FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. SIMILARITY: Belongs to the RnpA family.


FUNCTION: Catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate, with a reduction of O2 to H2O2. In extant N2-fixing cyanobacteria such as Nostoc, this enzyme primarily serves as an O2- scavenging enzyme, protecting nitrogenase that is extremely sensitive to O2, and is therefore an essential partner in N2 fixation. Also shows clear oxidase activity with glyoxylate in vitro, and low activity with glycerate, hydroxypyruvate and glycolate. The very low glycolate oxidase activity indicates that this enzyme is unlikely to be involved in photorespiratory glycolate metabolism, a pathway that seems to exist in this cyanobacterium, but in which the oxidation of glycolate is taken over by glycolate dehydrogenase (GlcD). Is not able to use D- lactate as substrate and does not show any dehydrogenase activity with NAD(+) or NADP(+). SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.


FUNCTION: Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the NIP7 family.


FUNCTION: Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L- alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction. FUNCTION: Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L- alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E- BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF- kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P- 5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet- derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. FUNCTION: One of the few specific substrates of AKT2 identified so far is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Phosphorylates CLK2 on 'Thr-343'. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell membrane; Peripheral membrane protein Early endosome Note=Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N- terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3. Colocalizes with WDFY2 in early endosomes. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.


FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate. SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.


FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. SIMILARITY: Belongs to the PTPS family.


FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase H family.


FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors. Plays a role in associative learning and in long-term memory consolidation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane Postsynaptic density. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PRA-PH family.


FUNCTION: Responsible for the reduction of the keto group on the C-3 of sterols. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.


FUNCTION: May act as an acid--thiol ligase that activates carboxylic acids by forming acyl-CoAs. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the KdpC family.


FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. SIMILARITY: Belongs to the RNase Z family.


FUNCTION: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics (PubMed:7758472). Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes (By similarity). In vitro, catalyzes the N- oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L- carnitine (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FMO family.


FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.


FUNCTION: Auxiliary spliceosomal protein involved in splicing of specific pre-mRNAs that affect multiple aspects of development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RED family.


FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class II subfamily.


FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS. SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Cell projection, dendritic spine Postsynaptic density membrane. SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.


FUNCTION: Required for chromosome pairing and genetic recombination. MER1 may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product.


FUNCTION: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys. FUNCTION: Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (PubMed:15546957, PubMed:16709924, PubMed:19380772). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival (By similarity). In humans, the immunological role in the monocytic/macrophage/dendritic cell (DC) lineage is unsure. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic granule Note=Localized in azurophil granules of neutrophils (PubMed:15546957). SIMILARITY: Belongs to the arginase family.


FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.


FUNCTION: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily.


FUNCTION: Involved in the regulation of flowering time under short day (SD) and long day (LD) conditions. Functions as floral promoter by negatively regulating GHD7, a repressor of the photoperiodic control of flowering (PubMed:22399582, PubMed:22422935, PubMed:22912900). Acts as floral activator in the LD photoperiodic pathway (PubMed:22888152). Involved in blue light-induced activation of EHD1 expression to promote flowering under SD conditions (PubMed:22912900). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Receptor for ecdysone (PubMed:1913820, PubMed:30293839). Binds to ecdysone response elements (ECRES) following ecdysone-binding, and recruitment of a complex containing the histone methyltransferase trr, leads to activate transcription of target genes (PubMed:1913820, PubMed:30293839). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.


FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Seems to contribute to the inhibition of germination during stress (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.


FUNCTION: Catalyzes the esterification of bacteriochlorophyllide a by geranylgeraniol-PPi. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily.


FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.


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 1 subfamily.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular lipids, exerting anti-inflammatory and immunosuppressive functions (PubMed:10531313, PubMed:23690440, PubMed:26392224, PubMed:10455175). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). In draining lymph nodes, selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are precursors of the anti-inflammatory lipid mediators, resolvins (PubMed:23690440). During the resolution phase of acute inflammation drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses dendritic cell activation and T-helper 1 immune response (PubMed:23690440, PubMed:27226632). May act in an autocrine and paracrine manner. Via a mechanism independent of its catalytic activity, promotes differentiation of regulatory T cells (Tregs) and participates in the maintenance of immune tolerance (PubMed:19564598). May contribute to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (PubMed:11694541). SUBCELLULAR LOCATION: [Isoform 1]: Secreted Cell membrane Note=Localizes to cell membrane likely through binding to heparan sulfate proteoglycans. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Probably plays an important role in intracellular peptide degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M17 family.


FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP (PubMed:10404228, PubMed:11452035). Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions (PubMed:11452035). Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than XTP, and has nearly no activity toward the canonical nucleotides ATP, CTP, and TTP, and toward 6-N-hydroxylaminopurine deoxynucleoside triphosphate (dHAPTP) (PubMed:10404228, PubMed:11452035). Displays neither endonuclease nor 3'-exonuclease activities (PubMed:11452035). SIMILARITY: Belongs to the HAM1 NTPase family.


FUNCTION: In insects, FMRFamide and related peptides have modulatory actions at skeletal neuromuscular junctions, and peptides that are immunologically related to FMRFamide are released into the circulation from neurohemal organs. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.


FUNCTION: Antiviral interferon-stimulated protein that plays a role in innate immunity and in the suppression of viruses through different mechanisms (PubMed:33147462, PubMed:36594413). Plays a role in the late phase response of TLR-induced immune effector expression (By similarity). During influenza infection, interacts with PB2, PB1, and PA to disrupt the formation of the viral RdRp complex (PubMed:33147462). Inhibits zika virus by interacting with the capsid protein in the nucleolus and reducing its abundance through proteasomal degradation (PubMed:36594413). Strong transcriptional coactivator (PubMed:10982866). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). SIMILARITY: Belongs to the GST superfamily. Omega family.


FUNCTION: Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (PubMed:23719382). Orchestrates hematopoietic stem and progenitor cell emergence from the hemogenic endothelium, a type of specialized endothelium manifesting hematopoietic potential. YJEFN3-mediated cholesterol efflux activates endothelial SREBF2, the master transcription factor for cholesterol biosynthesis, which in turn transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence (PubMed:30705153).


FUNCTION: Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.


FUNCTION: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CAF1 family.


FUNCTION: Transglycosidase operating by a ping-pong reaction mechanism. Involved in the synthesis of raffinose, a major soluble carbohydrate in seeds, roots and tubers (By similarity). SIMILARITY: Belongs to the glycosyl hydrolases 36 family.


FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.


FUNCTION: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. SIMILARITY: Belongs to the YjjX NTPase family.


FUNCTION: Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6- methoxy-1,4-benzoquinol during ubiquinone biosynthesis. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the COQ7 family.


SIMILARITY: Belongs to the GTP cyclohydrolase I family.


FUNCTION: Secreted immune-induced peptide induced by Toll signaling. Has a role in resistance to bacterial and fungal infections (PubMed:25915418, PubMed:29920489). The strength of antimicrobial activity appears to correlate with the overall level of expression (PubMed:29920489). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bomanin family.


FUNCTION: Essential for pollen development. Involved in protein N- glycosylation in the endoplasmic reticulum (ER), especially in the female gametophyte. Mediates pollen tube (PT) reception in synergids through protein glycosylation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the polyprenol kinase family.


FUNCTION: Elicits an increase in arterial blood pressure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family.


FUNCTION: Mediates the deactivation of rap1 during multicellular development and is required for normal morphogenesis. Also required for the correct patterning of specific subtypes of prestalk cells.


FUNCTION: Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the THI4 family.


FUNCTION: The VP3 protein is one of the five proteins (with VP1, VP4, VP6 and VP7) which form the inner capsid of the virus. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the orbivirus VP3 family.


FUNCTION: Orphan receptor. May be a receptor for RFamide-family neuropeptides such as NPFF and NPAF, which are analgesic in vivo. May regulate nociceptor function and/or development, including the sensation or modulation of pain. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily.


SIMILARITY: Belongs to the jacalin lectin family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.


FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.


SIMILARITY: Belongs to the FAM106 family.


FUNCTION: Involved in the export and assembly of FimA fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family.


FUNCTION: Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell. SIMILARITY: Belongs to the GlnE family.


FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HisA/HisF family.


FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerS subfamily.


FUNCTION: Midgut thrombin inhibitor that plays a major role in keeping the midgut microenvironment at low hemostatic and inflammatory tonus (PubMed:18286181) (By similarity). Also inhibits FXIa (F11), kallikrein (KLK1), neutrophil elastase (ELANE) and cathepsin G (CTSG), which play a role in the contact pathway of the coagulation cascade (PubMed:18286181) (By similarity). Also abrogates platelet aggregation by cathepsin G and plasmin, and attenuates tissue factor (F3) pathway inhibitor cleavage by elastase (PubMed:18286181) (By similarity). In vivo, inhibits thrombosis and promotes bleeding in mice (By similarity). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Involved in calcium binding and microtubule stabilization. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCTP family.


FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.


FUNCTION: Mediates electron flow from quinones to the NapAB complex. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the NapC/NirT/NrfH family.


FUNCTION: One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. FUNCTION: Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.


FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 30 kDa subunit family.


FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.


FUNCTION: Rod linker protein, associated with allophycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=This protein occurs in the rod, it is associated with allophycocyanin. SIMILARITY: Belongs to the phycobilisome linker protein family.


FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton Chromosome Lipid droplet Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.


FUNCTION: Probably mediates zinc uptake from the rhizosphere. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.


FUNCTION: Involved in primary cell wall organization. Required for the accumulation of crystalline cellulose. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family.


FUNCTION: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.


FUNCTION: Has a function in the early stage of chloroplast development and palisade cell morphogenesis (PubMed:8861949). Required for correct plastid ribosome assembly. Required for processing and maturation of 4.5S rRNA (PubMed:15010617). SUBCELLULAR LOCATION: Plastid, chloroplast.


FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Golgi apparatus, trans- Golgi network membrane; Single-pass type I membrane protein Endosome membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Late endosome membrane; Single-pass type I membrane protein Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation. SIMILARITY: Belongs to the MHC class II family.


FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acyl carrier protein (ACP) family.


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


SIMILARITY: Belongs to the SRP1/TIP1 family. Seripauperin subfamily.


FUNCTION: The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TrpB family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the macin family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 6 family.


FUNCTION: Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevent their translation. Prevents translation of unlocalized nos in the bulk cytoplasm via the recruitment of cup (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SMAUG family.


FUNCTION: Required for neoxanthin biosynthesis. Probably not involved directly in the enzymatic conversion of violaxanthin to neoxanthin. Is necessary but not sufficient for neoxanthin synthesis. Seems not required for abscisic acid (ABA) biosynthesis in response to drought stress.


FUNCTION: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.


FUNCTION: Component of the core of the flagella. SUBCELLULAR LOCATION: Periplasmic flagellum. Periplasm. SIMILARITY: Belongs to the bacterial flagellin family.


FUNCTION: Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex. SIMILARITY: Belongs to the eIF-6 family.


FUNCTION: Thiol S-methyltransferase that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine to hydrogen sulfide and other thiol compounds including dithiothreitol, 7alpha-thiospironolactone, L- penicillamine, and captopril. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Lipid droplet Note=Highly concentrated in the perinuclear area of the endoplasmic reticulum (ER) and surrounding lipid droplets. May be associated with the specific regions of the LR that form lipid droplets and targeted to the initial deposits of lipids where the lipid droplets form. SIMILARITY: Belongs to the methyltransferase superfamily.


FUNCTION: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscL family.


FUNCTION: May play a role in neuronal cell development. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAM114 family.


FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbK family.


SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the CBF/MAK21 family.


SIMILARITY: Belongs to the peptidase C19 family.


FUNCTION: Involved in the transport of maltose and maltodextrins. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family.


FUNCTION: Probable NADPH-dependent quinone reductase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L- tryptophan by the aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain (PubMed:17704773). TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5 (PubMed:17704773, PubMed:18029206). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC120, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localizes to the subdistal appendages of centrioles (PubMed:28422092).


FUNCTION: Involved in C-to-U editing of mitochondrial RNA. Functions as minor mitochondrial editing factor. Controls 6 percent of the mitochondrial editing sites. SUBCELLULAR LOCATION: Mitochondrion.


FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AdoMet synthase family.


FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone. SIMILARITY: Belongs to the F420-dependent glucose-6-phosphate dehydrogenase family.


FUNCTION: Involved in zinc efflux across the cytoplasmic membrane, thus reducing zinc accumulation in the cytoplasm and rendering bacteria more resistant to zinc. It may contribute to zinc homeostasis at low concentrations of zinc. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.


FUNCTION: Involved in mRNA splicing. Helps to stabilize the U1 snRNP-5' splice site interaction (By similarity). FUNCTION: Involved in mRNA splicing. Helps to stabilize the U1 snRNP-5' splice site interaction. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SWT21 family.


FUNCTION: Probable transcription regulator that functions in the development of the carpel margin meristem similarly to SEUSS (SEU). In association with SEU, supports organ development from meristematic regions by facilitating auxin response and thus organ initiation, and by sustaining meristematic potential through the maintenance of PHABULOSA expression (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the adn1/SEU family.


FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (By similarity). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (PubMed:20149843, PubMed:8558235). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family.


FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L- methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non- enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate- dependent dioxygenase easH which introduces a hydroxyl group into N-(D- lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: Molecular chaperone. Has ATPase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family.


FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. SIMILARITY: Belongs to the NifH/BchL/ChlL family.


SIMILARITY: Belongs to the peptidase M18 family. SIMILARITY: Belongs to the peptidase M18 family.


FUNCTION: The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the YAE1 family.


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


FUNCTION: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Blocked by external barium or cesium (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane; Lipid-anchor. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ2 subfamily.


FUNCTION: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation). SIMILARITY: Belongs to the SELO family.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


SIMILARITY: Belongs to the GAGE family.


FUNCTION: Constituent of viral factories. Binds to ssRNA and dsRNA (By similarity). SUBCELLULAR LOCATION: Host cytoplasm Note=Constituent of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the phytoreovirus RNA-binding protein family.


FUNCTION: Probable regulator of exocrine pancreas development. SIMILARITY: Belongs to the PPDPF family.


FUNCTION: Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. FieF subfamily.


FUNCTION: Essential for neural crest development, converting cells from an epidermal fate to a neural crest cell fate. Binds to DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family.


FUNCTION: Sodium- and chloride-dependent glycine transporter which is essential for regulating glycine concentrations at inhibitory glycinergic synapses. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A9 subfamily.


FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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. SIMILARITY: Belongs to the histone H2A family.


FUNCTION: Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A26 family.


FUNCTION: May be involved in regulating the specificity of expression of the catecholamine biosynthetic genes. Acts as a transcription activator/factor. Could maintain the noradrenergic phenotype (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family.


FUNCTION: Involved in stress signaling pathway that mediates cell death in response to endoplasmic reticulum (ER) stress and osmotic stress. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: This protein binds directly to 23S rRNA. Interacts with the A site tRNA. SIMILARITY: Belongs to the universal ribosomal protein uL16 family.


FUNCTION: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.


FUNCTION: The antenna complex functions as a light receptor, it captures and delivers excitation energy to photosystems II and I. The Prochlorales pcb genes are not related to higher plant LHCs. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. IsiA/Pcb subfamily.


FUNCTION: Orphan receptor. Possible candidate for amine-like G-protein coupled receptor (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


SIMILARITY: Belongs to the beta-eliminating lyase family.


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. 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 to 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). FUNCTION: This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP- dependent manner (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol 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. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. SIMILARITY: Belongs to the WD repeat COPB2 family.


FUNCTION: Responsible for the low-affinity transport of potassium into the cell. Likely operates as a K(+):H(+) symporter. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72) family.


FUNCTION: Snake venom serine protease that activates plasminogen. Weakly hydrolyzes the alpha chain of human fibrinogen without releasing fibrinopeptide A. Does not hydrolyze plasma kallikrein or factor Xa. Does not clot fibrinogen. Does not affect platelet function. Induces hypotensive effects on rats. Shows a preferential cleavage at Lys-|-Xaa over Arg-|-Xaa bonds. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.


FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.


FUNCTION: Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic.


FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family.


FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AccD/PCCB family.


FUNCTION: Highly active in the 15-alpha-hydroxylation of testosterone. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin. SIMILARITY: Belongs to the GTP cyclohydrolase IV family.


SIMILARITY: Belongs to the DEAD box helicase family.


SUBCELLULAR LOCATION: Cytoplasm Secreted. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation. SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PSRP subfamily.


FUNCTION: Catalyzes reversively the conversion of L-aspartate beta- semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination with L-glutamate. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily.


FUNCTION: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane protein Note=Localizes to the Z ring in an FtsZ-dependent manner. SIMILARITY: Belongs to the ZipA family.


FUNCTION: May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.


FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP- dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin- independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family.


SIMILARITY: Belongs to the UPF0251 family.


FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus Host cytoplasm. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B family.


FUNCTION: Degrades both double-stranded linear and covalently closed circular DNA. Likely to play a scavenging role in order to supply nutrients under starvation conditions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: To B.subtilis NucA/ComI.


FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, involved in both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. In the cytoplasm, stimulates translation initiation and regulates mRNA decay through translation termination- coupled poly(A) shortening, probably mediated by PAN (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.


FUNCTION: Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PpaX family.


FUNCTION: Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation. SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase family.


FUNCTION: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm. Polymerizes into shorter and less stable actin filaments compared to ACT2/actin-2; this is thought to facilitate gliding motility and host cell invasion. Has ATPase activity. ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi. ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP- Pi-bound actin. Plays an essential role during the asexual blood stage. At the segmented schizont stage, required for apicoplast migration and segregation into individual daughter merozoites. Also, required for the separation of daughter merozoites in the final stages of cytokinesis. Essential for merozoite invasion of, but not adhesion to or reorientation towards, host erythrocytes. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton Note=During host erythrocyte invasion, filamentous actin localizes close to the junction between merozoites and the host cell. In schizonts, filamentous actin appears to connect apicoplasts (By similarity). Prior to gametocyte activation in the mosquito midgut, localizes to both the cytoplasm and the nucleus. Following gametocyte activation, relocalizes completely to the cytoplasm, in an ACT2-dependent manner (By similarity). SIMILARITY: Belongs to the actin family.


SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the Psb28 family.


FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. In addition to the protease activity, also mediates delipidation of PE-conjugated ATG8 proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C54 family.


FUNCTION: Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type III membrane protein.


FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein.


SIMILARITY: Belongs to the PurH family. SIMILARITY: Belongs to the PurH family.


FUNCTION: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Heme (hemin) importer (TC 3.A.1.14.5) family.


FUNCTION: May act as an inhibitor of TGF-beta signaling. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein Secreted.


FUNCTION: May regulate MCM3AP phosphorylation through phosphatase recruitment. May act as a negative regulator of ABCB1 expression and function through the dephosphorylation of ABCB1 by TFPI2/PPP2R3C complex. May play a role in the activation-induced cell death of B- cells. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Excluded from the nucleoli. Localization is cell cycle-dependent. Localizes to the cytoplasm during cytokinesis.


FUNCTION: Transcription activator involved in oxidative stress response and cadmium resistance (PubMed:9439570). Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways. Activity of the transcription factor is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Activation by alkyl hydroperoxides or cadmium induces nuclear accumulation and as a result YAP1 transcriptional activity (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Oxidized YAP1 is found predominantly in the nucleus, while reduced YAP1 is continuously exported to the cytoplasm by CRM1/exportin 1. SIMILARITY: Belongs to the bZIP family. YAP subfamily.


FUNCTION: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. SUBCELLULAR LOCATION: Cytoplasm Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. SIMILARITY: Belongs to the FtsZ family.


FUNCTION: Host-defense peptide that maintains sterility in the urogenital system (By similarity). Has antimicrobial activity against a wide range of bacteria, including Gram-negative E.coli, P.aeruginosa and S.typhimurium, and Gram-positive E.aerogenes, S.aureus, B.cereus, E.faecium and L.monocytogenes (By similarity). Confers resistance to intestinal infection by S.typhimurium (By similarity). Exhibits antimicrobial activity against enteric commensal bacteria such as B.adolescentis, L.acidophilus, B.breve, L.fermentum, B.longum and S.thermophilus (By similarity). Binds to bacterial membranes and causes membrane disintegration (By similarity). Induces the secretion of the chemokine IL-8 by intestinal epithelial cells (By similarity). Binds to B.antracis lef/lethal factor, a major virulence factor from B.anthracis, and neutralizes its enzymatic activity (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasmic vesicle, secretory vesicle Note=Stored as propeptide HD5(20-94) in secretory granules of small intestinal Paneth cells and found in the ileum lumen as processed mature peptides, predominantly in the HD5(63-94) form. Peptides HD5(20- 94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94) being the predominant intracellular form. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the most abundant form (By similarity). Secreted into the female genital tract lumen (By similarity). SIMILARITY: Belongs to the alpha-defensin family.


FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylate kinase family.


FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (PubMed:19744929, PubMed:22311970, PubMed:21900231, PubMed:27484799). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (PubMed:27484799). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (PubMed:19744929). Autoacetylates in vivo (PubMed:19744929). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (PubMed:19744929). Component of N-alpha- acetyltransferase complexes containing NAA10 and NAA15, which has N- alpha-acetyltransferase activity (PubMed:16507339, PubMed:29754825, PubMed:27484799, PubMed:32042062). Does not influence the acetyltransferase activity of NAA10 (PubMed:16507339, PubMed:27484799). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (PubMed:32042062). The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (PubMed:16507339, PubMed:27484799). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (PubMed:17502424, PubMed:27422821). FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (By similarity). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (By similarity). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (By similarity). Autoacetylates in vivo (By similarity). The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo (By similarity). Component of N-alpha-acetyltransferase complexes containing NAA10 and NAA15, which has N-alpha-acetyltransferase activity (By similarity). Does not influence the acetyltransferase activity of NAA10 (By similarity). However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex) (By similarity). The multiprotein complexes probably constitute the major contributor for N- terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides (By similarity). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes to the cytoplasm in interphase cells (PubMed:17502424). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes to the cytoplasm in interphase cells. SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.


FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.


FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA53 to GA20 via a three-step oxidation at C-20 of the GA skeleton (PubMed:12077303, PubMed:11961544, PubMed:30002253). Catalyzes the conversion of GA12 to GA9 via a three- step oxidation at C-20 of the GA skeleton (PubMed:30002253). Contributes to the promotion of internode elongation in response to submergence via ethylene and gibberellin signalings (PubMed:30002253). FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA53 to GA20 via a three-step oxidation at C-20 of the GA skeleton. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family. GA20OX subfamily.


FUNCTION: One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SIMILARITY: Belongs to the universal ribosomal protein uL3 family.


FUNCTION: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. AraH/RbsC subfamily.


FUNCTION: Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MatP family.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.


FUNCTION: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.


FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin. SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.


FUNCTION: Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family.


FUNCTION: Catalyzes the regio- and stereoselective reversible NAD- dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL29 family.


FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbE/PsbF family.


FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 3 family.


FUNCTION: Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL15 family.


FUNCTION: Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (By similarity). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF- kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Synapse Postsynaptic density Secreted Note=Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into nucleus (By similarity). Secreted by astrocytes, but not by neurons (By similarity). SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.


FUNCTION: Essential for the organization of sarcomeric actin thin filaments in skeletal muscle (PubMed:25250574). Increases the rate of actin polymerization (PubMed:25250574). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, myofibril, sarcomere, M line Cytoplasm, myofibril, sarcomere, A band Cytoplasm, cytoskeleton Note=Highly expressed in nonstriated areas of developing myotubes, where it shows a granular cytoplasmic pattern. In sarcomeres, highly expressed in the M band region and, at lower levels, along actin thin filaments. Not detected in Z-disks. In sarcomeres, may be located near, but not at, actin thin filament pointed end. SIMILARITY: Belongs to the tropomodulin family.


FUNCTION: Plays an essential role in transcription initiation and cap- stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7- methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the influenza viruses PB2 family.


FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. SIMILARITY: Belongs to the GcvH family.


FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. SIMILARITY: Belongs to the type-I 3-dehydroquinase family.


FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UbiC family.


FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily.


FUNCTION: Involved in spore and ascus formation. Required for the efficient assembly of the precursors of the prospore membrane to a continuous prospore membrane (By similarity). SUBCELLULAR LOCATION: Prospore membrane; Multi-pass membrane protein Note=Localizes to prospore membrane. SIMILARITY: Belongs to the SMA2 family.


FUNCTION: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of endo alpha-(1->5)-L-arabinofuranosyl residues in debranched arabinan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 43 family.


SIMILARITY: Belongs to the protein-tyrosine phosphatase family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL38 family.


FUNCTION: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Maf family.


FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cell projection, dendrite Note=Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.


FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. A probable antitoxin for the putative mRNA interferase YeoB (By similarity). SIMILARITY: Belongs to the phD/YefM antitoxin family.


FUNCTION: Converts (3-methyl-)-quinoline to (3-methyl-)2-oxo-1,2- dihydroquinoline.


FUNCTION: Involved in the viral transport within, and between cells. SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the mastrevirus movement protein family.


FUNCTION: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UvrB family.


FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Ribose importer (TC 3.A.1.2.1) family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 07 (U7-Lctx) subfamily.


FUNCTION: Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNF2/RAD54 helicase family.


FUNCTION: Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side Note=Possibly in the inner surface of the inner mitochondrial membrane. SIMILARITY: Belongs to the alternative oxidase family.


FUNCTION: This protein binds beta-galactoside. Its physiological function is not yet known.


SIMILARITY: Belongs to the UPF0235 family.


FUNCTION: Component of the TLR4 signaling complex. Mediates the innate immune response to bacterial lipopolysaccharide (LPS) leading to cytokine secretion. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UvrC family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus. SIMILARITY: Belongs to the WD repeat ARPC1 family.


FUNCTION: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2- succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.


FUNCTION: Subunit of the V0 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 (By similarity). 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 (By similarity). Essential component of the endosomal pH-sensing machinery (PubMed:16415858). May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (PubMed:18157129). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endosome membrane. Note=In kidney proximal tubules, also detected in subapical vesicles. SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.


FUNCTION: Odorant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Receptor for cAMP. Coordinates the aggregation of individual cells into a multicellular organism and regulates the expression of a large number of developmentally regulated genes. The activity of this receptor is mediated by G proteins. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 5 family.


FUNCTION: Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. SIMILARITY: Belongs to the SpaM family.


FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (hsp70-5) via its interaction with tim14/pam18. May act by positioning tim14/pam18 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TIM16/PAM16 family.


FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.


FUNCTION: This protein is a zinc metalloprotease from snake venom that possesses hemorrhagic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily.


FUNCTION: Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). SIMILARITY: Belongs to the TFIIB family.


FUNCTION: May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Cema family.


FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the kynureninase family.


FUNCTION: Putative adenovirus Bcl-2 homolog that inhibits apoptosis induced by TNF or FAS pathways, as well as p53-mediated apoptosis. Without E1B 19K function, virus production is compromised because of premature death of host cell. Interacts with Bax protein in cell lysates. SUBCELLULAR LOCATION: Host cell membrane. Host nucleus envelope. Host nucleus lamina. Note=Associated with the plasma and nuclear membranes, and with the insoluble nuclear lamina. SIMILARITY: Belongs to the adenoviridae E1B 19 kDa protein family.


SIMILARITY: Belongs to the PHP family.


FUNCTION: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. SUBCELLULAR LOCATION: Cellular chromatophore membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.


FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.


SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion.


FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.


FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.


FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.


FUNCTION: Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity. May play a role in hypoxia-induced oncogenesis. SUBCELLULAR LOCATION: Nucleus Chromosome Note=localized in nuclei but not in nucleoli in interphase. Colocalized with chromosomes in mitosis, with a gradually increased during G1 progression and a maximum level during late G1 phase (G1/S).


FUNCTION: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.


SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaM family.


SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatB family.


FUNCTION: Mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. Binds cholesterol and may promote ER retention of the SCAP-SREBF complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane. SIMILARITY: Belongs to the band 7/mec-2 family.


FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). SIMILARITY: Belongs to the QueC 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. 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. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.


FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to the sesquiterpene germacrene A. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Functions as a transcriptional repressor through its association with the NuRD complex. Recruits the NuRD complex to the promoter of MDM2, leading to the repression of MDM2 transcription and subsequent stability of p53/TP53. SUBCELLULAR LOCATION: Nucleus Note=Predominantly associated with chromatin.


FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the purine permeases (TC 2.A.7.14) family.