6949 Peptidase_S41_CPP
Thalassiosira pseudonana

Chromosome Product Transcript Start End Strand Short Name
6949 chr_7 Peptidase_S41_CPP 883178 886527 + Peptidase_S41_CPP
Expression Profile Conditional Changes Cluster Dendrogram
Thaps_hclust_0138
Normalized Mean Residue
Thaps_bicluster_0047
0.45
ERG4_ERG24 superfamily
0.8683
metallo-dependent_hydrolases superfamily
0.8503
Zip superfamily
0.844
hypothetical protein
0.8389
hypothetical protein
0.8349
NA
0.8343
(GCD1) GCD
0.8335
Aa_trans superfamily
0.8326
Peptidase_S41_CPP
0.8312
ALDH-SF superfamily
0.8308
Name CD Accession Definition Superfamily Bitscore E-Value From - To Hit Type PSSM ID
Peptidase_S41_CPP C-terminal processing peptidase; serine protease family S41; The C-terminal processing peptidase (... cl02526 186.849 8.15E-54 519 - 714 specific 143476
Peptidase_S41 superfamily C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing peptidase... - 186.849 8.15E-54 519 - 714 superfamily 261325
T. pseudonana P. tricornutum P. tricornutum DiatomCyc F. cylindrus Pseudo-nitzschia multiseries E. huxleyi C. reinhardtii A. thaliana P. sojae
Not available PHATRDRAFT_49652 PHATRDRAFT_49652 209175 249736 Not available Not available Not available Not available
KEGG description KEGG Pathway
Not available Not available
GO:0005515 GO:0006508 GO:0008236 -

protein binding

Details: 
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
GO Category: 
MF

proteolysis

Details: 
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO Category: 
BP

serine-type peptidase activity

Details: 
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
GO Category: 
MF
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