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Search results 2701 to 2800 out of 202262 for *

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Category: OntologyTerm
Type Details Score
Ontology Term  
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Description: NULL
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Description: Nicastrin and presenilin are two major components of the gamma-secretase complex, which executes the intramembrane proteolysis of type I integral membrane proteins such as the amyloid precursor protein (APP) and Notch. Nicastrin is synthesised in fibroblasts and neurons as an endoglycosidase-H-sensitive glycosylated precursor protein (immature nicastrin) and is then modified by complex glycosylation in the Golgi apparatus and by sialylation in the trans-Golgi network (mature nicastrin) [1]. A region featured in this family has a fold similar to human transferrin receptor (TfR, Swiss:P02786) and a bacterial aminopeptidase (Swiss:P80561). It is implicated in the pathogenesis of Alzheimer's disease [4].
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Description: This family consists of several plant proteins and includes RHO1, an interactor of the exocyst subunit Exo70A1 and has been shown to be required for seed coat mucilage deposition [1].
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Description: This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with Pfam:PF05057.
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Description: This domain is conserved from plants to humans. It is a signature protein motif found in components of CSN (COP9 signalosome) where it functions as a structural scaffold for subunit-subunit interactions within the complex and is a key regulator of photomorphogenic development [1]. It is found in Eukaryotic translation initiation factor 3 subunit K, a component of the eukaryotic translation initiation factor 3 (eIF-3) complex required for the initiation of protein synthesis [2]. It is also found in 26S proteasome non-ATPase regulatory subunit 8 (PSMD8), a regulatory subunit of the 26S proteasome [3].
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Description: Members of this family have very varied localisations within the eukaryotic cell. pinin is known to localise at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque [1]. SDK2/3 is a dynamically localised nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing [2]. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions [3].
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Description: This family represents a conserved region with eukaryotic lung seven transmembrane receptors and related proteins.
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Description: NULL
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Description: NULL
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Description: Members of this family are components of the mitotic spindle. It has been shown that Ndc80/HEC from yeast is part of a complex called the Ndc80p complex [1]. This complex is thought to bind to the microtubules of the spindle.
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Description: This family identifies a conserved region found in a number of plastid lipid-associated proteins (PAPs), and in a number of putative fibrillin proteins.
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Description: Members of this family are implicated in bringing cargo forward from the ER and binding to coat proteins by their cytoplasmic domains. This domain corresponds closely to the beta-strand rich GOLD domain described in [2]. The GOLD domain is always found combined with lipid- or membrane-association domains [2].
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Description: ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
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Description: This family contains a region from the common kinase core found in the type I phosphatidylinositol-4-phosphate 5-kinase (PIP5K) family as described in [1]. The family consists of various type I, II and III PIP5K enzymes. PIP5K catalyses the formation of phosphoinositol-4,5-bisphosphate via the phosphorylation of phosphatidylinositol-4-phosphate a precursor in the phosphinositide signaling pathway.
Ontology Term
Description: The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii [1]. It has been hypothesised to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton [1].
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Description: The RuvB protein makes up part of the RuvABC revolvasome which catalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein [1]. This family contains the N-terminal region of the protein.
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Description: NULL
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Description: The two associated zinc ions and the active site are entirely enclosed within the C-terminal catalytic domain in leucine aminopeptidase.
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Description: This family has been called SPFH [1], Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.
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Description: NULL
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Description: This domain represents the endonuclease region of retrotransposons from a range of bacteria, archaea and eukaryotes. These are enzymes largely from class EC:2.7.7.49.
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Description: This domain is found in plant proteins including THH1/TOM1/TOM3 from Arabidopsis. TOM1 and TOM3 are transmembrane proteins necessary for the efficient multiplication of tobamoviruses [1]. THH1 supports tobamovirus multiplication, but to a lesser extent than TOM1 and TOM3 [2]. Members containing this domain are part of the GPCR superfamily and involved in stress tolerance [3,4].
Ontology Term
Description: This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases [1,2]. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
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Description: Members of this family belong to glycosyl transferase family 20 [1]. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex, [2].
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Description: Iwr1 is involved in transcription from polymerase II promoters; it interacts with with most of the polymerase II subunits [3]. Deletion of this protein results in hypersensitivity to the K1 killer toxin [1].
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Description: This domain includes syntaxin-like domains including from the Vam3p protein [1].
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Description: NULL
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Description: NULL
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Description: This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognise a significant number of members.
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Description: NULL
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Description: The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
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Description: Members of this family of proteins may have a role in the beta-catenin-Tcf/Lef signaling pathway, as well as in the process of myelination of the central and peripheral nervous system. Defects in Hyccin are the cause of hypomyelination with congenital cataracts [MIM:610532]. This disorder is characterised by congenital cataracts, progressive neurologic impairment, and diffuse myelin deficiency. Affected individuals experience progressive pyramidal and cerebellar dysfunction, muscle weakness and wasting prevailing in the lower limbs [1][2].
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Description: This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines [2]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [3]. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [1]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
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Description: This family includes the vacuolar Fe2+/Mn2+ uptake transporter Swiss:P47818, Ccc1 [1] and the vacuolar iron transporter VIT1 Swiss:Q9ZUA5.
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Description: This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyse the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine [1][2].
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Description: This protein is found to be part of a large ribonucleoprotein complex containing the U3 snoRNA [1]. Depletion of the Utp proteins impedes production of the 18S rRNA, indicating that they are part of the active pre-rRNA processing complex. This large RNP complex has been termed the small subunit (SSU) processome [1].
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Description: This family is found in Bacteria and Streptophyta includes members such as NdhS (NAD(P)H-quinone oxidoreductase subunit S). NdhS, also known as CRR31 (chlororespiratory reduction 31), is a subunit of the chloroplast NADH dehydrogenase-like (NDH) complex [1]. It is also a subunit of the cyanobacterial NDH-1 complex [2] [3]. NAD(P)H-oxidizing subunits have not been found in chloroplasts or cyanobacteria, where ferredoxin is probably the electron donor. NdhS contributes to the formation of a ferredoxin binding site of NDH [1] and is necessary for high affinity binding of ferredoxin [4]. The cyanobacterial NDH-1 complex, also known as NADPH:plastoquinone oxidoreductase or type I NAD(P)H dehydrogenase, is involved in plastoquinone reduction and cyclic electron transfer (CET) around photosystem I. The chloroplast NDH is more similar to cyanobacterial NDH-1, which is believed to be the origin of chloroplast NDH, than to mitochondrial NADH dehydrogenase present in the same species [5] [6]. The NDH complexes of chloroplasts, however, contain many subunits that are absent from cyanobacterial NDH-1 complexes.
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Description: eIF5A, previously thought to be an initiation factor, has been shown to be required for peptide chain elongation in yeast [1].
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