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Search results 1601 to 1700 out of 202262 for *

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Category: OntologyTerm
Type Details Score
Ontology Term
Description: The misato protein contains three distinct, conserved domains, segments I, II and III. Segments I and III are common to Tubulins Pfam:PF00091, but segment II aligns with myosin heavy chain sequences from D. melanogaster (PIR C35815), rabbit (SP P04460), and human (PIR S12458). Segment II of misato is a major contributor to its greater length compared with the various tubulins. The most significant sequence similarities to this 54-amino acid region are from a motif found in the heavy chains of myosins from different organisms. A comparison of segment II with the vertebrate myosin heavy chains reveals that it is homologous to a myosin peptide in the hinge region linking the S2 and LMM domains. Segment II also contains heptad repeats which are characteristic of the myosin tail alpha-helical coiled-coils [1]. This myosin-like homology may be due only to the fact that both myosin and Misato carry coiled-coils, which appear similar but are not necessarily homologous (Wood V, personal communication).
Ontology Term
Description: This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Misato from Drosophila and Dml1p from fungi are descendants of an ancestral tubulin-like protein, and exhibit regions with similarity to members of a GTPase family that includes eukaryotic tubulin and prokaryotic FtsZ. Dml1p and Misato have been co-opted into a role in mtDNA inheritance in yeast, and into a cell division-related mechanism in flies, respectively. Dml1p might additionally function in the partitioning of the mitochondrial organelle itself, or in the segregation of chromosomes, thereby explaining its essential requirement. This domain subject to extensive post-translational modifications.
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Description: The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.
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Description: TMEM131_like is a family of bacterial, plant and other metazoa transmembrane proteins. Many of the members are multi-pass transmembrane proteins. This domain represents the N-terminal region which contains a conserved homology domain (CHD1) [1].
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Description: NULL
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Description: This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers [2]. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids [2]. Members of this family have been found also in vertebrates.
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Description: NULL
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Description: This entry represents the conserved N-terminal region of SWAP (suppressor-of-white-apricot protein) proteins. This region contains two highly conserved motifs, viz: DRY and EERY, which appear to be the sites for alternative splicing of exons 2 and 3 of the SWAP mRNA [1]. These proteins are thus thought to be involved in auto-regulation of pre-mRNA splicing. Most family members are associated with two Surp domains Pfam:PF01805 and an Arginine- serine-rich binding region towards the C-terminus.
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Description: NULL
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Description: This family includes members from the HSP60 chaperone family and the TCP-1 (T-complex protein) family.
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Description: Nicotinate phosphoribosyltransferase (EC:2.4.2.11) is the rate limiting enzyme that catalyses the first reaction in the NAD salvage synthesis. This family also includes Pre-B cell enhancing factor that is a cytokine Swiss:P43490. This family is related to Quinolinate phosphoribosyltransferase Pfam:PF01729.
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Description: Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase Swiss:P21964, caffeoyl-CoA O-methyltransferase Swiss:Q43095 and a family of bacterial O-methyltransferases that may be involved in antibiotic production [1].
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Description: This family of proteins plays a role in xylan biosynthesis in plant cell walls. IRX15/IRX15-L precise role in xylan biosynthesis is unknown [1,2]. Glucuronoxylan methyltransferase (GXMT) catalyzes 4-O-methylation of the glucuronic acid substituents of this polysaccharide. AtGXMT1 specifically transfers the methyl group from S-adenosyl-l-methionine to O-4 of alpha-d-glucopyranosyluronic acid residues that are linked to O-2 of the xylan backbone [3]. The function of members of this family in animals and fungi is not known.
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Description: This zinc binding domain was identified by Babu and colleagues and found associated with the WRKY domain Pfam:PF03106 [1].
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Description: NULL
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Description: RER1 family protein are involved in involved in the retrieval of some endoplasmic reticulum membrane proteins from the early golgi compartment. The C terminus of yeast Rer1p interacts with a coatomer complex [1].
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Description: The CH domain is found in both cytoskeletal proteins and signal transduction proteins [1]. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity [4]. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin and Swiss:P15498 have only a single copy.
Ontology Term
Description: This motif is found at the C-terminus of proteins that are related to the EB1 protein. The EB1 proteins contain an N-terminal CH domain Pfam:PF00307. The human EB1 protein was originally discovered as a protein interacting with the C-terminus of the APC protein. This interaction is often disrupted in colon cancer, due to deletions affecting the APC C-terminus. Several EB1 orthologues are also included in this family. The interaction between EB1 and APC has been shown to have a potent synergistic effect on microtubule polymerisation. Neither of EB1 or APC alone has this effect. It is thought that EB1 targets APC to the + ends of microtubules, where APC promotes microtubule polymerisation. This process is regulated by APC phosphorylation by Cdc2, which disrupts APC-EB1 binding. Human EB1 protein can functionally substitute for the yeast EB1 homologue Mal3. In addition, Mal3 can substitute for human EB1 in promoting microtubule polymerisation with APC.
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Description: NULL
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Description: This presumed domain appears to be related to other Myb/SANT like DNA binding domains. In particular Pfam:PF10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
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Description: The natural resistance-associated macrophage protein (NRAMP) family consists of Nramp1, Nramp2, and yeast proteins Smf1 and Smf2. The NRAMP family is a novel family of functional related proteins defined by a conserved hydrophobic core of ten transmembrane domains [5]. This family of membrane proteins are divalent cation transporters. Nramp1 is an integral membrane protein expressed exclusively in cells of the immune system and is recruited to the membrane of a phagosome upon phagocytosis [1]. By controlling divalent cation concentrations Nramp1 may regulate the interphagosomal replication of bacteria [1]. Mutations in Nramp1 may genetically predispose an individual to susceptibility to diseases including leprosy and tuberculosis conversely this might however provide protection form rheumatoid arthritis [1]. Nramp2 is a multiple divalent cation transporter for Fe2+, Mn2+ and Zn2+ amongst others it is expressed at high levels in the intestine; and is major transferrin-independent iron uptake system in mammals [1]. The yeast proteins Smf1 and Smf2 may also transport divalent cations [3].
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Description: Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (Pfam:PF00077), which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.
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Description: This family consist of proteins found in plants and algal chloroplasts, and in cyanobacteria. It includes CGLD27 (Conserved in the green lineage and diatoms 27), which has been described as one out of 14 Fe-responsive orthologues in Chlamydomonas and Arabidopsis, indicating that it is an important component of the iron deficiency response of the plant lineage [1].
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Description: MFS_5 is a family of sugar-transporters from both prokaryotes and eukaryotes.
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Description: This is small family of metazoan zinc-binding proteins.
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Description: Q_salvage proteins occur in most Eukarya as well as in a few bacteria possible via horizontal gene-transfer. Queuosine (Q) is a chemical modification found at the wobble position of tRNAs that have GUN anticodons. Most bacteria synthesize queuosine de novo, whereas eukaryotes rely solely on salvaging this essential component from the environment or the gut flora. The exact enzymatic function of the domain has yet to be determined, but structural similarity with DNA glycosidases suggests a ribonucleoside hydrolase role [1].
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Description: This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
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Description: NULL
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Description: The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.
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Description: This domain family is found in eukaryotes, and is approximately 150 amino acids in length. This family is part of a non-SMC subunit of condensin II which is involved in maintenance of the structural integrity of chromosomes. Condensin II is made up of SMC (structural maintenance of chromosomes) and non-SMC subunits. The non-SMC subunits bind to the catalytic ends of the SMC subunit dimer. The condensin holocomplex is able to introduce superhelical tension into DNA in an ATP hydrolysis- dependent manner, resulting in the formation of positive supercoils in the presence of topoisomerase I and of positive knots in the presence of topoisomerase II.
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Description: NULL
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Description: Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. This family represents 5 transmembrane helices.
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Description: This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with Pfam:PF00689, Pfam:PF00122, Pfam:PF00702, Pfam:PF00690. There is a conserved RRFR sequence motif. There are two completely conserved residues (F and W) that may be functionally important. This family is the N terminal autoinhibitory domain of an endosomal Ca2+-ATPase.
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Description: NULL
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Description: Enzyme that catalyses the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
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Description: The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller [1].
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Description: This domain catalyses N-acetyltransferase reactions.
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Description: This entry includes a group of nuclear envelope integral membrane proteins from animals and plants, including NEMP1 from Xenopus laevis. NEMP1 is a RanGTP-binding protein and is involved in eye development [1,2].
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Description: Members of this family are integral membrane proteins. This family includes a protein with hemolytic activity from Bacillus cereus [1]. It has been proposed that YOL002c encodes a Saccharomyces cerevisiae protein that plays a key role in metabolic pathways that regulate lipid and phosphate metabolism [2]. In eukaryotes, members are seven-transmembrane pass molecules found to encode functional receptors with a broad range of apparent ligand specificities, including progestin and adipoQ receptors, and hence have been named PAQR proteins [3]. The mammalian members include progesterone binding proteins [4]. Unlike the case with GPCR receptor proteins, the evolutionary ancestry of the members of this family can be traced back to the Archaea. This family belongs to the CREST superfamily [5], which are distantly related to GPCRs.
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Description: This domain contains a distinctive -FW- motif. It is found in a family of eukaryotic transcription factors as well as a set of proteins of unknown function.
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