NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|110347485|ref|NP_033745|]
View 

disintegrin and metalloproteinase domain-containing protein 17 isoform 1 preproprotein [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 223-477 1.24e-151

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: 443.74  E-value: 1.24e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 223 NTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGVQIEQIRILKSPQEVKPGERHFNmaK 302
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 303 SFPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYNPtVKKNIYLNS 382
Cdd:cd04270   79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYS-NGKKKYLNT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270  151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                        250
                 ....*....|....*
gi 110347485 463 ESKAQECFQERSNKV 477
Cdd:cd04270  230 EVKSNSCFVERSQSF 244
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 581-642 6.94e-30

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: 112.44  E-value: 6.94e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347485  581 FCKREQELESCACVDTDNSCKVCCRNLSGPCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 642
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 484-559 4.95e-25

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: 98.92  E-value: 4.95e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347485   484 DEGEECDPGIMYLNNDTCCNS-DCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPG 559
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDP 74
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 52-167 1.51e-04

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: 42.30  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485   52 QHSIRKRDLQS-ATHLETL-LTFSALKRHFKLYLTSSTERFSQNLRVVV--VDGKE-ESEYSVKWQNFFSGHVVGEPDSR 126
Cdd:pfam01562   9 DPSRRRRSLASeSTYLDTLsYRLAAFGKKFHLHLTPNRLLLAPGFTVTYylDGGTGvESPPVQTDHCYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 110347485  127 VLAHIGDDDVTVrINTDGAEYNVEPLWRFVNDTKDKRMLVY 167
Cdd:pfam01562  89 VALSTCSGLRGF-IRTENEEYLIEPLEKYSREEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 223-477 1.24e-151

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: 443.74  E-value: 1.24e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 223 NTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGVQIEQIRILKSPQEVKPGERHFNmaK 302
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 303 SFPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYNPtVKKNIYLNS 382
Cdd:cd04270   79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYS-NGKKKYLNT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270  151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                        250
                 ....*....|....*
gi 110347485 463 ESKAQECFQERSNKV 477
Cdd:cd04270  230 EVKSNSCFVERSQSF 244
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 246-458 2.79e-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: 118.12  E-value: 2.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  246 TTTNYLIELIDRVDDIYRNtswDNagFKGYGVQIEQIRILKSPQEVKPGerhfnmaksFPNEEKDAWDVKMLLEqfsFDI 325
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATTSASDSG---------NNYCNSPTTIVRRLNF---LSQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  326 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYNPtvkkniYLNSGLTSTKNYGKTILTKEADLVTTH 405
Cdd:pfam13574  65 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347485  406 ELGHNFGAEHDPDGLA-------ECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 458
Cdd:pfam13574 131 EVGHNFGATHDCDGSQyassgceRNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 188
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 581-642 6.94e-30

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: 112.44  E-value: 6.94e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347485  581 FCKREQELESCACVDTDNSCKVCCRNLSGPCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 642
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 484-559 4.95e-25

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: 98.92  E-value: 4.95e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347485   484 DEGEECDPGIMYLNNDTCCNS-DCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPG 559
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDP 74
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 580-642 2.99e-23

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: 93.59  E-value: 2.99e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347485 580 PFCKREQeLESCACVDTDNSCKVCCRNLSGPCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 642
Cdd:cd14246    1 PFCEREN-LQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
Disintegrin pfam00200
Disintegrin;
484-558 1.37e-22

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 91.92  E-value: 1.37e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347485  484 DEGEECDPG-IMYLNNDTCCN-SDCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 558
Cdd:pfam00200   1 EEGEECDCGsLEECTNDPCCDaKTCKLKPGAQCS--SGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 52-167 1.51e-04

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: 42.30  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485   52 QHSIRKRDLQS-ATHLETL-LTFSALKRHFKLYLTSSTERFSQNLRVVV--VDGKE-ESEYSVKWQNFFSGHVVGEPDSR 126
Cdd:pfam01562   9 DPSRRRRSLASeSTYLDTLsYRLAAFGKKFHLHLTPNRLLLAPGFTVTYylDGGTGvESPPVQTDHCYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 110347485  127 VLAHIGDDDVTVrINTDGAEYNVEPLWRFVNDTKDKRMLVY 167
Cdd:pfam01562  89 VALSTCSGLRGF-IRTENEEYLIEPLEKYSREEGGHPHVVY 128
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 478-514 9.72e-04

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: 37.35  E-value: 9.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 110347485  478 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKPGVQC 514
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 ...
 223-477 1.24e-151

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: 443.74  E-value: 1.24e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 223 NTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGVQIEQIRILKSPQEVKPGERHFNmaK 302
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 303 SFPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYNPtVKKNIYLNS 382
Cdd:cd04270   79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYS-NGKKKYLNT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270  151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                        250
                 ....*....|....*
gi 110347485 463 ESKAQECFQERSNKV 477
Cdd:cd04270  230 EVKSNSCFVERSQSF 244
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 223-463 1.35e-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: 200.72  E-value: 1.35e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 223 NTCKLLVVADHRFYKYMgRGEESTTTNYLIELIDRVDDIYRNTSwdnaGFKGYGVQIEQIRILKSPQEVKPGErhfnmak 302
Cdd:cd04267    1 REIELVVVADHRMVSYF-NSDENILQAYITELINIANSIYRSTN----LRLGIRISLEGLQILKGEQFAPPID------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 303 sfpneekdaWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDF-DMGTLGLAYVGSPranshggvcpkayynptvkKNIYLN 381
Cdd:cd04267   69 ---------SDASNTLNSFSFWRAEGPIRHDNAVLLTAQDFiEGDILGLAYVGSM-------------------CNPYSS 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 382 SGLTSTKNYgktilTKEADLVTTHELGHNFGAEHDPDGlaECAPNEDQGGKYVMYPIAVSgdhENNKMFSNCSKQSIYKT 461
Cdd:cd04267  121 VGVVEDTGF-----TLLTALTMAHELGHNLGAEHDGGD--ELAFECDGGGNYIMAPVDSG---LNSYRFSQCSIGSIREF 190


                 ..
gi 110347485 462 IE 463
Cdd:cd04267  191 LD 192
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 246-458 2.79e-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: 118.12  E-value: 2.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  246 TTTNYLIELIDRVDDIYRNtswDNagFKGYGVQIEQIRILKSPQEVKPGerhfnmaksFPNEEKDAWDVKMLLEqfsFDI 325
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATTSASDSG---------NNYCNSPTTIVRRLNF---LSQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  326 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYNPtvkkniYLNSGLTSTKNYGKTILTKEADLVTTH 405
Cdd:pfam13574  65 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347485  406 ELGHNFGAEHDPDGLA-------ECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 458
Cdd:pfam13574 131 EVGHNFGATHDCDGSQyassgceRNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 188
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 581-642 6.94e-30

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: 112.44  E-value: 6.94e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110347485  581 FCKREQELESCACVDTDNSCKVCCRNLSGPCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 642
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 223-462 2.84e-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: 2.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 223 NTCKLLVVADHRFYkymgrgEESTTTNYLIELIDRVDDIYRNtswdnagfkgygvqIEQIRILKSPQEVKpgerhfnmak 302
Cdd:cd00203    1 KVIPYVVVADDRDV------EEENLSAQIQSLILIAMQIWRD--------------YLNIRFVLVGVEID---------- 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 303 sfpneekdawdvkmlleqfsfdiaeeasKVCLAHLFTYQDFDMGTLGLAYVGSPRaNSHGGVcpkayynptvkkniylns 382
Cdd:cd00203   51 ----------------------------KADIAILVTRQDFDGGTGGWAYLGRVC-DSLRGV------------------ 83

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 383 GLTSTKNYGktilTKEADLVTTHELGHNFGAEHDPDGLAEC--------APNEDQGGKYVMYPIAVSGDHENNKMFSNCS 454
Cdd:cd00203   84 GVLQDNQSG----TKEGAQTIAHELGHALGFYHDHDRKDRDdyptiddtLNAEDDDYYSVMSYTKGSFSDGQRKDFSQCD 159


                 ....*...
gi 110347485 455 KQSIYKTI 462
Cdd:cd00203  160 IDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
223-451 1.34e-25

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 104.81  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  223 NTCKLLVVADHRFYKYMGrGEEstTTNYLIELIDRVDDIYRNTSwdnagfkgyGVQIeQIRILKSPQEVKPGERHFNMAk 302
Cdd:pfam13688   3 RTVALLVAADCSYVAAFG-GDA--AQANIINMVNTASNVYERDF---------NISL-GLVNLTISDSTCPYTPPACST- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  303 sfpneekdaWDVKMLLEQFSFDIAEE-ASKVCLAHLFTYQDFDMGtlGLAYVGSPRANSHGGVCpkayyNPTVKKNiyln 381
Cdd:pfam13688  69 ---------GDSSDRLSEFQDFSAWRgTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSV-----STRVSGN---- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347485  382 sgltstknyGKTILTKEADLVTTHELGHNFGAEHDPDGLA---ECAPN---EDQGGKYVMYPIAVSgdheNNKMFS 451
Cdd:pfam13688 129 ---------NVVVSTATEWQVFAHEIGHNFGAVHDCDSSTssqCCPPSnstCPAGGRYIMNPSSSP----NSTDFS 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 484-559 4.95e-25

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: 98.92  E-value: 4.95e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347485   484 DEGEECDPGIMYLNNDTCCNS-DCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPG 559
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDP 74
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 580-642 2.99e-23

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: 93.59  E-value: 2.99e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110347485 580 PFCKREQeLESCACVDTDNSCKVCCRNLSGPCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 642
Cdd:cd14246    1 PFCEREN-LQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
Disintegrin pfam00200
Disintegrin;
484-558 1.37e-22

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 91.92  E-value: 1.37e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110347485  484 DEGEECDPG-IMYLNNDTCCN-SDCTLKPGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 558
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 ...
 226-469 1.20e-20

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: 90.37  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 226 KLLVVADHRFYKYMGRgEESTTTNYLIELIDRVDDIYRN----------TSWDNAgfkgygvqiEQIRILKSPQEVkpge 295
Cdd:cd04269    4 ELVVVVDNSLYKKYGS-NLSKVRQRVIEIVNIVDSIYRPlnirvvlvglEIWTDK---------DKISVSGDAGET---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 296 rhfnmAKSFPNeekdaWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVgspranshGGVCPKAYynptvk 375
Cdd:cd04269   70 -----LNRFLD-----WKRSNLLPRKPHDNA---------QLLTGRDFDGNTVGLAYV--------GGMCSPKY------ 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 376 kniylnSGLTSTknYGKTILTKEADLVtTHELGHNFGAEHDPDGlaeCapnEDQGGKYVMYPIAVSGdhenNKMFSNCSK 455
Cdd:cd04269  117 ------SGGVVQ--DHSRNLLLFAVTM-AHELGHNLGMEHDDGG---C---TCGRSTCIMAPSPSSL----TDAFSNCSY 177

                        250
                 ....*....|....
gi 110347485 456 QSIYKTIESKAQEC 469
Cdd:cd04269  178 EDYQKFLSRGGGQC 191
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 227-473 2.68e-13

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: 69.25  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  227 LLVVADHRFYKYMGRGEEsTTTNYLIELIDRVDDIYR--NTS--------WdNAGfkgygvqiEQIRILKSPQEVKpgeR 296
Cdd:pfam01421   5 LFIVVDKQLFQKMGSDTT-VVRQRVFQVVNLVNSIYKelNIRvvlvgleiW-TDE--------DKIDVSGDANDTL---R 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  297 HFNMaksfpneekdaWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVGspranshgGVCpKAYYNPTVKK 376
Cdd:pfam01421  72 NFLK-----------WRQEYLKKRKPHDVA---------QLLSGVEFGGTTVGAAYVG--------GMC-SLEYSGGVNE 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  377 NIYLNSGLTSTknygktiltkeadlVTTHELGHNFGAEHDPDGLA-ECAPnedqGGKYVMYPIAVsgdHENNKMFSNCSK 455
Cdd:pfam01421 123 DHSKNLESFAV--------------TMAHELGHNLGMQHDDFNGGcKCPP----GGGCIMNPSAG---SSFPRKFSNCSQ 181

                         250
                  ....*....|....*...
gi 110347485  456 QSIYKTIESKAQECFQER 473
Cdd:pfam01421 182 EDFEQFLTKQKGACLFNK 199
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 227-469 1.00e-12

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: 68.03  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 227 LLVVADHRFYKYMGRgeeSTTTNYLIELIDRVDDIYRNTSWDNAgfkgYGVQIEQIRILKSPQEvkPGERHFN---MAKS 303
Cdd:cd04273    5 TLVVADSKMVEFHHG---EDLEHYILTLMNIVASLYKDPSLGNS----INIVVVRLIVLEDEES--GLLISGNaqkSLKS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 304 F--------PNEEKDA--WDVKMLLEQFSFDIAeeaSKVClahlftyqdfdmGTLGLAYVGspranshgGVCpKAYYNPT 373
Cdd:cd04273   76 FcrwqkklnPPNDSDPehHDHAILLTRQDICRS---NGNC------------DTLGLAPVG--------GMC-SPSRSCS 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 374 VKKNIYLNSGLTstknygktiltkeadlvTTHELGHNFGAEHDPDGlAECAPNEDQGgkYVMYPIAVSGDHEnnKMFSNC 453
Cdd:cd04273  132 INEDTGLSSAFT-----------------IAHELGHVLGMPHDGDG-NSCGPEGKDG--HIMSPTLGANTGP--FTWSKC 189

                        250
                 ....*....|....*.
gi 110347485 454 SKQSIYKTIESKAQEC 469
Cdd:cd04273  190 SRRYLTSFLDTGDGNC 205
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 322-416 2.42e-09

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: 55.84  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  322 SFDIAEEASKVCLAHLFTYQDFDmGTLGLAYVGspranshgGVCPKAYynptvKKNIylnsgltstkNYGKTILTKEADL 401
Cdd:pfam13582  52 VNDTRIGQYGYDLGHLFTGRDGG-GGGGIAYVG--------GVCNSGS-----KFGV----------NSGSGPVGDTGAD 107

                          90
                  ....*....|....*
gi 110347485  402 VTTHELGHNFGAEHD 416
Cdd:pfam13582 108 TFAHEIGHNFGLNHT 122
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 401-465 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 110347485 401 LVTTHELGHNFGAEHD---------PDGLAECAPNE----DQGGKYVMYPIAVSGDHEnnkmFSNCSKQSIYKTIESK 465
Cdd:cd04271  147 QVFAHEIGHTFGAVHDctsgtcsdgSVGSQQCCPLStstcDANGQYIMNPSSSSGITE----FSPCTIGNICSLLGRN 220
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 226-471 1.04e-05

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 47.35  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 226 KLLVVADHRFYKYMGRGEEstTTNYLIELIDRVDDIYRNTSWDNAGFKGYGVQIEqirilKSPQEvKPGERHFNMA---- 301
Cdd:cd04272    4 ELFVVVDYDHQSEFFSNEQ--LIRYLAVMVNAANLRYRDLKSPRIRLLLVGITIS-----KDPDF-EPYIHPINYGyida 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 302 -------KSFPNEEKDawdvkmlleQFSFDIAEEASKVCLAHlFTYQDFDMGTLGLAYVGSprANSHGGVC-----PKAY 369
Cdd:cd04272   76 aetlenfNEYVKKKRD---------YFNPDVVFLVTGLDMST-YSGGSLQTGTGGYAYVGG--ACTENRVAmgedtPGSY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 370 YnptvkkniylnsGLtstknygktiltkeadLVTTHELGHNFGAEHdpDGLAECAPNEDQGGK--------YVMypiaVS 441
Cdd:cd04272  144 Y------------GV----------------YTMTHELAHLLGAPH--DGSPPPSWVKGHPGSldcpwddgYIM----SY 189

                        250       260       270
                 ....*....|....*....|....*....|.
gi 110347485 442 GDHENNKM-FSNCSKQSIYKTIESKAQECFQ 471
Cdd:cd04272  190 VVNGERQYrFSQCSQRQIRNVFRRLGASCLH 220
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 52-167 1.51e-04

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: 42.30  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485   52 QHSIRKRDLQS-ATHLETL-LTFSALKRHFKLYLTSSTERFSQNLRVVV--VDGKE-ESEYSVKWQNFFSGHVVGEPDSR 126
Cdd:pfam01562   9 DPSRRRRSLASeSTYLDTLsYRLAAFGKKFHLHLTPNRLLLAPGFTVTYylDGGTGvESPPVQTDHCYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 110347485  127 VLAHIGDDDVTVrINTDGAEYNVEPLWRFVNDTKDKRMLVY 167
Cdd:pfam01562  89 VALSTCSGLRGF-IRTENEEYLIEPLEKYSREEGGHPHVVY 128
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 478-514 9.72e-04

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: 37.35  E-value: 9.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 110347485  478 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKPGVQC 514
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTT-SGDG-CSATCRLEEGFAC 38
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 334-468 1.03e-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: 41.07  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485  334 LAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYNptVKKNIYLnsglTSTKNYGktiltkeadlVTTHELGHNFGA 413
Cdd:pfam13583  94 LAYLTLMTGPSGQNVGVAWVG--------ALCSSARQN--AKASGVA----RSRDEWD----------IFAHEIGHTFGA 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110347485  414 EHDPDGLAECAPN--EDQGGKYVMYPIA-VSGDHennkmFSNCSKQSIYKTIESKAQE 468
Cdd:pfam13583 150 VHDCSSQGEGLSSstEDGSGQTIMSYAStASQTA-----FSPCTIRNINGNPCSQANY 202
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 338-445 9.58e-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: 9.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347485 338 FTYQDFDMGTLGLAYVGSpRANSHGGvcpkayynptvkkNIYLNSGLTSTKNYGktILTKEADLVTTHELGHNFGAEHDP 417
Cdd:cd04268   49 SVIRWIPYNDGTWSYGPS-QVDPLTG-------------EILLARVYLYSSFVE--YSGARLRNTAEHELGHALGLRHNF 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 110347485 418 DGLAECAPNEDQGGKY----VMYPIAVSGDHE 445
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH