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Search results 4201 to 4300 out of 202262 for *

Category restricted to OntologyTerm (x)

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Categories

Category: OntologyTerm
Type Details Score
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Description: NULL
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Description: NULL
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Description: Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)
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Description: NULL
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Description: This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
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Description: Members of this family catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 (Swiss:Q9HGN6) from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 (Swiss:P53720) acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD [1]. Some family members may be targeted to the mitochondria and even have a role in mitochondria [1].
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Description: NULL
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Description: NULL
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Description: This is a family of proteins that are flavin-dependent thymidylate synthases.
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Description: This domain is found at the N-terminus of member of the DUF761 family Pfam:PF05553. Many members are plant proteins.
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Description: NULL
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Description: COPI-coated vesicles function in retrograde transport from the Golgi to the ER, and in intra-Golgi transport. This is the platform subdomain of the coatomer gamma subunit appendage domain. It carries a protein-protein interaction site at UniProt:P53620, residue W776, which in yeast binds to the ARFGAP Glo3p, and in mammalian gamma-COP binds to a Glo3p orthologue, ARFGAP2 [1].
Ontology Term
Description: This eukaryotic family includes a number of plant organ-specific proteins. The predicted amino acid sequence suggests that these proteins could be exported and glycosylated [1]. Family members consist of an N-terminal region with no repeats and a C-terminal region which carries multiple tandem repeats. The N-terminal region ends before the repeats region and is defined as the area that extends from the end of the signal peptide to the start of the tandem repeat region. Its length varies considerably, ranging from 30 to 80 amino acids. Generally, these proteins vary in size where it is suggested that thirty-six percent of the sequences had fewer than 150 amino acids; 41% ranged from 150 to 250, and 23% had more than 250 amino acids. Accordingly, these proteins belong to category II of proteins having repeats in tandem; that is, those with the repeats ranging in length from 20 to 40 residues. The second region (C-terminal) in the mature protein is the tandem repeat oligopeptide area. The repeats start with a common hexapeptide (E/D)FEPRP and end with X4Y i .e. (D/E)FEPRPX4Y. Full-length sequences revealed considerable variability in the number of repeats, ranging from 2 to 17. The length of the repeats also varied, ranging from 12 amino acids to 34 amino acids [2].
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Description: PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested [2] to be involved in substrate presentation.
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Description: This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA [1].
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Description: Ribophorin I is an essential subunit of oligosaccharyltransferase (OST), which is also known as Dolichyl-diphosphooligosaccharide--protein glycosyltransferase, (EC:2.4.1.119). OST catalyses the transfer of an oligosaccharide from dolichol pyrophosphate to selected asparagine residues of nascent polypeptides as they are translocated into the lumen of the rough endoplasmic reticulum. Ribophorin I and OST48 are though to be responsible for OST catalytic activity [1]. Both yeast and mammalian proteins are glycosylated but the sites are not conserved. Glycosylation may contribute towards general solubility but is unlikely to be involved in a specific biochemical function [2] Most family members are predicted to have a transmembrane helix at the C terminus of this region.
Ontology Term
Description: The function of this domain is unknown, it does contain three conserved cysteines and a histidine, that suggests this may be a zinc binding domain (Bateman A pers. observation). This domain is found associated with CBS domains in some proteins Pfam:PF00571.
Ontology Term
Description: This family of proteins, found from plants to humans, is PRAT4 (A and B), a Protein Associated with Toll-like receptor 4. The Toll family of receptors - TLRs - plays an essential role in innate recognition of microbial products, the first line of defence against bacterial infection [1]. PRAT4A influences the subcellular distribution and the strength of TLR responses and alters the relative activity of each TLR. PRAT4B regulates TLR4 trafficking to the cell surface and the extent of its expression there [2][3]. TLR4 recognizes lipopolysaccharide (LPS), one of the most immuno-stimulatory glycolipids constituting the outer membrane of the Gram-negative bacteria. This family has also been described as a SAP-like MIR-interacting protein family.
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Description: This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.
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Description: The transmembrane protein Patched Swiss:P18502 is a receptor for the morphogene Sonic Hedgehog. This protein associates with the smoothened protein to transduce hedgehog signals.
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Description: This family represents a small conserved region within catalase enzymes (EC:1.11.1.6). All members also contain the Catalase family, Pfam:PF00199 domain. Catalase decomposes hydrogen peroxide into water and oxygen, serving to protect cells from its toxic effects [1]. This domain carries the immune-responsive amphipathic octa-peptide that is recognised by T cells [2].
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Description: NULL
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Description: It is clear from the structures of bacterial members of MaoC dehydratase, Pfam:PF01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerise to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.
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Description: This unusual 7-stranded beta-propeller domain protects the catalytic triad of prolyl oligopeptidase (see Pfam:PF00326), excluding larger peptides and proteins from proteolysis in the cytosol.
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Description: This domain is found in plant proteins of unknown function. It can be found in association with F-box domain Pfam:PF00646.
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Description: NULL
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Description: This domain is found to the C-terminus of a methyltransferase domain (Pfam:PF08241) in fungal and plant sterol methyltransferases [1].
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Description: Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.
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Description: NULL
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Description: This eukaryotic domain is found at the C-terminus of 26S proteasome regulatory subunits such as the non-ATPase Rpn3 subunit which is essential for proteasomal function [1]. It occurs together with the PCI/PINT domain (Pfam:PF01399).
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Description: This domain is closely related to Pfam:PF00043.
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Description: This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Ontology Term
Description: This region is always found associated with Pfam:PF02141. It is predicted to form a globular domain [1]. Although not statistically supported it has been suggested that this domain may be similar to members of the Rho/Rac/Cdc42 GEF family [1]. This N-terminal region of DENN folds into a longin module, consisting of a central antiparallel beta-sheet layered between helix H1 and helices H2 and H3 (strands S1-S5). Rab35 interacts with dDENN via residues in helix 1 and in the loop S3-S4 [2].
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Description: This domain is found in plants and higher eukaryotes, and is the N-terminal region of micro-spherule proteins which repress the transactivation activities of Nrf1 (p45 nuclear factor-erythroid 2 (p45 NF-E2)-related factor 1) [2]. In conjunction with DIPA the full-length protein acts as a transcription repressor [1]. The exact function of the region is not known.
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Description: This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to Pfam:PF00834.
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Description: This family of transporters has ten alpha helical transmembrane segments [1]. The structure of a bacterial homologue of SLAC1 shows it to have a trimeric arrangement. The pore is composed of five helices with a conserved Phe residue involved in gating. One homologue, Mae1 from the yeast Schizosaccharomyces pombe, functions as a malate uptake transporter; another, Ssu1 from Saccharomyces cerevisiae and other fungi including Aspergillus fumigatus, is characterised as a sulfite efflux pump; and TehA from Escherichia coli is identified as a tellurite resistance protein by virtue of its association in the tehA/tehB operon. In plants, this family is found in the stomatal guard cells functioning as an anion-transporting pore [2]. Many homologues are incorrectly annotated as tellurite resistance or dicarboxylate transporter (TDT) proteins.
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Description: Accurate transcription in vivo requires at least six general transcription initiation factors, in addition to RNA polymerase II. Transcription initiation factor IIF (TFIIF) is a tetramer of two beta subunits associate with two alpha subunits which interacts directly with RNA polymerase II. The beta subunit of TFIIF is required for recruitment of RNA polymerase II onto the promoter.
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