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Search results 5201 to 5300 out of 202262 for *

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Category: OntologyTerm
Type Details Score
Ontology Term
Description: L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesised by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide [1,2].
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Description: This domain is found at the N-terminus of ribosomal S13 and S15 proteins. This domain is also identified as NUC021 [1].
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Description: This entry is the conserved central region of a group of proteins that are putative transcriptional repressors. The structure contains a putative 14-3-3 binding motif involved in the subcellular localisation of various regulatory molecules, and it may be that interaction with the transcription factor DREF could be regulated through this motif. DREF regulates proliferation-related genes in Drosophila [1]. Mlf1IP is expressed in both the nuclei and the cytoplasm and thus may have multi-functions [2].
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Description: At hooks are DNA binding motifs with a preference for A/T rich regions.
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Description: This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.
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Description: This domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.
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Description: This domain is found in Elongation Factor G. It shares a similar structure with domain V (Pfam:PF00679). Structural studies in drosophila indicate this is domain 3 [1].
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Description: Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family[4]. Their protein structures have been revealed[5].
Ontology Term
Description: UreD is a urease accessory protein. Urease Pfam:PF00449 hydrolyses urea into ammonia and carbamic acid [2]. UreD is involved in activation of the urease enzyme via the UreD-UreF-UreG-urease complex [1] and is required for urease nickel metallocenter assembly [3]. See also UreF Pfam:PF01730, UreG Pfam:PF01495.
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Description: The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway [1]. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled by Atg14 [2]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [3].
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Description: This family represents Cwf15/Cwc15 (from Schizosaccharomyces pombe and Saccharomyces cerevisiae respectively) and their homologues. The function of these proteins is unknown, but they form part of the spliceosome and are thus thought to be involved in mRNA splicing [1].
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Description: NULL
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Description: NULL
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Description: This family of enzymes utilise NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
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Description: This family of enzymes utilise NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
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Description: DWNN is a ubiquitin like domain found at the N terminus of the RBBP6 family of splicing-associated proteins [1]. The DWNN domain is independently expressed in higher vertebrates so it may function as a novel ubiquitin-like modifier of other proteins [1].
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Description: In eukaryotes, this domain is involved in mitochondrial biogenesis [1]. Its function in prokaryotes in unknown.
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Description: The GO annotation for this family indicates that it is a single-pass membrane protein, and it appears to be found in mitochondrial membranes. Sphingolipids play important roles in regulating cellular responses, and although mitochondria contain sphingolipids, direct regulation of their levels in mitochondria or mitochondria-associated membranes is mostly unclear. Sphingomyelin phosphodiesterases catalyse the hydrolysis of sphingomyelin to ceramide and phosphocholine, and these metabolites are involved in signalling pathways.
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Description: Part of the ATP synthase CF(1). These subunits are part of the head unit of the ATP synthase. This subunit is called epsilon in bacteria and delta in mitochondria. In bacteria the delta (D) subunit is equivalent to the mitochondrial Oligomycin sensitive subunit, OSCP (Pfam:PF00213).
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Description: NULL
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Description: The surfeit locus protein SURF-6 is shown to be a component of the nucleolar matrix and has a strong binding capacity for nucleic acids [1].
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Description: RRP14 is a family of nucleolar 60S ribosomal biogenesis proteins from eukaryotes. RRP14 functions in ribosome synthesis as it is required for the maturation of both small and large subunit rRNAs and it helps to prevent premature cleavage of the pre-rRNA at site C2 [1]. It also plays a role in cell polarity and/or spindle positioning 2],
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Description: NULL
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Description: This family contains the C-terminal domain of ribosomal protein TL5. The N-terminal domain, which binds to 5S rRNA, is contained in family Ribosomal_L25p, Pfam:PF01386. Full length (N- and C-terminal domain) homologues of TL5 are also known as CTC proteins. TL5 or CTC are not found in Eukarya or Archaea. In some Bacteria, including E. coli, this ribosomal subunit occurs as a single domain protein (named Ribosomal subunit L25), where the only domain is homologous to TL5 N-terminal domain (hence included in family Pfam:PF01386). The function of the C-terminal domain of TLC is at present unknown.
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Description: This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with Pfam:PF00117 located in the C-terminal region of the protein. CTP synthase catalyses the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position [1].
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Description: Atg101 is a critical autophagy factor that functions together with ULK, Atg13 and FIP200 [1, 2]. Atg101 has been shown to be a HORMA (Hop1, Rev7 and MAD2) domain protein with an open conformation [3].
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Description: Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate [1]. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterised by neurological dysfunction but relatively mild somatic manifestations [2]. The structure shows that the enzyme is composed of three domains. This C-terminal domain has an all alpha helical fold [3].
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Description: This entry represents NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), initially identified in Neurospora crassa as a 21 kDa protein [1,2]. It is believed that members of this family are not to be involved in catalysis.
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Description: NULL
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Description: This domain of approximately 75 residues contains a highly conserved SATSv/iFN motif. The function is unknown but the domain is conserved from plants to humans.
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Description: This family is frequently found N-terminal to the Pribosyltran, Pfam:PF00156.
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Description: This is a family of endoribonucleases involved in RNA biosynthesis which has been named XendoU in Xenopus laevis. XendoU is a U-specific metal dependent enzyme that produces products with a 2'-3' cyclic phosphate termini.
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Description: Sec20 is a membrane glycoprotein associated with secretory pathway.
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Description: This domain is found at the C-terminal of CCD97. In some proteins, this domain is found as two conserved domains separated by a region of low complexity, spanning some 200 residues. The function is unknown.
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Description: This family represents the conserved barrel domain of the 'cupin' superfamily [1] ('cupa' is the Latin term for a small barrel).
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Description: Proline rich domain found in numerous spliceosome associated proteins.
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Description: This family consists of several plant specific allene oxide cyclase proteins (EC:5.3.99.6). The allene oxide cyclase (AOC)-catalysed step in jasmonate (JA) biosynthesis is important in the wound response of tomato [1].
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Description: This family of proteins has no known function.
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Description: This domain is found in wax ester synthase genes such as Swiss:Q8GGG1. In these proteins this domain catalyses the CoA dependent acyltransferase reaction with fatty alcohols to form wax esters [1].
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Description: This domain is found at the C-terminus of wax ester synthases (WS)/diacylglycerol O-acyltransferases (DGAT). These enzymes are utilised for the in vivo production of biodiesel and other wax esters [1].
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Description: NULL
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Description: This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with Pfam:PF00101. There is a conserved APF sequence motif. There are two completely conserved residues (L and P) that may be functionally important. This family is the small subunit of ribulose-1,5-bisphosphate.
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Description: This is the C-terminal domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), which contains antiparallel beta-strands in an extended jelly roll topology with short loops connecting the strands [1].
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Description: This is a family of EPL1 (Enhancer of polycomb-like) proteins. The EPL1 protein is a member of a histone acetyltransferase complex which is involved in transcriptional activation of selected genes [3].
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Description: NULL
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Description: This family represents Homologous recombination OB-fold protein (HROB). During homologous recombination, HROB acts by recruiting the MCM8-MCM9 helicase complex to sites of DNA damage to promote DNA repair synthesis [1,2].
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