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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).

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