Skip to main content

Table 6 Identical sequences of FL8 present across multiple clusters with GO MF propensity calculated using level 3*

From: Functionally important segments in proteins dissected using Gene Ontology and geometric clustering of peptide fragments

PDB [reference]†

Molecule

Putative fragment function

Sequence (propensity)§

P-value

1u19A‡ [53]

Rhodopsin

Part of extracellular domain intradiskal loop involved in cell signaling

11: VPFSNKTG (47)

0.02

1edsA [54]

Bovine rhodopsin

Same as above

17: GCNLEGFF (93)

0.01

   

21: EGFFATLG (39)

0.03

   

22: GFFATLGG (130)

0.008

1edvA [54]

Bovine rhodopsin

Same as above

16: CGIDYYTPP (96)

0.01

1edxA [54]

Bovine rhodopsin

Same as above

11: VPFSNKTG (22)

0.04

1tgj‡ [45]

Human transforming growth factor β3

Structure destabilized on dislufide bond reduction

72: ASASPCCV (157)

0.006

1kl9A‡ [55]

Human translation initiation factor 2α

Linker for the penultimate 310 helix and the last α-helix in domain 1

163: DSLDLNED (35)

0.03

   

164: SLDLNEDE (35)

0.003

1q9bA‡ [56]

Hevein (IgE bonding natural allergen)

Part of conformational epitope

6: QAGGKLCP (62)

1.3e-08

   

8: GGKLCPNN (299)

2.3e-08

   

9: GGLCPNNL (123)

9.8e-12

   

11: LCPNNLCC (25)

1.3e-06

   

12: CPNNLCCS (28)

2.0e-08

   

14: NNLCCSQW (28)

≈ 0

   

15: NLCCSQWG (79)

1.5e-08

1wpgA‡ [57]

Sarcoplasmic/endoplasmic reticulum calcium ATPase

Phosphorylation of D351 causes the protein to switch conformation

349: CSDKTGTL (41)

0.002

   

350: SDKTGTLT (56)

0.001

1mhsA‡ [58]

Proton ATPase

Phosphorylation of D378 causes the protein to switch conformation

631: MTGDGVND (22)

0.008

   

633: GDGVNDAP (25)

0.04

   

376: CSDKTGTL (41)

0.002

   

377: SDKTGTLT (56)

0.001

  1. *The highest propensity fragment from only one cluster is shown. †Files indicated in regular font denote an NMR-derived structure. ‡An X-ray-derived structure. The chain identifier is indicated after the four letter PDB code, wherever present. §Disulfide bonded Cys are underlined.