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Conserved domains on  [gi|73747889|ref|NP_003174|]
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disintegrin and metalloproteinase domain-containing protein 17 preproprotein [Homo sapiens]

Protein Classification

ZnMc_TACE_like and ADAM17_MPD domain-containing protein (domain architecture ID 10922949)

protein containing domains Pep_M12B_propep, ZnMc_TACE_like, DISIN, and ADAM17_MPD

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 ...
223-477 5.53e-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  Cd Length: 244  Bit Score: 446.05  E-value: 5.53e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 223 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 302
Cdd:cd04270   1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 303 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 382
Cdd:cd04270  79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270 151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229
                       250
                ....*....|....*
gi 73747889 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 ...
581-641 7.86e-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 dimerisation and substrate recognition, where it catalyzes an isomerisation of disulfide bridges within the thioredoxin motif CXXC. this isomerisation 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: 318829  Cd Length: 61  Bit Score: 117.42  E-value: 7.86e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73747889   581 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKC 641
Cdd:pfam16698   1 FCETKQNLQSCACNETEDSCKRCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKC 61
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
484-560 7.50e-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: 98.15  E-value: 7.50e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73747889    484 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 560
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 ...
56-152 8.83e-06

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: 307618  Cd Length: 125  Bit Score: 46.01  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889    56 RKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVV--VDGKNESEYTVKWQD-FFTGHVVGEPDSRV----- 127
Cdd:pfam01562  14 RRRSLSSEYPDRLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETyrEDGTEVTDQPPIQDHcHYQGHVEGEPDSSAalstc 93
                          90       100
                  ....*....|....*....|....*..
gi 73747889   128 --LAHIrdddviirINTDGAEYNIEPL 152
Cdd:pfam01562  94 sgLRGV--------IRTGDEEYFIEPL 112
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
223-477 5.53e-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  Cd Length: 244  Bit Score: 446.05  E-value: 5.53e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 223 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 302
Cdd:cd04270   1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 303 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 382
Cdd:cd04270  79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270 151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229
                       250
                ....*....|....*
gi 73747889 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 ...
581-641 7.86e-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 dimerisation and substrate recognition, where it catalyzes an isomerisation of disulfide bridges within the thioredoxin motif CXXC. this isomerisation 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: 318829  Cd Length: 61  Bit Score: 117.42  E-value: 7.86e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73747889   581 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKC 641
Cdd:pfam16698   1 FCETKQNLQSCACNETEDSCKRCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKC 61
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
246-458 9.59e-30

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


Pssm-ID: 316130  Cd Length: 192  Bit Score: 118.49  E-value: 9.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   246 TTTNYLIELIDRVDDIYRNtswDNagFKGYGIQIEQIRILKSPqevkpgekhyNMAKSYPNEEKDAWDVKMLLEqfsFDI 325
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATT----------SASDSGNNCNSPTTIVRRLNF---LSQ 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   326 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPvgkkniYLNSGLTSTKNYGKTILTKEADLVTTH 405
Cdd:pfam13574  64 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSANYPTQEWDVVAH 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747889   406 ELGHNFGAEHDPD-------GLAECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 458
Cdd:pfam13574 130 EVGHNFGATHDCDgsqyassGCERNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 187
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
580-642 7.03e-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: 100.53  E-value: 7.03e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747889 580 PFCEReQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 642
Cdd:cd14246   1 PFCER-ENLQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
484-560 7.50e-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: 98.15  E-value: 7.50e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73747889    484 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 560
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
484-558 5.40e-23

Disintegrin;


Pssm-ID: 306668  Cd Length: 73  Bit Score: 95.34  E-value: 5.40e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73747889   484 DEGEECDPG-IMYLNNDTCCNSDCTLKEGVQCSDrnSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 558
Cdd:pfam00200   1 EEGEECDCGgRKECALDPCCDATCKLKNGAHCSD--GPCCNNCQFKPAGTVCREAVN-ECDLPEYCDGDSAQCPPD 73
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
56-152 8.83e-06

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: 307618  Cd Length: 125  Bit Score: 46.01  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889    56 RKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVV--VDGKNESEYTVKWQD-FFTGHVVGEPDSRV----- 127
Cdd:pfam01562  14 RRRSLSSEYPDRLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETyrEDGTEVTDQPPIQDHcHYQGHVEGEPDSSAalstc 93
                          90       100
                  ....*....|....*....|....*..
gi 73747889   128 --LAHIrdddviirINTDGAEYNIEPL 152
Cdd:pfam01562  94 sgLRGV--------IRTGDEEYFIEPL 112
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
478-514 3.93e-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  Cd Length: 38  Bit Score: 37.35  E-value: 3.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 73747889   478 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKEGVQC 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 5.53e-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  Cd Length: 244  Bit Score: 446.05  E-value: 5.53e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 223 NTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNmaK 302
Cdd:cd04270   1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDWDGGGFKGIGFQIKRIRIHTTPDEVDPGNKFYN--K 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 303 SYPNEEKDAWDVKMLLEQFSFDiaeeaskVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKnIYLNS 382
Cdd:cd04270  79 SFPNWGVEKFLVKLLLEQFSDD-------VCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKK-KYLNT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 383 GLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGlAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTI 462
Cdd:cd04270 151 GLTTTVNYGKRVPTKESDLVTAHELGHNFGSPHDPDI-AECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVL 229
                       250
                ....*....|....*
gi 73747889 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 5.80e-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: 200.34  E-value: 5.80e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 223 NTCKLLVVADHRFYRYMgRGEESTTTNYLIELIDRVDDIYRNTSwdnaGFKGYGIQIEQIRILKSPQEVKPGEkhynmak 302
Cdd:cd04267   1 REIELVVVADHRMVSYF-NSDENILQAYITELINIANSIYRSTN----LRLGIRISLEGLQILKGEQFAPPID------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 303 sypneekdaWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDF-DMGTLGLAYVGSPranshggvcpkayyspvgkKNIYLN 381
Cdd:cd04267  69 ---------SDASNTLNSFSFWRAEGPIRHDNAVLLTAQDFiEGDILGLAYVGSM-------------------CNPYSS 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 382 SGLTSTKNYgktilTKEADLVTTHELGHNFGAEHDPDGlaECAPNEDQGGKYVMYPIAVSgdhENNKMFSNCSKQSIYKT 461
Cdd:cd04267 121 VGVVEDTGF-----TLLTALTMAHELGHNLGAEHDGGD--ELAFECDGGGNYIMAPVDSG---LNSYRFSQCSIGSIREF 190

                ..
gi 73747889 462 IE 463
Cdd:cd04267 191 LD 192
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
581-641 7.86e-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 dimerisation and substrate recognition, where it catalyzes an isomerisation of disulfide bridges within the thioredoxin motif CXXC. this isomerisation 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: 318829  Cd Length: 61  Bit Score: 117.42  E-value: 7.86e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73747889   581 FCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKC 641
Cdd:pfam16698   1 FCETKQNLQSCACNETEDSCKRCCRDLNGTCSPYLDANGSFLYLRDGKPCTVGFCDGKGKC 61
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
246-458 9.59e-30

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


Pssm-ID: 316130  Cd Length: 192  Bit Score: 118.49  E-value: 9.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   246 TTTNYLIELIDRVDDIYRNtswDNagFKGYGIQIEQIRILKSPqevkpgekhyNMAKSYPNEEKDAWDVKMLLEqfsFDI 325
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEP---DD--ININGGLVNPGEIPATT----------SASDSGNNCNSPTTIVRRLNF---LSQ 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   326 AEEASKVCLAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPvgkkniYLNSGLTSTKNYGKTILTKEADLVTTH 405
Cdd:pfam13574  64 WRGEQDYCLAHLVTMGTFSGGELGLAYVG--------QICQKGASSP------KTNTGLSTTTNYGSANYPTQEWDVVAH 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747889   406 ELGHNFGAEHDPD-------GLAECAPN--EDQGGKYVMYPIAVSgdheNNKMFSNCSKQSI 458
Cdd:pfam13574 130 EVGHNFGATHDCDgsqyassGCERNAATsvCSANGSFIMNPASKS----NNDLFSPCSISLI 187
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
223-462 1.39e-27

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  Cd Length: 167  Bit Score: 111.46  E-value: 1.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 223 NTCKLLVVADHRFYrymgrgEESTTTNYLIELIDRVDDIYRNtswdnagfkgygiqIEQIRILKSPQEVKpgekhynmak 302
Cdd:cd00203   1 KVIPYVVVADDRDV------EEENLSAQIQSLILIAMQIWRD--------------YLNIRFVLVGVEID---------- 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 303 sypneekdawdvkmlleqfsfdiaeeasKVCLAHLFTYQDFDMGTLGLAYVGSPRaNSHGGVcpkayyspvgkkniylns 382
Cdd:cd00203  51 ----------------------------KADIAILVTRQDFDGGTGGWAYLGRVC-DSLRGV------------------ 83
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 383 GLTSTKNYGktilTKEADLVTTHELGHNFGAEHDPDGLAEC--------APNEDQGGKYVMYPIAVSGDHENNKMFSNCS 454
Cdd:cd00203  84 GVLQDNQSG----TKEGAQTIAHELGHALGFYHDHDRKDRDdyptiddtLNAEDDDYYSVMSYTKGSFSDGQRKDFSQCD 159

                ....*...
gi 73747889 455 KQSIYKTI 462
Cdd:cd00203 160 IDQINKLY 167
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
580-642 7.03e-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: 100.53  E-value: 7.03e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747889 580 PFCEReQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKnLFLRKGKPCTVGFCDMnGKCE 642
Cdd:cd14246   1 PFCER-ENLQSCACNEVENSCKRCCRDSNGTCSPYVDAGPF-LYLRDGKPCTVGFCDS-GKCE 60
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
223-451 2.90e-24

Metallo-peptidase family M12;


Pssm-ID: 316230  Cd Length: 188  Bit Score: 102.47  E-value: 2.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   223 NTCKLLVVADHRFYRYMGrGEEstTTNYLIELIDRVDDIYRNTSwdnagfkgyGIQIEQIRILKSPQEvkpgekhynmaK 302
Cdd:pfam13688   3 RTVALLVAADCSYVAAFG-GDA--AQANIINMVNTASNVYERNF---------NISLGLVNLTITDYT-----------D 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   303 SYPNEEKDAWDVKMLLEQFSFDIAEE-ASKVCLAHLFTYQDFDMGtlGLAYVGSPRANSHGGVCpkayyspvgkkniyln 381
Cdd:pfam13688  60 PYTSSPTSSGNASDLLNRFQSFSAWRgTQNDDLAHLFLDTNCSGG--GLAWLGQLCNSGSAGSV---------------- 121
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73747889   382 sgltsTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAE---CAPN---EDQGGKYVMYPIAVSgdheNNKMFS 451
Cdd:pfam13688 122 -----STSVNVVVGTATEWQVFAHEIGHNFGAVHDCDSSTTsqcCPPSsstCPAGGRYIMNYASSP----NSTYFS 188
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
484-560 7.50e-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: 98.15  E-value: 7.50e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73747889    484 DEGEECDPGIMYLNNDTCCNS-DCTLKEGVQCSdrNSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPPGN 560
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPaTCKLKPGAQCA--SGPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
484-558 5.40e-23

Disintegrin;


Pssm-ID: 306668  Cd Length: 73  Bit Score: 95.34  E-value: 5.40e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73747889   484 DEGEECDPG-IMYLNNDTCCNSDCTLKEGVQCSDrnSPCCKNCQFETAQKKCQEAINaTCKGVSYCTGNSSECPPP 558
Cdd:pfam00200   1 EEGEECDCGgRKECALDPCCDATCKLKNGAHCSD--GPCCNNCQFKPAGTVCREAVN-ECDLPEYCDGDSAQCPPD 73
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
226-469 3.70e-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  Cd Length: 194  Bit Score: 87.67  E-value: 3.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 226 KLLVVADHRFYRYMGRgEESTTTNYLIELIDRVDDIYRN----------TSWDNAgfkgygiqiEQIRILKSPQEVkpge 295
Cdd:cd04269   4 ELVVVVDNSLYKKYGS-NLSKVRQRVIEIVNIVDSIYRPlnirvvlvglEIWTDK---------DKISVSGDAGET---- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 296 khynmAKSYPNeekdaWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVgspranshGGVCPKAYyspvgk 375
Cdd:cd04269  70 -----LNRFLD-----WKRSNLLPRKPHDNA---------QLLTGRDFDGNTVGLAYV--------GGMCSPKY------ 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 376 kniylnSGLTSTknYGKTILTKEADLVtTHELGHNFGAEHDPDGlaeCapnEDQGGKYVMYPIAVSGdhenNKMFSNCSK 455
Cdd:cd04269 117 ------SGGVVQ--DHSRNLLLFAVTM-AHELGHNLGMEHDDGG---C---TCGRSTCIMAPSPSSL----TDAFSNCSY 177
                       250
                ....*....|....
gi 73747889 456 QSIYKTIESKAQEC 469
Cdd:cd04269 178 EDYQKFLSRGGGQC 191
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
226-473 2.45e-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 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 307535  Cd Length: 199  Bit Score: 70.38  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   226 KLLVVADHRFYRYMGRGEEsTTTNYLIELIDRVDDIYR--NTS--------WDNAgfkgygiqiEQIRILKSPQEVKpge 295
Cdd:pfam01421   4 ELFIVVDKQLFQKMGSDVN-VVRQRVFQVVNLVNSIYKelNIRvvlvgleiWTDE---------DKIDVSGDANDTL--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   296 khynmaksypnEEKDAWDVKMLLEQFSFDIAeeaskvclaHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPV-- 373
Cdd:pfam01421  71 -----------RNFLKWRQEYLKKRKPHDVA---------QLLSGRTFGGTTVGAAYPG--------GMCSPSYSGGVnl 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   374 -GKKNIYLNSGLTStknygktiltkeadlvttHELGHNFGAEHDPDGLAECAPnedqGGKYVMYPIAVsgdHENNKMFSN 452
Cdd:pfam01421 123 dHKINVEGFAVTMA------------------HELGHNLGMTHDDITGCKCPP----GGGCIMNPSAG---SSFGRKFSN 177
                         250       260
                  ....*....|....*....|.
gi 73747889   453 CSKQSIYKTIESKAQECFQER 473
Cdd:pfam01421 178 CSQDDFEQFLLKQKGACLFNK 198
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
227-469 2.67e-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: 70.35  E-value: 2.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 227 LLVVADHRFYRYMGRgeeSTTTNYLIELIDRVDDIYRNTSWDNAgfkgygIQIEQIRILKSPQEVKPGEKHYNMAKS--- 303
Cdd:cd04273   5 TLVVADSKMVEFHHG---EDLEHYILTLMNIVASLYKDPSLGNS------INIVVVRLIVLEDEESGLLISGNAQKSlks 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 304 --------YPNEEKDA--WDVKMLLEQFSFDIaeeASKVClahlftyqdfdmGTLGLAYVgspranshGGVCpkayySPV 373
Cdd:cd04273  76 fcrwqkklNPPNDSDPehHDHAILLTRQDICR---SNGNC------------DTLGLAPV--------GGMC-----SPS 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 374 GKKNIYLNSGLTSTknygktiltkeadLVTTHELGHNFGAEHDPDGlAECAPNEDQGgkYVMYPIAVSGDHEnnKMFSNC 453
Cdd:cd04273 128 RSCSINEDTGLSSA-------------FTIAHELGHVLGMPHDGDG-NSCGPEGKDG--HIMSPTLGANTGP--FTWSKC 189
                       250
                ....*....|....*.
gi 73747889 454 SKQSIYKTIESKAQEC 469
Cdd:cd04273 190 SRRYLTSFLDTGDGNC 205
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
250-416 1.32e-09

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


Pssm-ID: 316138  Cd Length: 122  Bit Score: 57.74  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   250 YLIELIDRVDDIYRNTSwdnagfkgyGIQIEQIRIlkspqevkpgeKHYNMAKSYPNEEKDAWDVKMLLEqfSFDIAEEA 329
Cdd:pfam13582   2 AIAALVNRANQIYERDS---------GIRLQLVAI-----------IYTDPASDDYTTSDALEILDELQQ--VIDTRYRQ 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   330 SKVCLAHLFTYQDFDmGTLGLAYVGSpranshggVCPKAYyspvgKKNIYLNSGlTSTKNYGKTiltkeadlvTTHELGH 409
Cdd:pfam13582  60 YGYDLGHLFTGRDVG-GGGGLAYVGS--------VCNSGS-----KAGVNGGSS-PYGDCGVDT---------FAHEIGH 115

                  ....*..
gi 73747889   410 NFGAEHD 416
Cdd:pfam13582 116 NFGANHT 122
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
401-465 1.18e-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  Cd Length: 228  Bit Score: 50.11  E-value: 1.18e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73747889 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 1.45e-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: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 226 KLLVVADHRFYRYMGRGEEstTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEqirilKSPQEvKPGEKHYNMA---- 301
Cdd:cd04272   4 ELFVVVDYDHQSEFFSNEQ--LIRYLAVMVNAANLRYRDLKSPRIRLLLVGITIS-----KDPDF-EPYIHPINYGyida 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 302 -------KSYPNEEKDawdvkmlleQFSFDIAEEASKVCLAHlFTYQDFDMGTLGLAYVGspranshgGVCPKaYYSPVG 374
Cdd:cd04272  76 aetlenfNEYVKKKRD---------YFNPDVVFLVTGLDMST-YSGGSLQTGTGGYAYVG--------GACTE-NRVAMG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 375 KKNIYLNSGLtstknygktiltkeadLVTTHELGHNFGAEHdpDGLAECAPNEDQGGK--------YVMypiaVSGDHEN 446
Cdd:cd04272 137 EDTPGSYYGV----------------YTMTHELAHLLGAPH--DGSPPPSWVKGHPGSldcpwddgYIM----SYVVNGE 194
                       250       260
                ....*....|....*....|....*.
gi 73747889 447 NKM-FSNCSKQSIYKTIESKAQECFQ 471
Cdd:cd04272 195 RQYrFSQCSQRQIRNVFRRLGASCLH 220
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
56-152 8.83e-06

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: 307618  Cd Length: 125  Bit Score: 46.01  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889    56 RKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVV--VDGKNESEYTVKWQD-FFTGHVVGEPDSRV----- 127
Cdd:pfam01562  14 RRRSLSSEYPDRLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETyrEDGTEVTDQPPIQDHcHYQGHVEGEPDSSAalstc 93
                          90       100
                  ....*....|....*....|....*..
gi 73747889   128 --LAHIrdddviirINTDGAEYNIEPL 152
Cdd:pfam01562  94 sgLRGV--------IRTGDEEYFIEPL 112
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
334-468 4.55e-04

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


Pssm-ID: 316139  Cd Length: 203  Bit Score: 42.22  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889   334 LAHLFTYQDFDMGTLGLAYVGspranshgGVCPKAYYSPVGkkniylNSGLTSTKNYGktiltkeadlVTTHELGHNFGA 413
Cdd:pfam13583  94 LAYLTLMTRPSQNEVGVAWVG--------ALCSSAYQNAKA------NGVARSRDEWD----------IFAHEIGHTFGA 149
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 73747889   414 EHDPDGLAECAPN--EDQGGKYVMYPIA-VSGDHennkmFSNCSKQSIYKTIESKAQE 468
Cdd:pfam13583 150 VHDCSSQGEGLSSstEDGSGQTIMSYAStASQTA-----FSPCTIRNINGNPCSQANY 202
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
478-514 3.93e-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  Cd Length: 38  Bit Score: 37.35  E-value: 3.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 73747889   478 CGNSRVDEGEECDPGIMYlNNDTcCNSDCTLKEGVQC 514
Cdd:TIGR02232   4 CGDGIIEPGEECDDGNTT-SGDG-CSATCRLEEGFAC 38
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
338-445 8.54e-03

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


Pssm-ID: 239796  Cd Length: 165  Bit Score: 37.86  E-value: 8.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747889 338 FTYQDFDMGTLGLAYVGSpRANSHGGvcpkayyspvgkkNIYLNSGLTSTKNYGktILTKEADLVTTHELGHNFGAEHDP 417
Cdd:cd04268  49 SVIRWIPYNDGTWSYGPS-QVDPLTG-------------EILLARVYLYSSFVE--YSGARLRNTAEHELGHALGLRHNF 112
                        90       100       110
                ....*....|....*....|....*....|..
gi 73747889 418 DGLAECAPNEDQGGKY----VMYPIAVSGDHE 445
Cdd:cd04268 113 AASDRDDNVDLLAEKGdtssVMDYAPSNFSIQ 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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