Table II

A survey of known structures, functions, and interaction domains for each FG Nup with refined domain boundaries based on AA conservation

Known structures and functions are in regular text; previously predicted structures and functions are in italics; new predictions of structure and function based on AACB value and AA sequence conservation are in bold italics. FG domain plus regions include the FG domain plus flanking, highly substituted sequences. hs RNA, heat shock RNA.

Nup domains defined by AA conservationDomain AAsPercent AA conservationAA composition (percent disorder/order)AACB valueActual or predicted structure (AAs)Actual or predicted function (AAs)Refs.
%
Nup159
    Cluster I1–3866845/414β-Propeller (2–387)Dbp5 binding (2–387) 29
    FG domain plus387–10712062/2240Natively unfolded (441–881)Kap binding (441–881)9, 46
    Cluster II1072–12666548/3513 Structured Molecular interaction
    Between Clusters II and III1267–13312538/43−5Coiled coil (1281–1316) Structural bridge or spacer 47
    Cluster III1332–14576749/3613Coiled coil (1392–1412)NPC anchor, Nup82 binding (1223–1460)48–50
Nup42
    FG domain plus1–3822256/2927 Natively unfolded Kap binding (1–430) 5
    Cluster I383–4307954/3717 Structured hs RNA export; NPC anchor (365–430)51, 52
Nup49
    FG domain plus1–2516059/3029 Natively unfolded Kap binding (1–472) 5
    Cluster I252–4589045/378Coiled coil (350–400) NPC anchor 49
Nup57
    FG domain plus1–2556158/2632 Natively unfolded Kap binding (1–541) 5
    Cluster I256–5308953/3419Coiled coil (350–425) NPC anchor 53
Nup100
    FG domain plus1–8004952/3418Natively unfolded (1–640)Kap binding (1–640)5, 9
    Cluster I801–9528441/46−5β-Sheet (814–959)NPC anchor (559–959) 28
Nup116
    FG domain plus1–9606157/3027 Natively unfolded Kap binding (165–715); Gle2 binding (110–166)5, 9, 23
    Cluster I962–11118246/424β-Sheet (967–1113)NPC anchor (706–1113)26, 28
nNup145a
    FG domain plus1–43367a53/3221 Natively unfolded Kap binding 9
    Cluster I434–60581a47/3710β-Sheet (458–605)NPC anchor (247–606); autoproteolysis (398–613)28, 54
Nsp1
    FG domain plus1–6175163/2241Natively unfolded (1–603)Kap binding (1–603)9, 55
    Cluster I618–8099143/403Coiled coils (630–823)NPC anchor (591–823) 27
Nup53
    Cluster I8–1776556/3224 Natively unfolded Molecular interaction
    Between Clusters I and II178–2532750/2822 Natively unfolded Flexible linker or spacer
    Cluster II254–3577248/426RRM fold (247–352) Homodimerization 25
    Between Clusters II and III358–4002460/2832 Natively unfolded Flexible linker or spacer
    Cluster III401–4758855/3916Amphipathic α-helix (459–475)Kap121 binding (401–448); membrane binding (449–475)24, 56
Nup59
    N terminus1–803656/3224 Natively unfolded Molecular interaction
    Cluster I81–4286644/395RRM fold (265–394) Homodimerization 25
    Between Clusters I and II429–4942242/411 Structured Structural bridge or spacer
    Cluster II495–5287950/3812 Structured Membrane binding
Nup60
    N terminus1–1173956/3125 Natively unfolded Kap123 binding (1–187) 57
    Cluster I118–3017758/3127 Natively unfolded Molecular interaction
    Between Cluster I and Box 12302–3493364/2539 Natively unfolded Flexible linker or spacer
    Box 12350–3868970/2248 Natively unfolded Molecular interaction
    FG domain plus387–5393956/3224 Natively unfolded Kap95/60 binding (389–539)9, 57
Nup2
    Cluster I1–518857/2037 Natively unfolded Kap60 binding (26–51)31, 32
    FG domain plus52–6004159/2534Natively unfolded (186–561)Kap binding (186–561)8, 58
    Cluster II601–7088251/3417β-Sheet (583–720)Gsp1/Ran binding (560–720)30, 57
Nup1
    N terminus1–854653/3122 Natively unfolded Molecular interaction
    Cluster I86–1208652/439 Structured NPC anchor (4–212) 59
    FG domain plus121–10763951/2631Natively unfolded (300–1076)Kap binding (432–816); Kap60 binding (1059–1076); Kap95 binding (975–987 and 1004–1009)9, 21, 58, 60
  • a A case where AA sequences from only three of the four yeast species were used.