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1.A.54.2.2
Presenilin homologue (DUF1119) of 301 aas and 9 TMSs with known 3-d structure. The amino-terminal domain, consisting of TM1-6, forms a horseshoe-shaped structure, surrounding TM7-9 of the carboxy-terminal domain. The two catalytic aspartate residues are located on the cytoplasmic side of TMS 6 and TMS 7, spatially close to each other and approximately 8 Å into the lipid membrane surface. Water molecules gain constant access to the catalytic aspartates through a large cavity between the amino- and carboxy-terminal domains. (Li et al. 2013).  Both protease and ion channel activities have been demostrated, and these two activities share the same active site (Kuo et al. 2015). Cleavage is controlled by both positional and chemical factors (Naing et al. 2018).

Accession Number:A3CWV0
Protein Name:Uncharacterized protein
Length:301
Molecular Weight:31823.00
Species:Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [368407]
Number of TMSs:8
Substrate Ca2+

Cross database links:

Structure:
4HYC   4HYD   4HYG   4Y6K     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MQIRDWLPLL GMPLMLLFVQ IIAIVLVMPM QAAGLVAFED PESVANPLIF IGMLLAFTLV 
61:	LLVLLRTGGR RFIAAFIGFA LFMTFLYIFG ALSLLALGPT TAAAAGTLIG AVAVTALLYL 
121:	YPEWYVIDIL GVLISAGVAS IFGISLAVLP VLVLLVLLAV YDAISVYRTK HMITLAEGVL 
181:	ETKAPIMVVV PKRADYSFRK EGLNISEGEE RGAFVMGMGD LIMPSILVAS SHVFVDAPAV 
241:	LWTLSAPTLG AMVGSLVGLA VLLYFVNKGN PQAGLPPLNG GAILGFLVGA ALAGSFSWLP 
301:	F