Summary: TAL effector repeat
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TAL effector Edit Wikipedia article
TAL (transcription activator-like) effectors (often referred to as TALEs but not to be confused with the three amino acid loop extension family of proteins) are proteins secreted by Xanthomonas bacteria via their type III secretion system when they infect various plant species. These proteins can bind promoter sequences in the host plant and activate the expression of plant genes that aid bacterial infection. They recognize plant DNA sequences through a central repeat domain consisting of a variable number of ~34 amino acid repeats. There appears to be a one-to-one correspondence between the identity of two critical amino acids in each repeat and each DNA base in the target sequence. These proteins are interesting to researchers both for their role in disease of important crop species and the relative ease of retargeting them to bind new DNA sequences. Similar proteins can be found in the pathogenic bacterium Ralstonia solanacearum and Burkholderia rhizoxinica., as well as as yet unidentified marine microorganisms. The term TALE-likes is used to refer to the putative protein family encompassing the TALEs and these related proteins.
Function in plant pathogenesis
Xanthomonas are Gram-negative bacteria that can infect a wide variety of plant species including pepper, rice, citrus, cotton, tomato, and soybeans. Some types of Xanthomonas cause localized leaf spot or leaf streak while others spread systemically and cause black rot or leaf blight disease. They inject a number of effector proteins, including TAL effectors, into the plant via their type III secretion system. TAL effectors have several motifs normally associated with eukaryotes including multiple nuclear localization signals and an acidic activation domain. When injected into plants, these proteins can enter the nucleus of the plant cell, bind plant promoter sequences, and activate transcription of plant genes that aid in bacterial infection. Plants have developed a defense mechanism against type III effectors that includes R (resistance) genes triggered by these effectors. Some of these R genes appear to have evolved to contain TAL-effector binding sites similar to site in the intended target gene. This competition between pathogenic bacteria and the host plant has been hypothesized to account for the apparently malleable nature of the TAL effector DNA binding domain.
The most distinctive characteristic of TAL effectors is a central repeat domain containing between 1.5 and 33.5 repeats that are usually 34 residues in length (the C-terminal repeat is generally shorter and referred to as a “half repeat”). A typical repeat sequence is LTPEQVVAIASHDGGKQALETVQRLLPVLCQAHG, but the residues at the 12th and 13th positions are hypervariable (these two amino acids are also known as the repeat variable diresidue or RVD). Two separate groups have shown that there is a simple relationship between the identity of these two residues in sequential repeats and sequential DNA bases in the TAL effector’s target site. The first group, headed by Adam Bogdanove, broke this code computationally by searching for patterns in protein sequence alignments and DNA sequences of target promoters. The second group deduced the code through molecular analysis of the TAL effector AvrBs3 and its target DNA sequence in the promoter of a pepper gene activated by AvrBs3. The experimentally validated code between RVD sequence and target DNA base can be expressed as NI = A, HD = C, NG = T, NN = R (G or A), and NS = N (A, C, G, or T). Further studies have shown that the RVD NK can target G, although TAL effector nucleases (TALEN) that exclusively use NK instead of NN to target G can be less active. The crystal structure of a TAL effector bound to DNA indicates that each repeat comprises two alpha helices and a short RVD-containing loop where the second residue of the RVD makes sequence-specific DNA contacts while the first residue of the RVD stabilizes the RVD-containing loop. Target sites of TAL effectors also tend to include a thymine flanking the 5’ base targeted by the first repeat; this appears to be due to a contact between this T and a conserved tryptophan in the region N-terminal of the central repeat domain. However, this "zero" position does not always contain a thymine, as some scaffolds are more permissive.
Engineering TAL effectors
This simple correspondence between amino acids in TAL effectors and DNA bases in their target sites makes them useful for protein engineering applications. Numerous groups have designed artificial TAL effectors capable of recognizing new DNA sequences in a variety of experimental systems. Such engineered TAL effectors have been used to create artificial transcription factors that can be used to target and activate or repress endogenous genes in tomato, Arabidopsis thaliana, and human cells.
Genetic constructs to encode TAL effector-based proteins can be made using either conventional gene synthesis or modular assembly. A plasmid kit for assembling custom TALEN® and other TAL effector constructs is available through the public, not-for-profit repository Addgene. Webpages providing access to public software, protocols, and other resources for TAL effector-DNA targeting applications include the TAL Effector-Nucleotide Targeter and taleffectors.com.
TAL effectors can induce susceptibility genes that are members of the NODULIN3 (N3) gene family. These genes are essential for the development of the disease. In rice two genes,Os-8N3 and Os-11N3, are induced by TAL effectors. Os-8N3 is induced by PthXo1 and Os-11N3 is induced by PthXo3 and AvrXa7. Two hypotheses exist about possible functions for N3 proteins:
- They are involved in copper transport, resulting in detoxification of the environment for bacteria. The reduction in copper level facilitates bacterial growth.
- They are involved in glucose transport, facilitating glucose flow. This mechanism provides nutrients to bacteria and stimulates pathogen growth and virulence
Engineered TAL effectors can also be fused to the cleavage domain of FokI to create TAL effector nucleases (TALEN) or to meganucleases (nucleases with longer recognition sites) to create "megaTALs." Such fusions share some properties with zinc finger nucleases and may be useful for genetic engineering and gene therapy applications.
TALEN-based approaches are used in the emerging fields of gene editing and genome engineering. TALEN fusions show activity in a yeast-based assay, at endogenous yeast genes, in a plant reporter assay, at an endogenous plant gene, at endogenous zebrafish genes, at an endogenous rat gene, and at endogenous human genes. The human HPRT1 gene has been targeted at detectable, but unquantified levels. In addition, TALEN constructs containing the FokI cleavage domain fused to a smaller portion of the TAL effector still containing the DNA binding domain have been used to target the endogenous NTF3 and CCR5 genes in human cells with efficiencies of up to 25%. TAL effector nucleases have also been used to engineer human embryonic stem cells and induced pluripotent stem cells (IPSCs) and to knock out the endogenous ben-1 gene in C. elegans.
- Heuer, H.; Yin, Y. -N.; Xue, Q. -Y.; Smalla, K.; Guo, J. -H. (2007). "Repeat Domain Diversity of avrBs3-Like Genes in Ralstonia solanacearum Strains and Association with Host Preferences in the Field". Applied and Environmental Microbiology 73 (13): 4379–4384. doi:10.1128/AEM.00367-07. PMC 1932761. PMID 17468277.
- Lixin Li; Ahmed Atef; Agnieszka Piatek; Zahir Ali; Marek Piatek; Mustapha Aouida; Altanbadralt Sharakuu; Ali Mahjoub; Guangchao Wang; Suhail Khan; Nina V Fedoroff; Jian-Kang Zhu; Magdy M Mahfouz (July 2013). "Characterization and DNA-binding specificities of Ralstonia TAL-like effectors". Molecular plant 6 (4): 1318–1330. doi:10.1093/mp/sst006. PMC 3716395. PMID 23300258.
- de Lange, Orlando; Christina Wolf; Jörn Dietze; Janett Elsaesser; Robert Morbitzer; Thomas Lahaye (2014). "Programmable DNA-binding proteins from Burkholderia provide a fresh perspective on the TALE-like repeat domain". Nucleic Acids Research 42 (11): 7436–49. doi:10.1093/nar/gku329. PMC 4066763. PMID 24792163.
- de Lange, Orlando; Wolf, Christina; Thiel, Philipp; Krüger, Jens; Kleusch, Christian; Kohlbacher, Oliver; Lahaye, Thomas (19 October 2015). "DNA-binding proteins from marine bacteria expand the known sequence diversity of TALE-like repeats". Nucleic Acids Research: gkv1053. doi:10.1093/nar/gkv1053.
- Boch J, Bonas U (September 2010). "XanthomonasAvrBs3 Family-Type III Effectors: Discovery and Function". Annual Review of Phytopathology 48: 419–36. doi:10.1146/annurev-phyto-080508-081936. PMID 19400638.
- Voytas DF, Joung JK (December 2009). "Plant science. DNA binding made easy". Science 326 (5959): 1491–2. Bibcode:2009Sci...326.1491V. doi:10.1126/science.1183604. PMID 20007890.
- Moscou MJ, Bogdanove AJ (December 2009). "A simple cipher governs DNA recognition by TAL effectors". Science 326 (5959): 1501. Bibcode:2009Sci...326.1501M. doi:10.1126/science.1178817. PMID 19933106.
- Boch J, Scholze H, Schornack S, et al. (December 2009). "Breaking the code of DNA binding specificity of TAL-type III effectors". Science 326 (5959): 1509–12. Bibcode:2009Sci...326.1509B. doi:10.1126/science.1178811. PMID 19933107.
- Morbitzer, R.; Romer, P.; Boch, J.; Lahaye, T. (2010). "Regulation of selected genome loci using de novo-engineered transcription activator-like effector (TALE)-type transcription factors". Proceedings of the National Academy of Sciences 107 (50): 21617–21622. Bibcode:2010PNAS..10721617M. doi:10.1073/pnas.1013133107. PMC 3003021. PMID 21106758.
- Miller, J. C.; Tan, S.; Qiao, G.; Barlow, K. A.; Wang, J.; Xia, D. F.; Meng, X.; Paschon, D. E.; Leung, E.; Hinkley, S. J.; Dulay, G. P.; Hua, K. L.; Ankoudinova, I.; Cost, G. J.; Urnov, F. D.; Zhang, H. S.; Holmes, M. C.; Zhang, L.; Gregory, P. D.; Rebar, E. J. (2010). "A TALE nuclease architecture for efficient genome editing". Nature Biotechnology 29 (2): 143–148. doi:10.1038/nbt.1755. PMID 21179091.
- Huang, P.; Xiao, A.; Zhou, M.; Zhu, Z.; Lin, S.; Zhang, B. (2011). "Heritable gene targeting in zebrafish using customized TALENs". Nature Biotechnology 29 (8): 699–700. doi:10.1038/nbt.1939.
- Mak, A. N. -S.; Bradley, P.; Cernadas, R. A.; Bogdanove, A. J.; Stoddard, B. L. (2012). "The Crystal Structure of TAL Effector PthXo1 Bound to Its DNA Target". Science 335: 716–719. doi:10.1126/science.1216211.
- Deng, D.; Yan, C.; Pan, X.; Mahfouz, M.; Wang, J.; Zhu, J. -K.; Shi, Y.; Yan, N. (2012). "Structural Basis for Sequence-Specific Recognition of DNA by TAL Effectors". Science 335: 720–3. doi:10.1126/science.1215670. PMC 3586824. PMID 22223738.
- Stella, Stefano; Molina, Rafael; Yefimenko, Igor; Prieto, Jesús; Silva, George; Bertonati, Claudia; Juillerat, Alexandre; Duchateau, Phillippe; Montoya, Guillermo (2013-09-01). "Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism". Acta Crystallographica Section D 69 (Pt 9): 1707–1716. doi:10.1107/S0907444913016429. ISSN 1399-0047. PMC 3760130. PMID 23999294.
- Christian M, Cermak T, Doyle EL, et al. (July 2010). "TAL Effector Nucleases Create Targeted DNA Double-strand Breaks". Genetics 186 (2): 757–61. doi:10.1534/genetics.110.120717. PMC 2942870. PMID 20660643.
- Zhang, F.; Cong, L.; Lodato, S.; Kosuri, S.; Church, G. M.; Arlotta, P. (2011). "Efficient construction of sequence-specific TAL effectors for modulating mammalian transcription". Nature Biotechnology 29 (2): 149–53. doi:10.1038/nbt.1775. PMC 3084533. PMID 21248753.
- Mahfouz, M. M.; Li, L.; Shamimuzzaman, M.; Wibowo, A.; Fang, X.; Zhu, J. -K. (2011). "De novo-engineered transcription activator-like effector (TALE) hybrid nuclease with novel DNA binding specificity creates double-strand breaks". Proceedings of the National Academy of Sciences 108 (6): 2623–8. doi:10.1073/pnas.1019533108. PMC 3038751. PMID 21262818.
- Cong, Le; Ruhong Zhou; Yu-chi Kuo; Margaret Cunniff; Feng Zhang (24 July 2012). "Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains". Nature Communications. 968 3 (7): 968. Bibcode:2012NatCo...3E.968C. doi:10.1038/ncomms1962. PMID 22828628.
- Geiβler, R.; Scholze, H.; Hahn, S.; Streubel, J.; Bonas, U.; Behrens, S. E.; Boch, J. (2011). Shiu, Shin-Han, ed. "Transcriptional Activators of Human Genes with Programmable DNA-Specificity". PLoS ONE 6 (5): e19509. doi:10.1371/journal.pone.0019509. PMC 3098229. PMID 21625585.
- Li, T.; Huang, S.; Zhao, X.; Wright, D. A.; Carpenter, S.; Spalding, M. H.; Weeks, D. P.; Yang, B. (2011). "Modularly assembled designer TAL effector nucleases for targeted gene knockout and gene replacement in eukaryotes". Nucleic Acids Research 39: 6315–6325. doi:10.1093/nar/gkr188.
- Cermak, T.; Doyle, E. L.; Christian, M.; Wang, L.; Zhang, Y.; Schmidt, C.; Baller, J. A.; Somia, N. V.; Bogdanove, A. J.; Voytas, D. F. (2011). "Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting". Nucleic Acids Research 39 (12): e82. doi:10.1093/nar/gkr218. PMC 3130291. PMID 21493687.
- Morbitzer, R.; Elsaesser, J.; Hausner, J.; Lahaye, T. (2011). "Assembly of custom TALE-type DNA binding domains by modular cloning". Nucleic Acids Research 39: 5790–5799. doi:10.1093/nar/gkr151.
- Weber, E.; Gruetzner, R.; Werner, S.; Engler, C.; Marillonnet, S. (2011). Bendahmane, Mohammed, ed. "Assembly of Designer TAL Effectors by Golden Gate Cloning". PLoS ONE 6 (5): e19722. doi:10.1371/journal.pone.0019722.
- Sanjana, N. E.; Cong, L.; Zhou, Y.; Cunniff, M. M.; Feng, G.; Zhang, F. (2012). "A transcription activator-like effector toolbox for genome engineering". Nature Protocols 7 (1): 171–192. doi:10.1038/nprot.2011.431. PMID 22222791.
- Boissel, Sandrine; Jarjour, Jordan; Astrakhan, Alexander; Adey, Andrew; Gouble, Agnès; Duchateau, Philippe; Shendure, Jay; Stoddard, Barry L.; Certo, Michael T. (2014-02-01). "megaTALs: a rare-cleaving nuclease architecture for therapeutic genome engineering". Nucleic Acids Research 42 (4): 2591–2601. doi:10.1093/nar/gkt1224. ISSN 1362-4962. PMC 3936731. PMID 24285304.
- Laura DeFrancesco (2011). "Move over ZFNs". Nature Biotechnology 29 (8): 681–684. doi:10.1038/nbt.1935.
- Li T, Huang S, Jiang WZ, et al. (August 2010). "TAL nucleases (TALNs): hybrid proteins composed of TAL effectors and FokI DNA-cleavage domain". Nucleic Acids Res 39 (1): 359–72. doi:10.1093/nar/gkq704. PMC 3017587. PMID 20699274.
- Sander, J. D.; Cade, L.; Khayter, C.; Reyon, D.; Peterson, R. T.; Joung, J. K.; Yeh, J. R. J. (2011). "Targeted gene disruption in somatic zebrafish cells using engineered TALENs". Nature Biotechnology 29 (8): 697–698. doi:10.1038/nbt.1934.
- Tesson, L.; Usal, C.; Ménoret, S. V.; Leung, E.; Niles, B. J.; Remy, S. V.; Santiago, Y.; Vincent, A. I.; Meng, X.; Zhang, L.; Gregory, P. D.; Anegon, I.; Cost, G. J. (2011). "Knockout rats generated by embryo microinjection of TALENs". Nature Biotechnology 29 (8): 695–696. doi:10.1038/nbt.1940. PMID 21822240.
- Hockemeyer, D.; Wang, H.; Kiani, S.; Lai, C. S.; Gao, Q.; Cassady, J. P.; Cost, G. J.; Zhang, L.; Santiago, Y.; Miller, J. C.; Zeitler, B.; Cherone, J. M.; Meng, X.; Hinkley, S. J.; Rebar, E. J.; Gregory, P. D.; Urnov, F. D.; Jaenisch, R. (2011). "Genetic engineering of human pluripotent cells using TALE nucleases". Nature Biotechnology 29 (8): 731–734. doi:10.1038/nbt.1927. PMC 3152587. PMID 21738127.
- Wood, A. J.; Lo, T. -W.; Zeitler, B.; Pickle, C. S.; Ralston, E. J.; Lee, A. H.; Amora, R.; Miller, J. C.; Leung, E.; Meng, X.; Zhang, L.; Rebar, E. J.; Gregory, P. D.; Urnov, F. D.; Meyer, B. J. (2011). "Targeted Genome Editing Across Species Using ZFNs and TALENs". Science 333 (6040): 307. doi:10.1126/science.1207773. PMC 3489282. PMID 21700836.
- TALengineering.org A comprehensive, publicly available resource for engineered TAL effector technology
- TALengineering newsgroup Newsgroup for discussion of engineered TAL effector technology
- Boch & Schornack. "ISMPMIReporter1001". International Society for Molecular Plant-Microbe Interactions. Retrieved 2010.
- www.taleffectors.com An open resource for TAL effector constructs
- Life Technologies A TAL effector commercial supplier
- PDB Molecule of the Month An entry in the Protein Database's monthly structural highlight
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
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Bai J, Choi SH, Ponciano G, Leung H, Leach JE; , Mol Plant Microbe Interact 2000;13:1322-1329.: Xanthomonas oryzae pv. oryzae avirulence genes contribute differently and specifically to pathogen aggressiveness. PUBMED:11106024 EPMC:11106024
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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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 132 members:Adaptin_N Alkyl_sulf_dimr ANAPC3 ANAPC5 API5 Arm Arm_2 Arm_3 B56 BTAD CAS_CSE1 ChAPs CLASP_N Clathrin Clathrin-link Clathrin_H_link Clathrin_propel Cnd1 Cnd3 Coatomer_E Cohesin_HEAT Cohesin_load COPI_C CRM1_C Cse1 DNA_alkylation Drf_FH3 Drf_GBD DUF1822 DUF2019 DUF2225 DUF3385 DUF3458 DUF3808 DUF3856 DUF4042 DUF924 EST1 EST1_DNA_bind FAT Fis1_TPR_C Fis1_TPR_N Foie-gras_1 GUN4_N HAT HEAT HEAT_2 HEAT_EZ HEAT_PBS HemY_N IBB IBN_N IFRD KAP Leuk-A4-hydro_C LRV LRV_FeS MA3 MIF4G MIF4G_like MIF4G_like_2 Mo25 MRP-S27 NARP1 Neurochondrin Nipped-B_C Nro1 NSF Paf67 ParcG PC_rep PHAT PI3Ka PknG_TPR PPP5 PPR PPR_1 PPR_2 PPR_3 PPR_long PPTA Proteasom_PSMB PUF Rab5-bind Rapsyn_N RPN7 Sel1 SHNi-TPR SNAP SPO22 SRP_TPR_like ST7 Suf SusD SusD-like SusD-like_2 SusD-like_3 TAF6_C TAL_effector TAtT Tcf25 TIP120 TOM20_plant 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_3 TPR_4 TPR_5 TPR_6 TPR_7 TPR_8 TPR_9 Upf2 V-ATPase_H_C V-ATPase_H_N Vac14_Fab1_bd Vitellogenin_N Vps39_1 W2 Xpo1 YfiO
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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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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.
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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.
|Seed source:||Pfam-B_3936 (release 6.6)|
|Author:||Mifsud W, Bateman A|
|Number in seed:||31|
|Number in full:||363|
|Average length of the domain:||32.70 aa|
|Average identity of full alignment:||68 %|
|Average coverage of the sequence by the domain:||56.36 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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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 More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
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The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
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The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
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.
There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 TAL_effector domain has been found. There are 574 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 seqence.
Loading structure mapping...