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Search results 4401 to 4500 out of 202262 for *

Category restricted to OntologyTerm (x)

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Categories

Category: OntologyTerm
Type Details Score
Ontology Term  
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Ontology Term
Description: This presumed domain is found at the C-terminus of lariat debranching enzyme. This domain is always found in association with Pfam:PF00149.
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Description: NULL
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Description: The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function [1].
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Description: This Pfam entry includes some of the AAA proteins not detected by the Pfam:PF00004 model.
Ontology Term
Description: This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, Pfam:PF00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly [1]. The domain is associated with two Clp_N, Pfam:PF02861, at the N-terminus as well as AAA, Pfam:PF00004 and AAA_2, Pfam:PF07724.
Ontology Term
Description: This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site [1]. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another [2,3].
Ontology Term
Description: CHD proteins (name derived from the presence of a Chromodomain, SWI2/SNF2 ATPase/Helicase and a motif with sequence similarity to a DNA)binding domain) are ATP-dependent chromatin remodelers found in plant and animals. In eukaryotes, there are three subfamilies, I, II and III. This domain is found in members of subfamily II which play a role in repression of genes involved in developmental regulation, including Mi-2 from Drosophila melanogaster, CHD3/4/5 from animals and PICKLE (a CHD3/4-related protein) from Arabidopsis. Sequence analysis revealed that this domain has a considerable similarity to SANT domains suggesting that it fold into this type of domain and it is integral to the DNA binding domain of CHD remodelers in subfamily II [1].
Ontology Term
Description: This domain is found in chromatin remodelling factors (CHDs) from subfamily II [1] including CHD3/4/5 from animals and PICKLE. from Arabidopsis. The exact function is, as yet, unknown.
Ontology Term
Description: The CHDCT2 C-terminal domain is found in PHD/RING finger and chromo domain-associated CHD-like helicases [1].
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Description: NULL
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Description: This family comprises sequences bearing significant similarity to the mouse transcriptional regulator protein HCNGP (Swiss:Q02614). This protein is localised to the nucleus and is thought to be involved in the regulation of beta-2-microglobulin genes.
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Description: Covalent intermediates between topoisomerase I and DNA can become dead-end complexes that lead to cell death. Tyrosyl-DNA phosphodiesterase can hydrolyse the bond between topoisomerase I and DNA [1].
Ontology Term
Description: This presumed domain is named after Emsy N Terminus (ENT). Emsy is a protein that is amplified in breast cancer and interacts with BRCA2. The N terminus of this protein is found to be similar to other vertebrate and plant proteins of unknown function. This domain has a completely conserved histidine residue that may be functionally important.
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Description: This family includes only cysteinyl tRNA synthetases.
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Description: This is the beta-sandwich domain found in ER membrane protein complex subunit 7 (EMC7) [1,2], which is an integral membrane component of the EMC. EMC is widely conserved and involved in membrane protein biogenesis. It mediates the insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins in an energy-independent manner, both post-translational insertions of tail-anchored proteins and co-translational insertion of multipass membrane proteins [3,4]. This entry includes UPF0620 protein C83.10 from S. pombe, an orthologue of animal EMC7. This domain is also found in nodal modulators, which have been identified as part of a protein complex that participates in the nodal signalling pathway during vertebrate development [5].
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Description: This domain has a four-helix bundle structure. It contains four disulfide bonds, of which three function to keep the C- and N-terminal parts of the molecule in place [1].
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Description: Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in Pfam:PF00006
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Description: This family of proteins are eukaryotic RNA dependent RNA polymerases. These proteins are involved in post transcriptional gene silencing where they are thought to amplify dsRNA templates.
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Description: This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
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Description: KHA is the tetramerisation domain of eukaryotic voltage-dependent potassium ion-channel proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus.
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Description: TamB is an integral inner membrane protein that forms a complex - the translocation and assembly module or TAM [2] - with the outer membrane protein, TamA. TAM is responsible for the efficient secretion of the adhesin protein Ag43 in E.coli K-12 [1].
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Description: This domain, found in various hypothetical bacterial and eukaryotic metal-binding proteins is a probably zinc-ribbon.
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Description: This domain binds a light harvesting cofactor.
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Description: This eukaryotic protein is a component of the inner kinetochore subcomplex of the centromere. It has been shown to be involved in chromosome segregation via regulation of the spindle in both yeast and human [1][2].
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Description: The yeast SAGA complex is a multifunctional coactivator that regulates transcription by RNA polymerase II [1,2]. It is formed of five major modular subunits and shows a high degree of structural conservation to human TFTC and STAGA [3]. The complex can also be conceived of as consisting of two histone-fold-containing core subunits, and this family is one of these. As a family it is likely to carry binding regions for interactions with a number of the other components of the complex.
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Description: Peptidyl-tRNA hydrolases are enzymes that release tRNAs from peptidyl-tRNA during translation.
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Description: This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
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Description: RNases H are enzymes that specifically hydrolyse RNA when annealed to a complementary DNA and are present in all living organisms. In yeast RNase H2 is composed of a complex of three proteins (Rnh2Ap, Ydr279p and Ylr154p), this family represents the homologues of Ydr279p [1]. It is not known whether non yeast proteins in this family fulfil the same function.
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Description: The ChaC family of proteins function as gamma-glutamyl cyclotransferases acting specifically to degrade glutathione but not other gamma-glutamyl peptides [1, 2]. It is is conversed across all phyla and represents a new pathway for glutathione degradation in living cells.
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Description: GGACT, gamma-glutamylamine cyclotransferase, is a ubiquitous enzyme found in bacteria, plants, and metazoans from Dictyostelium through to humans. It converts gamma-glutamylamines to free amines and 5-oxoproline.
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Description: NULL
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Description: This family consists of several cofactor of BRCA1 (COBRA1) like proteins. It is thought that COBRA1 along with BRCA1 is involved in chromatin unfolding. COBRA1 is recruited to the chromosome site by the first BRCT repeat of BRCA1, and is itself sufficient to induce chromatin unfolding. BRCA1 mutations that enhance chromatin unfolding also increase its affinity for, and recruitment of, COBRA1. It is thought that that reorganisation of higher levels of chromatin structure is an important regulated step in BRCA1-mediated nuclear functions [1].
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Description: This family includes several uncharacterised proteins.
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Description: This family of heme binding proteins are found mainly in bacteria. However they can also be found in some protozoa and plants as well.
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