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Conserved domains on  [gi|14318661|gb|AAH09132|]
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Adam15 protein [Mus musculus]

Protein Classification

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 ...
 214-412 8.93e-82

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: 250.23  E-value: 8.93e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:cd04269   1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGhsCPCPGpa 372
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14318661 373 paKSCIMEASTDFLPgLNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-147 4.50e-12

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.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 63.10  E-value: 4.50e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318661    74 LELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLS 147
Cdd:pfam01562  31 LAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 104
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 214-412 8.93e-82

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: 250.23  E-value: 8.93e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:cd04269   1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGhsCPCPGpa 372
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14318661 373 paKSCIMEASTDFLPgLNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 214-414 1.86e-70

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: 221.41  E-value: 1.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPgpa 372
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 14318661   373 PAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFER 414
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-147 4.50e-12

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: 63.10  E-value: 4.50e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318661    74 LELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLS 147
Cdd:pfam01562  31 LAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 104
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
347-393 6.31e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.63  E-value: 6.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 14318661 347 IAHELGHSLGLDHdspghsCPCPGpapaksCIMeastdflpglNFSN 393
Cdd:COG1913 127 AVHELGHLFGLGH------CPNPR------CVM----------HFSN 151
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 305-359 9.72e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 36.56  E-value: 9.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318661    305 VTVTSFSGPMVGMAIQNSICS------PDFSGGVNMDHSTSILGVassIAHELGHSLGLDH 359
Cdd:smart00235  43 VERTGTADIYISFGSGDSGCTlshagrPGGDQHLSLGNGCINTGV---AAHELGHALGLYH 100
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 214-412 8.93e-82

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: 250.23  E-value: 8.93e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:cd04269   1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGhsCPCPGpa 372
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14318661 373 paKSCIMEASTDFLPgLNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 214-414 1.86e-70

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: 221.41  E-value: 1.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPgpa 372
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 14318661   373 PAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFER 414
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 216-403 1.41e-25

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: 102.88  E-value: 1.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 216 VELVIVADNSEVRKYP-DFQQLLNRTLEAALLLDTFFQ----PLNVRVALVGLEAWTQHNLI-EMSSNPAVLLDNFLRWR 289
Cdd:cd04267   3 IELVVVADHRMVSYFNsDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSFWR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 290 RTDLlPRlpHDSAQLVTVTSF-SGPMVGMAIQNSICSPDFSGGVNMDHSTSILgVASSIAHELGHSLGLDHDsPGHSCPC 368
Cdd:cd04267  83 AEGP-IR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHD-GGDELAF 157

                       170       180       190
                ....*....|....*....|....*....|....*
gi 14318661 369 PGPApAKSCIMEASTDFLPGLNFSNCSRQALEKAL 403
Cdd:cd04267 158 ECDG-GGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 214-412 5.23e-23

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: 96.15  E-value: 5.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 214 KIVELVIVADNSEVRKY--PDFQQ----LLNrtlEAALLldtFFQPL---NVRVALVGLEAWT--QHNLiEMSSNPAVLL 282
Cdd:cd04273   1 RYVETLVVADSKMVEFHhgEDLEHyiltLMN---IVASL---YKDPSlgnSINIVVVRLIVLEdeESGL-LISGNAQKSL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 283 DNFLRWRRTdLLPRLP-----HDSAQLVTVTSFSGP-----MVGMAIQNSICSPDFSGGVNMDHStsiLGVASSIAHELG 352
Cdd:cd04273  74 KSFCRWQKK-LNPPNDsdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELG 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318661 353 HSLGLDHDSPGHSCpcpGPAPAKSCIMEASTDFLPG-LNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04273 150 HVLGMPHDGDGNSC---GPEGKDGHIMSPTLGANTGpFTWSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
213-379 6.25e-13

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 67.06  E-value: 6.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   213 TKIVELVIVADNSEVRKYP-DF-QQLLNRTLEAALllDTFFQPLNVRVALVGLEAWTQHNLI----EMSSNPAVLLDNFL 286
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGgDAaQANIINMVNTAS--NVYERDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   287 R---WRRTDllprlPHDSAQLVTVTSFSGPmvGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHSLGLD 358
Cdd:pfam13688  80 DfsaWRGTQ-----NDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHNFGAV 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 14318661   359 HD----SPGHSCP-----CPGPApakSCIM 379
Cdd:pfam13688 153 HDcdssTSSQCCPpsnstCPAGG---RYIM 179
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-147 4.50e-12

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: 63.10  E-value: 4.50e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14318661    74 LELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLS 147
Cdd:pfam01562  31 LAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 104
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 254-360 4.73e-12

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: 62.77  E-value: 4.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   254 LNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTdllpRLPHDSAQLVTV--TSFSGPMVGMAIQNSICSPDFSGG 331
Cdd:pfam13582  18 LGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYDLGHLftGRDGGGGGGIAYVGGVCNSGSKFG 93

                          90       100
                  ....*....|....*....|....*....
gi 14318661   332 VNMDHSTSILGVASSIAHELGHSLGLDHD 360
Cdd:pfam13582  94 VNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 214-403 9.79e-10

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: 57.53  E-value: 9.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 214 KIVELVIVADNSEVrkypDFQQLLNRTLEAALLLDTFF-QPLNVRVALVGLEawtqhnliemssnpavlldnflrwrrtd 292
Cdd:cd00203   1 KVIPYVVVADDRDV----EEENLSAQIQSLILIAMQIWrDYLNIRFVLVGVE---------------------------- 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 293 llpRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDS--------PGH 364
Cdd:cd00203  49 ---IDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHdrkdrddyPTI 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 14318661 365 SCPCPGPAPAKSCIMEASTDFLPGLN---FSNCSRQALEKAL 403
Cdd:cd00203 126 DDTLNAEDDDYYSVMSYTKGSFSDGQrkdFSQCDIDQINKLY 167
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 300-396 5.80e-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: 52.63  E-value: 5.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   300 DSAQLVTVTSFSGPMVGMAIQNSIC-------------SPDFSGGVNMDHSTSILgvasSIAHELGHSLGLDHDSPGHSC 366
Cdd:pfam13574  72 CLAHLVTMGTFSGGELGLAYVGQICqkgasspktntglSTTTNYGSFNYPTQEWD----VVAHEVGHNFGATHDCDGSQY 147

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 14318661   367 PCPG-PAPAKSCIMEASTDFL----PGLN---FSNCSR 396
Cdd:pfam13574 148 ASSGcERNAATSVCSANGSFImnpaSKSNndlFSPCSI 185
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 302-414 2.29e-07

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 51.61  E-value: 2.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 302 AQLVTVTSFSGPMVGMAIQNS--------ICSPD--FSGGVN----------MDHSTSILGVASSI--AHELGHSLGLDH 359
Cdd:cd04270 104 AHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAyyYSNGKKkylntgltttVNYGKRVPTKESDLvtAHELGHNFGSPH 183

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14318661 360 DSPGHSCpCPGPAPAKSCIMEA---STDFLPGLNFSNCSRQALEKALLEGMGSCLFER 414
Cdd:cd04270 184 DPDIAEC-APGESQGGNYIMYAratSGDKENNKKFSPCSKKSISKVLEVKSNSCFVER 240
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 282-383 4.56e-06

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: 47.42  E-value: 4.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 282 LDNFLRWRRtdllpRLPHDSAQLVTV-TSF-SGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHS 354
Cdd:cd04271  82 LSIFSQWRG-----QQPDDGNAFWTLmTACpSGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHT 156

                        90       100
                ....*....|....*....|....*....
gi 14318661 355 LGLDHDSPGHSCPCPGPAPAKSCIMEAST 383
Cdd:cd04271 157 FGAVHDCTSGTCSDGSVGSQQCCPLSTST 185
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 316-397 1.36e-04

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 43.11  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 316 GMAIQNSICSpDFSGGVNMDHSTSILGVaSSIAHELGHSLGLDHDSPGHSCPCPGPAPAKSC------IMeaSTDF--LP 387
Cdd:cd04272 120 GYAYVGGACT-ENRVAMGEDTPGSYYGV-YTMTHELAHLLGAPHDGSPPPSWVKGHPGSLDCpwddgyIM--SYVVngER 195

                        90
                ....*....|
gi 14318661 388 GLNFSNCSRQ 397
Cdd:cd04272 196 QYRFSQCSQR 205
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 254-397 3.64e-04

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


Pssm-ID: 404471  Cd Length: 203  Bit Score: 41.45  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   254 LNVRVALVGLeawTQHNLIEMSSNPAVLLDN-----------FLRWRRTdllprLPHDSAQLVTVTSFSGPMVGMAIQNS 322
Cdd:pfam13583  44 FNVSLALISD---RDVIYTDSSTDSFNADCSggdlgnwrlatLTSWRDS-----LNYDLAYLTLMTGPSGQNVGVAWVGA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661   323 ICSPDFSggvNMDHStsilGVASS------IAHELGHSLGLDHDSPGHSCP-----CPGPApakSCIME-ASTDFLPglN 390
Cdd:pfam13583 116 LCSSARQ---NAKAS----GVARSrdewdiFAHEIGHTFGAVHDCSSQGEGlssstEDGSG---QTIMSyASTASQT--A 183


                  ....*..
gi 14318661   391 FSNCSRQ 397
Cdd:pfam13583 184 FSPCTIR 190
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 280-393 1.81e-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: 39.20  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 280 VLLDNFLRWrrtdLLPRLPHDSAQLVTVTSFSGPM------VGMAIQNS---ICS-----PDFSGGVNmDHSTSILGVAS 345
Cdd:cd11375  51 YLADDILDA----LLKLKPPDADCVLGVTDVDLYEpglnfvFGLADGGSgvaVVStarlrPEFYGLPP-DEGLFLERLLK 125

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 14318661 346 SIAHELGHSLGLDHdspghscpCPGPApaksCIMeastdflpglNFSN 393
Cdd:cd11375 126 EAVHELGHLFGLDH--------CPYYA----CVM----------NFSN 151
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 331-361 2.00e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 38.75  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 14318661   331 GVNMDHSTSILGVAssiAHELGHSLGLDHDS 361
Cdd:pfam00413  99 GSDPPHGINLFLVA---AHEIGHALGLGHSS 126
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
347-393 6.31e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.63  E-value: 6.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 14318661 347 IAHELGHSLGLDHdspghsCPCPGpapaksCIMeastdflpglNFSN 393
Cdd:COG1913 127 AVHELGHLFGLGH------CPNPR------CVM----------HFSN 151
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 305-359 9.72e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 36.56  E-value: 9.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14318661    305 VTVTSFSGPMVGMAIQNSICS------PDFSGGVNMDHSTSILGVassIAHELGHSLGLDH 359
Cdd:smart00235  43 VERTGTADIYISFGSGDSGCTlshagrPGGDQHLSLGNGCINTGV---AAHELGHALGLYH 100
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 263-362 9.81e-03

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 36.67  E-value: 9.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14318661 263 LEAWTQHNLIEMSSNPAVLLD--NFLRWRRTDLLPRlphdSAQLVTVTSFSGPMVGmaiqNSICSPDFSGGVNMDHSTSI 340
Cdd:cd04279  30 AAEWENVGPLKFVYNPEEDNDadIVIFFDRPPPVGG----AGGGLARAGFPLISDG----NRKLFNRTDINLGPGQPRGA 101

                        90       100
                ....*....|....*....|..
gi 14318661 341 LGVASSIAHELGHSLGLDHDSP 362
Cdd:cd04279 102 ENLQAIALHELGHALGLWHHSD 123
 
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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