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Search results 5301 to 5400 out of 202262 for *

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Categories

Category: OntologyTerm
Type Details Score
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Description: This family consists of Helicases from the Herpes viruses. Helicases are responsible for the unwinding of DNA and are essential for replication and completion of the viral life cycle.
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Description: This family includes the N-terminus of HAUS augmin-like complex subunit 6. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis [1-2].
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Description: This family includes yeast MRPL37 a mitochondrial ribosomal protein [1].
Ontology Term
Description: Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes [1, 2]. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20 [3].
Ontology Term
Description: Family of eukaryotic beta-1,3-glucanases. Within the Aspergillus fumigatus protein Swiss:Q9UVV0 two perfectly conserved Glu residues (E550 or E554) have been proposed as putative nucleophiles of the active site of the Engl1 endoglucanase, while the proton donor would be D475. The endo-beta-1,3-glucanase activity is essential for efficient spore release [1]. This entry represents the N-terminal beta sandwich domain.
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Description: This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.
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Description: This domain is found in molybdopterin cofactor (Mo-co) oxidoreductases. It is involved in dimer formation, and has an Ig-fold structure [1].
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Description: This is an integral membrane protein family. Family members include TMEM33/Pom33 proteins. Budding yeast Pom33 is a transmembrane nucleoporin that contributes to proper distribution and/or efficient assembly of nuclear pores [1]. Proteins in this entry also include Tts1 from fission yeasts [2], Kr-h2 (krueppel homologue 2) from flies [3] and TMEM33 from vertebrates [4]. Tts1 is required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator [2]. Kr-h2 is a member of the dosage-dependent hierarchy effective upon white gene expression [3]. TMEM33 regulates the tubular structure of endoplasmic reticulum by suppressing the membrane-shaping activity of reticulons [4].
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Description: This family consists of several plant specific mitochondrial import receptor subunit TOM20 (translocase of outer membrane 20 kDa subunit) proteins. Most mitochondrial proteins are encoded by the nuclear genome, and are synthesised in the cytosol. TOM20 is a general import receptor that binds to mitochondrial pre-sequences in the early step of protein import into the mitochondria [1].
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Description: In voltage-gated K+ channels this domain is responsible for subfamily-specific assembly of alpha-subunits into functional tetrameric channels [1]. In KCTD1 (Swiss:Q719H9) this domain functions as a transcriptional repressor [2]. It also mediates homomultimerisation of KCTD1 and interaction of KCTD1 with the transcription factor AP-2-alpha [2-3].
Ontology Term
Description: This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
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Description: This is a family of vitamin-B12 independent methionine synthases or 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferases, EC:2.1.1.14 from bacteria and plants. Plants are the only higher eukaryotes that have the required enzymes for methionine synthesis [1]. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to homocysteine [1]. The aligned region makes up the carboxy region of the approximately 750 amino acid protein except in some hypothetical archaeal proteins present in the family, where this region corresponds to the entire length. This domain contains the catalytic residues of the enzyme [2].
Ontology Term
Description: The N-terminal domain and C-terminal domains of cobalamin-independent synthases together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilise a loop from the C-terminal domain [1].
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Description: YIF1 (Yip1 interacting factor) is an integral membrane protein that is required for membrane fusion of ER derived vesicles [1]. It also plays a role in the biogenesis of ER derived COPII transport vesicles [2].
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Description: Members of this family of proteins play a role in cellular proliferation, as well as in the biogenesis of specialized organelles of the endosomal-lysosomal system.
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Description: This domain is the catalytic domain of ATP-sulfurylase or sulfate adenylyltransferase EC:2.7.7.4 some of which are part of a bifunctional polypeptide chain associated with adenosyl phosphosulphate (APS) kinase Pfam:PF01583. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulphate [2]. ATP sulfurylase catalyses the synthesis of adenosine-phosphosulfate APS from ATP and inorganic sulphate [1].
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Description: This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes.
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Description: Previously known as uncharacterized protein family UPF0015, a single member of this family Swiss:O82827 has been identified as an undecaprenyl diphosphate synthase [1].
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Description: NULL
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Description: This entry is a region of approximately 100 residues containing three pairs of cysteine residues. The region is conserved from plants to humans but its function is unknown.
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Description: This domain family is found in eukaryotes, and is typically between 91 and 105 amino acids in length. This family is the N terminal of Ipi1, a component of the Rix1 complex which works in conjunction with Rea1 to mature the 60S ribosome.
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Description: This domain lies towards the C-terminus of nipped-B or sister chromatid cohesion proteins.
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Description: NULL
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Description: This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, Pfam:PF04564, which has ligase activity.
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Description: This family contains the NADP binding domain of saccharopine dehydrogenase. In some organisms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.
Ontology Term
Description: Chorismate mutase EC:5.4.99.5 catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine [2,3].
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Description: Hus1, Rad1, and Rad9 are three evolutionarily conserved proteins required for checkpoint control in fission yeast. These proteins are known to form a stable complex in vivo [1]. Hus1-Rad1-Rad9 complex may form a PCNA-like ring structure, and could function as a sliding clamp during checkpoint control.
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Description: V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this [1]. This domain is the N-terminal half of the V-Snare proteins.
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Description: This family of proteins are functionally uncharacterised.
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Description: This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics [1]. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Ontology Term
Description: This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction ([1]).
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Description: These proteins are amidohydrolases that are related to Pfam:PF01979 [1].
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Description: This domain family is found in bacteria and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with Pfam:PF00271. The yeast mitochondrial degradosome (mtEXO) is an NTP-dependent exoribonuclease involved in mitochondrial RNA metabolism. mtEXO is made up of two subunits: an RNase (DSS1) and an RNA helicase (SUV3). These co-purify with mitochondrial ribosomes.
Ontology Term
Description: This conserved domain is found in Thyroid adenoma-associated proteins (THADA) and the yeast homologue, TRM732. Trm732 forms a complex with the methyltransferase Trm7 to 2'- O-methylate tRNA residue 32 (Nm32), being required for Trm7 methylation activity. In humans, mutations of the Trm7 homologue FTSJ1, which interacts with THADA, impair Nm32 modifications, associated with non-syndromic X-linked intellectual disability [1,2,3]. It has been suggested that these proteins may play a role in additional biological processes not related to translation. This domain contains a RRSAGLP conserved motif that is required for tRNA modification activity (Funk HM et.al., Preprint from bioRxiv, 03 Jun 2021 DOI: 10.1101/2021.06.03.446962) [1,2,3].
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Description: Family of uncharacterised eukaryotic proteins.
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Description: This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals [1, 2].
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Description: This region is found N terminal to the pectate lyase domain (Pfam:PF00544) in some plant pectate lyase enzymes.
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Description: This family includes Rttp106, a histone chaperone involved in heterochromatin-mediated silencing [1]. This domain belongs to the Pleckstrin homology domain superfamily.
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Description: Family of hypothetical proteins. Some family members contain a two copies of the domain.
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Description: This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone [1][2].
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Description: NULL
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Description: Members of this family function as part of the Mediator (Med) complex, which links DNA-bound transcriptional regulators and the general transcription machinery, particularly the RNA polymerase II enzyme. They play a role in basal transcription by mediating activation or repression according to the specific complement of transcriptional regulators bound to the promoter [1][2].
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Description: This family contains the paired amphipathic helix repeat. The family contains the yeast SIN3 gene Swiss:P22579 (also known as SDI1) that is a negative regulator of the yeast HO gene [1]. This repeat may be distantly related to the helix-loop-helix motif, which mediate protein-protein interactions.
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Description: NULL
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Description: SecE is part of the SecYEG complex in bacteria which translocates proteins from the cytoplasm. In eukaryotes the complex, made from Sec61-gamma and Sec61-alpha translocates protein from the cytoplasm to the ER. Archaea have a similar complex.
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