NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|755498543|ref|XP_011237557|]
View 

disintegrin and metalloproteinase domain-containing protein 33 isoform X4 [Mus musculus]

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 10480567)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 211-361 2.41e-49

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: 165.87  E-value: 2.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755498543 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVStapfparlQRLQPPP------AAHLLpqrGRSLPLQH 361
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVV--------QDHSRNLllfavtMAHEL---GHNLGMEH 147
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-153 1.54e-27

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: 105.86  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543   39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562   1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498543  119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 211-361 2.41e-49

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: 165.87  E-value: 2.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755498543 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVStapfparlQRLQPPP------AAHLLpqrGRSLPLQH 361
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVV--------QDHSRNLllfavtMAHEL---GHNLGMEH 147
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 211-361 3.11e-45

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: 155.15  E-value: 3.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543  211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 289
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755498543  290 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTAP------FPARLqrlqpppaAHLLpqrGRSLPLQH 361
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHsknlesFAVTM--------AHEL---GHNLGMQH 147
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-153 1.54e-27

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: 105.86  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543   39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562   1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498543  119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 211-361 2.41e-49

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: 165.87  E-value: 2.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755498543 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVStapfparlQRLQPPP------AAHLLpqrGRSLPLQH 361
Cdd:cd04269   81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVV--------QDHSRNLllfavtMAHEL---GHNLGMEH 147
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 211-361 3.11e-45

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: 155.15  E-value: 3.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543  211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 289
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755498543  290 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTAP------FPARLqrlqpppaAHLLpqrGRSLPLQH 361
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHsknlesFAVTM--------AHEL---GHNLGMQH 147
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 39-153 1.54e-27

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: 105.86  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543   39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562   1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498543  119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562  79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 211-330 2.20e-16

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: 77.08  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLD----IQLVLTGLEVW-TEQDLSRITQDANETLWAFLQ 285
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755498543 286 WRRGVWARrpHDSTQLLTGRTF-QGTTVGLAPVEGICRAESSGGVS 330
Cdd:cd04267   81 WRAEGPIR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVV 124
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 211-326 1.53e-11

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: 63.41  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543 211 RYLELYIVADHTLFLLQHQNlnHTRQRLLEVANCVDQILR--TL--DIQLVLTGLEVWT-EQDLSRITQDANETLWAFLQ 285
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEdEESGLLISGNAQKSLKSFCR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755498543 286 WRRGVWARRP-----HDSTQLLTGRTFQG-----TTVGLAPVEGICRAESS 326
Cdd:cd04273   79 WQKKLNPPNDsdpehHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRS 129
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
215-331 1.96e-06

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 48.18  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498543  215 LYIVADHTlFLLQHQNlNHTRQRLLEVANCVDQIL-RTLDIQLVLTGLEVWTEQDLS----RITQDANETLWAFlQWRRG 289
Cdd:pfam13688   7 LLVAADCS-YVAAFGG-DAAQANIINMVNTASNVYeRDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEF-QDFSA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755498543  290 VWARRPHDSTQLLTGRTFQGTtvGLAPVEGICRAESSGGVST 331
Cdd:pfam13688  84 WRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVST 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH