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Category: OntologyTerm
Type Details Score
Ontology Term
Description: NULL
Ontology Term  
Ontology Term
Description: This family of proteins bind FAD as a cofactor.
Ontology Term
Description: This domain found associated with Pfam:PF00732.
Ontology Term
Description: This family contains hypothetical plant proteins of unknown function. Family members contain a number of conserved cysteine residues.
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Description: The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops [1]. It is found at the C terminus of Scd6p-like SM domains [1][2]. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain [1].
Ontology Term
Description: The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from the newt Pleurodeles walt, and its orthologs from fungi, animals, plants and apicomplexans [1]. The domain is also found in Dcp3p and the human EDC3/FLJ21128 protein where it is fused to the the Rossmanoid YjeF-N domain [1,2]. In addition both EDC3 and Scd6p are found fused to the FDF domain [1,2].
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Description: This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles [1]. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family[2]; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles [2].
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Description: Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Ontology Term
Description: Possible metal-binding domain in endoribonuclease RNase L inhibitor. Found at the N-terminal end of RNase L inhibitor proteins, adjacent to the 4Fe-4S binding domain, fer4, Pfam:PF00037. Also often found adjacent to the DUF367 domain Pfam:PF04034 in uncharacterised proteins. The RNase L system plays a major role in the anti-viral and anti-proliferative activities of interferons [1], and could possibly play a more general role in the regulation of RNA stability in mammalian cells. Inhibitory activity requires concentration-dependent association of RLI with RNase L [2].
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Description: Members of this family, found in several herpesviruses, include EBV BDLF4 Swiss:P03223, HCMV UL92 Swiss:P16798, HHV8 31 Swiss:P88920, HSV6 U63 Swiss:P24440. Their function is unknown. The N terminus of this protein contains 6 conserved cysteines and histidines that might form a zinc binding domain (A Bateman pers. obs.).
Ontology Term
Description: This is an F-box-like family.
Ontology Term
Description: This family includes the SWIB domain and the MDM2 domain [1]. The p53-associated protein (MDM2) is an inhibitor of the p53 tumour suppressor gene binding the transactivation domain and down regulating the ability of p53 to activate transcription. This family contains the p53 binding domain of MDM2 [2].
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Ontology Term
Description: This Zinc knuckle is found in FAM90A mammalian proteins.
Ontology Term
Description: This is a 45 residue conserved region at the N-terminal end of a family of proteins referred to as CIRs (CBF1-interacting co-repressors). CBF1 (centromere-binding factor 1) acts as a transcription factor that causes repression by binding specifically to GTGGGAA motifs in responsive promoters, and it requires CIR as a co-repressor. CIR binds to histone deacetylase and to SAP30 and serves as a linker between CBF1 and the histone deacetylase complex [1].
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Ontology Term
Description: COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
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Description: NULL
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Ontology Term
Description: This family represents a retinal pigment epithelial membrane receptor which is abundantly expressed in retinal pigment epithelium, and binds plasma retinal binding protein. The family also includes the sequence related neoxanthin cleavage enzyme in plants and lignostilbene-alpha,beta-dioxygenase in bacteria.
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Description: This cupin like domain shares similarity to the JmjC domain.
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Description: Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.
Ontology Term
Description: This domain is the central structural domain of the FERM domain.
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Description: This family includes the Rpb4 protein. This family also includes C17 (aka CGRP-RCP) is an essential subunit of RNA polymerase III. C17 forms a subcomplex with C25 [4] which is likely to be the counterpart of subcomplex Rpb4/7 in Pol II [3].
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Description: NULL
Ontology Term
Description: MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organisation. The C terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad [1]. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands [2].
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Description: This family includes auxin efflux carrier proteins and other transporter proteins from all domains of life.
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Description: This domain is know as ARID for AT-Rich Interaction Domain [1], and also known as the BRIGHT domain [3].
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Description: This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
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Ontology Term
Description: This family of proteins belongs to the PP-loop superfamily [1].
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Description: The HMG-CoA reductases catalyse the conversion of HMG-CoA to mevalonate, which is the rate-limiting step in the synthesis of isoprenoids like cholesterol. Probably because of the critical role of this enzyme in cholesterol homeostasis, mammalian HMG-CoA reductase is heavily regulated at the transcriptional, translational, and post-translational levels [2].
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Description: A family of plant integral membrane proteins, first discovered in barley. Mutants lacking wild-type Mlo proteins show broad spectrum resistance to the powdery mildew fungus, and dysregulated cell death control, with spontaneous cell death in response to developmental or abiotic stimuli. Thus wild-type Mlo proteins are thought to be inhibitors of cell death whose deficiency lowers the threshold required to trigger the cascade of events that result in plant cell death. Mlo proteins are localised in the plasma membrane and possess seven transmembrane regions; thus the Mlo family is the only major higher plant family to possess 7 transmembrane domains. It has been suggested that Mlo proteins function as G-protein coupled receptors in plants [1]; however the molecular and biological functions of Mlo proteins remain to be fully determined.
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Description: This domain is a endoribonuclease [1]. Specifically it cleaves an intron from Hac1 mRNA in humans, which causes it to be much more efficiently translated.
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Description: This family includes the four transmembrane regions of the ionotropic glutamate receptors and NMDA receptors.
Ontology Term
Description: This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognises Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
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Description: This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.
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Description: This family represents the C-terminal domain of the mutL/hexB/PMS1 family. This domain has a ribosomal S5 domain 2-like fold.
Ontology Term
Description: MutL and MutS are key components of the DNA repair machinery that corrects replication errors [1]. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation [3].
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Description: This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase [1]. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme [2]. The sequence carries both a Walker A and Walker B motif which together are characteristic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue [3].
Ontology Term
Description: Members of this family are probably coiled-coil proteins that are similar to the CHD5 (Congenital heart disease 5) protein. In Saccharomyces cerevisiae this protein localises to the ER and is thought to play a homeostatic role [2].
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Description: NULL
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Description: This domain is named RWP-RK after a conserved motif at the C terminus of the presumed domain. The domain is found in algal minus dominance proteins as well as plant proteins involved in nitrogen-controlled development [1].
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Description: This Pfam family represents a protein domain which shows homology to the yeast protein SacI Swiss:P32368. The SacI homology domain is most notably found at the amino terminal of the inositol 5'-phosphatase synaptojanin.
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Description: This region encompasses much of the RNA and SrmB binding motifs on polymerase A.
Ontology Term
Description: This family includes nucleic acid independent RNA polymerases, such as Poly(A) polymerase, which adds the poly (A) tail to mRNA EC:2.7.7.19. This family also includes the tRNA nucleotidyltransferase that adds the CCA to the 3' of the tRNA EC:2.7.7.25. This family is part of the nucleotidyltransferase superfamily.
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Ontology Term
Description: This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites [5].
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Ontology Term
Description: The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in [4,5].
Ontology Term
Description: The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants [2] and bacteria [1].
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Description: NULL
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Description: SBP domains (for SQUAMOSA-pROMOTER BINDING PROTEIN) are found in plant proteins. It is a sequence specific DNA-binding domain [1]. Members of family probably function as transcription factors involved in the control of early flower development [1]. The domain contains 10 conserved cysteine and histidine residues that probably are zinc ligands.
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Description: NULL
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Description: NULL
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