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Category: OntologyTerm
Type Details Score
Ontology Term  
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Description: NULL
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Description: Plant protein of unknown function.
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Description: Predicted transmembrane protein found in plants, chloroplasts and cyanobacteria. This family is also known as YCF20.
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Description: NULL
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Description: This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification [1]. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy [2]. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated [1]. EC:2.3.1.234
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Description: This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit Swiss:P37941 EC:1.2.4.4. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
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Description: NULL
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Description: Sec6 is a component of the multiprotein exocyst complex. Sec6 interacts with Sec8, Sec10 and Exo70.These exocyst proteins localise to regions of active exocytosis-at the growing ends of interphase cells and in the medial region of cells undergoing cytokinesis-in an F-actin-dependent and exocytosis- independent manner [1].
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Description: This family consists of a series of plant proteins which are related to the Papaver rhoeas S1 self-incompatibility protein. Self incompatibility (SI) is the single most important outbreeding device found in angiosperms and is a mechanism that regulates the acceptance or rejection of pollen. S1 is known to exhibit specific pollen-inhibitory properties [1].
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Description: NULL
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Description: The non-homologous end joining (NHEJ) pathway is one method by which double stranded breaks in chromosomal DNA are repaired. Ku is a component of a multi-protein complex that is involved in the NHEJ. Ku has affinity for DNA ends and recruits the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). This domain is found at the C terminal of Ku which binds to DNA-PKcs [1].
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Description: This is a Plants and Prokaryotes Conserved (PPC) domain found in proteins that contain AT-hook motifs Pfam:PF02178 which strongly suggests a DNA-binding function for the proteins as a whole. Proteins with PPC domains are found in Bacteria, Archaea and the plant kingdom [1, 2].The PPC domain has a single alpha-helix packed against an antiparallel beta-sheet, which is formed by five beta-strands. There are three highly conserved histidine residues, eg at 117, 119 and 133 in Swiss:Q46QL5 which appear to form a zinc-binding site, and the domain has been observed to form homotrimers. The domain co-occurs with a thioredoxin-like domain in uncharacterized cyanobacterial proteins [2].
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Description: The lateral organ boundaries (LOB) gene encodes a plant-specific protein of unknown function that is expressed at the adaxial base of initiating lateral organs. The N-terminal of the LOB protein contains an approximately 100-amino acid conserved domain (the LOB domain) that is present in 42 other Arabidopsis thaliana proteins as well as in proteins from a variety of other plant species. The LOB domain contains conserved blocks of amino acids that identify the LOB domain (LBD) gene family. In particular, a conserved C-x(2)-C-x(6)-C-x(3)-C motif, which is the defining feature of the LOB domain, is present in all LBD proteins [1].
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Description: Members of this family are found in a range of archaea and eukaryotes and have hypothesised ATP binding activity.
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Description: The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the Pfam:PF00025 family [2].
Ontology Term
Description: The full-length Sec7 functions proximally in the secretory pathway as a protein binding scaffold for the coat protein complexes COPII-COPI. The COPII-COPI-protein switch is necessary for maturation of the vesicular-tubular cluster, VTC, intermediate compartments for Golgi compartment biogenesis. This N-terminal domain however does not appear to be binding either of the COP or the ARF [2].
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Description: Members of this family of functionally uncharacterised domains are found in various plant and yeast protein transport proteins.
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Description: NULL
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Description: The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive features: a putative nuclear localisation signal and a zinc-finger motif (C3H). It is suggested that the WRC domain functions in DNA binding [1].
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Description: we have identified a conserved motif in the LOC118487 protein that we have called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterised proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesise the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation [2]. Eukaryotic NADH-ubiquinone oxidoreductase 19 kDa (NDUFA8) subunit [3]. The CHCH domain was previously called DUF657 [4].
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Description: This dimerisation region is found at the C terminus of the transposases of elements belonging to the Activator superfamily (hAT element superfamily). The isolated dimerisation region forms extremely stable dimers in vitro [1].
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Description: The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.
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Description: This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle [1]. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU [2]. The domain has been found in non EF-TS proteins such as alpha-NAC Swiss:P70670 and MJ0280 Swiss:Q57728 [1].
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Description: NULL
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Description: NULL
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Description: The EAR motif is the ethylene-responsive element binding factor-associated amphiphilic repression motif. This motif binds to the Groucho/Tup1-type co-repressor TOPLESS (TPL) and TPL-related proteins. The motif is frequently to be find at the N-terminus of NINJA, or Novel INteractor of JAZ, proteins [1]. The EAR motif, defined by the consensus sequence patterns of either LxLxL or DLN xxP, is the most predominant form of transcriptional repression motif so far identified in plants. It is highly conserved in transcriptional regulators that are known to function as negative regulators in a broad range of developmental and physiological processes across evolutionarily diverse plant species [2]. This family is closely related to family AUX_IAA Pam:PF02309 which also has an LxLxL signature.
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Description: Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See Pfam:PF00009 Pfam:PF00025, Pfam:PF00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices [1].
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Description: The K-box region is commonly found associated with SRF-type transcription factors see Pfam:PF00319. The K-box is a possible coiled-coil structure [2]. Possible role in multimer formation [1].
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Description: This entry represents a group of uncharacterised plant proteins, including B3 domain-containing protein At2g31720 (also known as Protein AUXIN RESPONSE FACTOR 70) from Arabidopsis. These are DNA-binding proteins likely to be involved in stress response [1].
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Description: Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants [4]. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing [5]. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes [4]. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome [1][2].
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Description: This family of proteins are functionally uncharacterised.
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Description: This family represents the C-terminus (approximately 250 residues) of protein ENHANCED DISEASE RESISTANCE 2 (EDR2) from plants. EDR2 is a negative regulator of the salicylic acid (SA)-mediated resistance to pathogens, including the biotrophic powdery mildew pathogens Golovinomyces cichoracearum and Blumeria graminis, and the downy mildew pathogen Hyaloperonospora parasitica, probably by limiting the initiation of cell death and the establishment of the hypersensitive response (HR) [1,2].
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Description: NULL
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Description: This family is equally distributed in both metazoa and plants. Annotation associated with Swiss:Q9SLW7 suggest that it may be involved in response to viral attack in plants. However, no clear function has been assigned to this family.
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Description: Mob1 is an essential Saccharomyces cerevisiae protein, identified from a two-hybrid screen, that binds Mps1p, a protein kinase essential for spindle pole body duplication and mitotic checkpoint regulation. Mob1 contains no known structural motifs; however MOB1 is a member of a conserved gene family and shares sequence similarity with a nonessential yeast gene, MOB2. Mob1 is a phosphoprotein in vivo and a substrate for the Mps1p kinase in vitro. Conditional alleles of MOB1 cause a late nuclear division arrest at restrictive temperature [1]. This family also includes phocein Swiss:Q9QYW3, a rat protein that by yeast two hybrid interacts with striatin [2].
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Description: The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions [1].
Ontology Term
Description: This entry includes chloroplastic protein PAM68 and the Sll0933 homolog from Cyanobacteria (blue-green algae) [1]. PAM68 is involved in early steps in photosystem II (PSII) biogenesis and in maturation and stability of newly synthesized psbA protein [2].
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Description: The BREVIS RADIX (BRX) domain was characterised as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root [1,2]. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot [3]. The family features a short region of alpha-helix, approximately 60 residues in length, which is found repeated up to three times [1]. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action [4].
Ontology Term
Description: The BREVIS RADIX (BRX) domain was characterised as being a transcription factor in plants regulating the extent of cell proliferation and elongation in the growth zone of the root [1,2]. BRX is rate limiting for auxin-responsive gene-expression by mediating cross-talk with the brassino-steroid pathway. BRX has a ubiquitous, although quantitatively variable role in modulating the growth rate in both the root and the shoot [3]. This family features a short region, also alpha-helical, N-terminal to the repeated alpha-helices of family BRX, Pfam:PF08381 [1]. BRX is expressed in the vasculature and is rate-limiting for transcriptional auxin action [4].
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Description: This family is a putative S-adenosyl-L-methionine (SAM)-dependent methyltransferase [1,2].
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Description: This family includes protein BPS1 (Protein BYPASS 1) from Arabidopsis, which is required for normal root and shoot development. It prevents constitutive production of a root mobile carotenoid-derived signalling compound that is capable of arresting shoot and leaf development [1,2].
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Description: BAR domains are dimerisation, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like Pfam:PF00169 and Pfam:PF00787 domains in beta centaurins and sorting nexins respectively.
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Description: NULL
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