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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.