LiteFold/DisProt huggingface dataset:
Protein: DP02976 (UniProt Q05193)
Region: residues 500	to 517
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered. 
The PH domain is interconnected between α3S and α4S of the stalk by two disordered loops, L1SP and L2SP, and shows only minor deviations from the isolated PH domain of dynamin 1 (refs 14, 15; r.m.s.d. of 0.8 Å for 102 Cα atoms).
The IDR spanning residues 500-517 is a flexible linker connecting the Stalk in the middle domain (MD) and the PH domain as shown in Fig 1.
Cross-references: PDB:3SNH
Protein: DP02976 (UniProt Q05193)
Region: residues 632	to 652
Annotation: flexible linker (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered. 
The PH domain is interconnected between α3S and α4S of the stalk by two disordered loops, L1SP and L2SP, and shows only minor deviations from the isolated PH domain of dynamin 1 (refs 14, 15; r.m.s.d. of 0.8 Å for 102 Cα atoms).  
The IDR spanning residues 632-652  is a flexible linker connecting the PH domain and the Stalk of the GTPase effector domain (GED) as shown in Fig 1.
Cross-references: PDB:3SNH
Protein: DP02976 (UniProt Q05193)
Region: residues 394	to 404
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered. 
α1S in dynamin 1 is subdivided into α1NS, α1MS and α1CS by two disordered loops, L1NS and L1CS, compared to a single break of the corresponding helix in MxA.
Cross-references: PDB:3SNH
Protein: DP02976 (UniProt Q05193)
Region: residues 500	to 517
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered.
Cross-references: PDB:3SNH
Protein: DP02976 (UniProt Q05193)
Region: residues 632	to 652
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered.
Cross-references: PDB:3SNH
Protein: DP02977 (UniProt O75962)
Region: residues 1494	to 1507
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The PDB shows this region lacks electron density, indicating it is disordered.
Cross-references: PDB:2NZ8
Protein: DP02978 (UniProt Q9BSQ5)
Region: residues 160	to 190
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Based on our crystal structure, CCM2PTB comprises residues Ser60–Tyr221 with a 32-residue flexible loop (loop β6/β7) inserted between strands β6 and β7 (residues Asp160–Glu191), for which we do not observe density in any of the four copies of CCM2PTB
Cross-references: PDB:4WJ7
Protein: DP02978 (UniProt Q9BSQ5)
Region: residues 377	to 420
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The long loop (residues 377–420) connecting CCM2cts and CCM2-chelix, and the remaining residues beyond α6, are omitted in the final model due to the lack of interpretable electron density, indicative of their high intrinsic flexibility.
Cross-references: PDB:4YKC
Protein: DP02980 (UniProt Q4V8K1)
Region: residues 1	to 18
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
These are as follows: first, a short loop between α5 and β7 (residues 147–149), which is also poorly ordered in Steap3 (residues 157–162); second, the N-terminal 18 residues are also disordered.
Cross-references: PDB:2YJZ
Protein: DP02981 (UniProt P04275)
Region: residues 1478	to 1493
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The crystal asymmetric unit contains three A2 molecules that are essentially identical and comprise residues 1,478–1,674; we do not observe interpretable density for amino-terminal residues 1,478–1,493, most likely because of flexibility.
Cross-references: PDB:3ZQK
Protein: DP02982 (UniProt O01479)
Region: residues 196	to 221
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
A large part of the N-terminus, including residues 196–221, is completely disordered, which was also observed in the homologous structure 1IO0
Cross-references: PDB:1PGV
Protein: DP02983 (UniProt Q9DEA6)
Region: residues 146	to 164
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The first N-terminal 19 residues, Gly160–Pro178, do not give any clear electron density, and these are likely to be flexible and disordered.
Gly160 and Pro178 in this construct correspond to Gly146 and Pro164 in Tropomodulin real sequence.
Cross-references: PDB:1IO0
Protein: DP02984 (UniProt P09446)
Region: residues 615	to 640
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In accordance with solution studies of E. coli DnaK [16] and the crystal structure of rat Hsc70 [14], the final 26 C terminal residues were found to be disordered
The complete sequence of the construct used was mgsshhhhhhssGLVPRGSHMASGLESYAFNLKQTIEDEKLKDKISPEDKKKIEDKCDEILKWLDSNQTAEKEEFEHQQKDLEGLANPIISKLYQSaggappgaapggaaggaggptieevd; recombinant tag residues in italic, disordered residues in lowercase.
Cross-references: PDB:2P32
Protein: DP02985 (UniProt P0A6Y8)
Region: residues 606	to 638
Annotation: disorder (Structural state)
Evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion
Supporting statements:
The domain was shown to be comprised of a rigid structure consisting of four helices and a flexible C-terminal subdomain of approximately 33 amino acids. The mobility of the flexible region is maintained in the context of the full-length protein and does not appear to be modulated by the nucleotide state.
In addition, the last 33 amino acids constitute a highly flexible subdomain of the molecule.
In contrast to the apparently rigid structure of the helical portion of the molecule, the carboxy-terminal 33 residues are highly flexible.
Protein: DP02986 (UniProt P63018)
Region: residues 622	to 646
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The remaining residues of the four molecules, A621–A646, B619–B646, C622–C646, and D615–D646, could not be traced due to their poor electron density maps.
The numbering of the IDR refers to chain C
Cross-references: PDB:1UD0
Protein: DP02987 (UniProt Q22942)
Region: residues 1	to 31
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N terminus of the protein begins with 31 unobserved and presumably disordered residues, followed by a small subdomain that contains two helices
The final model includes residues 32–265 and residues 296–426 for subunit A, residues 40–265 and residues 296–426 for subunit B, one calcium ion for each subunit, and a total of 342 water molecules. Residues not included in the model are Caenorhabditis elegans: cloning, expression, purification, and those that are not visible and assumed to be disordered.
Cross-references: PDB:1NW1
Protein: DP02987 (UniProt Q22942)
Region: residues 265	to 296
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
In addition, strands 10 and 11 are connected by a long stretch of sequence (residues 265– 296) that appears to extend away from the core structure. Since there is no electron density observed for this sequence, it is assumed to be disordered
The final model includes residues 32–265 and residues 296–426 for subunit A, residues 40–265 and residues 296–426 for subunit B, one calcium ion for each subunit, and a total of 342 water molecules. Residues not included in the model are Caenorhabditis elegans: cloning, expression, purification, and those that are not visible and assumed to be disordered.
Cross-references: PDB:1NW1
Protein: DP02988 (UniProt P34704)
Region: residues 165	to 175
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final model includes all of the HER-1GM sequence except 11 C-terminal residues (165–175) for which electron density was not interpretable.
Cross-references: PDB:1SZH
Protein: DP02989 (UniProt Q03611)
Region: residues 1	to 105
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues M1 to I105 and N621 to K733, which constitute most of the amino terminus and the distal C terminus beyond the CNBD, respectively, were not modelled because their densities were weak or missing.
The density of residues 1–105 was missing in the map
Cross-references: PDB:5H3O
Protein: DP02989 (UniProt Q03611)
Region: residues 621	to 733
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues M1 to I105 and N621 to K733, which constitute most of the amino terminus and the distal C terminus beyond the CNBD, respectively, were not modelled because their densities were weak or missing.
Residues 621–733 were not visible in the density map. There was weak density under the C-linker/CNBD region. This density could represent the coiled coil region, but it was too weak for model building.
Cross-references: PDB:5H3O
Protein: DP02989 (UniProt Q03611)
Region: residues 1	to 103
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues M1 to V103 (N terminus), G162 to L164, and D620 to K733 (distal C terminus) were not modeled because of weak or missing densities.
Cross-references: PDB:6WEL
PDB:6WEJ
PDB:6WEK
Protein: DP02989 (UniProt Q03611)
Region: residues 620	to 733
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Residues M1 to V103 (N terminus), G162 to L164, and D620 to K733 (distal C terminus) were not modeled because of weak or missing densities.
Cross-references: PDB:6WEL
PDB:6WEJ
PDB:6WEK
Protein: DP02990 (UniProt Q9U489)
Region: residues 730	to 757
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The final crystallographic model encompasses residues 691–729 and 758–820, whereas a long insert (730–757) that is only found in Caenorhabditis LIN-41 protein sequences could not be built due to high flexibility.
The disordered sequence stretch 730–757 which is not included in the model is displayed as grey dots.
Cross-references: PDB:4UMG
Protein: DP02991 (UniProt Q9XTW2)
Region: residues 120	to 129
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C-terminal 25 residues are missing from all four molecules and are presumably disordered. Residues 120–129 have poor electron densities and are built in only one molecule
Cross-references: PDB:4KQB
PDB:4KQA
Protein: DP02991 (UniProt Q9XTW2)
Region: residues 488	to 512
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The C-terminal 25 residues are missing from all four molecules and are presumably disordered. Residues 120–129 have poor electron densities and are built in only one molecule
Cross-references: PDB:4KQB
PDB:4KQA
Protein: DP02993 (UniProt Q9RFD6)
Region: residues 1	to 29
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The N-terminus (1-29)
on both the subunits was not resolved in electron density
maps even after several rounds of refinement. 
Cross-references: PDB:3FWY
Protein: DP02993 (UniProt Q9RFD6)
Region: residues 16	to 29
Annotation: disorder to order (Structural transition)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
Unexpectedly, although the N-terminus is disordered in previous DPOR L-protein structures (residues 1-29 in 3FWY and
residues 1-27 in 2YNM), we observe electron
density at the N-terminus of chain C in our
nucleotide-free structure, which we were able
to model as residues 16 to 29 (Supplemental
Fig. 1b).
Interestingly, in chain C, we observe
the flexible N-terminus bound across the
[4Fe-4S] cluster (Fig. 2a, dark blue) covering
a surface that is normally used to interface
with BchNB (Fig. 2c, purple).
Protein: DP02993 (UniProt Q9RFD6)
Region: residues 16	to 29
Annotation: self-inhibition (Disorder function)
Evidence: x-ray crystallography evidence used in manual assertion
Supporting statements:
The position and specific interactions of the N-terminal residues in our
nucleotide-free structure suggests a possible
auto-inhibitory role by forming a barrier to
docking and shielding the [4Fe-4S] cluster of
BchL.
The masking of the [4Fe-4S] cluster by the flexible N-terminal region and the
associated inhibition of activity is a novel
mechanism of regulation in metalloproteins.
Protein: DP02993 (UniProt Q9RFD6)
Region: residues 16	to 29
Annotation: order to disorder (Structural transition)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
Hydrogen deuterium exchange mass spectrometry shows that ATPbinding to BchL produces specific conformational changes leading to release of the flexible N-terminus from the docking interface. 
The HDX data suggest a direct path
of communication between the N-terminal
flexible region and the ATP binding pocket.
Perturbations in the N-terminal flexible region allosterically modulates changes in the
ATP-binding pocket (and vice versa).
Protein: DP02993 (UniProt Q9RFD6)
Region: residues 1	to 29
Annotation: self-inhibition (Disorder function)
Evidence: mutant phenotype evidence used in manual assertion
Supporting statements:
We show that amino acid
substitutions within this flexible N-terminal
region enhance the kinetics of Pchlide reduction, pointing to a functionally auto-inhibitory role.
 Both BchLS17A and
BchL4A are active for Pchlide reduction and
show Chlide formation rates ~2 fold higher
than that of wild type BchL (kobs= 0.026 ±
0.002, 0.041 ± 0.008, and 0.045 ± 0.007 min1
for BchL, BchLS17A and BchL4A, respectively; Fig. 3b).
Protein: DP02993 (UniProt Q9RFD6)
Region: residues 1	to 29
Annotation: self-inhibition (Disorder function)
Evidence: nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion
Supporting statements:
The HDX data suggest a direct path of communication between the N-terminal flexible region and the ATP binding pocket. Perturbations in the N-terminal flexible region allosterically modulates changes in the ATP-binding pocket (and vice versa).
The HDX-MS data support an elegant
allosteric mechanism for the ATP-binding
driven release of autoinhibition, as helix 8
physically connects the DFD patch and the
flexible N-terminal region (Supplemental
Fig. 6b-c).
Protein: DP02995 (UniProt Q84MC7)
Region: residues 1	to 12
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
The map obtained showed clear electron density for most of the protein residues and the ABA–bound molecule, whereas no models were built for 12 N‐terminal and 5 C‐terminal residues, which were not observed in the electron density map.
Cross-references: PDB:3W9R
Protein: DP02995 (UniProt Q84MC7)
Region: residues 1	to 17
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
This region lacks electron density, indicating it is disordered.
Cross-references: PDB:3OQU
Protein: DP02996 (UniProt O85041)
Region: residues 260	to 603
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) spectra indicated that only the NTD has α-helical content (Fig. 1b).
Protein: DP02996 (UniProt O85041)
Region: residues 604	to 839
Annotation: disorder (Structural state)
Evidence: far-UV circular dichroism evidence used in manual assertion
Supporting statements:
Circular dichroism (CD) spectra indicated that only the NTD has α-helical content (Fig. 1b).
Protein: DP02999 (UniProt P34808)
Region: residues 1	to 172
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Six regions of the polypeptide chain (residues 1–172, 186–190, 263–269, 297–306,
324–332, 467–472) are not well resolved and presumed disordered
Cross-references: PDB:5WCB
PDB:5WC0
PDB:5WC1
Protein: DP02999 (UniProt P34808)
Region: residues 297	to 306
Annotation: disorder (Structural state)
Evidence: X-ray crystallography-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Six regions of the polypeptide chain (residues 1–172, 186–190, 263–269, 297–306,
324–332, 467–472) are not well resolved and presumed disordered
Cross-references: PDB:5WCB
PDB:5WC0
PDB:5WC1
Protein: DP02999 (UniProt P34808)
Region: residues 85	to 140
Annotation: flexible linker (Disorder function)
Evidence: small-angle X-ray scattering evidence used in manual assertion
Supporting statements:
Domain diagram of katanin p60; MIT, microtubule interacting and trafficking domain, yellow; flexible linker, pink; AAA domain, gray; fishhook-shaped linker element, light blue; α1, dark blue; α12 and C-terminal residues 468–472, dark orange. NBD and HBD are highlighted by light green and dark green hatches, respectively. Residue numbers for C. elegans katanin.
Pink region in figure 1D is comprised between residues 85-140
This region connects microtubule interacting and trafficking (MIT) domain to the AAA ATPase domain
Cross-references: PDB:5WCB
PDB:5WC0
PDB:5WC1
Protein: DP02999 (UniProt P34808)
Region: residues 1	to 156
Annotation: disorder (Structural state)
Evidence: cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion
Supporting statements:
Disordered segments not visible in reconstruction marked with hatches. Residue numbers for C. elegans katanin.
Hatched regions are comprised between residues 1-156 in Figure 2E
No density was visible for the rest of the linker and the MIT domain, consistent with their flexibility as previously shown (Zehr et al., 2017)." 
Cross-references: PDB:6UGD
PDB:6UGF
PDB:6UGE
Protein: DP02999 (UniProt P34808)
Region: residues 1	to 172
Annotation: molecular adaptor activity (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
A disordered region outside the AAA core anchors katanin to the microtubule while the AAA motor exerts the forces that extract tubulin dimers and sever the microtubule
Thus, our structural and functional work reveals how tubulin tails template the assembly and ATPase activation of the katanin hexamer, and shows how katanin uses complex multivalent interactions with the microtubule through flexible and intrinsically disordered elements to generate the forces needed to extract tubulin subunits out of the microtubule
Cross-references: PDB:6UGF
PDB:6UGE
PDB:6UGD
Protein: DP02999 (UniProt P34808)
Region: residues 1	to 84
Annotation: molecular adaptor activity (Molecular function)
Evidence: cryogenic electron microscopy evidence used in manual assertion
Supporting statements:
Our structural and functional work shows that katanin, unlike other AAA ATPases characterized so far, uses a double-spiral system to coordinate the tubulin tail through the central pore and multivalent contacts through a low complexity disordered region outside the ordered AAA core to anchor the enzyme to the microtubule
Cross-references: PDB:6UGF
PDB:6UGE
PDB:6UGD
Protein: DP02999 (UniProt P34808)
Region: residues 85	to 172
Annotation: protein binding (Molecular function)
Evidence: fluorescence microscopy evidence used in manual assertion
Supporting statements:
A Positively Charged Disordered Linker Region Is Critical for Severing
Mutation of the equivalent Ser to a phosphomimetic residue (Ser135Glu) in C. elegans katanin causes a ∼50% decrease in ATPase (Figure 5A) as well as microtubule severing and nanodamage activity (Figures 5B, 5D, 5E, and S7A). Thus, the introduction of negative charges in this linker region inhibits katanin
Our results indicate that both microtubule binding and mechanochemical coupling are impaired when positively charged residues are mutated in the linker, with K119 and K120 having the most drastic effect. Thus, elements outside the structured AAA and MIT domains are critical for severing
Our functional work reveals that clusters of positively charged residues in the disordered linker connecting the AAA and MIT domains are required for katanin microtubule binding and severing
High-affinity microtubule binding requires the disordered linker (Eckert et al., 2012, Jiang et al., 2017), consistent with our finding that positively charged linker residues are critical for katanin severing
Cross-references: PDB:6UGF
PDB:6UGE
PDB:6UGD
Protein: DP03000 (UniProt Q997F2)
Region: residues 1	to 456
Annotation: disorder (Structural state)
Evidence: sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion
Supporting statements:
This aberrant migration during electrophoresis is a hallmark of intrinsically disordered proteins (IDPs) and is often due to their typically high content of acidic residues35 and/or low compaction.
Protein: DP03000 (UniProt Q997F2)
Region: residues 1	to 456
Annotation: pre-molten globule (Structural state)
Evidence: chromatography evidence used in manual assertion
Supporting statements:
The experimentally observed values of the Rs are very close to the values expected for a PMG form (i.e. an extended conformation possessing nevertheless some residual structure38) (∼45 Å) (see Table 1).