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Conserved domains on  [gi|156105679|ref|NP_000438.2|]
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presenilin-2 isoform 1 [Homo sapiens]

Protein Classification

Presenilin domain-containing protein (domain architecture ID 10471201)

Presenilin domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Presenilin pfam01080
Presenilin; Mutations in presenilin-1 are a major cause of early onset Alzheimer's disease. It ...
82-438 0e+00

Presenilin; Mutations in presenilin-1 are a major cause of early onset Alzheimer's disease. It has been found that presenilin-1 binds to beta-catenin in-vivo. This family also contains SPE proteins from C.elegans.


:

Pssm-ID: 307294  Cd Length: 396  Bit Score: 561.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   82 KYGAKHVIMLFVPVTLCMIVVVATIKSVRFYT--EKNGQ-LIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVV 158
Cdd:pfam01080   1 KYGAKQVIKLFVPVSLCMLLVVATIRSVSFYSsqSNDEAsLVYTPFHEESDSTGTKLWNSLLNALIFIGVIVVMTFLLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  159 LYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISAL 238
Cdd:pfam01080  81 LYKYRCYKFIHGWLILSSLLLLFLFSGQYLGELLRAYNIPMDYITFAFILWNFGVVGMIAIFWKGPLLLQQAYLILISAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  239 MALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTV------GMAKLDPSSQ 312
Cdd:pfam01080 161 MALVFIKYLPEWTTWVLLVAISIWDLFAVLCPKGPLRMLVETAQERNEPIFPALIYSATMVWLVagetenAMADEGTDRE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  313 GALQLPYDPEMEEDSYDSFGEPSY--------------------------------PEVFEPPLTGYPGEELEEEEERGV 360
Cdd:pfam01080 241 TVKQEISNYSGAEAGDSSFPQSSRsssdainpdsslteelsserseeesspssssaEEPSEPKELSSSQDTQDEEEERGV 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105679  361 KLGLGDFIFYSVLVGKAAATgsGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFM 438
Cdd:pfam01080 321 KLGLGDFIFYSVLVGKAAMY--GDWNTVIACFVAILIGLCLTLLLLAIFRKALPALPISITFGLIFYFLTRLLVEPFV 396
 
Name Accession Description Interval E-value
Presenilin pfam01080
Presenilin; Mutations in presenilin-1 are a major cause of early onset Alzheimer's disease. It ...
82-438 0e+00

Presenilin; Mutations in presenilin-1 are a major cause of early onset Alzheimer's disease. It has been found that presenilin-1 binds to beta-catenin in-vivo. This family also contains SPE proteins from C.elegans.


Pssm-ID: 307294  Cd Length: 396  Bit Score: 561.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   82 KYGAKHVIMLFVPVTLCMIVVVATIKSVRFYT--EKNGQ-LIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVV 158
Cdd:pfam01080   1 KYGAKQVIKLFVPVSLCMLLVVATIRSVSFYSsqSNDEAsLVYTPFHEESDSTGTKLWNSLLNALIFIGVIVVMTFLLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  159 LYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISAL 238
Cdd:pfam01080  81 LYKYRCYKFIHGWLILSSLLLLFLFSGQYLGELLRAYNIPMDYITFAFILWNFGVVGMIAIFWKGPLLLQQAYLILISAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  239 MALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTV------GMAKLDPSSQ 312
Cdd:pfam01080 161 MALVFIKYLPEWTTWVLLVAISIWDLFAVLCPKGPLRMLVETAQERNEPIFPALIYSATMVWLVagetenAMADEGTDRE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  313 GALQLPYDPEMEEDSYDSFGEPSY--------------------------------PEVFEPPLTGYPGEELEEEEERGV 360
Cdd:pfam01080 241 TVKQEISNYSGAEAGDSSFPQSSRsssdainpdsslteelsserseeesspssssaEEPSEPKELSSSQDTQDEEEERGV 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105679  361 KLGLGDFIFYSVLVGKAAATgsGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFM 438
Cdd:pfam01080 321 KLGLGDFIFYSVLVGKAAMY--GDWNTVIACFVAILIGLCLTLLLLAIFRKALPALPISITFGLIFYFLTRLLVEPFV 396
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
136-434 6.09e-75

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 238.30  E-value: 6.09e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   136 LNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKtynvaMDYPTLLLTVWNFGAVG 215
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFR-----VDYPTLLILLLNFAVVG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   216 MVCIHWKgpLVLQQAYLIMISALMALVFIKYLP-EWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPI--FPAL 292
Cdd:smart00730  76 FWCIHRK--GAWIQQDLIGISLCMAILFILRLPsEWTAWILLGALFIYDIFAVFGTPGPLRVMVEVATGRDEPIkvFPAL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   293 IYSSAMVWtvgmakldpssqgalqlpyDPEMEEDSydsfgepsypevfeppltgypgeeleeeeeRGVKLGLGDFIFYSV 372
Cdd:smart00730 154 LYVPRLVV-------------------SFEDDEEE------------------------------RFSMLGLGDIVFPGI 184
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105679   373 LVGKAAATGS---GDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLV 434
Cdd:smart00730 185 LVASAARFDVsvrSDSNYFLACFVAYGIGLILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
 
Name Accession Description Interval E-value
Presenilin pfam01080
Presenilin; Mutations in presenilin-1 are a major cause of early onset Alzheimer's disease. It ...
82-438 0e+00

Presenilin; Mutations in presenilin-1 are a major cause of early onset Alzheimer's disease. It has been found that presenilin-1 binds to beta-catenin in-vivo. This family also contains SPE proteins from C.elegans.


Pssm-ID: 307294  Cd Length: 396  Bit Score: 561.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   82 KYGAKHVIMLFVPVTLCMIVVVATIKSVRFYT--EKNGQ-LIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVV 158
Cdd:pfam01080   1 KYGAKQVIKLFVPVSLCMLLVVATIRSVSFYSsqSNDEAsLVYTPFHEESDSTGTKLWNSLLNALIFIGVIVVMTFLLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  159 LYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISAL 238
Cdd:pfam01080  81 LYKYRCYKFIHGWLILSSLLLLFLFSGQYLGELLRAYNIPMDYITFAFILWNFGVVGMIAIFWKGPLLLQQAYLILISAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  239 MALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTV------GMAKLDPSSQ 312
Cdd:pfam01080 161 MALVFIKYLPEWTTWVLLVAISIWDLFAVLCPKGPLRMLVETAQERNEPIFPALIYSATMVWLVagetenAMADEGTDRE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679  313 GALQLPYDPEMEEDSYDSFGEPSY--------------------------------PEVFEPPLTGYPGEELEEEEERGV 360
Cdd:pfam01080 241 TVKQEISNYSGAEAGDSSFPQSSRsssdainpdsslteelsserseeesspssssaEEPSEPKELSSSQDTQDEEEERGV 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105679  361 KLGLGDFIFYSVLVGKAAATgsGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFM 438
Cdd:pfam01080 321 KLGLGDFIFYSVLVGKAAMY--GDWNTVIACFVAILIGLCLTLLLLAIFRKALPALPISITFGLIFYFLTRLLVEPFV 396
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
136-434 6.09e-75

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 238.30  E-value: 6.09e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   136 LNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKtynvaMDYPTLLLTVWNFGAVG 215
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFR-----VDYPTLLILLLNFAVVG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   216 MVCIHWKgpLVLQQAYLIMISALMALVFIKYLP-EWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPI--FPAL 292
Cdd:smart00730  76 FWCIHRK--GAWIQQDLIGISLCMAILFILRLPsEWTAWILLGALFIYDIFAVFGTPGPLRVMVEVATGRDEPIkvFPAL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105679   293 IYSSAMVWtvgmakldpssqgalqlpyDPEMEEDSydsfgepsypevfeppltgypgeeleeeeeRGVKLGLGDFIFYSV 372
Cdd:smart00730 154 LYVPRLVV-------------------SFEDDEEE------------------------------RFSMLGLGDIVFPGI 184
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105679   373 LVGKAAATGS---GDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLV 434
Cdd:smart00730 185 LVASAARFDVsvrSDSNYFLACFVAYGIGLILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
 
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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