Enzyme that degrades nucleic acids into shorter oligonucleotides or single nucleotide subunits by hydrolyzing sugar-phosphate bonds in the nucleic acid backbone
Protein involved in the synthesis of a nucleotide, a phosphate ester of a nucleoside consisting of a purine or pyrimidine base linked to ribose or deoxyribose phosphates
Protein involved in the biochemical reactions of nucleotides Nucleotides are phosphate esters of a nucleoside consisting of a purine or pyrimidine base linked to ribose or deoxyribose phosphates
Protein which is derived from an RNA which has been modified by RNA editing, a process that changes the nucleotide sequence of an RNA from that of the DNA template encoding it. RNA editing can be due to nucleotide conversion, insertion and/or deletion
Antibody produced by a single clone of B cells and thus consisting of a population of identical antibody molecules all specicfic for a single antigenic determinant. They are produced from cultured hybridoma cell lines for research and commercial purposes
Protein involved in the biosynthesis of the pyridine nucleotides NAD and NADP. NAD may be synthesized de novo from aspartate and dihydroxyacetone phosphate or from tryptophan. NAD may also be synthesized from nicotinamide or nicotinic acid. NADP is formed via the phosphorylation of NAD by NAD+ kinase
Protein which is involved in the formation, organization and maintenance of the peroxisome. The peroxisome is a small eukaryotic organelle limited by a single membrane, specialized for carrying out oxidative reactions
Protein which contains at least one homeobox, a conserved sequence originally detected, on the nucleotide level, in many of the genes which give rise to homeotic and segmentation mutants in Drosophila The homeobox, also termed homeodomain, consists of about 60 amino acids and is involved in DNA-binding
Protein with an helicase activity. Helicases are ATPases that catalyze the unwinding of double-stranded nucleic acids. They are tightly integrated (or coupled) components of various macromolecular complexes which are involved in processes such as DNA replication, recombination, and nucleotide excision repair, as well as RNA transcription and splicing
Protein which, if defective, causes microphthalmia, a developmental anomaly in which the eyeballs are abnormally small. Disease severity ranges from moderate reduction of the size of a single eye to complete bilateral absence of ocular tissues. Microphthalmia can occur in isolation or as part of a syndrome
Protein which is posttranslationally modified by the attachment of either a single phosphate group, or of a complex molecule, such as 5'- phospho-DNA, through a phosphate group. Target amino acid is usually serine, threonine or tyrosine residues (mostly in eukaryotes), aspartic acid or histidine residues (mostly in prokaryotes)
Protein involved in the modification (capping) of the 5' end of eukaryotic mRNAs. This modification occurs after the beginning of transcription in the nucleus, and consists of adding a guanosine nucleotide to the 5'-end of mRNAs and then, methylating the guanosine Capping protects mRNAs at their termini against attack by phosphatases and other nucleases and promotes mRNA function at the level of initiation of translation
Enzyme that catalyzes the removal of the ammonia group from glutamine and transfers it to a substrate to form a new carbon-nitrogen group Glutamine amidotransferase (GATase) domains can occur either as single polypeptides or as domains in larger multifunctional proteins. There exist two classes of glutamine amidotransferases domains: I and II
Protein involved in the repair of DNA, the various biochemical processes by which damaged DNA can be restored. DNA repair embraces, for instance, not only the direct reversal of some types of damage (such as the enzymatic photoreactivation of thymine dimers), but also multiple distinct mechanisms for excising damaged base; termed nucleotide excision repair (NER), base excision repair (BER) and mismatch repair (MMR); or mechanisms for repairing double-strand breaks
Viral protein that is involved in or facilitates the conversion of a linear double stranded DNA viral genome into a circular form, either by homologous recombination between redundant ends or by association of complementary single stranded ends (sticky ends). Circular genomes can support rolling circle replication and, for many viruses, genome circularization is also necessary for latency
Protein located in or on the host thylakoid, a membranous cellular structure containing the photosynthetic pigments, reaction centers and electron-transport chain. In host chloroplast, thylakoids stack up to form the grana or stay as single cisternae and interconnect the grana Thylakoid, where photosynthesis occurs, are found in chloroplasts, cyanelles and in photosynthetic bacteria where they are the extensive invaginations of the plasma membrane
Protein involved in quorum sensing (QS). QS is a phenomenon whereby the accumulation of signaling molecules enables a single cell to sense the number of bacteria (cell density). The bacterial reponse to QS includes adaptation to availability of nutrients, defence against other microorganisms which may compete for the same nutrients and the avoidance of toxic compounds potentially dangerous for the bacteria
The kinetochore is a complex assembled at centromeric region of DNA, which provides the major attachment point for the spindle microtubules. In monocentric chromosomes, the kinetochores of point centromeres bind a single microtubule and the larger kinetochores of regional centromeres interact with a number of microtubules. In holocentric chromosomes, the kinetochores bind the diffuse centromere along the length of the chromosomes
Protein located in or on the thylakoid, a membranous cisterna of the chloroplast. Thylakoids stack up to form the grana or stay as single cisternae and interconnect the grana. The thylakoid contains the photosynthetic pigments, reaction centers and electron-transport chain. Thylakoid, where photosynthesis occurs, are also found in cyanelles and in photosynthetic bacteria where they are the extensive invaginations of the plasma membrane
Protein associated with the kinetoplast DNA (kDNA), the mitochondrial DNA of trypanosomatid protozoa. kDNA is a massive network, composed of thousands of topologically interlocked DNA circles. Each cell contains one network condensed into a disk-shaped structure within the matrix of its single mitochondrion. The kDNA circles are of two types, maxicircles present in a few dozen copies and minicircles present in several thousand copies
Protein found in or associated with the peroxisome, a small eukaryotic organelle limited by a single membrane, specialized for carrying out oxidative reactions. Contains mainly peroxidases, several other oxidases and catalase. The catalase regulates the contents of the produced toxic hydrogen peroxide thus protecting the cell. Beta- oxidation of fatty acids is another major function of peroxisomes. In plants and fungi this degradation occurs only in this cellular compartment
Protein of the DNA-directed RNA polymerase complexes, which catalyze RNA synthesis the by addition of ribonucleotide units to a RNA chain using DNA as a template. They can initiate a chain de novo Prokaryotes have a single enzyme for the three RNA types that is subject to stringent regulatory mechanisms. Eukaryotes have type I that synthesizes all rRNA except the 5S component, type II that synthesizes mRNA and hnRNA and type III that synthesizes tRNA and the 5S component of rRNA
Enzymes capable of altering the degree of supercoiling of double- stranded DNA molecules. Various topoisomerases can increase or relax supercoiling, convert single-stranded rings to intertwined double- stranded rings, tie and untie knots in single stranded and duplex rings or catenate and decatenate duplex rings. Any enzyme that cleaves only one strand of a DNA duplex and then reseals it is classified as a type I topoisomerase (Topo I). Type II topoisomerases (Topo II) change DNA topology by breaking and rejoining double-stranded DNA
Protein which binds at least one S-adenosyl-L-methionine (SAM), or protein whose function is SAM-dependent. S-adenosyl-L-methionine, a conjugate of the nucleotide adenosine and the amino acid methionine, is a substrate/cofactor in numerous enzyme-catalyzed reactions Enzymatic reactions that involve interactions of proteins with S- adenosyl-L-methionine include transfer of methyl, thiomethyl, aminoalkyl and adenosyl groups. It not only provides methyl groups to be transferred in numerous biological reactions, but also acts as a precursor in the biosynthesis of polyamines and metal ion chelating compounds. It is also a source of catalytic 5'-deoxyadenosyl radicals produced as reaction intermediates by a superfamily of radical enzymes. It is also involved in decarboxylation reactions
Protein which, if defective, causes rhizomelic chondrodysplasia punctata (RCDP). This lethal autosomal recessive disease is characterized by proximal limb shortening, severely disturbed endochondrial bone formation, and intellectual disability. RCDP type 1 (RCDP1) is the classical and most common form. It is a peroxisome biogenesis disorder caused by mutations in the PEX7 gene, which encodes the PTS2-receptor peroxin-7. RCDP type 2 (RCDP2) and RCDP type 3 (RCDP3) result from single peroxisomal enzyme deficiencies: dihydroxyacetone phosphate synthase is deficient in RCDP2 and dihydroxyacetone phosphate acyltransferase in RCDP3. Both enzymes are involved in the biosynthesis of plasmalogens
Protein which, if defective, causes any one of a clinically heterogeneous group of disorders arising from dysfunction of the mitochondrial respiratory chain. The phenotypic spectrum ranges from isolated diseases affecting single organs to severe multisystem disorders. Common clinical features include ptosis, external ophthalmoplegia, proximal myopathy and exercise intolerance, cardiomyopathy, sensorineural deafness, optic atrophy, pigmentary retinopathy, encephalopathy, seizures, stroke-like episodes, ataxia, and spasticity. Mitochondrial disorders can be caused by mutations of mitochondrial DNA or nuclear DNA that either affect oxidative phosphorylation proteins directly, or affect respiratory chain function by impacting the production of the complex machinery needed to run this process
Protein involved in the synthesis of cobalamin. Cobalamin, which is synthesized by microorganisms, has equatorial sites occupied by a modified porphyrin ring system, with two of the four pyrrol rings fused directly (without an intervening methine bridge). The modified porphyrin system binds a cobalt(III) ion in the center, and this is called a corrin ring system. One axial site is occupied usually by an intramolecularly-bound dimethylbenzimidazole nucleotide and the other axial site is occupied by a number of different ligands such as water (aquacobalamin), cyanide (cyanocobalamine=vitamin B12), glutathione (glutathionylcobalamine), 5'deoxyadenosine (adenosylcobalamine=coenzyme B12) or a methyl group (methylcobalamin) Vitamin B12, for instance, is a prosthetic group of certain mammalian enzymes, where it is essential for the normal maturation and development of erythrocytes. A deficiency in the diet or more frequently the failure to absorb the vitamin B12 give rise to pernicious anemia
A clinically variable and genetically heterogeneous malformation in which the developing forebrain fails to correctly separate into right and left hemispheres. In its most severe form (alobar holoprosencephaly), the forebrain consists of a single ventricle, and midbrain structures may be malformed as well. In the most extreme cases, anophthalmia or cyclopia is evident along with a congenital absence of the mature nose. In milder forms (semilobar or lobar holoprosencephaly), rudimentary midline structures are present. The less severe form features facial dysmorphia characterized by ocular hypertelorism, defects of the upper lip and/or nose, and absence of the olfactory nerves or corpus callosum. The majority of cases are sporadic, although families with both autosomal dominant and autosomal recessive holoprosencephaly have been described
Protein involved in RNA-mediated gene silencing. This term describes a number of related processes which use 21- to 25-nucleotide RNAs to repress the expression of specific target genes. These processes include the post-transcriptional regulation of mRNA by either RNA interference (RNAi) or endogenously encoded microRNAs (miRNAs) and the transcriptional regulation of mRNA by RNAi-mediated chromatin silencing. RNAi is generally triggered by the presence of dsRNA produced by bidirectional transcription or by the transcription of an inverted repeat or hairpin sequence. dsRNA is processed into small interfering RNAs (siRNAs) of around 21 nucleotide which are then incorporated into the RNA-induced silencing complex (RISC), which cleaves mRNAs with sequences fully complementary to the siRNA. miRNAs differ from siRNAs principally in their biogenesis. miRNA genes encode precursors with complex hairpin structures which are processed by endonucleolytic cleavage to form mature miRNAs. Like siRNAs, miRNAs function in RISC-like complexes. Animal miRNAs generally inhibit translation of target mRNAs following imperfect base pairing to the 3'-untranslated region (3'-UTR), while most plant miRNAs show nearly precise complementarity to coding regions of target mRNAs and trigger mRNA degradation similar to siRNAs. Finally, in RNAi-mediated chromatin silencing, siRNAs derived from repeat element transcripts are incorporated into the nuclear RNAi-induced initiator of transcriptional silencing complex (RITS), where they guide chromatin modifications such as histone methylation which lead to transcriptional silencing
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