Summary: Tudor domain
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Tudor domain
| Structure of a TUDOR domain. | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | TUDOR | ||||||||
| Pfam | PF00567 | ||||||||
| Pfam clan | CL0049 | ||||||||
| InterPro | IPR008191 | ||||||||
| SMART | TUDOR | ||||||||
| PROSITE | PDOC50304 | ||||||||
| SCOP | 3fdr | ||||||||
| SUPERFAMILY | 3fdr | ||||||||
| CDD | cd04508 | ||||||||
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In molecular biology a tudor domain is a conserved protein structural motif originally identified as a region of 50 amino acids found in the Tudor protein encoded in Drosophila. The structurally characterized Tudor domain in human SMN (survival of motor neuron) is a strongly bent anti-parallel β-sheet consisting of five β-strands with a barrel-like fold and recognizes symmetrically dimethylated arginine.[1]
The proteins TP53BP1 (Tumor suppressor p53-binding protein 1) and its fission yeast homolog Crb2[2] and JMJD2A (Jumonji domain containing 2A) contain either tandem or double Tudor domains and recognize methylated histones.[3][4]
Other tudor domain containing proteins include AKAP1 (A-kinase anchor protein 1)[5] and ARID4A (AT rich interactive domain 4A) among others. A well known Tudor domain containing protein is Staphylococcal Nuclease Domain Containing 1 (SND1)/Tudor-SN/p100 co activator.[6] SND1 is involved in RISC complex and interacts with AEG-1 oncogene.[7] SND1 is also acts as an oncogene and plays very important role in HCC and colon cancer.[8] The SND1 tudor domain binds to methylated arginine in the PIWIL1 protein.[9]Tudor containing SND1 promotes tumor angiogenesis in human hepatocellular carcinoma through a novel pathway which involves NF-kappaB and miR-221.[10] Tudor SND1 is also present in the Drosophila melanogaster. [11]
[edit] References
- ^ Sprangers R, Groves MR, Sinning I, Sattler M (March 2003). "High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues". J. Mol. Biol. 327 (2): 507–20. doi:10.1016/S0022-2836(03)00148-7. PMID 12628254.
- ^ Botuyan MV, Lee J, Ward IM, et al. (December 2006). "Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair". Cell 127 (7): 1361–73. doi:10.1016/j.cell.2006.10.043. PMC 1804291. PMID 17190600. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1804291.
- ^ Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM (May 2006). "Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A". Science 312 (5774): 748–51. doi:10.1126/science.1125162. PMID 16601153.
- ^ Lee J, Thompson JR, Botuyan MV, Mer G (January 2008). "Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor". Nat. Struct. Mol. Biol. 15 (1): 109–11. doi:10.1038/nsmb1326. PMC 2211384. PMID 18084306. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2211384.
- ^ Rogne M, Landsverk HB, Van Eynde A, et al. (December 2006). "The KH-Tudor domain of a-kinase anchoring protein 149 mediates RNA-dependent self-association". Biochemistry 45 (50): 14980–9. doi:10.1021/bi061418y. PMID 17154535.
- ^ Caudy AA, Ketting RF, Hammond SM, Denli AM, Bathoorn AM, Tops BB, Silva JM, Myers MM, Hannon GJ, Plasterk RH (September 2003). "A micrococcal nuclease homologue in RNAi effector complexes". Nature 425 (6956): 411–4. doi:10.1038/nature01956. PMID 14508492.
- ^ Yoo BK, Santhekadur PK, Gredler R, Chen D, Emdad L, Bhutia S, Pannell L, Fisher PB, Sarkar D (2011). "Increased RNA-induced silencing complex (RISC) activity contributes to hepatocellular carcinoma". Hepatology 53 (5): 1538–48. doi:10.1002/hep.24216. PMC 3081619. PMID 21520169. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3081619.
- ^ Yoo BK, Emdad L, Lee SG, Su ZZ, Santhekadur P, Chen D, Gredler R, Fisher PB, Sarkar D (April 2011). "Astrocyte elevated gene-1 (AEG-1): A multifunctional regulator of normal and abnormal physiology". Pharmacol. Ther. 130 (1): 1–8. doi:10.1016/j.pharmthera.2011.01.008. PMC 3043119. PMID 21256156. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3043119.
- ^ Liu K, Chen C, Guo Y, et al. (October 2010). "Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain". Proc. Natl. Acad. Sci. U.S.A. 107 (43): 18398–403. doi:10.1073/pnas.1013106107. PMC 2972943. PMID 20937909. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2972943.
- ^ Santhekadur PK, Das SK, Gredler R, et al. (April 2012). "Multifunction Protein Staphylococcal Nuclease Domain Containing 1 (SND1) Promotes Tumor Angiogenesis in Human Hepatocellular Carcinoma through Novel Pathway That Involves Nuclear Factor κB and miR-221". J. Biol. Chem. 287 (17): 13952–8. doi:10.1074/jbc.M111.321646. PMID 22396537.
- ^ Muying Ying, Dahua Chen (2012). "Tudor domain-containing proteins of Drosophila melanogaster.". Development, Growth & Differentiation.
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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.
Tudor domain
No Pfam abstract.
Literature references
-
Ponting CP; , Trends Biochem Sci 1997;22:51-52.: Tudor domains in proteins that interact with RNA. PUBMED:9048482
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Callebaut I, Mornon JP; , Biochem J 1997;321:125-132.: The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development. PUBMED:9003410
Clan
This family is a member of clan Tudor (CL0049), which has a total of 12 members.
External database links
| PANDIT: | PF00567 |
| Pseudofam: | PF00567 |
| SMART: | TUDOR |
| SYSTERS: | TUDOR |
This tab holds annotation information from the InterPro database.
InterPro entry IPR008191
There are multiple copies of this domain in the Drosophila melanogaster tudor protein and it has been identified in several RNA-binding proteins [PUBMED:9048482]. Although the function of this domain is unknown, in Drosophila melanogaster the tudor protein is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation [PUBMED:9003410].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 Tudor (CL0049), which contains the following 12 members:
53-BP1_Tudor 7kD_DNA_binding Agenet Chromo Chromo_shadow DUF1325 MBT PWWP Rad9_Rad53_bind SMN TUDOR Tudor-knotAlignments
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External links
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Trees
This page displays the phylogenetic tree for this family. 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 or full alignments.
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Curation and family details
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Curation
| Seed source: | Alignment kindly provided by SMART |
| Previous IDs: | none |
| Type: | Domain |
| Author: | SMART |
| Number in seed: | 48 |
| Number in full: | 1819 |
| Average length of the domain: | 118.20 aa |
| Average identity of full alignment: | 18 % |
| Average coverage of the sequence by the domain: | 9.75 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 122 | ||||||||||||
| Family (HMM) version: | 19 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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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 TUDOR domain has been found. There are 12 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.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence