FUNCTION: Thiol-disulfide oxidoreductase probably involved in the redox regulation of a number of cytosolic enzymes. Possesses insulin disulfide bonds reducing activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.


FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)- ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32001091). In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity). SUBCELLULAR LOCATION: Apical cell membrane Melanosome Cytoplasm Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cysteine-rich repeat secretory protein family.


FUNCTION: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.


FUNCTION: Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.


FUNCTION: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes and is involved in DNA repair. Also involved in pre-rRNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RuvB family.


FUNCTION: Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host chloroplast envelope. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Binds to sodium channels (Nav) and affects the channel activation process. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.


FUNCTION: Catalyzes the reductive methylation of deoxyuridylate to thymidylate. SIMILARITY: Belongs to the thymidylate synthase family.


FUNCTION: Does not have 2'-5'-OAS activity, but can bind double- stranded RNA. SIMILARITY: Belongs to the 2-5A synthase family.


FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Participates in the interconnection of tauA with tauB via its contacts with TFC3 and TFC6. Serves as a scaffold critical for tauA-DNA spatial configuration and tauB-DNA stability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIIC subunit 5 family.


FUNCTION: RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up- regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits TUT4 and TUT7 uridylyltransferases (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). This results in the terminal uridylation of target pre-miRNAs (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity). SUBCELLULAR LOCATION: Cytoplasm Rough endoplasmic reticulum Cytoplasm, P-body Cytoplasm, Stress granule Nucleus, nucleolus Note=Predominantly cytoplasmic (PubMed:22118463). In the cytoplasm, localizes to peri-endoplasmic reticulum regions and detected in the microsomal fraction derived from rough endoplasmic reticulum (RER) following subcellular fractionation. May be bound to the cytosolic surface of RER on which ER-associated mRNAs are translated (By similarity). Shuttle from the nucleus to the cytoplasm requires RNA-binding (PubMed:17617744). Nucleolar localization is observed in 10-15% of the nuclei in differentiated myotubes (By similarity). SIMILARITY: Belongs to the lin-28 family.


FUNCTION: Repressor of the mexAB-oprM multidrug resistance operon. Also represses its own expression. Many variants lead to increased expression of the mexAB-oprM operon.


FUNCTION: Kills Lactococci.


FUNCTION: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines. SUBCELLULAR LOCATION: Secreted Note=In ovarian carcinoma, secreted and also observed at the apical membrane and in cytoplasm at the invasive front. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.


FUNCTION: Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.


FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. SIMILARITY: Belongs to the COPE family.


FUNCTION: Probable ion channel required for the normal function of cochlear hair cells (PubMed:11850618). Component of the hair cell's mechanotransduction (MET) machinery. Involved in mechanosensitive responses of the hair cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localized to the stereocilia of the cochlear hair cells. SIMILARITY: Belongs to the TMC family.


FUNCTION: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the OadG family.


FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions. Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as heme deficiency, oxidative stress, osmotic shock, mitochondrial dysfunction and heat shock. EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming. Acts as a key sensor of heme-deficiency: in normal conditions, binds hemin via a cysteine thiolate and histidine nitrogenous coordination, leading to inhibit the protein kinase activity. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell: heme depletion relieves inhibition and stimulates kinase activity, activating the ISR. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. It thereby plays an essential protective role for RBC survival in anemias of iron deficiency. Also activates the ISR in response to mitochondrial dysfunction: HRI/EIF2AK1 protein kinase activity is activated upon binding to the processed form of DELE1 (S-DELE1), thereby promoting the ATF4-mediated reprogramming (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.


FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. Required for nodule development. SIMILARITY: Belongs to the ALAD family.


FUNCTION: May act as an antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Frog skin active peptide (FSAP) family. Septenin subfamily.


FUNCTION: This protein is a transcriptional activator. It may play a role in the formation of segmented structures of the embryo. May play an important role in the normal development of the vertebral column (By similarity). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Cytochrome P450 monooxygenase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker (PubMed:22870285). The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H (PubMed:17360612). The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-2,10(14)-diene-8-beta-ol (PubMed:22870285). The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C- 16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol (PubMed:22870285). The dioxygenase fc-dox then catalyzes the 16- oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al) (PubMed:21299202, PubMed:22870285). The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol (PubMed:21299202, PubMed:22870285). The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O- glycosyltransferase PaGT (PubMed:22870285). Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O- methyltransferase PaMT to yield fusicoccin P (PubMed:22870285). Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT (PubMed:22287087). Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2 (PubMed:22870285). Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A (PubMed:22870285). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Involved in pyrimidine catabolism. Catalyzes the deamination of 3-aminoacrylate to malonic semialdehyde, a reaction that can also occur spontaneously. RutC may facilitate the reaction and modulate the metabolic fitness, rather than catalyzing essential functions. SIMILARITY: Belongs to the RutC family.


FUNCTION: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma Note=Assembles into long tubular structures at the surface of the infected protoplast. SIMILARITY: Belongs to the alfamovirus movement protein family.


FUNCTION: GLC7 phosphatase-regulatory protein involved in GLC7 subcellular redistribution and chromosome segregation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GIP4 family.


FUNCTION: Cell signaling peptide that may regulate plant stress, growth, and development. Mediates a rapid alkalinization of extracellular space by mediating a transient increase in the cytoplasmic Ca(2+) concentration leading to a calcium-dependent signaling events through a cell surface receptor and a concomitant activation of some intracellular mitogen-activated protein kinases (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant rapid alkalinization factor (RALF) family.


FUNCTION: 2-hydroxyisoflavanone 4'-O-methyltransferase involved in the biosynthesis of formononetin. Can use 2,7,4'-trihydroxyisoflavanone as substrate, but not daidzein. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.


FUNCTION: The presence of this protein prevents gop protein from killing E.coli.


FUNCTION: Possesses quercetin 3-O-glucosyltransferase activity in vitro. Involved in stress or defense responses. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 13 family.


FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C- terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Plays a role in meiosis and sporulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ATG3 family.


FUNCTION: The subtype gamma methyltransferase (M) subunit of a type I restriction enzyme. The M and S subunits together form a methyltransferase (MTase) that methylates A-2 on the top and A-3 on the bottom strand of the sequence 5'-GAYN(5)GTAA-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage. SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.


FUNCTION: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38.


FUNCTION: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11809832). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:25208553). Required for the centralization of the mitotic spindle and symmetric division of zygotes (PubMed:25208553). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (By similarity). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration (PubMed:15649475). SUBCELLULAR LOCATION: Nucleus matrix Cytoplasm, cytoskeleton Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, lamellipodium Cell projection, growth cone Cell projection, axon Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. SIMILARITY: Belongs to the actin-binding proteins ADF family.


FUNCTION: Acts as a transcription factor that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many promoters (PubMed:16310763, PubMed:21502138). Involved in the development of the excretory duct cell, by positively modulating embryonic transcription of putative transcription factor lin-48, acting in concert with cell death specification protein ces-2 (PubMed:16310763). Negatively modulates expression of key autophagy- related genes, bec-1/ATG6 and lgg-1/ATG8, and may link together autophagy and apoptosis during development (PubMed:21502138). Positively modulates expression of neuropeptide pigment dispersing factor homologs pdf-1 and pdf-2 (PubMed:19686386). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER- associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress- induced autophagy, and may act as a tumor suppressor. Also plays a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation. Participates as well in T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.


FUNCTION: Sugar kinase that catalyzes the ATP-dependent phosphorylation of N-acetylmuramate (MurNAc) and N-acetylglucosamine (GlcNAc) at its C1 hydroxyl group, leading to MurNAc alpha-1P and GlcNAc alpha-1P, respectively (By similarity). Is likely involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc (PubMed:23831760). Is able to complement the fosfomycin sensitivity phenotype of a P.putida mutant lacking amgK (PubMed:23831760). SIMILARITY: Belongs to the kinase AmgK family.


FUNCTION: May play a role in ribosome biogenesis, being required for integration of the 5S RNP into the ribosomal large subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the NOP53 family.


FUNCTION: Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds.


FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Involved in the modulation of glucose- induced microautophagy of peroxisomes independent of its ability to metabolize glucose intermediates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.


FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.


FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pyridoxine kinase family.


FUNCTION: Inhibits all catalytic activities of RNA polymerase (RNAP) by partially occluding its substrate-binding site and preventing NTP binding. SIMILARITY: Belongs to the GreA/GreB family.


FUNCTION: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane (By similarity). Calcium-dependent NAD(P)H dehydrogenase. Binds calcium ions. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Peroxisome. SIMILARITY: Belongs to the NADH dehydrogenase family.


FUNCTION: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (By similarity). Also has an inhibitory role in some cells (By similarity). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (By similarity). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By similarity). Associates with natural killer (NK) cell receptors such as the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By similarity). Associates with TREM1 to mediate activation of neutrophils and monocytes (By similarity). Associates with TREM2 on monocyte- derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (By similarity). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (By similarity). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allosimulatory ability (By similarity). Negatively regulates B cell proliferation (By similarity). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the TYROBP family.


SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UPF0154 family.


FUNCTION: GA14 synthase; part of the gene cluster that mediates the biosynthesis of gibberellins (GAs), diterpenoids that may provide a selective advantage during infection of the preferred host plant, rice (PubMed:23825955, PubMed:9917370, PubMed:10347043, PubMed:12750377, PubMed:15925394). Gibberellins (GAs) are diterpenoids and are synthesized via the mevalonate pathway (PubMed:12750377). Biosynthesis of the major metabolite GA3 (gibberellic acid) from geranylgeranyl diphosphate (GGPP) requires 13 steps (PubMed:12750377). The GGPP produced by the geranylgeranyl diphosphate synthase GGS2 is converted to ent-kaurene via ent-copalyldiphosphate in a two-step cyclization reaction performed by the bifunctional ent-copalyl diphosphate synthase/ent-kaurene synthase enzyme (CPS/KS) (PubMed:9745028, PubMed:10803977, PubMed:12750377). Ent-Kaurene is metabolized to GAs by a series of oxidation reactions catalyzed by cytochrome P450 monooxygenases (PubMed:9917370, PubMed:12750377). Cytochrome P450 monooxygenase P450-4 is an ent-kaurene oxidase that catalyzes the three oxidation steps between ent-kaurene and ent-kaurenoic acid (PubMed:11472927). The highly multifunctional cytochrome P450 monooxygenase P450-1 then catalyzes four steps involving oxidation at two carbon atoms, in the main pathway from ent-kaurenoic acid to GA14 via GA12-aldehyde as well as producing kaurenolides and fujenoic acids as by-products (PubMed:11320210). The cytochrome P450 monooxygenase P450-2 then converts GA14 to GA4 by removal of C-20 (PubMed:11943776). GA4 is further converted to GA7 by the GA4 desaturase DES via 1,2- desaturation before cytochrome P450 monooxygenase P450-3, a 13- hydroxylase, hydroxylates GA7 to GA3, the final product of the GA- biosynthetic pathway (PubMed:12750377). SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit J family.


FUNCTION: Insecticidal toxin. Causes flaccid paralysis followed by death when injected into Heliothis virescens larvae. Does not induce any toxic effects when injected intravenously into adult mice at a dose of 1.1 mg/kg body weight. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 16 (SFI) family.


SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class II family.


FUNCTION: Displays phosphatase activity for serine/threonine residues. Has apparently no phosphoglycerate mutase activity. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.


FUNCTION: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein srd family.


FUNCTION: Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family.


FUNCTION: HPTA is an acidic heparin-binding growth factor for hepatocytes.


FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). SIMILARITY: Belongs to the ALAD family.


FUNCTION: Mediates the negative regulation of the lcrGVH operon by ATP or calcium. Acts as a modulator of the yop operon expression. SIMILARITY: Belongs to the LcrH/SycD chaperone family.


SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. IRG family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS11 family.


FUNCTION: This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil. SIMILARITY: Belongs to the leguminous lectin family.


FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity (By similarity). SIMILARITY: Belongs to the calcineurin regulatory subunit family.


FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ferrochelatase family.


FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3- phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity). Binds DNA in vitro (PubMed:22589465). Together with DNA polymerase II subunit B3-1 (DPB3-1) and GAPC1, enhances heat tolerance and promotes the expression of heat-inducible genes (PubMed:32651385). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Accumulates in the nucleus under heat stress. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.


FUNCTION: Involved in catabolism of D-apiose. Catalyzes the transfer of the glycolaldehyde group from apulose-4-phosphate to D-glyceraldehyde 3-phosphate, generating dihydroxyacetone phosphate and D-xylulose-5- phosphate. SIMILARITY: Belongs to the transketolase family.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily.


FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system (PubMed:8631948, PubMed:19965576). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:8631948, PubMed:19965576). Catalyzes the epoxidation of double bonds of PUFA (PubMed:8631948, PubMed:19965576). Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE), likely playing a major role in the epoxidation of endogenous cardiac arachidonic acid pools (PubMed:8631948). In endothelial cells, participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15- lipoxygenase metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs), which are precursors of vasodilatory trihydroxyicosatrienoic acids (THETAs). This hydroperoxide isomerase activity is NADPH- and O2-independent (PubMed:19737933). Catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone (PubMed:19923256). Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole (PubMed:23959307). Catalyzes the sulfoxidation of fenbedazole (PubMed:19923256). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Plastid thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family.


SIMILARITY: To A.muscaria DOPA 4,5-dioxygenase.


FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (PubMed:22467853). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the DDOST 48 kDa subunit family.


FUNCTION: Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin- modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260, PubMed:30327463). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (PubMed:30228260, PubMed:30327463). Plays a role in facilitating transcriptional elongation and repression of spurious transcription initiation through regulation of histone acetylation (By similarity). Essential for proper mitosis progression (PubMed:28645917). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiM family.


FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Inhibits the activity of both neurogenic (neurod1/neuroD) and myogenic (myod1/myoD) bHLH factors. May play a role in the regulation of the circadian clock (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Carboxylesterase present at high level in urine that regulates production of felinine, a probable pheromone precursor. Probably acts by hydrolyzing the peptide bond of the felinine precursor 3-methylbutanol cyteinylglycine, producing felinine and glycine in cat urine. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.


FUNCTION: Involved in the anomeric conversion of L-rhamnose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose mutarotase family.


SUBCELLULAR LOCATION: Secreted Secreted, cell wall.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM19 family.


FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). SIMILARITY: Belongs to the glycogen phosphorylase family.


FUNCTION: Alpha-2,8-sialyltransferase that prefers O-glycans to N- glycans or glycolipids as acceptor substrates. The minimal acceptor substrate is the NeuAc-alpha-2,3(6)-Gal sequence at the non-reducing end of their carbohydrate groups. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family.


FUNCTION: Efficiently catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4- didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4- didehydroretinal), also acts on all-trans retinal and all-trans retinoic acid. The replacement of 11-cis retinal chromophore in photopigments with 11-cis 3,4-didehydroretinal enhances sensitivity to long-wavelength light. This may improve vision in fresh water which is often turbid. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Stabilizes dimeric photosystem II (PSII). In its absence no dimeric PSII accumulates and there is a reduction of monomeric PSII. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single- pass membrane protein. Note=The N-terminus is found within the thylakoid lumen (By similarity). SIMILARITY: Belongs to the psbW family.


FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N- exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the EMC2 family.


FUNCTION: Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6- phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily.


FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the ku80 family.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.


FUNCTION: Flavonoid 3-O-glycosyltransferase involved in the biosynthesis of anthocyanins confering flower red/pink colors, mainly anthocyanidin 3-O-glycosides (PubMed:35651780). Catalyzes the addition of UDP-sugar to the 3-OH of anthocyanidin, with a preference for UDP- galactose (UDP-Gal) as sugar donor and cyanidin as substrate; able to use delphinidin, pelargonidin, peonidin, malvidin and petunidin as substrates in the presence of UDP-Gal (PubMed:35651780). Can also use UDP-glucose (UDP-Glu) as sugar donor with delphinidin, cyanidin and malvidin as substrates, but not active on pelargonidin, peonidin and petunidin (PubMed:35651780). SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Probable toxin. Does not show insecticidal, antimicrobial and antiparasitic activities. Does not induce increase in intracellular calcium in mouse DRG neurons, suggesting that it does not induce pain. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the limacoditoxin-12 family.


FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family.


FUNCTION: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. SUBCELLULAR LOCATION: Basal cell membrane; Multi-pass membrane protein. Note=Situated at the basal membrane of cochlear outer hair cells. SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.4/KCNQ4 sub-subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase type 2 family.


FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. The most favorable substrate is beechwood xylan. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.


FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. SIMILARITY: Belongs to the arabinose isomerase family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS3 family.


FUNCTION: Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN) (PubMed:30728519, PubMed:30763082). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor (PubMed:30728519, PubMed:30763082). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.


FUNCTION: Essential for male fertility and sperm mitochondrial sheath formation (By similarity). Required for proper mitochondrial elongation and coiling along the flagellum during the formation of the mitochondrial sheath (By similarity). Facilitates the growth and aggressiveness of neuroblastoma cells (PubMed:30026490). Increases the EZH2 activity and H3K27me3 levels in a RBBP4-dependent manner, and facilitates the enrichment of polycomb repressive complex 2 and H3K27me3 on gene promoters, resulting in transcriptional repression of tumor suppressors affecting the proliferation, invasion, and metastasis of tumor cells (PubMed:30026490). SUBCELLULAR LOCATION: Nucleus Mitochondrion outer membrane; Peripheral membrane protein.


FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. SIMILARITY: Belongs to the PTPS family. QueD subfamily.


FUNCTION: Long-chain fatty alcohol oxidase involved in the omega- oxidation pathway of lipid degradation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GMC oxidoreductase family.


FUNCTION: Catalyzes the hydrolysis of the phospho group from alpha- ribazole 5'-phosphate to form alpha-ribazole (PubMed:20363939). May also catalyze the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12) (By similarity). Has a possible role in B12 recycling, but the primary role of the C-terminal domain of this phosphatase enzyme could be phosphate generation to help bacterial survival within the macrophage, which is a phosphate-deprived environment (PubMed:20363939). FUNCTION: Endonuclease that displays both RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. As the only authenticated RNase HI in M.tuberculosis, probably plays an important role in the physiology of this organism, being likely involved in bacterial replication. SIMILARITY: In the C-terminal section; belongs to the histidine phosphatase superfamily. SIMILARITY: In the N-terminal section; belongs to the RNase H family.


FUNCTION: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6- sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6- sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone. SIMILARITY: Belongs to the glycosyl hydrolase 16 family.


FUNCTION: Involved in pre-mRNA splicing. May be involved in endoplasmic reticulum-associated protein degradation (ERAD) and required for growth at low and high temperatures (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DnaJ family.


SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


SIMILARITY: Belongs to the site-specific recombinase resolvase family.


FUNCTION: May be involved in the modulation of rDNA transcription. SIMILARITY: Belongs to the RRT5 family.


FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory- like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (By similarity). Costimulates NK cells and trigger lysis of target cells independently of IgG binding. Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (By similarity). FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory- like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation. Costimulates NK cells and trigger lysis of target cells independently of IgG binding (By similarity). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Secreted Note=Exists also as a soluble receptor.


FUNCTION: Involved in the oxidative degradation of abscisic acid. Plays an important role in determining abscisic acid levels in dry seeds and in the control of postgermination growth. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


SIMILARITY: Belongs to the urocanase family.


FUNCTION: May play an important role in trophoblast development and in the regulation of bone formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family.


FUNCTION: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1- phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (By similarity). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily.


FUNCTION: Myoactive; induces a rapid concentration-dependent muscle tension increase. FUNCTION: Active on neuromusculature. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.


FUNCTION: May act as transcriptional regulator. Induces apoptosis in infected cells. Element of infectious replication cycle (By similarity). SUBCELLULAR LOCATION: Host nucleus. Note=Host nucleus of infected cells. SIMILARITY: Belongs to the gyrovirus apoptin family.


FUNCTION: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Bacterial flagellum basal body. SIMILARITY: Belongs to the FliG family.


FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the catalase family. HPII subfamily.


FUNCTION: Catalyzes the reaction that attaches fucose through an O- glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP- fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DELTA1 or JAGGED1 (By similarity). Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 65 family.


FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.


FUNCTION: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the classical AGP family.


SIMILARITY: Belongs to the herpesviridae UL91 family.


FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily.


FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate, mediating L-threonine catabolism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family.


FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.


FUNCTION: Citrate synthase-like protein; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) (PubMed:27056201). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms (PubMed:27056201). These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase pks2, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product (By similarity). The phenylalanine ammonia lyase (PAL) M7 and the acyl-CoA ligase M9 are involved in transforming phenylalanine into benzoyl-CoA (By similarity). The citrate synthase- like protein R3 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit (By similarity). The potential hydrolytic enzymes, M8 and M10, are in close proximity to pks2 and may participate in product release (By similarity). On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase pks1 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase M4 (PubMed:11251290, PubMed:15489970, PubMed:28106181). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (PubMed:11251290, PubMed:15489970, PubMed:28106181). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (PubMed:11251290, PubMed:15489970, PubMed:28106181). The enoyl reductase and C-MeT of pks1 are not active in the final round of extension (PubMed:11251290, PubMed:15489970, PubMed:28106181). The acetyltransferase M4 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (Probable). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases M1, R1 and R2 (Probable). Finally, in support of the identification of the cluster as being responsible for SQS1 production, the cluster contains a gene encoding a putative squalene synthase (SS) R6, suggesting a likely mechanism for self-resistance (Probable). SIMILARITY: Belongs to the citrate synthase family.


FUNCTION: This enzyme participates in both the breakdown and synthesis of glucose. SIMILARITY: Belongs to the phosphohexose mutase family.


FUNCTION: Required for the calcium-dependent exocytosis of signal sequence-containing cytokines such as CCL5. Probably acts in cooperation with the SNARE machinery (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi- pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Note=Mainly localizes in Golgi apparatus membrane. Upon calcium-triggered exocytosis, it translocates to the cell membrane. Highly enriched in synaptic vesicles (By similarity). SIMILARITY: Belongs to the SCAMP family. SCAMP5 subfamily.


SUBCELLULAR LOCATION: Fimbrium. Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the N-Me-Phe pilin family.


FUNCTION: Cleaves the C-terminal D-alanine residue of UDP-muramyl- pentapeptide (UDP-MurNAc-L-Ala-D-Glu-mDAP-D-Ala-D-Ala) (PubMed:1510448). However the physiological substrate likely contains L-Lys instead of mDAP at the third position of the pentapeptide (Probable). Also releases the C-terminal D-lactate from UDP-MurNAc-L- Ala-D-Glu-mDAP-D-Ala-D-lactate, a depsipeptide produced by the vancomycin resistance protein VanA. Therefore, VanY should contribute in vivo to the hydrolysis of both the D-alanyl-D-alanine- and the depsipeptide-containing peptidoglycan precursors (PubMed:1510448). Is not necessary for vancomycin resistance of E.faecium BM4147 (PubMed:1398115). Does not display transpeptidase or beta-lactamase activities (PubMed:1510448). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase M15B family.


FUNCTION: Member of the two-component regulatory system NtrY/NtrX involved in nitrogen level control. Probably activates NtrX by phosphorylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


SIMILARITY: Belongs to the NTE family.


FUNCTION: Tyrosine decarboxylase that converts tyrosine into tyramine, a precursor of isoquinoline alkaloids and various amides. SIMILARITY: Belongs to the group II decarboxylase family.


FUNCTION: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of A1 at HMR. FUNCTION: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that, in a/alpha diploid cells, binds cooperatively with the ALPHA2 protein to a 21-bp DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MATA1 family.


FUNCTION: S-adenosyl-l-methionine-dependent Diels-Alderase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4- hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:31216742). IliD catalyzes the Diels-Alder reaction that converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H (PubMed:31216742). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (PubMed:31216742) (Probable). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.


FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:12917342). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5- dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity). In response to induction by transcription factor EGR1/NGFI-A in the hippocampus, may play a role in the behavioral and hypothalamic-pituitary-adrenal responses to stress in offspring (PubMed:15220929). FUNCTION: [Isoform A]: Has transcriptional activation and repression activity. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression. SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm Nucleus Mitochondrion Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=After ligand activation, translocates from the cytoplasm to the nucleus (By similarity). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (By similarity). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily.


FUNCTION: Required for respiration and the maintenance of the mitochondrial compartment. Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.


FUNCTION: Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PUR DNA-binding protein family.


FUNCTION: This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'. SIMILARITY: Belongs to the DnaT family.


FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H4 family.


FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. This includes the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. As part of a multisubunit ubiquitin ligase complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (By similarity). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (By similarity). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (PubMed:33590678). FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (PubMed:27863225, PubMed:27863226). FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed:7821821). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity). FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694, PubMed:26138980, PubMed:29779948, PubMed:30166453, PubMed:29775578). This includes the von Hippel-Lindau ubiquitination complex CBC(VHL) (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). By binding to BC- box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes (PubMed:10205047, PubMed:12004076, PubMed:12050673, PubMed:15590694). As part of a multisubunit ubiquitin ligase complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:26138980, PubMed:29779948, PubMed:29775578). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). FUNCTION: Core component of multiple cullin-RING-based ECS (ElonginB/C- CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. This includes the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes. As part of a multisubunit ubiquitin ligase complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (By similarity). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (By similarity). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity). FUNCTION: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SKP1 family.


FUNCTION: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking. SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein Endomembrane system; Single-pass type IV membrane protein Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein Note=Associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Associated with the trans-Golgi, but not with the cis-Golgi apparatus (By similarity). SIMILARITY: Belongs to the synaptobrevin family.


FUNCTION: Required for growth and/or survival at acidic conditions. FUNCTION: Required for growth and/or survival at acidic conditions (pH 4.5). Needed for the adaptation process at pH 4.5 that enables cells to survive at extremely low pH (pH 2.0). SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the Asr family. SIMILARITY: Belongs to the Asr family.


FUNCTION: Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.


FUNCTION: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (By similarity). In addition to autophagy, also plays a role in necrotic cell death (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Multi-pass membrane protein Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Mitochondrion membrane; Multi-pass membrane protein Note=Mainly localizes to the trans-Golgi network (TGN) and the endosomal system; cycles between them though vesicle trafficking. Export from the TGN to promote formation of autophagosomes is mediated by the AP-4 complex. Under amino acid starvation or rapamycin treatment, redistributes to preautophagosomal structure/phagophore assembly site (PAS). The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1. Upon autophagy induction, a small portion transiently localizes to the autophagic membranes. Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner. SIMILARITY: Belongs to the ATG9 family.


FUNCTION: Component of the nuclear pore complex that has a direct role in nuclear protein import (By similarity). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta- cargo complex and importin recycling (By similarity). Binds to transcriptionally active chromatin sites when located in the nucleoplasm and is involved in transcriptional activation (PubMed:20144760). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus envelope Chromosome Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side Note=Associates with chromatin (PubMed:20144760).


FUNCTION: Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family.


FUNCTION: Probable endonuclease. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family.


FUNCTION: Transcriptional activator required for growth on non- fermentable carbon sources and that regulates genes involved in fatty acid utilization (PubMed:11353088, PubMed:24998441). Acts as a direct activator that binds the promoters of oleate utilizing genes, encoded key enzymes in beta-oxidation and NADPH regeneration (POX1, FOX2,POT1 and IDP2), the glyoxylate shunt (MLS1 and ICL1), and gluconeogenesis (PCK1 and FBP1) (PubMed:24998441). Regulates also the abundance of peroxisomes that are vital for fatty acid oxidation (PubMed:24998441). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Prenyltransferase that mediates the formation of menaquinone- 4 (MK-4), a vitamin K2 isoform, thereby acting as a mitochondrial electron carrier. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. MK-4 acts as a membrane electron carrier downstream of a electron transport chain complex, improving mitochondrial oxygen consumption. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family.


FUNCTION: Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins (By similarity). SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.


FUNCTION: ATP-binding RNA helicase involved in ribosome assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1 subfamily.


FUNCTION: Exopeptidase that catalyzes the hydrolytic cleavage of multi- L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides. SIMILARITY: Belongs to the peptidase S51 family.


FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the mature virion (MV) membrane. The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. SIMILARITY: Belongs to the orthopoxvirus OPG086 family.


FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1C) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg- Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation. The CRL2(FEM1C) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding. SIMILARITY: Belongs to the fem-1 family.


FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). SIMILARITY: Belongs to the SepCysS family.


SIMILARITY: Belongs to the transcriptional antiterminator BglG family. GlcT subfamily.


FUNCTION: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Plays an important role in DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MCM family.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the RNA polymerase alpha chain family.


SIMILARITY: Belongs to the POTE family.


FUNCTION: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family.


FUNCTION: Anti-inflammatory antagonist of interleukin-1 family of proinflammatory cytokines such as interleukin-1beta/IL1B and interleukin-1alpha/IL1A. Protects from immune dysregulation and uncontrolled systemic inflammation triggered by IL1 for a range of innate stimulatory agents such as pathogens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-1 family.


FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin N superfamily.


FUNCTION: Putative transcription factor that functions in pseudohyphal growth. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EFG1/PHD1/stuA family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein.


FUNCTION: Member of the two-component regulatory system DltS/DltR. Regulates the expression of the dlt operon. Probably phosphorylates DltR (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the COG5 family.


FUNCTION: ATP:ADP antiporter that catalyzes the exchange of ATP and ADP across the endoplasmic reticulum (ER) membrane. Imports ATP from the cytosol to the ER lumen and exports ADP in the opposite direction. Regulates ER energy metabolism and protein biogenesis. Appears to be part of a calcium-dependent ER to cytosol low energy response axis, where calcium efflux from ER to the cytosol triggers ATP import into the ER lumen to maintain sufficient ATP supply. Provides ATP to ER chaperone HSPA5 that drives protein folding and trafficking in the ER. Can transport dATP, UTP or UDP in exchange for ATP, but the physiological relevance of this process remains to be established. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily.


FUNCTION: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor (PubMed:5412063). Other substrates include phenylethanolamine and octopamine (By similarity). Also methylates normetanephrine (PubMed:13863458, PubMed:5412063). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.


FUNCTION: Involved in ciliogenesis (PubMed:28625504). It is required for appropriate acetylation and polyglutamylation of ciliary microtubules, and regulation of cilium length (By similarity). Acts as a positive regulator of hedgehog (Hh) signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Cell projection, cilium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localized to the proximal region in cilia. Stimulation of Hh signaling leads to redistribution of ARMC9 toward the ciliary tip within 6 hours, follow by a gradual return to its original proximal location (By similarity). Localizes to the daughter centriole of the primary cilium in RPE1 cells (By similarity).


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0177 family.


FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. SIMILARITY: Belongs to the threonine aldolase family.


FUNCTION: Transcriptional coactivator that may regulate cell type- specific differentiation pathways. SIMILARITY: Belongs to the POU2AF family.


FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity). FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein OPG116 (PubMed:20861259). Serves as a bridge which links the DNA polymerase OPG071 and the uracil DNA glycosylase (PubMed:11711620). SIMILARITY: Belongs to the orthopoxvirus OPG148 family. SIMILARITY: Belongs to the poxviruses A20 family.


SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein Virion. SIMILARITY: Belongs to the asfivirus CP123L family.


FUNCTION: Involved in glycoprotein quality control as it is important for the targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations it further trims the carbohydrates to Man(5)GlcNAc(2). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 47 family.


FUNCTION: Involved in late/very late gene activation. SIMILARITY: Belongs to the baculoviridae LEF-11 family.


FUNCTION: Capsid protein p30 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). SUBCELLULAR LOCATION: [Matrix protein p15]: Virion. SUBCELLULAR LOCATION: [Capsid protein p30]: Virion.


FUNCTION: Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MtrA family.


FUNCTION: Plays a role in viral cell-to-cell propagation, by facilitating genome transport to neighboring plant cells through plasmosdesmata. May induce the formation of granular vesicles derived from the Endoplasmic reticulum, which align on actin filaments (By similarity). SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the Tymovirales TGBp3 protein family.


FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF- type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily.


FUNCTION: Salivary tick protein that modulates host immune response. This protein blocks dendritic cell (DC) differentiation from monocytes (PubMed:23825947). In addition, it inhibits up-regulation of costimulatory molecules and pro-inflammatory cytokines in response to stimuli and promotes up-regulation of co-inhibitory molecules and the anti-inflammatory cytokine interleukin-10. It has a pocket to accomodate cholesterol, which may have immune-modulatory roles, either directly or through interactions with the host gut microbiota (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CCR4/nocturin family.


FUNCTION: EF-1-beta and EF-1-beta' stimulate the exchange of GDP bound to EF-1-alpha to GTP. SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.


FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 4 subfamily.


FUNCTION: Controls stomatal patterning. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant cysteine rich small secretory peptide family. Epidermal patterning factor subfamily.


FUNCTION: RNA-binding protein that acts as a translational repressor. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PAT1 family.


FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in ribosomal protein rps2. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.


FUNCTION: Short chain dehydrogenase; part of the Fg3_54/C64 gene cluster that mediates the biosynthesis of the octapeptide fusaoctaxin A, a virulence factor that is required for cell-to-cell invasiveness of plant host (PubMed:30804501). The 2 nonribosomal peptide synthetases NRPS9 and NRPS5 form an assembly line which likely utilizes GABA as a starter unit (loaded on the unique module M1 of NRPS9) and sequentially incorporates seven extender units composed of the residues L-Ala, L- allo-Ile, L-Ser, L-Val, L-Ser, L-Leu and L-Leu, respectively (PubMed:30804501, PubMed:31100892). During the process, each of the residues that are tethered on modules M3-M7 of NRPS5 containing an E domain can undergo an epimerization reaction to produce a D- configuration before the transpeptidation reaction occurs (PubMed:30804501, PubMed:31100892). The elongation of the peptidyl chain might be terminated by module M8-mediated L-Leu incorporation, followed by R domain-catalyzed 4 electron reduction to release the resulting octapeptide from the assembly line as an alcohol (PubMed:30804501, PubMed:31100892). Fusaoctaxin A is cleaved by the cluster specific ABC transporter FGM5 to the pentapeptide fusapentaxin A and the tripeptide fusatrixin A (PubMed:31100892). The other enzymes from the cluster, FGM1, FGM2, FGM3 and FGM9 seem not to be involved in the biosynthesis of fusaoctaxin A and their functions have still to be determined (Probable). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Excitatory insect beta-toxins induce a spastic paralysis (PubMed:32442468). They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). In vivo, this recombinant protein is lethal to Locusta migratoria larvae after injection, but has no significant effect when orally administered. Is not toxic to mice after intracerebroventricular injection (PubMed:32442468). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.