Summary: NHL repeat
This is the Wikipedia entry entitled "NHL repeat". More...
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NHL repeat Edit Wikipedia article
|Structure of the brain tumor-Pumilio translation repressor complex.|
The NHL repeat, named after NCL-1, HT2A and Lin-41, is an amino acid sequence found largely in a large number of eukaryotic and prokaryotic proteins. For example, the repeat is found in a variety of enzymes of the copper type II, ascorbate-dependent monooxygenase family which catalyse the C-terminus alpha-amidation of biological peptides. In many it occurs in tandem arrays, for example in the RING finger beta-box, coiled-coil (RBCC) eukaryotic growth regulators. The 'Brain Tumor' protein (Brat) is one such growth regulator that contains a 6-bladed NHL-repeat beta-propeller.
The NHL repeats are also found in serine/threonine protein kinase (STPK) in diverse range of pathogenic bacteria. These STPK are transmembrane receptors with an intracellular N-terminal kinase domain and extracellular C-terminal sensor domain. In the STPK, PknD, from Mycobacterium tuberculosis, the sensor domain forms a rigid, six-bladed b-propeller composed of NHL repeats with a flexible tether to the transmembrane domain.
- Edwards TA, Wilkinson BD, Wharton RP, Aggarwal AK (October 2003). "Model of the brain tumor-Pumilio translation repressor complex". Genes Dev. 17 (20): 2508–2513. doi:10.1101/gad.1119403. PMC 218144. PMID 14561773. //www.ncbi.nlm.nih.gov/pmc/articles/PMC218144/.
- Kano S, Miyajima N, Fukuda S, Hatakeyama S (July 2008). "Tripartite motif protein 32 facilitates cell growth and migration via degradation of Abl-interactor 2". Cancer Res. 68 (14): 5572–5580. doi:10.1158/0008-5472.CAN-07-6231. PMID 18632609.
- Slack FJ, Ruvkun G (December 1998). "A novel repeat domain that is often associated with RING finger and B-box motifs". Trends Biochem. Sci. 23 (12): 474–5. doi:10.1016/S0968-0004(98)01299-7. PMID 9868369.
- Edwards TA, Pyle SE, Wharton RP, Aggarwal AK (April 2001). "Structure of Pumilio reveals similarity between RNA and peptide binding motifs". Cell 105 (2): 281–9. doi:10.1016/S0092-8674(01)00318-X. PMID 11336677.
NHL repeat Provide feedback
The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat PF00400. The repeats have a catalytic activity in P10731 proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localised to the repeats . Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats .
Husten EJ, Eipper BA; , J Biol Chem 1991;266:17004-17010.: The membrane-bound bifunctional peptidylglycine alpha-amidating monooxygenase protein. Exploration of its domain structure through limited proteolysis. PUBMED:1894599 EPMC:1894599
Fridell RA, Harding LS, Bogerd HP, Cullen BR; , Virology 1995;209:347-357.: Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. PUBMED:7778269 EPMC:7778269
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001258
The NHL repeat, named after NCL-1, HT2A and Lin-41, is found largely in a large number of eukaryotic and prokaryotic proteins. For example, the repeat is found in a variety of enzymes of the copper type II, ascorbate-dependent monooxygenase family which catalyse the C terminus alpha-amidation of biological peptides [PUBMED:1894599]. In many it occurs in tandem arrays, for example in the ringfinger beta-box, coiled-coil (RBCC) eukaryotic growth regulators [PUBMED:9868369]. The 'Brain Tumor' protein (Brat) is one such growth regulator that contains a 6-bladed NHL-repeat beta-propeller [PUBMED:14561773, PUBMED:11336677].
The NHL repeats are also found in serine/threonine protein kinase (STPK) in diverse range of pathogenic bacteria. These STPK are transmembrane receptors with a intracellular N-terminal kinase domain and extracellular C-terminal sensor domain. In the STPK, PknD, from Mycobacterium tuberculosis, the sensor domain forms a rigid, six-bladed b-propeller composed of NHL repeats with a flexible tether to the transmembrane domain.
|Molecular function||protein binding (GO:0005515)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
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EGFdomains, and finally a single
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Curation and family details
|Number in seed:||108|
|Number in full:||7067|
|Average length of the domain:||27.90 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||11.21 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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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 NHL domain has been found. There are 32 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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