Blast Analysis : gnl|CDD|119398

Analysis	rpsblast_cdd	Start	137
End	269	Strand	+
Length	133	Note	Gaps:49
Hit Coverage	98.82	Hit Length	85
Hit Pident	50.00	E Val	2e-19
Hit Description	cd06530 S26_SPase_I The S26 Type I signal peptidase (SPase LepB leader peptidase B leader peptidase I EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I which is the most intensively studied has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus secretory vesicles plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism..	Hit Pcons	15.48
Name	Qrob_P0010090.2

1 Protein

Protein Identifier	Organism . Name	Score	Score Type	Protein Description	Alias (in v1)	Code Enzyme	Gene Prediction Quality
Qrob_P0010090.2	Quercus robur	100.0	egn	(M=2) K03100 - signal peptidase I [EC:3.4.21.89]		EC:3.4.21.89	validated

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