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Conserved domains on  [gi|2217330497|ref|XP_047301566|]
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disintegrin and metalloproteinase domain-containing protein 17 isoform X1 [Homo sapiens]

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 10922949)

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_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 192-446 2.22e-152

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: 444.51  E-value: 2.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 192 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 271
Cdd:cd04270     1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 272 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 351
Cdd:cd04270    79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 352 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 431
Cdd:cd04270   151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                         250
                  ....*....|....*
gi 2217330497 432 ESKAQECFQERSNKV 446
Cdd:cd04270   230 EVKSNSCFVERSQSF 244
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 550-611 6.03e-33

Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a family of disintegrin and metalloproteinase domain-containing protein 17 found in metazoan species. ADAM17 is a major sheddase that is responsible for the regulation of a wide range of biological processes, such as cellular differentiation, regeneration, and cancer progression. This MPD region acts as the sheddase switch. PDI or protein-disulfide isomerase interacts with ADAM17 and to down-regulate its enzymatic activity. The interaction is directly with the MPD, the region of dimerization and substrate recognition, where it catalyzes an isomerization of disulfide bridges within the thioredoxin motif CXXC. this isomerization results in a major structural change between an active, open state and an inactive, closed state of the MPD. This change is thought to act as a molecular switch, allowing a global reorientation of the extracellular domains in ADAM17 and regulating its shedding activity.


:

Pssm-ID: 465239  Cd Length: 62  Bit Score: 120.92  E-value: 6.03e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217330497 550 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 611
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 453-529 2.08e-24

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: 96.99  E-value: 2.08e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330497  453 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 529
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 21-136 9.02e-05

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: 42.69  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497  21 QHSVRKRDLQ-TSTHVETL-LTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQD---FFTGHVVGEPDSR 95
Cdd:pfam01562   9 DPSRRRRSLAsESTYLDTLsYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217330497  96 VlahirdddvIIR--------INTDGAEYNIEPLWRFVNDTKDKRMLVY 136
Cdd:pfam01562  89 V---------ALStcsglrgfIRTENEEYLIEPLEKYSREEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 192-446 2.22e-152

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: 444.51  E-value: 2.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 192 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 271
Cdd:cd04270     1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 272 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 351
Cdd:cd04270    79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 352 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 431
Cdd:cd04270   151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                         250
                  ....*....|....*
gi 2217330497 432 ESKAQECFQERSNKV 446
Cdd:cd04270   230 EVKSNSCFVERSQSF 244
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 550-611 6.03e-33

Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a family of disintegrin and metalloproteinase domain-containing protein 17 found in metazoan species. ADAM17 is a major sheddase that is responsible for the regulation of a wide range of biological processes, such as cellular differentiation, regeneration, and cancer progression. This MPD region acts as the sheddase switch. PDI or protein-disulfide isomerase interacts with ADAM17 and to down-regulate its enzymatic activity. The interaction is directly with the MPD, the region of dimerization and substrate recognition, where it catalyzes an isomerization of disulfide bridges within the thioredoxin motif CXXC. this isomerization results in a major structural change between an active, open state and an inactive, closed state of the MPD. This change is thought to act as a molecular switch, allowing a global reorientation of the extracellular domains in ADAM17 and regulating its shedding activity.


Pssm-ID: 465239  Cd Length: 62  Bit Score: 120.92  E-value: 6.03e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217330497 550 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 611
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 215-427 1.51e-30

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: 118.89  E-value: 1.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 215 TTTNYLIELIDRVDDIYRNtswDNagFKGYGIQIEQIRILKSPQEVKPGekhynmaksYPNEEKDAWDVKMLLEqfsFDI 294
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATTSASDSG---------NNYCNSPTTIVRRLNF---LSQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 295 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPvgkkniYLNSGLTSTKNYGKTILTKEADLVTTH 374
Cdd:pfam13574  65 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217330497 375 ELGHNFGAEHDPDGLA-------ECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 427
Cdd:pfam13574 131 EVGHNFGATHDCDGSQyassgceRNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 188
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 549-611 2.01e-25

Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17.


Pssm-ID: 271205  Cd Length: 60  Bit Score: 99.37  E-value: 2.01e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217330497 549 PFCEReQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 611
Cdd:cd14246     1 PFCER-ENLQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 453-529 2.08e-24

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: 96.99  E-value: 2.08e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330497  453 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 529
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
453-527 1.02e-21

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 89.61  E-value: 1.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330497 453 DEGEECDPG-IMYLNNDTCCN-SDCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 527
Cdd:pfam00200   1 EEGEECDCGsLEECTNDPCCDaKTCKLKPGAQCS--SGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 21-136 9.02e-05

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: 42.69  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497  21 QHSVRKRDLQ-TSTHVETL-LTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQD---FFTGHVVGEPDSR 95
Cdd:pfam01562   9 DPSRRRRSLAsESTYLDTLsYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217330497  96 VlahirdddvIIR--------INTDGAEYNIEPLWRFVNDTKDKRMLVY 136
Cdd:pfam01562  89 V---------ALStcsglrgfIRTENEEYLIEPLEKYSREEGGHPHVVY 128
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 447-483 1.32e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 36.97  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2217330497 447 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKEGVQC 483
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTT-SGDG-CSATCRLEEGFAC 38
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 192-446 2.22e-152

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: 444.51  E-value: 2.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 192 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 271
Cdd:cd04270     1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 272 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 351
Cdd:cd04270    79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 352 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 431
Cdd:cd04270   151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                         250
                  ....*....|....*
gi 2217330497 432 ESKAQECFQERSNKV 446
Cdd:cd04270   230 EVKSNSCFVERSQSF 244
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 192-432 3.71e-59

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: 199.18  E-value: 3.71e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 192 NTCKLLVVADHRFYRYMgRGEESTTTNYLIELIDRVDDIYRNTSwdnaGFKGYGIQIEQIRILKSPQEVKPGEkhynmak 271
Cdd:cd04267     1 REIELVVVADHRMVSYF-NSDENILQAYITELINIANSIYRSTN----LRLGIRISLEGLQILKGEQFAPPID------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 272 sypneekdaWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDF-DMGTLGLAYVGSPranshggvcpkayyspvgkKNIYLN 350
Cdd:cd04267    69 ---------SDASNTLNSFSFWRAEGPIRHDNAVLLTAQDFiEGDILGLAYVGSM-------------------CNPYSS 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 351 SGLTSTKNYgktilTKEADLVTTHELGHNFGAEHDPDGlaECAPNEDQGGKYVMYPIAVSgdhENNKMFSNCSKQSIYKT 430
Cdd:cd04267   121 VGVVEDTGF-----TLLTALTMAHELGHNLGAEHDGGD--ELAFECDGGGNYIMAPVDSG---LNSYRFSQCSIGSIREF 190


                  ..
gi 2217330497 431 IE 432
Cdd:cd04267   191 LD 192
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 550-611 6.03e-33

Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a family of disintegrin and metalloproteinase domain-containing protein 17 found in metazoan species. ADAM17 is a major sheddase that is responsible for the regulation of a wide range of biological processes, such as cellular differentiation, regeneration, and cancer progression. This MPD region acts as the sheddase switch. PDI or protein-disulfide isomerase interacts with ADAM17 and to down-regulate its enzymatic activity. The interaction is directly with the MPD, the region of dimerization and substrate recognition, where it catalyzes an isomerization of disulfide bridges within the thioredoxin motif CXXC. this isomerization results in a major structural change between an active, open state and an inactive, closed state of the MPD. This change is thought to act as a molecular switch, allowing a global reorientation of the extracellular domains in ADAM17 and regulating its shedding activity.


Pssm-ID: 465239  Cd Length: 62  Bit Score: 120.92  E-value: 6.03e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217330497 550 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 611
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 215-427 1.51e-30

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: 118.89  E-value: 1.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 215 TTTNYLIELIDRVDDIYRNtswDNagFKGYGIQIEQIRILKSPQEVKPGekhynmaksYPNEEKDAWDVKMLLEqfsFDI 294
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATTSASDSG---------NNYCNSPTTIVRRLNF---LSQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 295 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPvgkkniYLNSGLTSTKNYGKTILTKEADLVTTH 374
Cdd:pfam13574  65 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217330497 375 ELGHNFGAEHDPDGLA-------ECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 427
Cdd:pfam13574 131 EVGHNFGATHDCDGSQyassgceRNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 188
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 192-431 2.70e-28

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: 111.46  E-value: 2.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 192 NTCKLLVVADHRFYrymgrgEESTTTNYLIELIDRVDDIYRNtswdnagfkgygiqIEQIRILKSPQEVKpgekhynmak 271
Cdd:cd00203     1 KVIPYVVVADDRDV------EEENLSAQIQSLILIAMQIWRD--------------YLNIRFVLVGVEID---------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 272 sypneekdawdvkmlleqfsfdiaeeasKVCLAHLFTYQDFDMGTLGLAYVGSPRaNSHGGVcpkayyspvgkkniylns 351
Cdd:cd00203    51 ----------------------------KADIAILVTRQDFDGGTGGWAYLGRVC-DSLRGV------------------ 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 352 GLTSTKNYGktilTKEADLVTTHELGHNFGAEHDPDGLAEC--------APNEDQGGKYVMYPIAVSGDHENNKMFSNCS 423
Cdd:cd00203    84 GVLQDNQSG----TKEGAQTIAHELGHALGFYHDHDRKDRDdyptiddtLNAEDDDYYSVMSYTKGSFSDGQRKDFSQCD 159


                  ....*...
gi 2217330497 424 KQSIYKTI 431
Cdd:cd00203   160 IDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
192-420 1.05e-26

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 107.89  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 192 NTCKLLVVADHRFYRYMGrGEEstTTNYLIELIDRVDDIYRNTSwdnagfkgyGIQIEQIRILKSPQEvkpgekhynmaK 271
Cdd:pfam13688   3 RTVALLVAADCSYVAAFG-GDA--AQANIINMVNTASNVYERDF---------NISLGLVNLTISDST-----------C 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 272 SYPNEEKDAWDVKMLLEQFSFDIAEE-ASKVCLAHLFTYQDFDMGtlGLAYVGSPRANSHGGVCpkayYSPVGKKNIYln 350
Cdd:pfam13688  60 PYTPPACSTGDSSDRLSEFQDFSAWRgTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSV----STRVSGNNVV-- 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217330497 351 sgltstknygktILTKEADLVTTHELGHNFGAEHDPDGLA---ECAPN---EDQGGKYVMYPIAVSgdheNNKMFS 420
Cdd:pfam13688 132 ------------VSTATEWQVFAHEIGHNFGAVHDCDSSTssqCCPPSnstCPAGGRYIMNPSSSP----NSTDFS 191
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 549-611 2.01e-25

Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a multi-domain protein that acts as a sheddase; is involved in the cleavage and release of the soluble ectodomain of tumor necrosis factor alpha from the cell surface and in the trans-Golgi network, as well as in the release of various other targets such as cytokines and cell adhesion molecules. This links ADAM17 to a variety of biological processes, including cellular differentiation and the progression of cancer. It was shown that the enzymatic activity of ADAM17 is regulated via a protein-disulfide isomerase (PDI). Specifically, the disulfide bridges within a CxxC motif of the membrane-proximal domain (MPD) are isomerized by PDI; the conversion triggers a conformational change between a closed and an opened form of the MPD, which may constitute a molecular switch that triggers the shedding activity of ADAM17.


Pssm-ID: 271205  Cd Length: 60  Bit Score: 99.37  E-value: 2.01e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217330497 549 PFCEReQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 611
Cdd:cd14246     1 PFCER-ENLQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 453-529 2.08e-24

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: 96.99  E-value: 2.08e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330497  453 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 529
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
453-527 1.02e-21

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 89.61  E-value: 1.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217330497 453 DEGEECDPG-IMYLNNDTCCN-SDCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 527
Cdd:pfam00200   1 EEGEECDCGsLEECTNDPCCDaKTCKLKPGAQCS--SGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 195-438 1.77e-19

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: 87.29  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 195 KLLVVADHRFYRYMGRgEESTTTNYLIELIDRVDDIYRN----------TSWDNAgfkgygiqiEQIRILKSPQEVkpge 264
Cdd:cd04269     4 ELVVVVDNSLYKKYGS-NLSKVRQRVIEIVNIVDSIYRPlnirvvlvglEIWTDK---------DKISVSGDAGET---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 265 khynmAKSYPNeekdaWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVgspranshGGVCPKAYyspvgk 344
Cdd:cd04269    70 -----LNRFLD-----WKRSNLLPRKPHDNA---------QLLTGRDFDGNTVGLAYV--------GGMCSPKY------ 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 345 kniylnSGLTSTknYGKTILTKEADLVtTHELGHNFGAEHDPDGlaeCapnEDQGGKYVMYPIAVSGdhenNKMFSNCSK 424
Cdd:cd04269   117 ------SGGVVQ--DHSRNLLLFAVTM-AHELGHNLGMEHDDGG---C---TCGRSTCIMAPSPSSL----TDAFSNCSY 177

                         250
                  ....*....|....
gi 2217330497 425 QSIYKTIESKAQEC 438
Cdd:cd04269   178 EDYQKFLSRGGGQC 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 196-438 2.09e-13

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: 69.96  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 196 LLVVADHRFYRYMGRgeeSTTTNYLIELIDRVDDIYRNTSWDNAgfkgygIQIEQIRILKSPQEVKPGEKHYNMAKS--- 272
Cdd:cd04273     5 TLVVADSKMVEFHHG---EDLEHYILTLMNIVASLYKDPSLGNS------INIVVVRLIVLEDEESGLLISGNAQKSlks 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 273 --------YPNEEKDA--WDVKMLLEQFSFDIAeeaSKVClahlftyqdfdmGTLGLAYVGspranshgGVCpkayySPV 342
Cdd:cd04273    76 fcrwqkklNPPNDSDPehHDHAILLTRQDICRS---NGNC------------DTLGLAPVG--------GMC-----SPS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 343 GKKNIYLNSGLTSTknygktiltkeadLVTTHELGHNFGAEHDPDGlAECAPNEDQGgkYVMYPIAVSGDHEnnKMFSNC 422
Cdd:cd04273   128 RSCSINEDTGLSSA-------------FTIAHELGHVLGMPHDGDG-NSCGPEGKDG--HIMSPTLGANTGP--FTWSKC 189

                         250
                  ....*....|....*.
gi 2217330497 423 SKQSIYKTIESKAQEC 438
Cdd:cd04273   190 SRRYLTSFLDTGDGNC 205
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 196-442 9.72e-12

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: 64.63  E-value: 9.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 196 LLVVADHRFYRYMGRGEEsTTTNYLIELIDRVDDIYrntswdnagfKGYGIQI-----------EQIRILKSPQEVKpge 264
Cdd:pfam01421   5 LFIVVDKQLFQKMGSDTT-VVRQRVFQVVNLVNSIY----------KELNIRVvlvgleiwtdeDKIDVSGDANDTL--- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 265 khYNMAKsypneekdaWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPV-- 342
Cdd:pfam01421  71 --RNFLK---------WRQEYLKKRKPHDVA---------QLLSGVEFGGTTVGAAYVG--------GMCSLEYSGGVne 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 343 -GKKNIYLNSGLTStknygktiltkeadlvttHELGHNFGAEHDPDGLA-ECAPnedqGGKYVMYPIAVsgdHENNKMFS 420
Cdd:pfam01421 123 dHSKNLESFAVTMA------------------HELGHNLGMQHDDFNGGcKCPP----GGGCIMNPSAG---SSFPRKFS 177

                         250       260
                  ....*....|....*....|..
gi 2217330497 421 NCSKQSIYKTIESKAQECFQER 442
Cdd:pfam01421 178 NCSQEDFEQFLTKQKGACLFNK 199
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 272-385 9.56e-10

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: 56.99  E-value: 9.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 272 SYPNEEKDA-WDVKMLLEqfSFDIAEEASKVCLAHLFTYQDFDmGTLGLAYVGspranshgGVCPKAYyspvgKKNIyln 350
Cdd:pfam13582  34 DTPYTSSDAlEILDELQE--VNDTRIGQYGYDLGHLFTGRDGG-GGGGIAYVG--------GVCNSGS-----KFGV--- 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217330497 351 sgltstkNYGKTILTKEADLVTTHELGHNFGAEHD 385
Cdd:pfam13582  95 -------NSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 370-434 1.49e-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: 50.11  E-value: 1.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330497 370 LVTTHELGHNFGAEHD---------PDGLAECAPNE----DQGGKYVMYPIAVSGDHEnnkmFSNCSKQSIYKTIESK 434
Cdd:cd04271   147 QVFAHEIGHTFGAVHDctsgtcsdgSVGSQQCCPLStstcDANGQYIMNPSSSSGITE----FSPCTIGNICSLLGRN 220
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 195-440 1.95e-06

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 49.66  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 195 KLLVVADHRFYRYMGRGEEstTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEqirilKSPQEvKPGEKHYNMA---- 270
Cdd:cd04272     4 ELFVVVDYDHQSEFFSNEQ--LIRYLAVMVNAANLRYRDLKSPRIRLLLVGITIS-----KDPDF-EPYIHPINYGyida 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 271 -------KSYPNEEKDawdvkmlleQFSFDIAEEASKVCLAHlFTYQDFDMGTLGLAYVGspranshgGVCPKaYYSPVG 343
Cdd:cd04272    76 aetlenfNEYVKKKRD---------YFNPDVVFLVTGLDMST-YSGGSLQTGTGGYAYVG--------GACTE-NRVAMG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 344 KKNIYLNSGLtstknygktiltkeadLVTTHELGHNFGAEHdpDGLAECAPNEDQGGK--------YVMypiaVSGDHEN 415
Cdd:cd04272   137 EDTPGSYYGV----------------YTMTHELAHLLGAPH--DGSPPPSWVKGHPGSldcpwddgYIM----SYVVNGE 194

                         250       260
                  ....*....|....*....|....*.
gi 2217330497 416 NKM-FSNCSKQSIYKTIESKAQECFQ 440
Cdd:cd04272   195 RQYrFSQCSQRQIRNVFRRLGASCLH 220
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 21-136 9.02e-05

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: 42.69  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497  21 QHSVRKRDLQ-TSTHVETL-LTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQD---FFTGHVVGEPDSR 95
Cdd:pfam01562   9 DPSRRRRSLAsESTYLDTLsYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTdhcYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217330497  96 VlahirdddvIIR--------INTDGAEYNIEPLWRFVNDTKDKRMLVY 136
Cdd:pfam01562  89 V---------ALStcsglrgfIRTENEEYLIEPLEKYSREEGGHPHVVY 128
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 447-483 1.32e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 36.97  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2217330497 447 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKEGVQC 483
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTT-SGDG-CSATCRLEEGFAC 38
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 303-437 1.50e-03

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: 40.68  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 303 LAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPVGkkniylNSGLTSTKNYGktiltkeadlVTTHELGHNFGA 382
Cdd:pfam13583  94 LAYLTLMTGPSGQNVGVAWVG--------ALCSSARQNAKA------SGVARSRDEWD----------IFAHEIGHTFGA 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217330497 383 EHDPDGLAECAPN--EDQGGKYVMYPIA-VSGDHennkmFSNCSKQSIYKTIESKAQE 437
Cdd:pfam13583 150 VHDCSSQGEGLSSstEDGSGQTIMSYAStASQTA-----FSPCTIRNINGNPCSQANY 202
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 307-414 9.14e-03

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 37.86  E-value: 9.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217330497 307 FTYQDFDMGTLGLAYVGSpRANSHGGvcpkayyspvgkkNIYLNSGLTSTKNYGktILTKEADLVTTHELGHNFGAEHDP 386
Cdd:cd04268    49 SVIRWIPYNDGTWSYGPS-QVDPLTG-------------EILLARVYLYSSFVE--YSGARLRNTAEHELGHALGLRHNF 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217330497 387 DGLAECAPNEDQGGKY----VMYPIAVSGDHE 414
Cdd:cd04268   113 AASDRDDNVDLLAEKGdtssVMDYAPSNFSIQ 144
 
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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