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Categories

Category: OntologyTerm
Type Details Score
Ontology Term
Description: This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues [1].
Ontology Term
Description: This entry represents the bifunctional nuclease (BFN) domain which is specific to bacteria and plant organisms. It has both RNase and DNase activities [1]. The dimer of the BFN domain forms a wedge, each monomer being a basic triangular shape. The BFN domain is composed of an eight-stranded, distorted beta-sheet consisting of a four-stranded antiparallel beta-sheet, and a four-stranded mixed beta-sheet. This domain can be found in M. tuberculosis Carbon monoxide resistance (Cor) proteins. Cor consists entirely of this domain with homologues in a variety of organisms, including most mycobacteria, Bacteroides sp., Chlamydia sp., Streptomyces sp., and Rhodococcussp. One of the homologs from Oryza minuta protein OmBBD was reported to exhibit DNase and RNAse activity in vitro [1]. OmBBD carries a C-terminal UvrB domain that is absent in the mycobacterial sequences. UvrB is one component of the UvrABC endonuclease system. Hence, it was proposed that OmBBD's observed nuclease activity may come not from this domain but from an interaction of the C-terminal UvrB with the catalytic UvrC nuclease [2].
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Description: Phosphatidylcholine-hydrolysing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, and/or asparagine residues which may contribute to the active site. aspartic acid. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.
Ontology Term
Description: This domain family is found in eukaryotes, and is approximately 70 amino acids in length. The family is found in association with Pfam:PF00168, Pfam:PF00614. There is a conserved FPD sequence motif. This family is the C terminal of phospholipase D. PLD is a major plant lipid-degrading enzyme which is involved in signal transduction.
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Ontology Term
Description: RNA polymerases catalyse the DNA dependent polymerisation of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 2, contains the active site. The invariant motif -NADFDGD- binds the active site magnesium ion [1,2].
Ontology Term
Description: RNA polymerases catalyse the DNA dependent polymerisation of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 3, represents the pore domain. The 3' end of RNA is positioned close to this domain. The pore delimited by this domain is thought to act as a channel through which nucleotides enter the active site and/or where the 3' end of the RNA may be extruded during back-tracking [1,2].
Ontology Term
Description: RNA polymerases catalyse the DNA dependent polymerisation of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 7, represents a mobile module of the RNA polymerase. Domain 7 forms a substantial interaction with the lobe domain of Rpb2 (Pfam:PF04561) [1,2].
Ontology Term
Description: RNA polymerases catalyse the DNA dependent polymerisation of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 6, represents a mobile module of the RNA polymerase. Domain 6 forms part of the shelf module [1,2]. This family appears to be specific to the largest subunit of RNA polymerase II.
Ontology Term
Description: RNA polymerases catalyse the DNA dependent polymerisation of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 1, represents the clamp domain, which a mobile domain involved in positioning the DNA, maintenance of the transcription bubble and positioning of the nascent RNA strand [1,2].
Ontology Term
Description: RNA polymerases catalyse the DNA dependent polymerisation of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial. and chloroplast polymerases). This domain, domain 4, represents the funnel domain. The funnel contain the binding site for some elongation factors [1,2].
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Description: This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily [1].
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Description: NULL
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Description: Members of this family usually also match to Pfam:PF00330. This domain undergoes conformational change in the enzyme mechanism [1].
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Description: NULL
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Description: This family includes Swiss:Q9NZF1, the Placenta-specific gene 8 protein.
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Description: Vacuolar protein sorting-associated protein (Vps) 35 is one of around 50 proteins involved in protein trafficking. In particular, Vps35 assembles into a retromer complex with at least four other proteins Vps5, Vps17, Vps26 and Vps29. Vps35 contains a central region of weaker sequence similarity, thought to indicate the presence of at least three domains[1].
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Description: The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide Swiss:P07547 [2]. 3-dehydroquinate (DHQ) synthase catalyses the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate [1]. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
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Description: This region is sometimes found at the N-terminus of putative plant bZIP proteins. Its function is not known. Structural modelling suggests this domain may bind nucleic acids [1].
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Description: This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.
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Description: This is the AAA ATPase senescence domain (SC) found at the C-terminal of plant senescence-associated proteins and spartin. In Hemerocallis, petals a genetically based program that leads to senescence and cell death approximately 24 hours after the flower opens, and it is believed that senescence proteins produced around that time have a role in this program [1]. This domain is also present at the C-terminal of Spartin, a protein from higher vertebrates associated with mitochondrial membranes and transportation along microtubules [2]. Spartin functions presynaptically with endocytic adaptor Eps15 to regulate synaptic growth and function. Mutations in human spartin gene cause Troyer syndrome, a hereditary spastic paraplegia [3]. This AAA ATPase domain, similar to other AAA proteins contain an alpha/beta nucleotide-binding domain (NBD) and a smaller four-helix bundle domain (HBD) [4]. Uniquely among AAA structures, spastin has two helices (N-terminal alpha1 and C-terminal alpha11) hat embrace the NBD [4].
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Description: Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
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Description: Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
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Description: Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase [1].
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Description: This motif is called the ubiquitin interaction motif. One of the proteins containing this motif is a receptor for poly-ubiquitination chains for the proteasome [1]. This motif has a pattern of conservation characteristic of an alpha helix.
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Description: NULL
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Description: Some members of this family probably do not have lipid kinase activity and are protein kinases, e.g. Swiss:P42345 [1].
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Description: The FAT domain is named after FRAP, ATM and TRRAP.
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Description: FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family Pfam:PF13943.
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Description: NULL
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Description: This presumed domain is functionally uncharacterised. This domain is found in eukaryotes. This domain is about 160 amino acids in length. This domain is found associated with Pfam:PF00225. This domain is found associated with Pfam:PF00225. This domain has two conserved sequence motifs: EVE and ESA.
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Description: NULL
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Description: PHAF1 and BCAS3 form a complex that affects the recruitment of several core autophagy proteins to the phagophore assembly site [1].
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Description: The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF domain is a proline-binding domain in CD2-binding protein Swiss:O95400.
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Description: This family consists of several uncharacterised eukaryotic proteins.
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Description: This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [1]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan [2].
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Description: This domain has a ferredoxin-like fold.
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Description: This family is the N terminal half of the Prosite family. The C-terminal half has been shown to be related to MiaB proteins [1,2]. This domain is a nearly always found in conjunction with Pfam:PF04055 and Pfam:PF01938 although its function is uncertain.
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Description: This small domain has no known function. However it may perform a nucleic acid binding role (Bateman A. unpublished observation).
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Description: Radical SAM proteins catalyse diverse reactions, including unusual methylations, isomerisation, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.
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Description: NULL
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Description: NULL
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Description: Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.
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Description: This family consists of several eukaryotic proteins of unknown function.
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Description: The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate [2].
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Description: The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate [2].
Ontology Term
Description: The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate [2].
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Description: This is a family of eukaryotic ER membrane proteins that are involved in the synthesis of glycosylphosphatidylinositol (GPI), a glycolipid that anchors many proteins to the eukaryotic cell surface. Proteins in this family are involved in transferring the second mannose in the biosynthetic pathway of GPI [1] [2].
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Description: Members of this family are found in various putative zinc finger proteins.
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Description: NULL
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Description: NULL
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