NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1843978386|ref|NP_001369706|]
View 

disintegrin and metalloproteinase domain-containing protein 17 isoform 2 [Homo sapiens]

Protein Classification

ZnMc_TACE_like and ADAM17_MPD domain-containing protein( domain architecture ID 10857782)

protein containing domains ZnMc_TACE_like, DISIN, and ADAM17_MPD

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 ...
 3-257 3.23e-154

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: 442.58  E-value: 3.23e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   3 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 82
Cdd:cd04270     1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  83 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 162
Cdd:cd04270    79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 163 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 242
Cdd:cd04270   151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                         250
                  ....*....|....*
gi 1843978386 243 ESKAQECFQERSNKV 257
Cdd:cd04270   230 EVKSNSCFVERSQSF 244
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 361-422 3.02e-31

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: 115.52  E-value: 3.02e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843978386 361 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 422
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 264-340 1.53e-22

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: 91.60  E-value: 1.53e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1843978386  264 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 340
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 3-257 3.23e-154

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: 442.58  E-value: 3.23e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   3 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 82
Cdd:cd04270     1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  83 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 162
Cdd:cd04270    79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 163 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 242
Cdd:cd04270   151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                         250
                  ....*....|....*
gi 1843978386 243 ESKAQECFQERSNKV 257
Cdd:cd04270   230 EVKSNSCFVERSQSF 244
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 361-422 3.02e-31

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: 115.52  E-value: 3.02e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843978386 361 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 422
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 26-238 8.69e-31

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: 8.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  26 TTTNYLIELIDRVDDIYRNtswDNagFKGYGIQIEQIRILKSPQEVKPGekhynmaksYPNEEKDAWDVKMLLEqfsFDI 105
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATTSASDSG---------NNYCNSPTTIVRRLNF---LSQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 106 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPvgkkniYLNSGLTSTKNYGKTILTKEADLVTTH 185
Cdd:pfam13574  65 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843978386 186 ELGHNFGAEHDPDGLA-------ECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 238
Cdd:pfam13574 131 EVGHNFGATHDCDGSQyassgceRNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 188
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 360-422 1.20e-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: 93.98  E-value: 1.20e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1843978386 360 PFCEReQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 422
Cdd:cd14246     1 PFCER-ENLQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 264-340 1.53e-22

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: 91.60  E-value: 1.53e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1843978386  264 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 340
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
264-338 6.26e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 83.83  E-value: 6.26e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1843978386 264 DEGEECDPG-IMYLNNDTCCN-SDCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 338
Cdd:pfam00200   1 EEGEECDCGsLEECTNDPCCDaKTCKLKPGAQCS--SGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 258-294 4.14e-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: 35.43  E-value: 4.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1843978386 258 CGNSRVDEGEECDPGimYLNNDTCCNSDCTLKEGVQC 294
Cdd:TIGR02232   4 CGDGIIEPGEECDDG--NTTSGDGCSATCRLEEGFAC 38
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 3-257 3.23e-154

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: 442.58  E-value: 3.23e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   3 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 82
Cdd:cd04270     1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  83 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 162
Cdd:cd04270    79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 163 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 242
Cdd:cd04270   151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229

                         250
                  ....*....|....*
gi 1843978386 243 ESKAQECFQERSNKV 257
Cdd:cd04270   230 EVKSNSCFVERSQSF 244
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 3-243 2.62e-60

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: 198.80  E-value: 2.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   3 NTCKLLVVADHRFYRYMgRGEESTTTNYLIELIDRVDDIYRNTSwdnaGFKGYGIQIEQIRILKSPQEVKPGEkhynmak 82
Cdd:cd04267     1 REIELVVVADHRMVSYF-NSDENILQAYITELINIANSIYRSTN----LRLGIRISLEGLQILKGEQFAPPID------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  83 sypneekdaWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDF-DMGTLGLAYVGSPranshggvcpkayyspvgkKNIYLN 161
Cdd:cd04267    69 ---------SDASNTLNSFSFWRAEGPIRHDNAVLLTAQDFiEGDILGLAYVGSM-------------------CNPYSS 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 162 SGLTSTKNYgktilTKEADLVTTHELGHNFGAEHDPDGlaECAPNEDQGGKYVMYPIAVSgdhENNKMFSNCSKQSIYKT 241
Cdd:cd04267   121 VGVVEDTGF-----TLLTALTMAHELGHNLGAEHDGGD--ELAFECDGGGNYIMAPVDSG---LNSYRFSQCSIGSIREF 190


                  ..
gi 1843978386 242 IE 243
Cdd:cd04267   191 LD 192
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 361-422 3.02e-31

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: 115.52  E-value: 3.02e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843978386 361 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCE 422
Cdd:pfam16698   1 FCETKSGLQSCACNETDDSCKVCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKCE 62
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 26-238 8.69e-31

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: 8.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  26 TTTNYLIELIDRVDDIYRNtswDNagFKGYGIQIEQIRILKSPQEVKPGekhynmaksYPNEEKDAWDVKMLLEqfsFDI 105
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATTSASDSG---------NNYCNSPTTIVRRLNF---LSQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 106 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPvgkkniYLNSGLTSTKNYGKTILTKEADLVTTH 185
Cdd:pfam13574  65 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843978386 186 ELGHNFGAEHDPDGLA-------ECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 238
Cdd:pfam13574 131 EVGHNFGATHDCDGSQyassgceRNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 188
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 3-242 1.73e-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: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   3 NTCKLLVVADHRFYrymgrgEESTTTNYLIELIDRVDDIYRNtswdnagfkgygiqIEQIRILKSPQEVKpgekhynmak 82
Cdd:cd00203     1 KVIPYVVVADDRDV------EEENLSAQIQSLILIAMQIWRD--------------YLNIRFVLVGVEID---------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  83 sypneekdawdvkmlleqfsfdiaeeasKVCLAHLFTYQDFDMGTLGLAYVGSPRaNSHGGVcpkayyspvgkkniylns 162
Cdd:cd00203    51 ----------------------------KADIAILVTRQDFDGGTGGWAYLGRVC-DSLRGV------------------ 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 163 GLTSTKNYGktilTKEADLVTTHELGHNFGAEHDPDGLAEC--------APNEDQGGKYVMYPIAVSGDHENNKMFSNCS 234
Cdd:cd00203    84 GVLQDNQSG----TKEGAQTIAHELGHALGFYHDHDRKDRDdyptiddtLNAEDDDYYSVMSYTKGSFSDGQRKDFSQCD 159


                  ....*...
gi 1843978386 235 KQSIYKTI 242
Cdd:cd00203   160 IDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
3-231 6.94e-27

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 107.89  E-value: 6.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   3 NTCKLLVVADHRFYRYMGrGEEstTTNYLIELIDRVDDIYRNTSwdnagfkgyGIQIEQIRILKSPQEvkpgekhynmaK 82
Cdd:pfam13688   3 RTVALLVAADCSYVAAFG-GDA--AQANIINMVNTASNVYERDF---------NISLGLVNLTISDST-----------C 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  83 SYPNEEKDAWDVKMLLEQFSFDIAEE-ASKVCLAHLFTYQDFDMGtlGLAYVGSPRANSHGGVCpkayYSPVGKKNIYln 161
Cdd:pfam13688  60 PYTPPACSTGDSSDRLSEFQDFSAWRgTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSV----STRVSGNNVV-- 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1843978386 162 sgltstknygktILTKEADLVTTHELGHNFGAEHDPDGLA---ECAPN---EDQGGKYVMYPIAVSgdheNNKMFS 231
Cdd:pfam13688 132 ------------VSTATEWQVFAHEIGHNFGAVHDCDSSTssqCCPPSnstCPAGGRYIMNPSSSP----NSTDFS 191
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 360-422 1.20e-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: 93.98  E-value: 1.20e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1843978386 360 PFCEReQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 422
Cdd:cd14246     1 PFCER-ENLQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 264-340 1.53e-22

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: 91.60  E-value: 1.53e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1843978386  264 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 340
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
264-338 6.26e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 83.83  E-value: 6.26e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1843978386 264 DEGEECDPG-IMYLNNDTCCN-SDCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 338
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 ...
 6-249 2.08e-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: 86.52  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   6 KLLVVADHRFYRYMGRgEESTTTNYLIELIDRVDDIYRN----------TSWDNAgfkgygiqiEQIRILKSPQEVkpge 75
Cdd:cd04269     4 ELVVVVDNSLYKKYGS-NLSKVRQRVIEIVNIVDSIYRPlnirvvlvglEIWTDK---------DKISVSGDAGET---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  76 khynmAKSYPNeekdaWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVgspranshGGVCPKAYyspvgk 155
Cdd:cd04269    70 -----LNRFLD-----WKRSNLLPRKPHDNA---------QLLTGRDFDGNTVGLAYV--------GGMCSPKY------ 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 156 kniylnSGLTSTknYGKTILTKEADLVtTHELGHNFGAEHDPDGlaeCapnEDQGGKYVMYPIAVSGdhenNKMFSNCSK 235
Cdd:cd04269   117 ------SGGVVQ--DHSRNLLLFAVTM-AHELGHNLGMEHDDGG---C---TCGRSTCIMAPSPSSL----TDAFSNCSY 177

                         250
                  ....*....|....
gi 1843978386 236 QSIYKTIESKAQEC 249
Cdd:cd04269   178 EDYQKFLSRGGGQC 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 7-249 2.24e-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: 69.19  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   7 LLVVADHRFYRYMGRgeeSTTTNYLIELIDRVDDIYRNTSWDNAgfkgygIQIEQIRILKSPQEVKPGEKHYNMAKS--- 83
Cdd:cd04273     5 TLVVADSKMVEFHHG---EDLEHYILTLMNIVASLYKDPSLGNS------INIVVVRLIVLEDEESGLLISGNAQKSlks 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  84 --------YPNEEKDA--WDVKMLLEQFSFDIAeeaSKVClahlftyqdfdmGTLGLAYVGspranshgGVCpkayySPV 153
Cdd:cd04273    76 fcrwqkklNPPNDSDPehHDHAILLTRQDICRS---NGNC------------DTLGLAPVG--------GMC-----SPS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 154 GKKNIYLNSGLTSTknygktiltkeadLVTTHELGHNFGAEHDPDGlAECAPNEDQGgkYVMYPIAVSGDHEnnKMFSNC 233
Cdd:cd04273   128 RSCSINEDTGLSSA-------------FTIAHELGHVLGMPHDGDG-NSCGPEGKDG--HIMSPTLGANTGP--FTWSKC 189

                         250
                  ....*....|....*.
gi 1843978386 234 SKQSIYKTIESKAQEC 249
Cdd:cd04273   190 SRRYLTSFLDTGDGNC 205
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 7-253 9.08e-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: 9.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   7 LLVVADHRFYRYMGRGEEsTTTNYLIELIDRVDDIYrntswdnagfKGYGIQI-----------EQIRILKSPQEVKpge 75
Cdd:pfam01421   5 LFIVVDKQLFQKMGSDTT-VVRQRVFQVVNLVNSIY----------KELNIRVvlvgleiwtdeDKIDVSGDANDTL--- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  76 khYNMAKsypneekdaWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPV-- 153
Cdd:pfam01421  71 --RNFLK---------WRQEYLKKRKPHDVA---------QLLSGVEFGGTTVGAAYVG--------GMCSLEYSGGVne 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 154 -GKKNIYLNSGLTStknygktiltkeadlvttHELGHNFGAEHDPDGLA-ECAPnedqGGKYVMYPIAVsgdHENNKMFS 231
Cdd:pfam01421 123 dHSKNLESFAVTMA------------------HELGHNLGMQHDDFNGGcKCPP----GGGCIMNPSAG---SSFPRKFS 177

                         250       260
                  ....*....|....*....|..
gi 1843978386 232 NCSKQSIYKTIESKAQECFQER 253
Cdd:pfam01421 178 NCSQEDFEQFLTKQKGACLFNK 199
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 83-196 7.08e-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: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  83 SYPNEEKDA-WDVKMLLEqfSFDIAEEASKVCLAHLFTYQDFDmGTLGLAYVGspranshgGVCPKAYyspvgKKNIyln 161
Cdd:pfam13582  34 DTPYTSSDAlEILDELQE--VNDTRIGQYGYDLGHLFTGRDGG-GGGGIAYVG--------GVCNSGS-----KFGV--- 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1843978386 162 sgltstkNYGKTILTKEADLVTTHELGHNFGAEHD 196
Cdd:pfam13582  95 -------NSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 6-251 1.56e-06

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 49.27  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386   6 KLLVVADHRFYRYMGRGEEstTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEqirilKSPQEvKPGEKHYNMA---- 81
Cdd:cd04272     4 ELFVVVDYDHQSEFFSNEQ--LIRYLAVMVNAANLRYRDLKSPRIRLLLVGITIS-----KDPDF-EPYIHPINYGyida 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386  82 -------KSYPNEEKDawdvkmlleQFSFDIAEEASKVCLAHlFTYQDFDMGTLGLAYVGspranshgGVCPKaYYSPVG 154
Cdd:cd04272    76 aetlenfNEYVKKKRD---------YFNPDVVFLVTGLDMST-YSGGSLQTGTGGYAYVG--------GACTE-NRVAMG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 155 KKNIYLNSGLtstknygktiltkeadLVTTHELGHNFGAEHdpDGLAECAPNEDQGGK--------YVMypiaVSGDHEN 226
Cdd:cd04272   137 EDTPGSYYGV----------------YTMTHELAHLLGAPH--DGSPPPSWVKGHPGSldcpwddgYIM----SYVVNGE 194

                         250       260
                  ....*....|....*....|....*.
gi 1843978386 227 NKM-FSNCSKQSIYKTIESKAQECFQ 251
Cdd:cd04272   195 RQYrFSQCSQRQIRNVFRRLGASCLH 220
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 181-245 3.16e-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: 48.57  E-value: 3.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1843978386 181 LVTTHELGHNFGAEHD---------PDGLAECAPNE----DQGGKYVMYPIAVSGDHEnnkmFSNCSKQSIYKTIESK 245
Cdd:cd04271   147 QVFAHEIGHTFGAVHDctsgtcsdgSVGSQQCCPLStstcDANGQYIMNPSSSSGITE----FSPCTIGNICSLLGRN 220
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 114-248 1.09e-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: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 114 LAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPVGkkniylNSGLTSTKNYGktiltkeadlVTTHELGHNFGA 193
Cdd:pfam13583  94 LAYLTLMTGPSGQNVGVAWVG--------ALCSSARQNAKA------SGVARSRDEWD----------IFAHEIGHTFGA 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1843978386 194 EHDPDGLAECAPN--EDQGGKYVMYPIA-VSGDHennkmFSNCSKQSIYKTIESKAQE 248
Cdd:pfam13583 150 VHDCSSQGEGLSSstEDGSGQTIMSYAStASQTA-----FSPCTIRNINGNPCSQANY 202
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 258-294 4.14e-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: 35.43  E-value: 4.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1843978386 258 CGNSRVDEGEECDPGimYLNNDTCCNSDCTLKEGVQC 294
Cdd:TIGR02232   4 CGDGIIEPGEECDDG--NTTSGDGCSATCRLEEGFAC 38
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 118-225 6.70e-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: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843978386 118 FTYQDFDMGTLGLAYVGSpRANSHGGvcpkayyspvgkkNIYLNSGLTSTKNYGktILTKEADLVTTHELGHNFGAEHDP 197
Cdd:cd04268    49 SVIRWIPYNDGTWSYGPS-QVDPLTG-------------EILLARVYLYSSFVE--YSGARLRNTAEHELGHALGLRHNF 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1843978386 198 DGLAECAPNEDQGGKY----VMYPIAVSGDHE 225
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