1 |
De novo motif search |
RRRSNTTTTY motif in the −300 bp (Supplementary Figure S1) |
This work, http://meme.sdsc.edu/meme/cgi-bin/meme.cgi
|
2 |
Homology |
Sequence identity to a known effector molecule; Blastp against effector database (e-value = 10−2) |
(6,8) |
3 |
Euk-like domains |
Presence of eukaryotic domain: 58 eukaryotic domains |
This work, Supplementary Table S1
|
4 |
Prok-like domains |
3617 Domain of Unknown Function (DUF) domains |
(29), http://pfam.sanger.ac.uk/search/
|
5 |
NLS (nuclear localization signal) |
Monopartite NLS; [KR]-[KR]-[KR]-[KR]-[KR] and bipartite NLS; K-[KR]-X(6,20)-[KR]-[KR]-X-[KR] |
(30,31) |
6 |
MLS (mitochondrial localization signal) |
Probability of a sequence containing a mitochondrial targeting peptide (P > 0.95) |
(32), http://www.bioperl.org/
|
7 |
Prenylation domain |
CaaX at the C-terminal; ‘C’ represents a cysteine residue, ‘a’ denotes an aliphatic amino acid and ‘X’ is one of four amino acids |
(1,33,34) |
8 |
Secondary structure |
Probability of a coiled-coil structure for windows of 28 residues through a protein sequence (P > 0.95) |
(35,36), http://emboss.bioinformatics.nl/cgi-bin/emboss/pepcoil
|
Coiled coils |
9 |
C-ter basicity |
≤3 [HRK] in the C-terminal 25 amino acids |
(3,7,22) |
10 |
C-ter charges |
Charge of C-terminal 25 amino acids ≥2; C-ter charge = number of [HRK]-number of [ED]-1 (COO-) |
(3,7,22) |
11 |
C-ter hydrophobicity |
Hydropathy of C-terminal 25 amino acids; Hydrophobic residue at the −3rd or −4th position |
(9,11,37,38) |
12 |
Global hydrophilicity |
Hydropathy of total protein <−200 |
(9,11,37) |
13 |
E-block |
EEXXE in the C-terminal 30 amino acids |
(39) |