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Conserved domains on  [gi|942313007|gb|JAN38436|]
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Disintegrin and metalloproteinase domain-containing protein [Daphnia magna]

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 11305529)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family| M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 241-492 1.10e-121

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: 364.39  E-value: 1.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 241 TRCPLLLVADYRFFREMGGGSTKTTINYLISLVDRVHALYAATIWrdgnenesDSPVLSGLGFVIKKIVVHTEATRVRES 320
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDW--------DGGGFKGIGFQIKRIRIHTTPDEVDPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 321 ELHYNMEKPTWDVRTLLEVFSREYSHKDYCLAHLFTDIKFEGGILGLAYVGSPRRNSVGGICTPEYFKS-GYTLYLNSGL 399
Cdd:cd04270   73 NKFYNKSFPNWGVEKFLVKLLLEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSnGKKKYLNTGL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 400 SSSRNhYGQRVVTREADLVTAHELGHNWGSEHDPDLPECSPPASQGGSYLMYTYSVSGYDVNNKKFSPCSLRSIRAVLLA 479
Cdd:cd04270  153 TTTVN-YGKRVPTKESDLVTAHELGHNFGSPHDPDIAECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEV 231

                        250
                 ....*....|...
gi 942313007 480 KAGRCFTEPEESF 492
Cdd:cd04270  232 KSNSCFVERSQSF 244
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 598-655 2.03e-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: 99.37  E-value: 2.03e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942313007 598 PFCETQNYQSCMCDTVADACKRCCRYHlNDTCFPFE---PYDILPDGTPCVHGFCNSGICE 655
Cdd:cd14246    1 PFCERENLQSCACNEVENSCKRCCRDS-NGTCSPYVdagPFLYLRDGKPCTVGFCDSGKCE 60
Disintegrin pfam00200
Disintegrin;
499-575 9.54e-20

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 83.83  E-value: 9.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942313007  499 EGKEECDAGLLGSEDNDSCCD-KFCNLRrnQGAVCSdkNSPCCKNCMLMPAGQKCREAQRaTCEQEAKCTGTSSECPA 575
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLK--PGAQCS--SGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPP 73
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 37-158 1.93e-09

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: 56.17  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007   37 QLGHSVVKRGIKESSHPYNSIkELSFSALGKDFRLILHPSKGILHHNF--QSYAVDGDGVEKPILGGETGFYQGRVFGET 114
Cdd:pfam01562   7 RLDPSRRRRSLASESTYLDTL-SYRLAAFGKKFHLHLTPNRLLLAPGFtvTYYLDGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 942313007  115 RSHVNAHIENGlLTASIVTKEDSFHVEPSWRHLPEPNQESMIVY 158
Cdd:pfam01562  86 DSSVALSTCSG-LRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 241-492 1.10e-121

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: 364.39  E-value: 1.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 241 TRCPLLLVADYRFFREMGGGSTKTTINYLISLVDRVHALYAATIWrdgnenesDSPVLSGLGFVIKKIVVHTEATRVRES 320
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDW--------DGGGFKGIGFQIKRIRIHTTPDEVDPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 321 ELHYNMEKPTWDVRTLLEVFSREYSHKDYCLAHLFTDIKFEGGILGLAYVGSPRRNSVGGICTPEYFKS-GYTLYLNSGL 399
Cdd:cd04270   73 NKFYNKSFPNWGVEKFLVKLLLEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSnGKKKYLNTGL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 400 SSSRNhYGQRVVTREADLVTAHELGHNWGSEHDPDLPECSPPASQGGSYLMYTYSVSGYDVNNKKFSPCSLRSIRAVLLA 479
Cdd:cd04270  153 TTTVN-YGKRVPTKESDLVTAHELGHNFGSPHDPDIAECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEV 231

                        250
                 ....*....|...
gi 942313007 480 KAGRCFTEPEESF 492
Cdd:cd04270  232 KSNSCFVERSQSF 244
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 264-477 9.41e-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: 119.66  E-value: 9.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  264 TTINYLISLVDRVHALYaatiwrdgnenESDSpVLSGLGFV-IKKIVVHTEAtrvreSELHYNMEK-PTWDVRTLLeVFS 341
Cdd:pfam13574   2 NVTENLVNVVNRVNQIY-----------EPDD-ININGGLVnPGEIPATTSA-----SDSGNNYCNsPTTIVRRLN-FLS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  342 REYSHKDYCLAHLFTDIKFEGGILGLAYvgsprrnsVGGICTPEYfksgYTLYLNSGLSSSRNhYGQRVVTREADLVTAH 421
Cdd:pfam13574  64 QWRGEQDYCLAHLVTMGTFSGGELGLAY--------VGQICQKGA----SSPKTNTGLSTTTN-YGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942313007  422 ELGHNWGSEHDPD--------LPECSPPA--SQGGSYLMYTYSVSgydvNNKKFSPCSLRSIRAVL 477
Cdd:pfam13574 131 EVGHNFGATHDCDgsqyassgCERNAATSvcSANGSFIMNPASKS----NNDLFSPCSISLICDVL 192
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 598-655 2.03e-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: 99.37  E-value: 2.03e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942313007 598 PFCETQNYQSCMCDTVADACKRCCRYHlNDTCFPFE---PYDILPDGTPCVHGFCNSGICE 655
Cdd:cd14246    1 PFCERENLQSCACNEVENSCKRCCRDS-NGTCSPYVdagPFLYLRDGKPCTVGFCDSGKCE 60
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 599-655 3.64e-21

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: 87.40  E-value: 3.64e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942313007  599 FCETQ-NYQSCMCDTVADACKRCCRyHLNDTCFPFEPY----DILPDGTPCVHGFCN-SGICE 655
Cdd:pfam16698   1 FCETKsGLQSCACNETDDSCKVCCR-DLNGTCSPYLDAngsfLYLRDGKPCTVGFCDgKGKCE 62
Disintegrin pfam00200
Disintegrin;
499-575 9.54e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 83.83  E-value: 9.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942313007  499 EGKEECDAGLLGSEDNDSCCD-KFCNLRrnQGAVCSdkNSPCCKNCMLMPAGQKCREAQRaTCEQEAKCTGTSSECPA 575
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLK--PGAQCS--SGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPP 73
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 499-575 2.29e-14

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: 68.49  E-value: 2.29e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942313007   499 EGKEECDAGLLGsEDNDSCCD-KFCNLRRnqGAVCSDknSPCCKNCMLMPAGQKCREAQRaTCEQEAKCTGTSSECPA 575
Cdd:smart00050   1 EEGEECDCGSPK-ECTDPCCDpATCKLKP--GAQCAS--GPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPP 72
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 37-158 1.93e-09

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: 56.17  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007   37 QLGHSVVKRGIKESSHPYNSIkELSFSALGKDFRLILHPSKGILHHNF--QSYAVDGDGVEKPILGGETGFYQGRVFGET 114
Cdd:pfam01562   7 RLDPSRRRRSLASESTYLDTL-SYRLAAFGKKFHLHLTPNRLLLAPGFtvTYYLDGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 942313007  115 RSHVNAHIENGlLTASIVTKEDSFHVEPSWRHLPEPNQESMIVY 158
Cdd:pfam01562  86 DSSVALSTCSG-LRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
364-469 3.73e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.17  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 364 ILGLAYvgspRRNSVGGICTPEYFKSGYtlylnsGLSSSRNHYGQRVVTrEAdlvtAHELGHNWGSEHDPDlPECsppas 443
Cdd:COG1913   87 VFGLAY----LGGRVAVVSTARLRPEFY------GLPPDEELFLERVLK-EA----VHELGHLFGLGHCPN-PRC----- 145

                         90       100
                 ....*....|....*....|....*.
gi 942313007 444 qggsyLMYtYSVSGYDVNNKKFSPCS 469
Cdd:COG1913  146 -----VMH-FSNSLEELDRKPPSFCP 165
 
Name Accession Description Interval E-value
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 241-492 1.10e-121

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: 364.39  E-value: 1.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 241 TRCPLLLVADYRFFREMGGGSTKTTINYLISLVDRVHALYAATIWrdgnenesDSPVLSGLGFVIKKIVVHTEATRVRES 320
Cdd:cd04270    1 NTCKLLLVADHRFYKYMGRGEEETTINYLISHIDRVDDIYRNTDW--------DGGGFKGIGFQIKRIRIHTTPDEVDPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 321 ELHYNMEKPTWDVRTLLEVFSREYSHKDYCLAHLFTDIKFEGGILGLAYVGSPRRNSVGGICTPEYFKS-GYTLYLNSGL 399
Cdd:cd04270   73 NKFYNKSFPNWGVEKFLVKLLLEQFSDDVCLAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSnGKKKYLNTGL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 400 SSSRNhYGQRVVTREADLVTAHELGHNWGSEHDPDLPECSPPASQGGSYLMYTYSVSGYDVNNKKFSPCSLRSIRAVLLA 479
Cdd:cd04270  153 TTTVN-YGKRVPTKESDLVTAHELGHNFGSPHDPDIAECAPGESQGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEV 231

                        250
                 ....*....|...
gi 942313007 480 KAGRCFTEPEESF 492
Cdd:cd04270  232 KSNSCFVERSQSF 244
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 264-477 9.41e-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: 119.66  E-value: 9.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  264 TTINYLISLVDRVHALYaatiwrdgnenESDSpVLSGLGFV-IKKIVVHTEAtrvreSELHYNMEK-PTWDVRTLLeVFS 341
Cdd:pfam13574   2 NVTENLVNVVNRVNQIY-----------EPDD-ININGGLVnPGEIPATTSA-----SDSGNNYCNsPTTIVRRLN-FLS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  342 REYSHKDYCLAHLFTDIKFEGGILGLAYvgsprrnsVGGICTPEYfksgYTLYLNSGLSSSRNhYGQRVVTREADLVTAH 421
Cdd:pfam13574  64 QWRGEQDYCLAHLVTMGTFSGGELGLAY--------VGQICQKGA----SSPKTNTGLSTTTN-YGSFNYPTQEWDVVAH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942313007  422 ELGHNWGSEHDPD--------LPECSPPA--SQGGSYLMYTYSVSgydvNNKKFSPCSLRSIRAVL 477
Cdd:pfam13574 131 EVGHNFGATHDCDgsqyassgCERNAATSvcSANGSFIMNPASKS----NNDLFSPCSISLICDVL 192
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
241-466 6.33e-29

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 114.05  E-value: 6.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  241 TRCPLLLVADYRFFREMGGGSTKTTInylISLVDRVHALYaatiwrdgnenESDSpvlsGLGFVIKKIVVHTEATRVres 320
Cdd:pfam13688   3 RTVALLVAADCSYVAAFGGDAAQANI---INMVNTASNVY-----------ERDF----NISLGLVNLTISDSTCPY--- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  321 elhYNMEKPTWDVRTLLEVFSREYS--HKD-YCLAHLFTDIKFEGGilGLAYVGSPRRNSVGGICtpeyfksgytlylns 397
Cdd:pfam13688  62 ---TPPACSTGDSSDRLSEFQDFSAwrGTQnDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSV--------------- 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942313007  398 glSSSRNHYGQRVVTREADLVTAHELGHNWGSEHDPDL----PECSPPAS---QGGSYLMYTYSVSgydvNNKKFS 466
Cdd:pfam13688 122 --STRVSGNNVVVSTATEWQVFAHEIGHNFGAVHDCDSstssQCCPPSNStcpAGGRYIMNPSSSP----NSTDFS 191
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 243-477 1.36e-26

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: 107.51  E-value: 1.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 243 CPLLLVADYRFFREMGGgSTKTTINYLISLVDRVHALYaatiwrdgneneSDSPVLSGLGFVIKKIvvhteaTRVRESEL 322
Cdd:cd04267    3 IELVVVADHRMVSYFNS-DENILQAYITELINIANSIY------------RSTNLRLGIRISLEGL------QILKGEQF 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 323 hynMEKPTWDVRTLLEVFS--REYSHKDYCLAHLFTDIKF-EGGILGLAYVGSprrnsvggICTPeyfksgytlYLNSGL 399
Cdd:cd04267   64 ---APPIDSDASNTLNSFSfwRAEGPIRHDNAVLLTAQDFiEGDILGLAYVGS--------MCNP---------YSSVGV 123

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942313007 400 SSSRNHygqrvvTREADLVTAHELGHNWGSEHDPDlPECSPPASQGGSYLMYtYSVSGydVNNKKFSPCSLRSIRAVL 477
Cdd:cd04267  124 VEDTGF------TLLTALTMAHELGHNLGAEHDGG-DELAFECDGGGNYIMA-PVDSG--LNSYRFSQCSIGSIREFL 191
ADAM17_MPD cd14246
Membrane-proximal domain of a disintegrin and metalloprotease 17 (ADAM17); ADAM17 is a ...
 598-655 2.03e-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: 99.37  E-value: 2.03e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942313007 598 PFCETQNYQSCMCDTVADACKRCCRYHlNDTCFPFE---PYDILPDGTPCVHGFCNSGICE 655
Cdd:cd14246    1 PFCERENLQSCACNEVENSCKRCCRDS-NGTCSPYVdagPFLYLRDGKPCTVGFCDSGKCE 60
ADAM17_MPD pfam16698
Membrane-proximal domain, switch, for ADAM17; ADAM17_MPD is the membrane-proximal domain of a ...
 599-655 3.64e-21

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: 87.40  E-value: 3.64e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942313007  599 FCETQ-NYQSCMCDTVADACKRCCRyHLNDTCFPFEPY----DILPDGTPCVHGFCN-SGICE 655
Cdd:pfam16698   1 FCETKsGLQSCACNETDDSCKVCCR-DLNGTCSPYLDAngsfLYLRDGKPCTVGFCDgKGKCE 62
Disintegrin pfam00200
Disintegrin;
499-575 9.54e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 83.83  E-value: 9.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942313007  499 EGKEECDAGLLGSEDNDSCCD-KFCNLRrnQGAVCSdkNSPCCKNCMLMPAGQKCREAQRaTCEQEAKCTGTSSECPA 575
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLK--PGAQCS--SGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPP 73
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 245-484 3.38e-16

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: 77.66  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 245 LLLVADYRFFREMGGGSTKTT------INYLISLVDRVH---ALYAATIWRDGNenesdspvlsglgfvikKIVVHTEAT 315
Cdd:cd04269    5 LVVVVDNSLYKKYGSNLSKVRqrvieiVNIVDSIYRPLNirvVLVGLEIWTDKD-----------------KISVSGDAG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 316 RVreseLHYNMEkptWDVRTLLevfsreySHKDYCLAHLFTDIKFEGGILGLAYvgsprrnsVGGICTPEYfksgytlyl 395
Cdd:cd04269   68 ET----LNRFLD---WKRSNLL-------PRKPHDNAQLLTGRDFDGNTVGLAY--------VGGMCSPKY--------- 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 396 nSGLSSS--RNHYGQRVVTreadlvTAHELGHNWGSEHDPdlPECSppaSQGGSYLMYTYSVSGydvnNKKFSPCSLRSI 473
Cdd:cd04269  117 -SGGVVQdhSRNLLLFAVT------MAHELGHNLGMEHDD--GGCT---CGRSTCIMAPSPSSL----TDAFSNCSYEDY 180

                        250
                 ....*....|.
gi 942313007 474 RAVLLAKAGRC 484
Cdd:cd04269  181 QKFLSRGGGQC 191
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 499-575 2.29e-14

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: 68.49  E-value: 2.29e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942313007   499 EGKEECDAGLLGsEDNDSCCD-KFCNLRRnqGAVCSDknSPCCKNCMLMPAGQKCREAQRaTCEQEAKCTGTSSECPA 575
Cdd:smart00050   1 EEGEECDCGSPK-ECTDPCCDpATCKLKP--GAQCAS--GPCCDNCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPP 72
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 331-477 5.09e-14

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: 70.63  E-value: 5.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 331 WDVRTLLEVFSREYSHKDYCLAHLFTDIKFEGGILGLAYVGSprrnsvggICTPEyfksgytlylNSGLSSSRNHYGqrv 410
Cdd:cd00203   34 WRDYLNIRFVLVGVEIDKADIAILVTRQDFDGGTGGWAYLGR--------VCDSL----------RGVGVLQDNQSG--- 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942313007 411 vTREADLVTAHELGHNWGSEHD---------PDLPECSPPASQGGSYLMYTYSVSGYDVNNKKFSPCSLRSIRAVL 477
Cdd:cd00203   93 -TKEGAQTIAHELGHALGFYHDhdrkdrddyPTIDDTLNAEDDDYYSVMSYTKGSFSDGQRKDFSQCDIDQINKLY 167
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 268-432 6.55e-13

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: 65.85  E-value: 6.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  268 YLISLVDRVHALYaatiwrdgnenESDSpvlsGLGFVIKKIVVHTEATRVreselhYNMEKPTWDVRTLLEVFSREYSHK 347
Cdd:pfam13582   2 RIVSLVNRANTIY-----------ERDL----GIRLQLAAIIITTSADTP------YTSSDALEILDELQEVNDTRIGQY 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  348 DYCLAHLFTDIKFEGGiLGLAYVGsprrnsvgGICTPEYFKSGYtlylnsglsssrnhYGQRVVTREADLVTAHELGHNW 427
Cdd:pfam13582  61 GYDLGHLFTGRDGGGG-GGIAYVG--------GVCNSGSKFGVN--------------SGSGPVGDTGADTFAHEIGHNF 117


                  ....*
gi 942313007  428 GSEHD 432
Cdd:pfam13582 118 GLNHT 122
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 245-484 4.90e-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: 65.78  E-value: 4.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  245 LLLVADYRFFREMGGgSTKTTINYLISLVDRVHALYAA----------TIWRDGNenesdspvlsglgfvikKIVVHTea 314
Cdd:pfam01421   5 LFIVVDKQLFQKMGS-DTTVVRQRVFQVVNLVNSIYKElnirvvlvglEIWTDED-----------------KIDVSG-- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  315 trvreselhynmekptwDVRTLLEVFS---REY--SHKDYCLAHLFTDIKFEGGILGLAYVGsprrnsvgGICTPEYfks 389
Cdd:pfam01421  65 -----------------DANDTLRNFLkwrQEYlkKRKPHDVAQLLSGVEFGGTTVGAAYVG--------GMCSLEY--- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  390 gytlylnsglSSSRNHYGQRVVTREADLVtAHELGHNWGSEHDPDLPECSPPasQGGSYLM--YTYSVSGydvnnKKFSP 467
Cdd:pfam01421 117 ----------SGGVNEDHSKNLESFAVTM-AHELGHNLGMQHDDFNGGCKCP--PGGGCIMnpSAGSSFP-----RKFSN 178

                         250
                  ....*....|....*..
gi 942313007  468 CSLRSIRAVLLAKAGRC 484
Cdd:pfam01421 179 CSQEDFEQFLTKQKGAC 195
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 245-486 1.19e-10

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 61.98  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 245 LLLVADYRFFREmgGGSTKTTINYLISLVDRVHALYAATiwrdgnENESDSPVLSGLgfvikkIVVHTEATrvrESELHY 324
Cdd:cd04272    5 LFVVVDYDHQSE--FFSNEQLIRYLAVMVNAANLRYRDL------KSPRIRLLLVGI------TISKDPDF---EPYIHP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 325 NMEKPTWDVRTLlEVFsREYSHK-----DYCLAHLFTD---IKFEGG-----ILGLAYVGsprrnsvgGICTpEYFksgy 391
Cdd:cd04272   68 INYGYIDAAETL-ENF-NEYVKKkrdyfNPDVVFLVTGldmSTYSGGslqtgTGGYAYVG--------GACT-ENR---- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 392 tlylnSGLSSSRNH--YGQRVVTreadlvtaHELGHNWGSEHDPDlPECSPPASQGGS--------YLMyTYSVSGydVN 461
Cdd:cd04272  133 -----VAMGEDTPGsyYGVYTMT--------HELAHLLGAPHDGS-PPPSWVKGHPGSldcpwddgYIM-SYVVNG--ER 195

                        250       260
                 ....*....|....*....|....*
gi 942313007 462 NKKFSPCSLRSIRAVLLAKAGRCFT 486
Cdd:cd04272  196 QYRFSQCSQRQIRNVFRRLGASCLH 220
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 37-158 1.93e-09

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: 56.17  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007   37 QLGHSVVKRGIKESSHPYNSIkELSFSALGKDFRLILHPSKGILHHNF--QSYAVDGDGVEKPILGGETGFYQGRVFGET 114
Cdd:pfam01562   7 RLDPSRRRRSLASESTYLDTL-SYRLAAFGKKFHLHLTPNRLLLAPGFtvTYYLDGGTGVESPPVQTDHCYYQGHVEGHP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 942313007  115 RSHVNAHIENGlLTASIVTKEDSFHVEPSWRHLPEPNQESMIVY 158
Cdd:pfam01562  86 DSSVALSTCSG-LRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 245-484 6.48e-09

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: 56.48  E-value: 6.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 245 LLLVADYRFFREMGGGSTKTtinYLISLVDRVHALYAatiwrdgnenesDSPVLSGLGFVIKKIVVHTEatrvRESELhy 324
Cdd:cd04273    5 TLVVADSKMVEFHHGEDLEH---YILTLMNIVASLYK------------DPSLGNSINIVVVRLIVLED----EESGL-- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 325 nmeKPTWDVRTLLEVF----SREYSHKDYCLAH-----LFT--DI---KFEGGILGLAYVGsprrnsvgGICTPEYFKSg 390
Cdd:cd04273   64 ---LISGNAQKSLKSFcrwqKKLNPPNDSDPEHhdhaiLLTrqDIcrsNGNCDTLGLAPVG--------GMCSPSRSCS- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 391 ytlyLN--SGLSSSrnhygqrvvtreadLVTAHELGHNWGSEHDPDLPECSPPASQGgsYLMytYSVSGYDVNNKKFSPC 468
Cdd:cd04273  132 ----INedTGLSSA--------------FTIAHELGHVLGMPHDGDGNSCGPEGKDG--HIM--SPTLGANTGPFTWSKC 189

                        250
                 ....*....|....*.
gi 942313007 469 SLRSIRAVLLAKAGRC 484
Cdd:cd04273  190 SRRYLTSFLDTGDGNC 205
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 337-473 2.07e-06

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: 49.15  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007  337 LEVFSREYSHKDYCLAHLFTDIKFEGGILGLAYVG---SPRRNSVGGictpeyfksgytlylnSGLSSSRNHYGqrvvtr 413
Cdd:pfam13583  80 LATLTSWRDSLNYDLAYLTLMTGPSGQNVGVAWVGalcSSARQNAKA----------------SGVARSRDEWD------ 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942313007  414 eadlVTAHELGHNWGSEHdpDLPECSPPASQ-----GGSYLMyTYsvsGYDVNNKKFSPCSLRSI 473
Cdd:pfam13583 138 ----IFAHEIGHTFGAVH--DCSSQGEGLSSstedgSGQTIM-SY---ASTASQTAFSPCTIRNI 192
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 337-473 1.69e-05

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: 46.65  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 337 LEVFSR---EYSHKDYCLAHLFTDIKfEGGILGLAYVGSprrnsvggICtpeyfksgytlylNSGLSSSRN--HYGQRVV 411
Cdd:cd04271   82 LSIFSQwrgQQPDDGNAFWTLMTACP-SGSEVGVAWLGQ--------LC-------------RTGASDQGNetVAGTNVV 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942313007 412 TREAD--LVTAHELGHNWGSEHDPDLPECSPPASQG--------------GSYLMYTYSVSGydvnNKKFSPCSLRSI 473
Cdd:cd04271  140 VRTSNewQVFAHEIGHTFGAVHDCTSGTCSDGSVGSqqccplststcdanGQYIMNPSSSSG----ITEFSPCTIGNI 213
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
364-469 3.73e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.17  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942313007 364 ILGLAYvgspRRNSVGGICTPEYFKSGYtlylnsGLSSSRNHYGQRVVTrEAdlvtAHELGHNWGSEHDPDlPECsppas 443
Cdd:COG1913   87 VFGLAY----LGGRVAVVSTARLRPEFY------GLPPDEELFLERVLK-EA----VHELGHLFGLGHCPN-PRC----- 145

                         90       100
                 ....*....|....*....|....*.
gi 942313007 444 qggsyLMYtYSVSGYDVNNKKFSPCS 469
Cdd:COG1913  146 -----VMH-FSNSLEELDRKPPSFCP 165
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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