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Search results 5501 to 5600 out of 202262 for *

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Category: OntologyTerm
Type Details Score
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Description: This family constitutes the major, conserved, portion of PRCC proteins. In humans this family interacts with MAD2B, the mitotic checkpoint protein [1,2]. In Schizosaccharomyces pombe this protein is part of the Cwf-complex that is known to be involved in pre-mRNA splicing [3].
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Description: This presumed domain is found at the C-terminus of the S. cerevisiae SRP40 protein Swiss:P32583 and its homologues. SRP40/nopp40 is a chaperone involved in nucleocytoplasmic transport. SRP40 is also a suppressor of mutant AC40 subunit of RNA polymerase I and III.
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Description: This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands.
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Description: This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport.
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Description: Nop52 believed to be involved in the generation of 28S rRNA [1].
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Description: Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli endonuclease I (EndoI) is a sequence independent endonuclease located in the periplasm. It is inhibited by different RNA species. It is thought to normally generate double strand breaks in DNA, except in the presence of high salt concentrations and RNA, when it generates single strand breaks in DNA. Its biological role is unknown [1]. Other family members are known to be extracellular [2]. This family also includes a non-specific, Mg2+ activated ribonuclease precursor (Swiss:Q03091) [3].
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Description: Eukaryotic N-glycosylation is catalysed in the ER lumen, where the enzyme oligosaccharyltransferase (OTase) transfers donor glycans from a dolichol pyrophosphate (DolP) carrier (Lipid-linked oligosaccharide; LLO) to polypeptides. The yeast OTase is a hetero-oligomeric complex composed of essential (Ost1, Ost2, Wbp1, Stt3, and Swp1) and nonessential (Ost3, Ost4, Ost5, and Ost6) subunits. This domain family is found in Ost5, Swiss:Q92316. The precise function of this subunit is not known, however Ost5 appears to form a sub-complex with Ost1, and this sub-complex associates with the catalytic Stt3 subunit of OTase. Down regulation of Ost5 resulted in a limited effect on glycosylation and no effect on the stability of Ost1 or Stt3 subunits [1, 2].
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Description: This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ (Swiss:Q09909). CwfJ is part of the Cdc5p complex involved in mRNA splicing [1].
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Description: Specific subunit for Pol III, the tRNA specific polymerase.
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Description: This family of proteins is related to TATA-binding protein (TBP). TBP is a highly conserved RNA polymerase II general transcription factor that binds to the core promoter and initiates assembly of the preinitiation complex. Human TRF has been shown to associate with an RNA polymerase II-SRB complex [1]. This Med20 subunit of Mediator is found in the non-essential part of the head [2].
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Description: This is the central domain of of novel family of hypothetical nucleolar proteins [1].
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Description: Ysc84 is a family of Las17-binding proteins found in metazoa. Together, Las17 and Ysc84 are essential for proper polymerisation of actin; Ysc84 is able to bind to and stabilise the actin dimer presented by Las17 and thereby promote polymerisation. An active actin cytoskeleton is necessary for adequate endocytosis. (Pfam:PF00018), or a FYVE zinc finger (Pfam:PF01363).
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Description: Sec34 and Sec35 form a sub-complex, in a seven protein complex that includes Dor1 (Pfam:PF04124). This complex is thought to be important for tethering vesicles to the Golgi [1].
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Description: NULL
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Description: This family consists of several 5' nucleotidase, deoxy (Pyrimidine), cytosolic type C (NT5C) proteins. 5'(3')-Deoxyribonucleotidase is a ubiquitous enzyme in mammalian cells whose physiological function is not known [1].
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Description: NULL
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Description: SNF5 is a component of the yeast SWI/SNF complex, which is an ATP-dependent nucleosome-remodelling complex that regulates the transcription of a subset of yeast genes. SNF5 is a key component of all SWI/SNF-class complexes characterised so far [1]. This family consists of the conserved region of SNF5, including a direct repeat motif. SNF5 is essential for the assembly promoter targeting and chromatin remodelling activity of the SWI-SNF complex [2]. SNF5 is also known as SMARCB1, for SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily b, member 1, and also INI1 for integrase interactor 1. Loss-of function mutations in SNF5 are thought to contribute to oncogenesis in malignant rhabdoid tumours (MRTs) [3].
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Description: Bucentaur or craniofacial development protein 1 (BCNT) in ruminents has a different domain architecture to that in mouse and human. For this reason it has been used as a model for molecular evolution [1-3]. Both bovine and human BCNTs are phosphorylated by casein kinase II in vitro [4].
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Description: This family represents the N-terminus of the 31kD subunit (42kD in drosophila) of transcription initiation factor IID (TAFII31). TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.
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Description: This is the highly conserved galactokinase signature sequence which appears to be present in all galactokinases irrespective of how many other ATP binding sites, etc that they carry [1]. The function of this domain appears to be to bind galactose [2], and the domain is normally at the N-terminus of the enzymes, EC:2.7.1.6 [3]. This domain is associated with the families GHMP_kinases_C, Pfam:PF08544 and GHMP_kinases_N, Pfam:PF00288.
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Description: Members of this family are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase [1]. The THI-4 protein, which is involved in thiamine biosynthesis, is also a member of this family. The C-terminal part of these proteins consistently show significant sequence similarity to TENA proteins. This similarity was first noted with the Neurospora crassa THI-4 [2]. This family includes bacterial coenzyme PQQ synthesis protein C or PQQC proteins. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria [3]. PQQC has been found to be required in the synthesis of PQQ but its function is unclear. The exact molecular function of members of this family is uncertain.
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Description: The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.
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Description: This entry represents the Serine/threonine-protein phosphatase 4 regulatory subunit 3 (also known as SMEK homologue) PP4R3, which forms a complex with the phosphatase 4 catalytic subunit (PP4c), localising it to the DNA damage repair machinery [1-4] and regulates its activity. PP4c is involved in developmental progression, chemotaxis, expression of stress response genes and cell movement.
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Description: This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle [1]. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms [1]. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites [3]. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerises this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli Swiss:P77608 is involved in the phenylpropionic acid pathway of E. coli and catalyses the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor [5]. OHED hydratase encoded by hpcG in E. coli Swiss:P42270 is involved in the homoprotocatechuic acid (HPC) catabolism [6]. XylI in P. putida Swiss:P49155 is a 4-Oxalocrotonate decarboxylase [7].
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Description: These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
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Description: This family also includes lambda crystallin. Some proteins include two copies of this domain.
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Description: This family also includes lambda crystallin.
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Description: The HAND domain adopts a secondary structure consisting of four alpha helices, three of which (H2, H3, H4) form an L-like configuration. Helix H2 runs antiparallel to helices H3 and H4, packing closely against helix H4, whilst helix H1 reposes in the concave surface formed by these three helices and runs perpendicular to them. The domain confers DNA and nucleosome binding properties to the protein [1].
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Description: The SLIDE domain adopts a secondary structure comprising a main core of three alpha-helices. It has a role in DNA binding, contacting DNA target sites similar to c-Myb (Pfam:PF00249) repeats or homeodomains [1].
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Description: This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyses the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).
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