id
stringlengths
14
19
title
stringlengths
1
124
text
stringlengths
12
2.83k
source
stringclasses
1 value
wiki_10000_chunk_0
Fatty acid metabolism regulator protein FadR
This single [repressor controls the transcription of the whole fad regulon. Binding of fadR is specifically inhibited by long chain fatty acyl-CoA compounds. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal winged-helix domain binds DNA, and the C-terminal domain binds acyl-CoA.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10001_chunk_0
Fatty acid metabolism regulator protein FadR
The binding of acyl-CoA to the C-terminal domain results in a conformational change that affects the DNA binding affinity of the N-terminal domain.FadR is a member of the GntR family of bacterial transcription regulators. The DNA-binding domain is well conserved for this family, whereas the C-terminal effector-binding ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10002_chunk_0
Ferric uptake regulator family
In molecular biology, the ferric uptake regulator family is a family of bacterial proteins involved in regulating metal ion uptake and in metal homeostasis. The family is named for its founding member, known as the ferric uptake regulator or ferric uptake regulatory protein (Fur). Fur proteins are responsible for contr...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10003_chunk_0
Five-prime cap
In molecular biology, the five-prime cap (5′ cap) is a specially altered nucleotide on the 5′ end of some primary transcripts such as precursor messenger RNA. This process, known as mRNA capping, is highly regulated and vital in the creation of stable and mature messenger RNA able to undergo translation during protein ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10004_chunk_0
Flagellar motor switch protein
In molecular biology, the flagellar motor switch protein (Flig) is one of three proteins in certain bacteria coded for by the gene fliG. The other two proteins are FliN coded for by fliN, and FliM coded for by fliM. The protein complex regulates the direction of flagellar rotation and hence controls swimming behaviour....
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10005_chunk_0
Forkhead-associated domain
In molecular biology, the forkhead-associated domain (FHA domain) is a phosphopeptide recognition domain found in many regulatory proteins. It displays specificity for phosphothreonine-containing epitopes but will also recognise phosphotyrosine with relatively high affinity. It spans approximately 80-100 amino acid res...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10006_chunk_0
Frataxin-like domain
In molecular biology, the frataxin-like domain is a protein domain found in proteins including eukaryotic frataxin and bacterial CyaY. The bacterial CyaY proteins are iron-sulphur cluster (FeS) metabolism proteins which are homologous to eukaryotic frataxin. Partial phylogenetic profiling suggests that CyaY most likely...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10007_chunk_0
Fungal fruit body lectin family
In molecular biology, the fungal fruit body lectin family consists of several fungal fruit body lectin proteins. Fruit body lectins are thought to have insecticidal activity and may also function in capturing nematodes. One member of this family, the lectin XCL from Boletus chrysenteron (formerly Xerocomus chrysenteron...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10008_chunk_0
Fungal fucose-specific lectin
In molecular biology, the fungal fucose-specific lectin family is a family of lectins. Lectins are proteins which are involved in many recognition events at the molecular or cellular level. These fungal lectins, such as Aleuria aurantia lectin AAL, specifically recognise fucosylated glycans. AAL is a dimeric protein, w...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10009_chunk_0
Galactose binding lectin domain
In molecular biology, the galactose binding lectin domain is a protein domain. It is found in many proteins including the lectin purified from sea urchin (Anthocidaris crassispina) eggs, SUEL. This lectin exists as a disulfide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10010_chunk_0
Glucose-methanol-choline oxidoreductase family
In molecular biology, the glucose-methanol-choline oxidoreductase family (GMC oxidoreductase) is a family of enzymes with oxidoreductase activity. The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases. These enzymes include a variety of proteins; choline dehydrogenase (CHD) EC 1.1.99....
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10011_chunk_0
Glutaredoxin 2 (bacterial)
In molecular biology, the glutaredoxin 2 family is a family of bacterial glutaredoxins. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase. Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxin...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10012_chunk_0
Glutaredoxin 2 (bacterial)
It is thought that the primary function of Grx2 is to catalyse reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress. These enzymes are not related to GLRX2. == References ==
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10013_chunk_0
Glycoside hydrolase family 53
In molecular biology, the glycoside hydrolase family 53 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10014_chunk_0
Group I pyridoxal-dependent decarboxylases
In molecular biology, the group I pyridoxal-dependent decarboxylases, also known as glycine cleavage system P-proteins, are a family of enzymes consisting of glycine cleavage system P-proteins (glycine dehydrogenase (decarboxylating)) EC 1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10015_chunk_0
Guanylate-binding protein
In molecular biology, the guanylate-binding proteins family is a family of GTPases that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma (Interferon-inducible GTPase) are key to the protective immunity against microbial and viral pathogens. These GTPases are classified into three groups: the small 47-...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10016_chunk_0
Guanylate-binding protein
Guanylate-binding proteins (GBP) fall into the last class. GBP genes have been universally recognized in mammalian as well as in most other vertebrate genomes. A single cluster of seven human GBP genes (GBP1-GBP7) is found on chromosome 1q22.2.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10017_chunk_0
Guanylate-binding protein
Unlike humans, in genetically controllable disease models such as mice and zebrafish, members of the GBPs gene family are organized in more than one cluster, in this case, 11 (Gbp2b- Gbp110 and 4 genes (Gbp1-Gbp4), respectively. Examinations of GBP-related sequences have shown that zebrafish gbp3 and gbp4 contain an ad...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10018_chunk_0
Guanylate-binding protein
The physiological relevance of the GBP's GDPase activity might yield important insights to elucidate GBP-specific defensive profile versus other INF-induced GTPases(e.g.IRGs). Evidence has suggested GBPs as important players in a variety of disease conditions ranging from infectious and metabolic inflammatory diseases ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10019_chunk_0
Haemagglutination activity domain
In molecular biology, the haemagglutination activity domain is a conserved protein domain found near the N terminus of a number of large, repetitive bacterial proteins, including many proteins of over 2500 amino acids. A number of the members of this family have been designated adhesins, filamentous haemagglutinins, ha...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10020_chunk_0
Haemolymph juvenile hormone-binding protein
In molecular biology, the haemolymph juvenile hormone-binding protein (JHPB) family of proteins consists of several insect specific haemolymph juvenile hormone binding proteins. Juvenile hormone (JH) has a profound effect on insects. It regulates embryogenesis, maintains the status quo of larva development and stimulat...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10021_chunk_0
Haemolymph juvenile hormone-binding protein
The folding pattern for this structure closely resembles that found in some tandem-repeat mammalian lipid-binding and bactericidal permeability-increasing proteins, with a similar organisation of the major cavity and a disulfide bond linking the long helix and the beta-sheet. It would appear that JHBP forms two cavitie...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10022_chunk_0
Haemolysin expression modulating protein family
In molecular biology, the haemolysin expression modulating protein family is a family of proteins. This family consists of haemolysin expression modulating protein (Hha) from Escherichia coli and its enterobacterial homologues, such as YmoA from Yersinia enterocolitica, and RmoA encoded on the R100 plasmid. These prote...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10023_chunk_0
Heat-labile enterotoxin
In molecular biology, the heat-labile enterotoxin family includes Escherichia coli heat-labile enterotoxin (Elt or LT) and cholera toxin (Ctx) secreted by Vibrio cholerae. lt is so named because it is inactivated at high temperatures.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10024_chunk_0
Hexon protein
In molecular biology, the hexon protein is a major coat protein found in adenoviruses. Hexon coat proteins are synthesised during late infection and form homo-trimers. The 240 copies of the hexon trimer that are produced are organised so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10025_chunk_0
Hexon protein
The penton complex, formed by the peripentonal hexons and penton base (holding in place a fibre), lie at each of the 12 vertices. The hexon coat protein is a duplication consisting of two domains with a similar fold packed together like the nucleoplasmin subunits. Within a hexon trimer, the domains are arranged around ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10026_chunk_0
Hexon protein
Hexon directly recruits the cellular motor protein dynein in a pH-dependent manner. The dynein-regulatory protein, dynactin, was found to play a clear role in regulating the dynein-adenovirus complex transport to the nucleus. == References ==
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10027_chunk_0
Hyccin protein family
In molecular biology, the hyccin protein family is a family of proteins which may have a role in the beta-catenin-Tcf/Lef signaling pathway, as well as in the process of myelination of the central and peripheral nervous system. One member of this family is hyccin, encoded by the FAM126A gene. Defects in Hyccin are the ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10028_chunk_0
Hydrogenase maturation protease family
In molecular biology, the hydrogenase maturation protease family is a family of aspartic endopeptidases belonging to MEROPS family A31. The large subunit of -hydrogenase, as well as other nickel metalloenzymes, is synthesized as a precursor devoid of the metalloenzyme active site. This precursor undergoes a complex pos...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10029_chunk_0
Insect pheromone-binding protein
In molecular biology, the insect pheromone-binding family A10/OS-D is a family of small helical proteins postulated to contribute to the specificity of the insect’s olfactory system by binding components of the natural pheromone mixtures. A class of small (14-20 Kd) water-soluble proteins, called pheromone binding prot...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10030_chunk_0
Interferon gamma receptor (IFNGR1) family
In molecular biology, the interferon gamma receptor (IFNGR1) family is a family of proteins which includes several eukaryotic and viral interferon gamma receptor proteins. Members of this family include: The human interferon gamma receptor 1, which is a member of the hematopoietic cytokine receptor superfamily. It is e...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10031_chunk_0
Interferon-inducible GTPase
In molecular biology, the interferon-inducible GTPase (IIGP) family of proteins is thought to play a role in intracellular defence. IIGP is predominantly associated with the Golgi apparatus and also localises to the endoplasmic reticulum and exerts a distinct role in IFN-induced intracellular membrane trafficking or pr...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10032_chunk_0
Iron dependent repressor
In molecular biology, the iron dependent repressors are a family of bacterial and archaeal transcriptional repressors. At their N-terminus they contain a dtxR-type HTH domain. This is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 65 amino acids present in metalloregulators of the dtxR/mntR family. The d...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10033_chunk_0
Iron dependent repressor
Iron-responsive metalloregulators such as dtxR and ideR occur in Gram-positive bacteria of the high GC branch, while manganese-responsive metalloregulators like mntR are described in diverse genera of Gram-positive and Gram-negative bacteria and also in Archaea. The metalloregulators like dtxR/mntR contain the DNA-bind...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10034_chunk_0
Iron dependent repressor
Furthermore, dtxR and ideR control iron uptake. Homeostasis of manganese, which is an essential nutrient, is regulated by mntR. A typical dtxR-type metalloregulator binds two divalent metal effectors per monomer, upon which allosteric changes occur that moderate binding to the cognate DNA operators.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10035_chunk_0
Iron dependent repressor
Iron-bound dtxR homodimers bind to an interrupted palindrome of 19 bp, protecting a sequence of ~30 bp. The crystal structures of iron-regulated and manganese-regulated repressors show that the DNA binding domain contains three alpha-helices and a pair of antiparallel beta-strands. Helices 2 and 3 comprise the helix-tu...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10036_chunk_0
Iron dependent repressor
This wHTH topology is similar to the lysR-type HTH. Most dtxR-type metalloregulators bind as dimers to the DNA major groove. Several proteins are known to contain a dtxR-type HTH domain.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10037_chunk_0
Iron dependent repressor
These include: Corynebacterium diphtheriae dtxR, a diphtheria toxin repressor, which regulates the expression of the high-affinity iron uptake system, other iron-sensitive genes, and the bacteriophage tox gene. Metal-bound dtxR represses transcription by binding the tox operator; if iron is limiting, conformational cha...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10038_chunk_0
Iron dependent repressor
The regulator represses genes for iron acquisition and activates iron storage genes, and is a positive regulator of oxidative stress responses. Bacillus subtilis mntR, a manganese transport regulator, binds Mn2+ as an effector and is a transcriptional repressor of transporters for the import of manganese. Treponema pal...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10039_chunk_0
Iron response element
In molecular biology, the iron response element or iron-responsive element (IRE) is a short conserved stem-loop which is bound by iron response proteins (IRPs, also named IRE-BP or IRBP). The IRE is found in UTRs (untranslated regions) of various mRNAs whose products are involved in iron metabolism. For example, the mR...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10040_chunk_0
Isocitrate/isopropylmalate dehydrogenase family
In molecular biology, the isocitrate/isopropylmalate dehydrogenase family is a protein family consisting of the evolutionary related enzymes isocitrate dehydrogenase, 3-isopropylmalate dehydrogenase and tartrate dehydrogenase.Isocitrate dehydrogenase (IDH), is an important enzyme of carbohydrate metabolism which cataly...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10041_chunk_0
Isocitrate/isopropylmalate dehydrogenase family
In Escherichia coli the activity of a NADP+-dependent form of the enzyme is controlled by the phosphorylation of a serine residue; the phosphorylated form of IDH is completely inactivated. 3-isopropylmalate dehydrogenase EC 1.1.1.85 (IMDH) catalyses the third step in the biosynthesis of leucine in bacteria and fungi, t...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10042_chunk_0
Jacalin-like lectin domain
In molecular biology, the jacalin-like lectin domain is a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B-cell functions, such as Jacalin, which binds to the T-antigen and act...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10043_chunk_0
Jacalin-like lectin domain
Database of jacalin like lectins and structure function relations. Proteins containing this domain include: Jacalin, a tetrameric plant seed lectin and agglutinin from Artocarpus heterophyllus (jackfruit), which is specific for galactose. Artocarpin, a tetrameric plant seed lectin from A. heterophyllus.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10044_chunk_0
Killer toxin Kp4 family
In molecular biology, the killer toxin Kp4 family is a family of killer toxins, which includes the Kp4 killer toxin from the smut fungus Ustilago maydis.Killer toxins are polypeptides secreted by some fungal species ("killer yeasts") that kill sensitive cells of the same or related species, often functioning by creatin...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10045_chunk_0
Killer toxin Kp4 family
KP4 inhibits voltage-gated calcium channels in mammalian cells, which in turn inhibits cell growth and division by blocking calcium import. KP4 adopts a structure consisting of a two-layer alpha/beta sandwich with a left-handed crossover. == References ==
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10046_chunk_0
Kinase binding protein CGI-121
In molecular biology, the kinase binding protein CGI-121 family of proteins includes the kinase binding protein CGI-121 and its homologues. CGI-121 has been shown to bind to the p53-related protein kinase (PRPK). CGI-121 is part of a conserved protein complex, KEOPS.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10047_chunk_0
Latexin family
In molecular biology, the latexin family is a family of proteins which family consists of several animal specific latexin and proteins related to latexin that belong to MEROPS proteinase inhibitor family I47, clan IH.Latexin, a protein possessing inhibitory activity against rat carboxypeptidase A1 (CPA1) and CPA2 (MERO...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10048_chunk_0
Latexin family
Tazarotene Induced Gene 1 (TIG1) is a putative transmembrane protein with a small N-terminal intracellular region, a single membrane-spanning hydrophobic region, and a large C-terminal extracellular region containing a glycosylation signal. TIG1 is up-regulated by retinoic acid receptor but not by retinoid X receptor-s...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10049_chunk_0
Leguminous lectin family
In molecular biology, the leguminous lectin family is a family of lectin proteins. It is one of the largest lectin families with more than 70 lectins reported in a review in 1990. Leguminous lectins consist of two or four subunits, each containing one carbohydrate-binding site. The interaction with sugars requires tigh...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10050_chunk_0
Leguminous lectin family
One of these loops contains transition metals, calcium and manganese, which keep the amino acid residues of the sugar-binding site at the required positions. Amino acid sequences of this loop play an important role in the carbohydrate-binding specificities of these lectins. These lectins bind either glucose, mannose or...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10051_chunk_0
Leguminous lectin family
The exact function of legume lectins is not known but they may be involved in the attachment of nitrogen-fixing bacteria to legumes and in the protection against pathogens.Some legume lectins are proteolytically processed to produce two chains, beta (which corresponds to the N-terminal) and alpha (C-terminal). The lect...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10052_chunk_0
Linker histone H1 variants
In molecular biology, the linker histone H1 is a protein family forming a critical component of eukaryotic chromatin. H1 histones bind to the linker DNA exiting from the nucleosome core particle, while the core histones (H2A, H2B, H3 and H4) form the octamer core of the nucleosome around which the DNA is wrapped.H1 for...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10053_chunk_0
Lipid-binding serum glycoprotein
In molecular biology, the lipid-binding serum glycoproteins family, also known as the BPI/LBP/Plunc family or LBP/BPI/CETP family represents a family which includes mammalian lipid-binding serum glycoproteins and/or proteins containing a structural motif known as the BPI fold. Members of this family include: Bactericid...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10054_chunk_0
Mir-219 microRNA precursor family
In molecular biology, the microRNA miR-219 was predicted in vertebrates by conservation between human, mouse and pufferfish and cloned in pufferfish. It was later predicted and confirmed experimentally in Drosophila. Homologs of miR-219 have since been predicted or experimentally confirmed in a wide range of species, i...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10055_chunk_0
Mir-219 microRNA precursor family
The hairpin precursors (represented here) are predicted based on base pairing and cross-species conservation; their extents are not known. In this case, the mature sequence is excised from the 5' arm of the hairpin. miR-219 has also been linked with NMDA receptor signalling in humans by targeting CaMKIIγ (a kind of pro...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10056_chunk_0
Myogenic determination factor 5
In molecular biology, the myogenic determination factor 5 proteins are a family of proteins found in eukaryotes. This family includes the Myf5 protein, which is responsible for directing cells to the skeletal myocyte lineage during development. Myf5 is likely to act in a similar way to the other MRF4 proteins such as M...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10057_chunk_0
Myogenic determination factor 5
Myogenic determination factor 5 proteins contain three conserved protein domains. A C-terminal Myf5 domain, a central basic helix-loop-helix (bHLH) domain and an N-terminal basic domain. The bHLH region mediates specific DNA binding.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10058_chunk_0
Myogenic determination factor 5
With 12 residues of the basic domain involved in DNA binding. The basic domain forms an extended alpha helix in the structure. == References ==
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10059_chunk_0
Octopine dehydrogenase family
In molecular biology, the octopine dehydrogenase family of enzymes act on the CH-NH substrate bond using NAD(+) or NADP(+) as an acceptor. The family includes octopine dehydrogenase EC 1.5.1.11, nopaline dehydrogenase EC 1.5.1.19, lysopine dehydrogenase EC 1.5.1.16 and opine dehydrogenase EC 1.5.1.-. NADPH is the prefe...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10060_chunk_0
Octopine dehydrogenase family
In bacteria, some of these opine dehydrogenases are involved in crown gall tumours that are produced by Agrobacterium spp., and which encode for the opine dehydrogenases on a Ti-plasmid. These bacteria can transfer a portion of this plasmid (T-DNA) to a susceptible plant cell; the T-DNA then integrates into the plant n...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10061_chunk_0
Octopine dehydrogenase family
Opine dehydrogenases are also found in the marine invertebrate cephalopods (octopuses, squid, and cuttlefish). For example, in marine cephalopods, octopine dehydrogenase activity in mantle muscle is significantly correlated with a species' ability to buffer the acidic end products of anaerobic metabolism, with activity...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10062_chunk_0
Plant calmodulin-binding domain
In molecular biology, the plant calmodulin-binding domain is a protein domain found repeated in a number of plant calmodulin-binding proteins. These domains are thought to constitute the calmodulin-binding domains of these proteins. Binding of the proteins to calmodulin depends on the presence of calcium ions. These pr...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10063_chunk_0
Polyketide synthesis cyclase family
In molecular biology, the polyketide synthesis cyclase family of proteins includes a number of cyclases involved in polyketide synthesis in a number of actinobacterial species. Aromatic polyketides are assembled by a type II (iterative) polyketide synthase in bacteria. Iterative type II polyketide syntheses produce pol...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10064_chunk_0
Pancreatic amylase
In molecular biology, the presence of amylase can serve as an additional method of selecting for successful integration of a reporter construct in addition to antibiotic resistance. As reporter genes are flanked by homologous regions of the structural gene for amylase, successful integration will disrupt the amylase ge...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10065_chunk_0
Sprouty protein
In molecular biology, the protein Sprouty is a developmental protein involved in cell signalling. It works by inhibiting the MAPK/ERK pathway.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10066_chunk_0
Adenosine deaminase z-alpha domain
In molecular biology, the protein domain Adenosine deaminase z-alpha domain refers to an evolutionary conserved protein domain. This family consists of the N-terminus and thus the z-alpha domain of double-stranded RNA-specific adenosine deaminase (ADAR), an RNA-editing enzyme. The z-alpha domain is a Z-DNA binding doma...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10067_chunk_0
S-Adenosylmethionine synthetase enzyme
In molecular biology, the protein domain S-adenosylmethionine synthetase, C-terminal domain refers to the C terminus of the S-adenosylmethionine synthetase
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10068_chunk_0
Phosphoribosylaminoimidazolesuccinocarboxamide synthase
In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase (EC 6.3.2.6). It is an enzyme that catalyzes the chemical reaction ATP + 5-amino-1-(5-phospho-D-ribosyl)i...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10069_chunk_0
Phosphoribosylaminoimidazolesuccinocarboxamide synthase
The systematic name of this enzyme class is 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate:L-aspartate ligase (ADP-forming). This enzyme participates in purine metabolism.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10070_chunk_0
Phosphoribosylaminoimidazolesuccinocarboxamide synthase
This particular protein family is of huge importance as it is found in all three domains of life. It is the seventh step in the pathway of purine biosynthesis. Purines are vital to all cells as they are involved in energy metabolism and DNA synthesis. Furthermore, they are of specific interest to scientific researchers...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10071_chunk_0
SAND DNA-binding protein domain
In molecular biology, the protein domain SAND is named after a range of proteins in the protein family: Sp100, AIRE-1, NucP41/75, DEAF-1. It is localised in the cell nucleus and has an important function in chromatin-dependent transcriptional control. It is found solely in eukaryotes.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10072_chunk_0
Serine O-acetyltransferase
In molecular biology, the protein domain SATase is short for Serine acetyltransferase and refers to an enzyme that catalyses the conversion of L-serine to L-cysteine in E. coli. More specifically, its role is to catalyse the activation of L-serine by acetyl-CoA.This entry refers to the N-terminus of the protein which h...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10073_chunk_0
Scavenger receptor cysteine-rich protein domain
In molecular biology, the protein domain SRCR is short for Scavenger receptor cysteine-rich domain. They are found solely in eukaryotes. These domains are present on the cell membrane and have a role in binding to specific ligands and are often found to be involved with the immune system.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10074_chunk_0
SWAP protein domain
In molecular biology, the protein domain SWAP is derived from the term Suppressor-of-White-APricot, a splicing regulator from the model organism Drosophila melanogaster. The protein domain is found in regulators that control splicing. It is found in splicing regulatory proteins. When a gene is expressed the DNA must be...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10075_chunk_0
Saccharopine dehydrogenase
In molecular biology, the protein domain Saccharopine dehydrogenase (SDH), also named Saccharopine reductase, is an enzyme involved in the metabolism of the amino acid lysine, via an intermediate substance called saccharopine. The Saccharopine dehydrogenase enzyme can be classified under EC 1.5.1.7, EC 1.5.1.8, EC 1.5....
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10076_chunk_0
Sda protein domain
In molecular biology, the protein domain Sda is short for suppressor of dnaA or otherwise known as sporulation inhibitor A. It is found only in bacteria. This protein domain is highly important to cell survival. When starved of nutrients, the cell is under extreme stress so undergoes a series of reactions to increase t...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10077_chunk_0
Sda protein domain
Sda protein domain is a checkpoint which prevents the formation of spores. The Sda domain affects cell signalling. It prevents the cell communicating the stress that it is under, which is crucial if the cell is to survive.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10078_chunk_0
SdrG C terminal protein domain
In molecular biology, the protein domain SdrG C terminal refers to the C terminus domain of an adhesin found only on the cell walls of bacteria. More specifically, SdrG is only found in gram-positive bacteria. This particular domain binds to a glycoprotein named fibrinogen.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10079_chunk_0
SdrG C terminal protein domain
SdrG stands for serine-aspartate dipeptide repeats, which as its name suggests, contains repeats of two amino acids, serine and aspartate.Gram-positive pathogens such as Staphylococci, Streptococci, and Enterococci, contain SdrG anchored to their cell walls; these proteins act as adhesins and help the bacteria adhere t...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10080_chunk_0
Sterile alpha motif
In molecular biology, the protein domain Ste50p mainly in fungi and some other types of eukaryotes. It plays a role in the mitogen-activated protein kinase cascades, a type of cell signalling that helps the cell respond to external stimuli, more specifically mating, cell growth, and osmo-tolerance in fungi.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10081_chunk_0
Sterile alpha motif
In molecular biology, the protein domain Sterile alpha motif (or SAM) is a putative protein interaction module present in a wide variety of proteins involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms. SAM domains have been shown to homo- a...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10082_chunk_0
Sterile alpha motif
Smaug, a protein that helps to establish a morphogen gradient in Drosophila embryos by repressing the translation of nanos (nos) mRNA, binds to the 3' untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal structure of the Smaug RNA-binding region shows a cluster of positively charged ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10083_chunk_0
Sterile alpha motif
These results suggest that the SAM domain might have a primary role in RNA binding. Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces. In the case of the SAM domain of EPHB2, each of these interfaces is able to form dimers. The presence of these two distinct...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10084_chunk_0
Stirrup protein domain
In molecular biology, the protein domain Stirrup is a domain, found only in found in the domain, archaea. The Stirrup protein domain is found in prokaryotic protein ribonucleotide reductases. It obtains its name due to its resemblance to an old fashioned Japanese stirrup. Stirrip has a molecular mass of 9 kDa and is fo...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10085_chunk_0
Apolipoprotein H
In molecular biology, the protein domain Sushi 2 is also known as the fifth protein domain of beta-2 glycoprotein 1 (β2-GP1). This protein domain is only found in eukaryotes. The first four domains found in Apolipoprotein H resemble each other, however the fifth one appears to be different.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10086_chunk_0
TCP protein domain
In molecular biology, the protein domain TCP is actually a family of transcription factors named after: teosinte branched 1 (tb1, Zea mays (Maize)), cycloidea (cyc) (Antirrhinum majus) (Garden snapdragon) and PCF in rice (Oryza sativa).
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10087_chunk_0
TyeA protein domain
In molecular biology, the protein domain TyeA is short for Translocation of Yops into eukaryotic cells A. It controls the release of Yersinia outer proteins (Yops) which help Yersinia evade the immune system. More specifically, it interacts with the bacterial protein YopN via hydrophobic residues located on the helices...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10088_chunk_0
VEK-30 protein domain
In molecular biology, the protein domain VEK-30, is a 30-amino acid long, internal peptide present within bacterial organisms that acts as an epitope or antigenic determinant. It increases the pathogenicity of the cell. More specifically, it is found in streptococcal M-like plasminogen (Pg)-binding protein (PAM) from g...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10089_chunk_0
WHEP-TRS protein domain
In molecular biology, the protein domain WHEP-TRS refers to helix-turn-helix domains. They are found in variable numbers in glutamyl-prolyl tRNA synthetase (EPRS). This protein domain has an important function in protein–protein interactions between synthetases. WHEP domains exhibit high-affinity interactions with tRNA...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10090_chunk_0
Whirly
In molecular biology, the protein domain Whirly is a transcription factor commonly found in plants. This means they aid the transcription of genes from DNA into a complementary copy of mRNA. In particular, in plants, they aid the transcription of plant defence genes.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10091_chunk_0
YopE protein domain
In molecular biology, the protein domain YopE refers to the secretion of virulence factors in Gram-negative bacteria involves transportation of the protein across two membranes to reach the cell exterior. It not only infects the host cell but also protects the bacteria. It undergoes several mechanisms to evade the host...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10092_chunk_0
Zeta toxin protein domain
In molecular biology, the protein domain Zeta (ζ) toxin refers to a protein domain found in prokaryotes, which acts as a UDP-N-acetylglucosamine kinase. Its function is to inhibit cell wall biosynthesis and it may act as a bactericide in nature. It is also thought that Zeta toxin induces reversible protective dormancy ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10093_chunk_0
B1 domain
In molecular biology, the protein domain b1 refers to the domain b1 of Protein L. L is a bacterial protein with immunoglobulin (Ig) light chain-binding properties. It contains a number of homologous b1 repeats towards the N terminus. These repeats have been found to be responsible for the interaction of protein L with ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10094_chunk_0
EIF-W2 protein domain
In molecular biology, the protein domain eIF4-gamma/eIF5/eIF2-epsilon is a family of evolutionarily related proteins. This domain is found at the C-terminus of several translation Initiation factors. It was first detected at the very C-termini of the yeast protein GCD6, eIF-2B epsilon, and two other eukaryotic translat...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10095_chunk_0
Shugoshin N terminal protein domain
In molecular biology, the protein domain named the Shugoshin N-terminal coiled-coil region is a domain found on the N-terminal region of the Shugoshin protein in eukaryotes. It has a role in attaching to the kinetochores, structures on the chromatids where microtubules attach. Shugoshin has a conserved coiled-coil N-te...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10096_chunk_0
Selenoprotein P
In molecular biology, the protein domain selenoprotein P (SelP) is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues. It is a secreted glycoprotein, often found in the plasma. Its precise function remains to be elucidated; however, it is thought to have antioxidant properties....
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10097_chunk_0
SurE, survival protein E
In molecular biology, the protein domain surE refers to survival protein E. It was originally found that cells that did not contain this protein, could not survive in the stationary phase, at above normal temperatures, and in high-salt media. Hence the name, survival protein E. It is a metal ion-dependent phosphatase t...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10098_chunk_0
WIF domain
In molecular biology, the protein domain, WIF N-terminal refers to the N terminal domain of the protein, WIF. It stands for, Wnt-inhibitory factor, whereby wnt is a signalling molecule also known as wingless. Wnt is a molecule in the wnt signaling pathway. The WIF domain binds to the wnt ligand since it inhibits it.
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus
wiki_10099_chunk_0
YTH domain
In molecular biology, the protein domain, YTH refers to a member of the YTH family that has been shown to selectively remove transcripts of meiosis-specific genes expressed in mitotic cells.This protein domain, the YTH-domain, is conserved across all eukaryotes and suggests that the conserved C-terminal region plays a ...
https://www.kaggle.com/datasets/conjuring92/wiki-stem-corpus