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Conserved domains on  [gi|328866196|gb|EGG14582|]
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gamma-secretase subunit [Cavenderia fasciculata]

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 ...
10-97 2.14e-32

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: 402042  Cd Length: 93  Bit Score: 108.07  E-value: 2.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328866196  10 NDDKMRNIAKKLWIIGFFFLPWVWLINILFFFPHRKQLS-----TDVFWYLKYSLIGFFVYSTIFMTWMGIYLVNRNNWG 84
Cdd:pfam10251  1 SDEEKLNLCRKYFLAGFALLPFLWLVNAVWFFPEAFRKPpfeeqKQIRKYVIRSAIGFLVWTVLLITWIIIFQINRALWG 80
                         90
                 ....*....|...
gi 328866196  85 ASGDNISIVIPYG 97
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 ...
10-97 2.14e-32

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: 402042  Cd Length: 93  Bit Score: 108.07  E-value: 2.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328866196  10 NDDKMRNIAKKLWIIGFFFLPWVWLINILFFFPHRKQLS-----TDVFWYLKYSLIGFFVYSTIFMTWMGIYLVNRNNWG 84
Cdd:pfam10251  1 SDEEKLNLCRKYFLAGFALLPFLWLVNAVWFFPEAFRKPpfeeqKQIRKYVIRSAIGFLVWTVLLITWIIIFQINRALWG 80
                         90
                 ....*....|...
gi 328866196  85 ASGDNISIVIPYG 97
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 ...
10-97 2.14e-32

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: 402042  Cd Length: 93  Bit Score: 108.07  E-value: 2.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328866196  10 NDDKMRNIAKKLWIIGFFFLPWVWLINILFFFPHRKQLS-----TDVFWYLKYSLIGFFVYSTIFMTWMGIYLVNRNNWG 84
Cdd:pfam10251  1 SDEEKLNLCRKYFLAGFALLPFLWLVNAVWFFPEAFRKPpfeeqKQIRKYVIRSAIGFLVWTVLLITWIIIFQINRALWG 80
                         90
                 ....*....|...
gi 328866196  85 ASGDNISIVIPYG 97
Cdd:pfam10251 81 EFGDYLSFIIPLG 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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