIEAK 339
Cdd:cd00203  24 QSLILIAMQIWRDYLNIRFVLV--------------GVEIDKADIAILVTRQDFDGGTGGWAyLGRVCDSLRGVGVLQDN 89

                        90       100
                ....*....|....*....|..
gi 7657319  340 KKNNVALVGVMSHELGHVLGMP 361
Cdd:cd00203  90 QSGTKEGAQTIAHELGHALGFY 111
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 241-377 6.74e-05

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 43.76  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657319    241 IRSFVFDVMNLLNVIY-NTIDVQVALVGME--IWSDG--DKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLLSGISFN 315
Cdd:pfam13583  25 LRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSstDSFNADCSGGDLGNWRLATLTSWRDSLNYDLAYLTLMTGPS 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7657319    316 NRRVGLAASNSLCSPSSvaviEAKKKNNVALVG----VMSHELGHVLGMPDVPFNTKCP--------SGSCVMN 377
Cdd:pfam13583 105 GQNVGVAWVGALCSSAR----QNAKASGVARSRdewdIFAHEIGHTFGAVHDCSSQGEGlssstedgSGQTIMS 174
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 349-377 5.32e-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: 5.32e-03
                        10        20
                ....*....|....*....|....*....
gi 7657319  349 VMSHELGHVLGMPdvpfntKCPSGSCVMN 377
Cdd:cd11375 126 EAVHELGHLFGLD------HCPYYACVMN 148
 
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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