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131  structures 1540  species 0  interactions 11597  sequences 456  architectures

Family: HEAT (PF02985)

Summary: HEAT repeat

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This is the Wikipedia entry entitled "HEAT repeat". More...

HEAT repeat Edit Wikipedia article

HEAT repeat
Alpha solenoid pp2a 2iae with single repeat center.png
An example of an alpha solenoid structure composed of 15 HEAT repeats. The protein phosphatase 2A regulatory subunit is shown with the N-terminus in blue at bottom and the C-terminus in red at top. A single helix-turn-helix motif is shown in the center with the outer helix in pink, the inner helix in green, and the turn in white. From PDB: 2IAE​.[1][2]
Identifiers
SymbolHEAT
PfamPF02985
InterProIPR000357
PROSITEPDOC50077
SCOP21b3u / SCOPe / SUPFAM

A HEAT repeat is a protein tandem repeat structural motif composed of two alpha helices linked by a short loop. HEAT repeats can form alpha solenoids, a type of solenoid protein domain found in a number of cytoplasmic proteins. The name "HEAT" is an acronym for four proteins in which this repeat structure is found: Huntingtin, elongation factor 3 (EF3), protein phosphatase 2A (PP2A),[3] and the yeast kinase TOR1.[4] HEAT repeats form extended superhelical structures which are often involved in intracellular transport; they are structurally related to armadillo repeats. The nuclear transport protein importin beta contains 19 HEAT repeats.

Various HEAT repeat proteins and their structures

Representative examples of HEAT repeat proteins include importin β (also known as karyopherin β) family,[5] regulatory subunits of condensin and cohesin,[6] separase,[7] PIKKs (phosphatidylinositol 3-kinase-related protein kinases) such as ATM (Ataxia telangiectasia mutated) and ATR (Ataxia telangiectasia and Rad3 related),[8][9] and the microtubule-binding protein XMAP215/Dis1/TOG[10] and CLASP.[11] Thus, cellular functions of HEAT repeat proteins are highly variable.

The structure of the following HEAT repeat proteins have been determined so far:

References

  1. ^ Cho, Uhn Soo; Xu, Wenqing (1 November 2006). "Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme". Nature. 445 (7123): 53–57. doi:10.1038/nature05351. PMID 17086192. S2CID 4408160.
  2. ^ a b Groves MR, Hanlon N, Turowski P, Hemmings BA, Barford D (January 1999). "The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs". Cell. 96 (1): 99–110. doi:10.1016/S0092-8674(00)80963-0. PMID 9989501. S2CID 14465060.
  3. ^ Kobe, Bostjan; Gleichmann, Thomas; Horne, James; Jennings, Ian G.; Scotney, Pierre D.; Teh, Trazel (1999-05-05). "Turn up the HEAT". Structure. 7 (5): R91–R97. doi:10.1016/S0969-2126(99)80060-4. ISSN 0969-2126. PMID 10378263.
  4. ^ Andrade MA, Bork P (October 1995). "HEAT repeats in the Huntington's disease protein". Nat. Genet. 11 (2): 115–6. doi:10.1038/ng1095-115. PMID 7550332. S2CID 6911746.
  5. ^ Malik HS, Eickbush TH, Goldfarb DS (1997). "Evolutionary specialization of the nuclear targeting apparatus". Proc. Natl. Acad. Sci. USA. 94 (25): 13738–13742. Bibcode:1997PNAS...9413738M. doi:10.1073/pnas.94.25.13738. PMC 28376. PMID 9391096.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Neuwald AF, Hirano T (2000). "HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions". Genome Res. 10 (10): 1445–52. doi:10.1101/gr.147400. PMC 310966. PMID 11042144.
  7. ^ Jäger H, Herzig B, Herzig A, Sticht H, Lehner CF, Heidmann S (2004). "Structure predictions and interaction studies indicate homology of separase N-terminal regulatory domains and Drosophila THR". Cell Cycle. 3 (2): 182–188. doi:10.4161/cc.3.2.605. PMID 14712087.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ Perry J, Kleckner N (2003). "The ATRs, ATMs, and TORs are giant HEAT repeat proteins". Cell. 112 (2): 151–155. doi:10.1016/s0092-8674(03)00033-3. PMID 12553904. S2CID 17261901.
  9. ^ Baretić D, Williams RL (2014). "PIKKs--the solenoid nest where partners and kinases meet". Curr. Opin. Struct. Biol. 29: 134–142. doi:10.1016/j.sbi.2014.11.003. PMID 25460276.
  10. ^ Ohkura, Hiroyuki; Garcia, Miguel A.; Toda, Takashi (1 November 2001). "Dis1/TOG universal microtubule adaptors - one MAP for all?". Journal of Cell Science. 114 (21): 3805–3812. doi:10.1242/jcs.114.21.3805. PMID 11719547.
  11. ^ Al-Bassam J, Kim H, Brouhard G, van Oijen A, Harrison SC, Chang F (2010). "CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule". Dev. Cell. 19 (2): 245–258. doi:10.1016/j.devcel.2010.07.016. PMC 3156696. PMID 20708587.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  12. ^ Xu Y, Xing Y, Chen Y, Chao Y, Lin Z, Fan E, Yu JW, Strack S, Jeffrey PD, Shi Y (2006). "Structure of the protein phosphatase 2A holoenzyme". Cell. 127 (6): 1239–1251. doi:10.1016/j.cell.2006.11.033. PMID 17174897. S2CID 18584536.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  13. ^ Cho US, Xu W (2007). "Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme". Nature. 445 (7123): 53–57. Bibcode:2007Natur.445...53C. doi:10.1038/nature05351. PMID 17086192. S2CID 4408160.
  14. ^ Goldenberg SJ, Cascio TC, Shumway SD, Garbutt KC, Liu J, Xiong Y, Zheng N (2004). "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases". Cell. 119 (4): 517–528. doi:10.1016/j.cell.2004.10.019. PMID 15537541. S2CID 1606360.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  15. ^ Takagi K, Kim S, Yukii H, Ueno M, Morishita R, Endo Y, Kato K, Tanaka K, Saeki Y, Mizushima T (2012). "Structural basis for specific recognition of Rpt1p, an ATPase subunit of 26 S proteasome, by proteasome-dedicated chaperone Hsm3p". J. Biol. Chem. 287 (15): 12172–12182. doi:10.1074/jbc.M112.345876. PMC 3320968. PMID 22334676.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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  17. ^ Chook YM, Blobel G (1999). "Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp". Nature. 399 (6733): 230–237. doi:10.1038/20375. PMID 10353245. S2CID 4413233.
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  23. ^ Stuwe T, Lin DH, Collins LN, Hurt E, Hoelz A (2014). "Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins". Proc. Natl. Acad. Sci. 111 (7): 2530–2535. Bibcode:2014PNAS..111.2530S. doi:10.1073/pnas.1311081111. PMC 3932873. PMID 24505056.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  24. ^ Scheer E, Delbac F, Tora L, Moras D, Romier C (2012). "TFIID TAF6-TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 protein". J. Biol. Chem. 287 (33): 27580–27592. doi:10.1074/jbc.M112.379206. PMC 3431708. PMID 22696218.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  25. ^ Wollmann P, Cui S, Viswanathan R, Berninghausen O, Wells MN, Moldt M, Witte G, Butryn A, Wendler P, Beckmann R, Auble DT, Hopfner KP (2011). "Structure and mechanism of the Swi2/Snf2 remodeller Mot1 in complex with its substrate TBP". Nature. 475 (7356): 403–407. doi:10.1038/nature10215. PMC 3276066. PMID 21734658.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  26. ^ Blattner C, Jennebach S, Herzog F, Mayer A, Cheung AC, Witte G, Lorenzen K, Hopfner KP, Heck AJ, Aebersold R, Cramer P (2011). "Molecular basis of Rrn3-regulated RNA polymerase I initiation and cell growth". Genes Dev. 25 (19): 2093–2105. doi:10.1101/gad.17363311. PMC 3197207. PMID 21940764.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  27. ^ Andersen CB, Becker T, Blau M, Anand M, Halic M, Balar B, Mielke T, Boesen T, Pedersen JS, Spahn CM, Kinzy TG, Andersen GR, Beckmann R (2006). "Structure of eEF3 and the mechanism of transfer RNA release from the E-site". Nature. 443 (7112): 663–668. Bibcode:2006Natur.443..663A. doi:10.1038/nature05126. hdl:11858/00-001M-0000-0010-8377-7. PMID 16929303. S2CID 14994883.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  28. ^ Marcotrigiano J, Lomakin IB, Sonenberg N, Pestova TV, Hellen CU, Burley SK (2001). "A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery". Mol. Cell. 7 (1): 193–203. doi:10.1016/s1097-2765(01)00167-8. PMID 11172724.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  29. ^ Nozawa K, Ishitani R, Yoshihisa T, Sato M, Arisaka F, Kanamaru S, Dohmae N, Mangroo D, Senger B, Becker HD, Nureki O (2013). "Crystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasm". Nucleic Acids Res. 41 (6): 3901–3914. doi:10.1093/nar/gkt010. PMC 3616705. PMID 23396276.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  30. ^ Sibanda BL, Chirgadze DY, Blundell TL (2010). "Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats". Nature. 463 (7277): 118–121. doi:10.1038/nature08648. PMC 2811870. PMID 20023628.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  31. ^ Kowal P, Gurtan AM, Stuckert P, D'Andrea AD, Ellenberger T (2007). "Structural determinants of human FANCF protein that function in the assembly of a DNA damage signaling complex". J. Biol. Chem. 282 (3): 2047–2055. doi:10.1074/jbc.M608356200. PMID 17082180.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  32. ^ Rubinson EH, Gowda AS, Spratt TE, Gold B, Eichman BF (2010). "An unprecedented nucleic acid capture mechanism for excision of DNA damage". Nature. 468 (7322): 406–411. Bibcode:2010Natur.468..406R. doi:10.1038/nature09428. PMC 4160814. PMID 20927102.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  33. ^ Takai H, Xie Y, de Lange T, Pavletich NP (2010). "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes". Genes Dev. 24 (18): 2019–2030. doi:10.1101/gad.1956410. PMC 2939364. PMID 20801936.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  34. ^ Hara K, Zheng G, Qu Q, Liu H, Ouyang Z, Chen Z, Tomchick DR, Yu H (2014). "Structure of cohesin subcomplex pinpoints direct shugoshin-Wapl antagonism in centromeric cohesion". Nat. Struct. Mol. Biol. 21 (10): 864–870. doi:10.1038/nsmb.2880. PMC 4190070. PMID 25173175.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  35. ^ Roig MB, Löwe J, Chan KL, Beckouët F, Metson J, Nasmyth K (2014). "Structure and function of cohesin's Scc3/SA regulatory subunit". FEBS Lett. 588 (20): 3692–3702. doi:10.1016/j.febslet.2014.08.015. PMC 4175184. PMID 25171859.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  36. ^ Li Y, Muir K, Bowler MW, Metz J, Haering CH, Panne D (2018). "Structural basis for Scc3-dependent cohesin recruitment to chromatin". eLife. 7: e38356. doi: 10.7554/eLife.38356. doi:10.7554/eLife.38356. PMC 6120753. PMID 30109982.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  37. ^ Chatterjee A, Zakian S, Hu XW, Singleton MR (2013). "Structural insights into the regulation of cohesion establishment by Wpl1". EMBO J. 32 (5): 677–687. doi:10.1038/emboj.2013.16. PMC 3590988. PMID 23395900.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  38. ^ Ouyang Z, Zheng G, Song J, Borek DM, Otwinowski Z, Brautigam CA, Tomchick DR, Rankin S, Yu H (2013). "Structure of the human cohesin inhibitor Wapl". Proc. Natl. Acad. Sci. USA. 110 (28): 11355–11360. Bibcode:2013PNAS..11011355O. doi:10.1073/pnas.1304594110. PMC 3710786. PMID 23776203.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  39. ^ Muir KW, Kschonsak M, Li Y, Metz J, Haering CH, Panne D. (2016). "Structure of the Pds5-Scc1 complex and implications for cohesin function". Cell Rep. 14 (9): 2116–2126. doi:10.1016/j.celrep.2016.01.078. PMID 26923589.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  40. ^ Lee BG, Roig MB, Jansma M, Petela N, Metson J, Nasmyth K, Löwe J (2016). "Crystal structure of the cohesin gatekeeper Pds5 and in complex with kleisin Scc1". Cell Rep. 14 (9): 2108–2115. doi:10.1016/j.celrep.2016.02.020. PMC 4793087. PMID 26923598.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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HEAT repeat Provide feedback

The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see PF00514).

Literature references

  1. Andrade MA, Bork P; , Nat Genet 1995;11:115-116.: HEAT repeats in the Huntington's disease protein. PUBMED:7550332 EPMC:7550332

  2. Groves MR, Hanlon N, Turowski P, Hemmings BA, Barford D; , Cell 1999;96:99-110.: The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. PUBMED:9989501 EPMC:9989501


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000357

The HEAT repeat is a tandemly repeated, 37-47 amino acid long module occurring in a number of cytoplasmic proteins, including the four name-giving proteins huntingtin, elongation factor 3 (EF3), the 65 Kd alpha regulatory subunit of protein phosphatase 2A (PP2A) and the yeast PI3-kinase TOR1 [ PUBMED:7550332 ]. Arrays of HEAT repeats consists of 3 to 36 units forming a rod-like helical structure and appear to function as protein-protein interaction surfaces. It has been noted that many HEAT repeat-containing proteins are involved in intracellular transport processes.

In the crystal structure of PP2A PR65/A [ PUBMED:9989501 ], the HEAT repeats consist of pairs of antiparallel alpha helices [ PUBMED:7550332 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan TPR (CL0020), which has the following description:

Tetratricopeptide-like repeats are found in a numerous and diverse proteins involved in such functions as cell cycle regulation, transcriptional control, mitochondrial and peroxisomal protein transport, neurogenesis and protein folding.

The clan contains the following 252 members:

14-3-3 AAR2 Aconitase_B_N Adaptin_N Alkyl_sulf_dimr ANAPC3 ANAPC5 ANAPC8 Apc1_MidN APC_rep API5 Aquarius_N Arm Arm_2 Arm_3 Arm_vescicular Atx10homo_assoc B56 BAF250_C BRO1 BTAD CAS_CSE1 ChAPs CHIP_TPR_N CID CLASP_N Clathrin Clathrin-link Clathrin_H_link Clathrin_propel Cnd1 Cnd1_N Cnd3 CNOT1_CAF1_bind CNOT1_HEAT_N CNOT1_TTP_bind Coatomer_E Cohesin_HEAT Cohesin_load ComR_TPR COPI_C CPL CRM1_C CRM1_repeat CRM1_repeat_3 Cse1 CTK3 CTNNBL Cullin DHR-2_Lobe_A DHR-2_Lobe_C DIL DNA-PKcs_N DNA_alkylation DNAPKcs_CC1-2 DNAPKcs_CC3 DNAPKcs_CC5 Dopey_N Drf_FH3 Drf_GBD DUF1822 DUF2019 DUF2225 DUF3385 DUF3458_C DUF3730 DUF3856 DUF4042 DUF4704 DUF5071 DUF5106 DUF5588 DUF5691 DUF6340 DUF6377 DUF6584 DUF924 E_motif EAD11 eIF-3c_N ELMO_ARM EST1 EST1_DNA_bind FA_FANCE FANCF FANCI_HD1 FANCI_HD2 FANCI_S1 FANCI_S1-cap FANCI_S2 FANCI_S3 FANCI_S4 FAT Fes1 Fis1_TPR_C Fis1_TPR_N Focadhesin Foie-gras_1 GET4 GLE1 GUN4_N HAT HEAT HEAT_2 HEAT_EZ HEAT_PBS HEAT_UF HemY_N HMW1C_N HPS6_C HrpB1_HrpK HSM3_C HSM3_N Hyccin IBB IBN_N IFRD Iml2-TPR_39 Importin_rep Importin_rep_2 Importin_rep_3 Importin_rep_4 Importin_rep_5 Importin_rep_6 Insc_C Ints3_N KAP Kinetochor_Ybp2 Laa1_Sip1_HTR5 Leuk-A4-hydro_C LRV LRV_FeS MA3 Mad3_BUB1_I MAP3K_TRAF_bd MIF4G MIF4G_like MIF4G_like_2 MIX MMS19_C Mo25 MRP-S27 Mtf2 MUN NatA_aux_su Neurobeachin Neurochondrin Nic96 Nipped-B_C Not1 Nro1 NSF Paf67 ParcG PAT1 PC_rep PDS5 Peptidase_M9_N PHAT PI3Ka PknG_TPR PPP5 PPR PPR_1 PPR_2 PPR_3 PPR_long PPTA Proteasom_PSMB PUF PUL RAI16-like Rapsyn_N Rcd1 RIH_assoc RINT1_TIP1 RIX1 RNPP_C RPM2 RPN6_N RPN7 RYDR_ITPR Sel1 SHNi-TPR SIL1 SLT_L SNAP SPO22 SRP_TPR_like ST7 STAG Suf SusD-like SusD-like_2 SusD-like_3 SusD_RagB SYCP2_ARLD SYMPK_PTA1_N TAF1_subA TAF6_C TAL_effector TAP42 TAtT Tcf25 TIP120 TOM20_plant TPR-S TPR_1 TPR_10 TPR_11 TPR_12 TPR_14 TPR_15 TPR_16 TPR_17 TPR_18 TPR_19 TPR_2 TPR_20 TPR_21 TPR_22 TPR_3 TPR_4 TPR_5 TPR_6 TPR_7 TPR_8 TPR_9 TPR_MalT Tra1_ring TRF TTC7_N Type_III_YscG UNC45-central Upf2 Uso1_p115_head V-ATPase_H_C V-ATPase_H_N Vac14_Fab1_bd Vitellogenin_N Vps16_C Vps35 Vps39_1 VPS53_C W2 Wap1 WSLR Wzy_C_2 Xpo1 YcaO_C YfiO Zmiz1_N

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(424)
Full
(11597)
Representative proteomes UniProt
(18410)
RP15
(1904)
RP35
(4603)
RP55
(8685)
RP75
(11972)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(424)
Full
(11597)
Representative proteomes UniProt
(18410)
RP15
(1904)
RP35
(4603)
RP55
(8685)
RP75
(11972)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(424)
Full
(11597)
Representative proteomes UniProt
(18410)
RP15
(1904)
RP35
(4603)
RP55
(8685)
RP75
(11972)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Reference [2]
Previous IDs: none
Type: Repeat
Sequence Ontology: SO:0001068
Author: Griffiths-Jones SR
Number in seed: 424
Number in full: 11597
Average length of the domain: 30.60 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 3.45 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 17.6
Trusted cut-off 23.5 17.6
Noise cut-off 23.4 17.5
Model length: 31
Family (HMM) version: 25
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...

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Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HEAT domain has been found. There are 131 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0G2JV05 View 3D Structure Click here
A0A0P0W1W1 View 3D Structure Click here
A0A0R0ESB5 View 3D Structure Click here
A0A0R0GJS0 View 3D Structure Click here
A0A0R0JTN1 View 3D Structure Click here
A0A0R4IFI0 View 3D Structure Click here
A0A1D6E6C0 View 3D Structure Click here
A0A1D6F946 View 3D Structure Click here
A0A1D6HNA8 View 3D Structure Click here
A0A1D6IHP1 View 3D Structure Click here
A0A1D6J9Y7 View 3D Structure Click here
A0A1D6JIW5 View 3D Structure Click here
A0A1D6JWX6 View 3D Structure Click here
A0A1D6KE00 View 3D Structure Click here
A0A1D6L0X5 View 3D Structure Click here
A0A1D6LKF6 View 3D Structure Click here
A0A1D6ME19 View 3D Structure Click here
A0A1D6QC47 View 3D Structure Click here
A0A1D6QT92 View 3D Structure Click here
A0A1P8B4P1 View 3D Structure Click here
A0A286YB17 View 3D Structure Click here
A0A2R8QJE9 View 3D Structure Click here
A0A2R8RYR9 View 3D Structure Click here
A0A2R8RZX0 View 3D Structure Click here
A4HT97 View 3D Structure Click here
A4HWJ0 View 3D Structure Click here
A5PMV7 View 3D Structure Click here
A7E2Y6 View 3D Structure Click here
A8WFS2 View 3D Structure Click here
B3CJ34 View 3D Structure Click here
B8A5E7 View 3D Structure Click here
B8ARW2 View 3D Structure Click here
B8JHR9 View 3D Structure Click here
B9FDR3 View 3D Structure Click here
C0P3E1 View 3D Structure Click here
D2I4M3 View 3D Structure Click here
D3ZDU2 View 3D Structure Click here
D3ZSM9 View 3D Structure Click here
D4A2D7 View 3D Structure Click here
D4A781 View 3D Structure Click here