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Search results 6101 to 6200 out of 202262 for *

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Category: OntologyTerm
Type Details Score
Ontology Term  
Ontology Term  
Ontology Term
Description: The soluble NSF attachment protein (SNAP) proteins are involved in vesicular transport between the endoplasmic reticulum and Golgi apparatus [1]. They act as adaptors between SNARE (integral membrane SNAP receptor) proteins and NSF (N-ethylmaleimide-sensitive factor) [2]. They are structurally similar to TPR repeats [2].
Ontology Term
Description: This eukaryotic family of proteins has no known function.
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Description: This family contains a number of eukaryotic cell division cycle 123 (Cdc123, also known as D123) proteins approximately 330 residues long. It has been shown that mutated variants of D123 exhibit temperature-dependent differences in their degradation rate [1]. D123 proteins are regulators of eIF2, the central regulator of translational initiation [2]. Family members include ATP-grasp enzymes belonging to the R2K clade, wherein one of the absolutely-conserved lysine residues has migrated to the RAGYNA domain which is a part of the core ATP-grasp module. This family is found in eukaryotes as well as NCDLVs and diverse bacteria. In eukaryotes, the domain is found in both the CDC123 enzymes and a related clade of proteins found in amoeboid organisms, while in bacteria it is observed embedded in polymorphic toxin loci [3].
Ontology Term
Description: Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerisation domain [1].
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Description: Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
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Description: This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 558 and 775 amino acids in length. There is a conserved TGG sequence motif. PNGase A is a protein which cleaves glycopeptides.
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Ontology Term
Description: This family represents a conserved region found in eukaryotic cohesins of the Rad21, Rec8 and Scc1 families. Members of this family mediate sister chromatid cohesion during mitosis and meiosis, as part of the cohesin complex [1]. Cohesion is necessary for homologous recombination (including double-strand break repair) and correct chromatid segregation. These proteins may also be involved in chromosome condensation. Dissociation at the metaphase to anaphase transition causes loss of cohesion and chromatid segregation [2].
Ontology Term
Description: This family represents a conserved N-terminal region found in eukaryotic cohesins of the Rad21, Rec8 and Scc1 families. Members of this family mediate sister chromatid cohesion during mitosis and meiosis, as part of the cohesin complex [1]. Cohesion is necessary for homologous recombination (including double-strand break repair) and correct chromatid segregation. These proteins may also be involved in chromosome condensation. Dissociation at the metaphase to anaphase transition causes loss of cohesion and chromatid segregation [2].
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Description: This associates with Pfam:PF00388 to form a single structural unit.
Ontology Term
Description: Members of this family are predominantly found in phosphoinositide-specific phospholipase C. They adopt a structure consisting of a core of four alpha helices, in an EF like fold, and are required for functioning of the enzyme [1].
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Description: This family represents the C-terminus (approximately 270 residues) of a number of plant Hs1pro-1 proteins, which are believed to confer nematode resistance [1].
Ontology Term
Description: This family represents the N-terminus (approximately 180 residues) of plant Hs1pro-1, which is believed to confer resistance to nematodes [1].
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Ontology Term
Description: Members of this family catalyse the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate [1].
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Description: This family consists of several microsomal signal peptidase 25 kDa subunit proteins. Translocation of polypeptide chains across the endoplasmic reticulum (ER) membrane is triggered by signal sequences. Subsequently, signal recognition particle interacts with its membrane receptor and the ribosome-bound nascent chain is targeted to the ER where it is transferred into a protein-conducting channel. At some point, a second signal sequence recognition event takes place in the membrane and translocation of the nascent chain through the membrane occurs. The signal sequence of most secretory and membrane proteins is cleaved off at this stage. Cleavage occurs by the signal peptidase complex (SPC) as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme. The signal peptidase complex is possibly also involved in proteolytic events in the ER membrane other than the processing of the signal sequence, for example the further digestion of the cleaved signal peptide or the degradation of membrane proteins. Mammalian signal peptidase is as a complex of five different polypeptide chains. This family represents the 25 kDa subunit (SPC25).
Ontology Term
Description: This domain is found at the C-terminus of adenylosuccinate lyase(ASL; PurB in E. coli). It has been identified in bacteria, eukaryotes and archaea and is found together with the lyase domain Pfam:PF00206. ASL catalyses the cleavage of succinylaminoimidazole carboxamide ribotide to aminoimidazole carboxamide ribotide and fumarate and the cleavage of adenylosuccinate to adenylate and fumarate [1].
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Description: NULL
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Description: This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (Pfam:PF00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyse the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated [1].
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Description: NULL
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Description: This domain lies at the C-terminus of the clathrin-adaptor protein complex-3 beta-1 subunit. The AP-3 complex is associated with the Golgi region of the cell as well as with more peripheral structures. The AP-3 complex may be directly involved in trafficking to lysosomes or alternatively it may be involved in another pathway, but that mis-sorting in that pathway may indirectly lead to defects in pigment granules [2].
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Description: NULL
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Description: This short domain is found in the Rad4 protein. This domain binds to DNA [1].
Ontology Term
Description: This short domain is found in the Rad4 protein. This domain binds to DNA [1].
Ontology Term
Description: This short domain is found in the Rad4 protein. This domain binds to DNA [1].
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Description: NULL
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Description: This family consists of several eukaryotic proteins of unknown function.
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Ontology Term
Description: Members of this family are related to the pre mRNA splicing factor PRP38 from yeast [1]. Therefore all the members of this family could be involved in splicing. This conserved region could be involved in RNA binding. The putative domain is about 180 amino acids in length. PRP38 is a unique component of the U4/U6.U5 tri-small nuclear ribonucleoprotein (snRNP) particle and is necessary for an essential step late in spliceosome maturation [2].
Ontology Term
Description: This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.
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Description: Apg5 is directly required for the import of aminopeptidase I via the cytoplasm-to-vacuole targeting pathway [1].
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Description: Members of this family adopt a multihelical structure, with an irregular array of long and short alpha-helices. They allow binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex [1].
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Description: Cohesin_load is a common cohesin loading factor protein that is conserved in fungi. It is associated with the cohesin complex and is required in G1 for cohesin binding to chromosomes but dispensable in G2 when cohesion has been established. It is referred to as both Ssl3, in pombe, and Scc4, in S.cerevisiae. It complexes with Mis4 [1].
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Description: This entry represents subunit 8 of the Cytochrome b-c1 complex [1].
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Description: This family consists of several eukaryotic Aph-1 proteins.Gamma-secretase catalyses the intramembrane proteolysis of Notch, beta-amyloid precursor protein, and other substrates as part of a new signaling paradigm and as a key step in the pathogenesis of Alzheimer's disease. It is thought that the presenilin heterodimer comprises the catalytic site and that a highly glycosylated form of nicastrin associates with it. Aph-1 and Pen-2, two membrane proteins genetically linked to gamma-secretase, associate directly with presenilin and nicastrin in the active protease complex. Co-expression of all four proteins leads to marked increases in presenilin heterodimers, full glycosylation of nicastrin, and enhanced gamma-secretase activity [1]. APH-1 proteins have a similar but different set of motifs as compared to other families. Their four motifs are: QExxR, Fxxxx, Hxxxs and Hxxxs respectively. Given the inferred homology between APH-1 and other membrane proteases such as type II CAAX proteases and PrsW proteases, it is speculated that APH-1 may possess protease activity [3].
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Description: Members of this family are thought to be integral membrane proteins. Some members of this family have been shown to cause apoptosis if mutated [1], these proteins are known as DAD for defender against death. The family also includes the epsilon subunit of the oligosaccharyltransferase that is involved in N-linked glycosylation [2].
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Description: This family consists of several eukaryotic GCN5-like protein 1 (GCN5L1) sequences. The function of this family is unknown [1,2].
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Description: This domain contains conserved cysteine and histidine residues [1]. It resembles zinc fingers, and binds to zinc [2]. This domain functions as an RNA-binding domain [2].
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Description: This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation [3]. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60) [1]. This protein has been found to interact with herpes simplex type 1 regulatory proteins [1].
Ontology Term
Description: The ubiquitin fold domain is found at the C-terminus of ubiquitin-activating E1 family enzymes. This domain binds to E2 enzymes [1].
Ontology Term  
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