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Conserved domains on  [gi|148223033|ref|NP_001088010|]
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presenilin enhancer gamma secretase subunit S homeolog [Xenopus laevis]

Protein Classification

PEN-2 domain-containing protein (domain architecture ID 10563016)

PEN-2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PEN-2 pfam10251
Presenilin enhancer-2 subunit of gamma secretase; This entry is a short 101 peptide protein ...
7-99 9.60e-49

Presenilin enhancer-2 subunit of gamma secretase; This entry is a short 101 peptide protein which is the smallest subunit of the gamma-secretase aspartyl protease complex that catalyzes the intramembrane cleavage of a subset of type I transmembrane proteins. The other active constituents of the complex are presenilin (PS) nicastrin and anterior pharynx defective-1 (APH-1) protein. PEN-2 adopts a hairpin orientation in the membrane with its N- and C-terminal domains facing the luminal/extracellular space, and the C-terminal domain maintains PS stability within the complex.


:

Pssm-ID: 313477  Cd Length: 93  Bit Score: 153.12  E-value: 9.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223033    7 PNEEKLQLCRKYYMGGFALLPFLWLVNVVWFFKEAFFKPAYTEQPLIQSYVKRSAFGLFVWVVILTTWISVYQTHRASWG 86
Cdd:pfam10251   1 SNEEKLNLCRKYFLAGFALLPFLWLVNFVWFFPEAFRKPPFEEQKQIRKYVIRSAIGFLVWTVLLITWIIIFQINRASWG 80
                          90
                  ....*....|...
gi 148223033   87 ATGDYLSFTIPLG 99
Cdd:pfam10251  81 EFGDYLSFIIPLG 93
 
Name Accession Description Interval E-value
PEN-2 pfam10251
Presenilin enhancer-2 subunit of gamma secretase; This entry is a short 101 peptide protein ...
7-99 9.60e-49

Presenilin enhancer-2 subunit of gamma secretase; This entry is a short 101 peptide protein which is the smallest subunit of the gamma-secretase aspartyl protease complex that catalyzes the intramembrane cleavage of a subset of type I transmembrane proteins. The other active constituents of the complex are presenilin (PS) nicastrin and anterior pharynx defective-1 (APH-1) protein. PEN-2 adopts a hairpin orientation in the membrane with its N- and C-terminal domains facing the luminal/extracellular space, and the C-terminal domain maintains PS stability within the complex.


Pssm-ID: 313477  Cd Length: 93  Bit Score: 153.12  E-value: 9.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223033    7 PNEEKLQLCRKYYMGGFALLPFLWLVNVVWFFKEAFFKPAYTEQPLIQSYVKRSAFGLFVWVVILTTWISVYQTHRASWG 86
Cdd:pfam10251   1 SNEEKLNLCRKYFLAGFALLPFLWLVNFVWFFPEAFRKPPFEEQKQIRKYVIRSAIGFLVWTVLLITWIIIFQINRASWG 80
                          90
                  ....*....|...
gi 148223033   87 ATGDYLSFTIPLG 99
Cdd:pfam10251  81 EFGDYLSFIIPLG 93
 
Name Accession Description Interval E-value
PEN-2 pfam10251
Presenilin enhancer-2 subunit of gamma secretase; This entry is a short 101 peptide protein ...
7-99 9.60e-49

Presenilin enhancer-2 subunit of gamma secretase; This entry is a short 101 peptide protein which is the smallest subunit of the gamma-secretase aspartyl protease complex that catalyzes the intramembrane cleavage of a subset of type I transmembrane proteins. The other active constituents of the complex are presenilin (PS) nicastrin and anterior pharynx defective-1 (APH-1) protein. PEN-2 adopts a hairpin orientation in the membrane with its N- and C-terminal domains facing the luminal/extracellular space, and the C-terminal domain maintains PS stability within the complex.


Pssm-ID: 313477  Cd Length: 93  Bit Score: 153.12  E-value: 9.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148223033    7 PNEEKLQLCRKYYMGGFALLPFLWLVNVVWFFKEAFFKPAYTEQPLIQSYVKRSAFGLFVWVVILTTWISVYQTHRASWG 86
Cdd:pfam10251   1 SNEEKLNLCRKYFLAGFALLPFLWLVNFVWFFPEAFRKPPFEEQKQIRKYVIRSAIGFLVWTVLLITWIIIFQINRASWG 80
                          90
                  ....*....|...
gi 148223033   87 ATGDYLSFTIPLG 99
Cdd:pfam10251  81 EFGDYLSFIIPLG 93
 
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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