FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MGMT family.


FUNCTION: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family.


FUNCTION: Induces relaxation of rat smooth muscle from tail artery and contraction of that from ileum, urinary bladder and uterus. Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Bradykinin-related peptide subfamily.


SIMILARITY: Belongs to the isochorismatase family.


FUNCTION: Functions as transcription regulator in the hedgehog (Hh) pathway. Functions as transcriptional activator. May also function as transcriptional repressor. Binds to the DNA sequence 5'-GAACCACCCA-3' (By similarity). Is involved in the smoothened (SHH) signaling pathway. Required for normal skeleton development (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, cilium. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.


FUNCTION: Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the PsaF family.


FUNCTION: Protease which specifically processes pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis. SUBCELLULAR LOCATION: Secreted.


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


FUNCTION: Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. This protein is one of 10 proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. SIMILARITY: To S.pombe SpCC613.14.


FUNCTION: Acetylates the free alpha-amino group of cysteine S- conjugates to form mercapturic acids. This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S-conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6- acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1. May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type II membrane protein Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the camello family.


FUNCTION: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome (PubMed:32669547). Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity (PubMed:9115366). SUBCELLULAR LOCATION: Nucleus, nucleolus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the ZNF593/BUD20 C2H2-type zinc-finger protein family.


FUNCTION: Serine protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family.


FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily.


FUNCTION: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols. Isoform 3 lacks transferase activity but acts as a negative regulator of isoform 1 (By similarity). SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Catalyzes the synthesis of GDP-perosamine from GDP-4-keto-6- deoxy-D-mannose and L-glutamate. Can use only L-glutamate as amino donor. SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.


FUNCTION: Involved in adhesion, phagocytosis of hydrophilic particles and intracellular killing of bacteria (PubMed:10944536, PubMed:12857872, PubMed:16367873). Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface (PubMed:25999474). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.


FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules at the hyphal tip and the mitotic spindle poles. SIMILARITY: Belongs to the WD repeat LIS1/nudF family.


FUNCTION: Possible component of hydrogenase 4. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family.


FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.


FUNCTION: Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the canopy family.


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 unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Plays a role in the assembly and stabilization of complex IV (PubMed:31155743). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.


FUNCTION: The B locus has at least 25 alleles, and any combination of two different B alleles yields a multimeric regulatory protein, that activates genes responsible for the pathogenicity and for the sexual development of the fungus within the corn plant. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/M-ATYP homeobox family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chemokine-like factor family.


FUNCTION: Involved in the biosynthesis of the streptose moiety of streptomycin. Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis (By similarity). SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase family.


FUNCTION: Acts partially redundantly with other irx members in neural patterning. Required for formation of the posterior forebrain, midbrain, hindbrain, and to a lesser extent, spinal cord. Patterns the neuroectoderm in both the anterior/posterior and dorsal/ventral axes. Does not appear to play a role in pronephros kidney development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/IRO homeobox family.


FUNCTION: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


SIMILARITY: Belongs to the FTR family.


FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetM family.


FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eIF-3 subunit I family.


FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor. SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 4]: Zona pellucida. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.


FUNCTION: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). Cooperatively binds Ori with host PIF and probably other host factors, which activate the nickase function of NS1. Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis. The helicase activity unwinds DNA in a 3'-5' direction on the longer strand. Inhibits the host cell cycle during the G1/S transition, the S-phase, and the G2/M transition. These arrests may provide essential cellular factors for viral DNA replication. Promotes apoptosis in host cell. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family.


FUNCTION: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities (PubMed:36452919). The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins (PubMed:36452919). Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B (PubMed:36452919). Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner (PubMed:36452919). Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C (PubMed:36452919). SIMILARITY: Belongs to the Diels-Alderase family.


SIMILARITY: Belongs to the hssA/B family.


FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the lariat debranching enzyme family.


FUNCTION: Hydrolyzes a variety of proteins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase A1 family.


FUNCTION: Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a ubiquitin receptor that associates with the 26S proteasomal docking subunit RPN10 for the indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP). SUBCELLULAR LOCATION: Nucleus Cytoplasm.


FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IPP isomerase type 2 family.


FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H2B family.


FUNCTION: One of the few identified sugar gustatory receptors identified so far and which promotes the starvation-induced increase of feeding motivation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Gustatory receptor (GR) family. Gr5a subfamily.


FUNCTION: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the mature virion (MV) membrane. The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. SIMILARITY: Belongs to the orthopoxvirus OPG143 family.


FUNCTION: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArgJ family.


FUNCTION: Transport into the cell of 7-keto 8-aminopelargonic acid. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily.


FUNCTION: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Transcription factor that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') and displays two biological functions, as regulator of metabolic and redox processes under normal cellular conditions, and as master transcription factor during integrated stress response (ISR) (PubMed:8506317, PubMed:11106749, PubMed:12667446, PubMed:23624402). Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (PubMed:8506317, PubMed:23624402). Core effector of the ISR, which is required for adaptation to various stress such as endoplasmic reticulum (ER) stress, amino acid starvation, mitochondrial stress or oxidative stress (PubMed:11106749, PubMed:12667446). During ISR, ATF4 translation is induced via an alternative ribosome translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced ATF4 acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (PubMed:11106749, PubMed:12667446). Promotes the transcription of genes linked to amino acid sufficiency and resistance to oxidative stress to protect cells against metabolic consequences of ER oxidation (PubMed:12667446). Activates the transcription of NLRP1, possibly in concert with other factors in response to ER stress (By similarity). Activates the transcription of asparagine synthetase (ASNS) in response to amino acid deprivation or ER stress (PubMed:15775988, PubMed:21159964). However, when associated with DDIT3/CHOP, the transcriptional activation of the ASNS gene is inhibited in response to amino acid deprivation (By similarity). Together with DDIT3/CHOP, mediates programmed cell death by promoting the expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the terminal unfolded protein response (terminal UPR), a cellular response that elicits programmed cell death when ER stress is prolonged and unresolved (PubMed:23624402). Together with DDIT3/CHOP, activates the transcription of the IRS-regulator TRIB3 and promotes ER stress-induced neuronal cell death by regulating the expression of BBC3/PUMA in response to ER stress (PubMed:15775988, PubMed:17369260, PubMed:21159964). May cooperate with the UPR transcriptional regulator QRICH1 to regulate ER protein homeostasis which is critical for cell viability in response to ER stress (By similarity). In the absence of stress, ATF4 translation is at low levels and it is required for normal metabolic processes such as embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (PubMed:10096021, PubMed:10885750, PubMed:11806972, PubMed:12925279, PubMed:15109498, PubMed:22298775). Acts as a regulator of osteoblast differentiation in response to phosphorylation by RPS6KA3/RSK2: phosphorylation in osteoblasts enhances transactivation activity and promotes expression of osteoblast-specific genes and post-transcriptionally regulates the synthesis of Type I collagen, the main constituent of the bone matrix (PubMed:15109498). Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (PubMed:22298775). Activates transcription of SIRT4 (PubMed:23663782). Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4 (PubMed:21768648, PubMed:22572884). Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes (PubMed:21768648, PubMed:22572884). Mainly acts as a transcriptional activator in cellular stress adaptation, but it can also act as a transcriptional repressor: acts as a regulator of synaptic plasticity by repressing transcription, thereby inhibiting induction and maintenance of long-term memory (PubMed:12925279). Regulates synaptic functions via interaction with DISC1 in neurons, which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (PubMed:31444471). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with GABBR1 in hippocampal neuron dendritic membranes. Colocalizes with NEK6 in the centrosome (By similarity). Recruited to nuclear speckles following interaction with EP300/p300 (By similarity). SIMILARITY: Belongs to the bZIP family.


FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit tbp, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of tbp and TBP-associated factors (TAFs). Mediates both basal and activator-dependent transcription. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the TAF8 family.


FUNCTION: Lethal neurotoxin. Selectively blocks tetrodotoxin-sensitive voltage-gated sodium channels (Nav). Does not affect tetrodotoxin- resistant voltage-gated sodium channels or calcium channels (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 51 (Hntx-8) subfamily.


FUNCTION: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. TrmA subfamily.


FUNCTION: Catalyzes the synthesis of GMP from XMP. FUNCTION: Catalyzes the synthesis of GMP from XMP.


FUNCTION: Phospho-beta-D-glucosidase that seems to be involved in the degradation of glucomannan. Is also capable of hydrolyzing aryl- phospho-beta-D-glucosides, although very weakly, and plays only a minor role, if any, in the degradation of these substrates in vivo. SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


FUNCTION: Catalyzes the synthesis of activated sulfate. SIMILARITY: Belongs to the APS kinase family.


FUNCTION: Catalyzes the ATP-dependent condensation of cysteine and glutamate to form the dipeptide gamma-glutamylcysteine (gamma-GC), the first and rate-limiting step in the production of glutathione (GSH). SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family.


FUNCTION: Secretory protein that plays a role in various cellular processes (PubMed:20969804, PubMed:24706764, PubMed:31883645). Acts as a chemorepellent acting on gonadotropin-releasing hormone (GnRH) expressing neurons regulating their migration to the hypothalamus (PubMed:31883645). Also promotes neuron migration, growth and survival as well as neurite outgrowth and is involved in the development of the olfactory system (PubMed:20969804, PubMed:31883645). May also act through the regulation of growth factors activity and downstream signaling (PubMed:31883645). Also regulates extracellular matrix assembly and cell adhesiveness (By similarity). Promotes endothelial cell survival, vessel formation and plays an important role in the process of revascularization through NOS3-dependent mechanisms (PubMed:24706764). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Catalyzes the selective oxidation of C1 hydroxyl moieties on mono-, oligo- and polysaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Carbohydrate oxidase is able to oxidize a variety of substrates including D-glucose, D-galactose, D-xylose, D-maltose, D- cellobiose, and lactose. In addition, among various oligosaccharides, the enzyme preferred tetrameric dextrins, indicating a favorable interaction of four linked glucose units with the substrate binding pocket. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. FUNCTION: Protein 3 may attach the radial spoke to the outer doublet microtubule or is required to form a stable spoke structure. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme Note=Radial spoke. SIMILARITY: Belongs to the flagellar radial spoke RSP3 family.


FUNCTION: Transcriptional cofactor that restricts GATA6 function by inhibiting DNA-binding, resulting in repression of GATA6 transcriptional activation of downstream target genes. Represses GATA6- mediated trans activation of lung- and cardiac tissue-specific promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC promoter (By similarity). Plays a critical role in the development of cardiac hypertrophy via activation of calcineurin/nuclear factor of activated T-cells signaling pathway. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=May shuttle between the cytoplasm and the nucleus.


FUNCTION: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. SIMILARITY: Belongs to the methylglyoxal synthase family.


FUNCTION: Nonprocessive beta-mannosyltransferase that catalyzes the transfer of a mannose residue from GDP-mannose to glucuronic acid-beta- 1,2-mannose-alpha-1,3-glucose-beta-1,4-glucose-PP-polyisoprenyl to form the lipid-linked pentasaccharide repeating unit of xanthan, Man-GlcA- Man-Glc(2)-PP-Pol. Is involved in the biosynthesis of the exopolysaccharide xanthan (By similarity). SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the glycosyltransferase 94 family.


FUNCTION: In tachyzoites, plays an essential role in microneme secretion that ensures parasite motility and attachment to, invasion of and egress from host cells (PubMed:31182647, PubMed:31206964). Also involved in the architecture of the peripheral annuli where it appears to regulate the localization of PAP2 (PubMed:31206964). In association with the myosin motor MyoJ, involved in the constriction of the basal complex at the end of daughter cell division in an actin-dependent manner; the basal complex is a cytoskeletal structure formed at the tachyzoite basal pole during daughter cell formation (PubMed:28593938). May be involved in parasite replication (PubMed:31182647). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=In tachyzoites, localizes to preconoidal rings, peripheral annuli, centrioles and basal complex (PubMed:18208326, PubMed:31206964, PubMed:31182647, PubMed:28593938). Recruitment to the daughter basal complex occurs at a late stage of daughter cell assembly (PubMed:18208326, PubMed:31182647). SIMILARITY: Belongs to the centrin family.


FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. FUNCTION: The transmembrane protein gp41 (TM) acts as a 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 fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) 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 target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. Since CD4 also displays a binding site for the disulfide-isomerase P4HB/PDI, a P4HB/PDI-CD4-CXCR4-gp120 complex may form. In that complex, P4HB/PDI could reach and reduce gp120 disulfide bonds, causing major conformational changes in gp120. TXN, another PDI family member could also be involved in disulfide rearrangements in Env during fusion. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl- ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). FUNCTION: The gp120-gp41 heterodimer seems to contribute to T-cell depletion during HIV-1 infection. The envelope glycoproteins expressed on the surface of infected cells induce apoptosis through an interaction with uninfected cells expressing the receptor (CD4) and the coreceptors CXCR4 or CCR5. This type of bystander killing may be obtained by at least three distinct mechanisms. First, the interaction between the 2 cells can induce cellular fusion followed by nuclear fusion within the syncytium. Syncytia are condemned to die from apoptosis. Second, the 2 interacting cells may not fuse entirely and simply exchange plasma membrane lipids, after a sort of hemifusion process, followed by rapid death. Third, it is possible that virus- infected cells, on the point of undergoing apoptosis, fuse with CD4- expressing cells, in which case apoptosis is rapidly transmitted from one cell to the other and thus occurs in a sort of contagious fashion (By similarity). FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of HIV-specific CD4+ cells (By similarity). SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Host endosome membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.


FUNCTION: Probable transporter of a GTP-driven Fe(2+) uptake system. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.


FUNCTION: Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta- hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family.


FUNCTION: Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. SIMILARITY: Belongs to the plant globin family.


SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family.


FUNCTION: Low-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Trehalose transporter subfamily.


FUNCTION: Transcription factor which regulates the transcription of various genes, including those involved in innate immunity and oxidative stress responses (PubMed:20369020, PubMed:28632756, PubMed:30789901). Binds to promoter regions of genes, probably at 5'- [GACGTCA]-3' consensus sequences (PubMed:30789901). Together with transcription factor daf-19, involved in regulation of the serotonergic response of ADF neurons to pathogenic food (PubMed:23505381). Modulates response to infection by the Gram-negative bacterium P.aeruginosa, acting downstream of the p38 signal transduction pathway effector serine/threonine kinase pmk-1 (PubMed:20369020, PubMed:30789901). May act with transcription factor elt-2 to control p38 gene induction in response to bacterial infection (PubMed:26016853). May be phosphorylated by pmk-1 (PubMed:20369020). Regulates transcription of the metallothionein gene, mtl-1, perhaps acting downstream of pmk-1 (PubMed:28632756). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity). SIMILARITY: Belongs to the LRRFIP family.


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: Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus Host mitochondrion Note=Mainly cytoplasmic as only a fraction is detected in the nucleus. In cytoplasm, a minor fraction associates with mitochondria or proteasomes. SIMILARITY: Belongs to the orthohepadnavirus protein X family.


FUNCTION: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, cilium axoneme Note=Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme. SIMILARITY: Belongs to the CFAP20 family.


FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Can also transport lithium. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.


FUNCTION: Involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs) (PubMed:28634299). Catalyzes the conversion of (3R)-3-[(carboxymethyl)amino]fatty acids such as (3R)-3- [(carboxymethyl)amino]butanoate (CABA) to (3R)-3-isocyanylbutanoate (INBA) through an oxidative decarboxylation mechanism, thereby generating the isonitrile group of INLPs (PubMed:29906336, PubMed:32074393, PubMed:33361191). SIMILARITY: Belongs to the TfdA dioxygenase family.


FUNCTION: Functions as an intracellular molybdate sensor. The ModE-Mo complex acts as a repressor of the modABC operon, which is involved in the transport of molybdate (PubMed:8550508). Binds modA promoter DNA in the absence of molybdate, however molybdate binding confers increased DNA affinity (PubMed:9210473, PubMed:9044285). Binds the promoter of moaA activating its transcription; binding is not enhanced by molybdate (PubMed:9044285). The protein dimer binds the consensus palindrome sequence 5'-TATAT-N7-TAYAT-3' and a variant 5'-TGTGT-N7-TGYGT-3' (PubMed:9210473, PubMed:9044285, PubMed:16205910). Acts as a regulator of the expression of 67 genes, many of which encode molybdoenzymes, acts both directly and indirectly (PubMed:9466267, PubMed:10206709, PubMed:16205910). ModE also binds tungstate (PubMed:9210473, PubMed:11259434). FUNCTION: The ModE-Mo complex acts as a repressor of the modABC operon, involved in the transport of molybdate. Upon binding molybdate, the conformation of the protein changes, promoting dimerization of ModE-Mo. The protein dimer is then competent to bind a DNA region, upstream of the modABC operon. Acts also as an enhancer of the expression of genes coding for molybdoenzymes, both directly and indirectly (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ModE family.


FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (By similarity). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photoreceptors (PubMed:21219924, PubMed:25416279). Involved in ensuring correct abundance and localization of retinal membrane proteins (PubMed:25416279). May increase spectral sensitivity in dim light (PubMed:11055434). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Cytoplasm, perinuclear region. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.


FUNCTION: Exporter of leucine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Rht family.


FUNCTION: Catalytic subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of Rab3-GAP and Rab3GAP1, which has both GTPase- activating protein (GAP) activity towards Rab3, and guanine nucleotide exchange factor (GEF) activity towards Rab18 (Probable). As part of the Rab3GAP complex, required for the rapid induction and sustained expression of synaptic homeostasis at the neuromuscular junction (NMJ) (Probable). Also participates in the regulation of autophagy in tissues such as larval fat cells and adult muscles (Probable). The Rab3GAP complex, acts as a GAP for Rab3 by converting active Rab3-GTP to the inactive form Rab3-GDP (By similarity). At the neuromuscular junction (NMJ), forms a presynaptic signaling mechanism with Rab3 that regulates progression of synaptic homeostasis at a late stage of vesicle release (Probable). Within this mechanism Rab3-GTP acts, directly or indirectly, to inhibit the progression of synaptic homeostasis, and Rab3-GAP functions to inactivate this action of Rab3-GTP (Probable). The Rab3GAP complex, acts as a GEF for Rab18 by promoting the conversion of inactive Rab18-GDP to the active form Rab18-GTP (By similarity). Regulates autophagy as part of a Rab3GAP-Rab18 module (PubMed:32248620). Once Rab18 is activated by the GEF Rab3GAP complex, the Rab3GAP-Rab18 module localizes to autophagosomes, and regulates autolysosome formation and maturation together with the Rab18 interacting effector, the PI3K/Vps34 Complex I (PubMed:32248620). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily.


FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Note=Distribution is 50- 50. SIMILARITY: Belongs to the SecA family.


FUNCTION: Involved in the anomeric conversion of L-fucose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase subfamily.


FUNCTION: May function by interacting with a small, flexible domain located at the C-terminus of the CP, forming a bridge between the virus particle and the internal surface of the vector nematode feeding apparatus. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the tobravirus protein 2b family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B subfamily.


SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.


FUNCTION: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation (By similarity). SUBCELLULAR LOCATION: Periplasm Note=Is capable of associating with the outer membrane.


SIMILARITY: Belongs to the UPF0637 family.


FUNCTION: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Recruited to resolve stalled replication forks during replication stress. Also involved in interstrand cross-link repair. SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome Note=Accumulated at sites of DNA damage. Recruited to stalled replication forks during replication stress. SIMILARITY: Belongs to the RecA family. RAD51 subfamily.


FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.


FUNCTION: Alpha-galactosidase. Removes both branched alpha-1,3-linked galactose residues of blood group B antigens and linear alpha-1,3- linked galactose structures. SIMILARITY: Belongs to the glycosyl hydrolase 110 family. B subfamily.


FUNCTION: Required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific vps34 PI3-kinase complex I. This complex is essential to recruit the atg8-phosphatidylinositol conjugate and the atg12-atg5 conjugate to the preautophagosomal structure. Atg14 mediates the specific binding of the vps34 PI3-kinase complex I to the preautophagosomal structure (PAS) (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG14 family.


FUNCTION: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis (By similarity). Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cleavage furrow Nucleus, nucleolus Nucleus, nucleoplasm Chromosome, centromere, kinetochore Nucleus speckle Midbody Mitochondrion. SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 25 family.


FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)- farnesyl diphosphate (FPP) to alloaromadendrene and bicyclo-germacrene. The product formation is dependent on the metal ions present and in presence of manganese, bicyclo-germacrene is greatly favored while both alloaromadendrene and bicyclo-germacrene are produced in equivalent amounts in the presence of magnesium. Can also convert geranyl diphosphate (GPP) to terpinolene, limonene and geraniol, and this conversion is not affected by the presence of magnesium or manganese. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Specifically methylates the N7 position of a guanine in 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Required for growth at higher temperatures. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.


FUNCTION: Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.


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, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbE/PsbF family.


FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. SIMILARITY: In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: High-affinity potassium transporter. Can also transport rubidium and cesium (Ref.1). Is essential with AKT1 for high-affinity potassium uptake in roots during seedling establishment and postgermination growth under low potassium conditions (PubMed:20413648). Mediates potassium uptake by plant roots in response to low potassium conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by the calcium sensors calcineurin B-like genes CBL1, CBL8, CBL9 and CBL10, and by phosphorylation by CIPK23 (PubMed:26474642). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72.3) family.


FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine (PubMed:34748729). Activity towards 2-iodophenol is weak (PubMed:34748729). SIMILARITY: Belongs to the nitroreductase family.


FUNCTION: Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the COX16 family.


FUNCTION: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide (PubMed:9491897, PubMed:26950369). Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding (PubMed:9491897, PubMed:26950369). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the protein sulfotransferase family.


FUNCTION: Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.


FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. SUBCELLULAR LOCATION: Vacuole membrane; Single-pass type II membrane protein Note=Lysosome-like vacuoles. SIMILARITY: Belongs to the peptidase S9B family.


FUNCTION: Virulence factor that affects the acute immune response to infection. Bcl-2-like protein which, through its interaction with the DEAD box RNA helicase DDX3X/DDX3, prevents TBK1/IKKepsilon-mediated IRF3 activation. Contributes to virulence by binding to the host TRAF6 and IRAK2 and preventing host NF-kappa-B activation. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the orthopoxvirus OPG044 family.


FUNCTION: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:29198525). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (PubMed:29198525). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (PubMed:29198525). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins (By similarity). Required for survival of B-cell progenitors and normal antibody production (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.


FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL29 family.


FUNCTION: Like parvalbumins, SCPs seem to be more abundant in fast contracting muscles, but no functional relationship can be established from this distribution.


FUNCTION: Thioesterase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA (PubMed:32077283). The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA (PubMed:32077283). A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively (PubMed:32077283). The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo- methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AMT4 thioesterase family.


FUNCTION: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export- competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. May also be involved in cytoplasmic mRNA decay by interaction with components of P-bodies (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Cytoplasm, P-body. SIMILARITY: Belongs to the ENY2 family.


FUNCTION: Required for disulfide bond formation in some proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. BdbC subfamily.


FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.


FUNCTION: Contributes to the formation of crescents and immature virions (IV). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Note=Probably transitorily part of the membrane of crescents during immature virions formation. Not incorporated into virions. Probably synthesized, but not retained in viral factories (By similarity). SIMILARITY: Belongs to the chordopoxvirinae H7 family.


FUNCTION: Involved in gene expression controlled by TOR kinase and nutrient signaling. May also be involved in positioning the proximal bud pole signal. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the prefoldin subunit alpha family.


FUNCTION: May be involved in virus-host protein interaction through the ankyrin repeats and PRANC regions. SIMILARITY: Belongs to the orthopoxvirus OPG003 family.


FUNCTION: Redox-active protein probably involved in electron transport during fermentation of acetate to methane. SIMILARITY: Belongs to the SsuE family. Isf subfamily.


FUNCTION: Acts as a radical domain for damaged PFL and possibly other radical proteins.


FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). Specifically binds guanine nucleotides. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA described here carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the trifunctional enzyme subunit beta/HADHB bears the 3-ketoacyl-CoA thiolase activity. Independently of the subunit beta, the trifunctional enzyme subunit alpha/HADHA also has a monolysocardiolipin acyltransferase activity. It acylates monolysocardiolipin into cardiolipin, a major mitochondrial membrane phospholipid which plays a key role in apoptosis and supports mitochondrial respiratory chain complexes in the generation of ATP. Allows the acylation of monolysocardiolipin with different acyl-CoA substrates including oleoyl-CoA for which it displays the highest activity. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane Note=Protein stability and association with mitochondrion inner membrane do not require HADHB. SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.


FUNCTION: Involved in the efflux of purine ribonucleosides, such as inosine and guanosine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. NepI (TC 2.A.1.2.26) subfamily.


FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein C1 family.


SIMILARITY: To E.coli YahG.


FUNCTION: Serine protease inhibitor that also shows protective effect in a cytotoxicity model (PubMed:32144281). It binds to all proteases tested (trypsin (Ki=52 nM), alpha-chymotrypsin, cathepsin G, kallikrein, and human neutrophil elastase) (PubMed:32144281). It significantly increases neuroblastoma cell viability in an in vitro neurotoxicity model, being a consequence of an effective decrease of reactive oxygen species (ROS) level in the cells (PubMed:32144281, PubMed:35563513). It also seems to protect cells by inhibiting ATP- induced purinoceptor (P2RX7) activation (PubMed:35563513). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily.


FUNCTION: Plays a key role in hydrogen peroxide removal. SUBCELLULAR LOCATION: Mitochondrion Plastid, chloroplast stroma. SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase subfamily.


FUNCTION: [Isoform c]: Plays a role in associative long-term memory (LTM) and learning. FUNCTION: Transcription factor (PubMed:12231504, PubMed:21331044). Transcriptional activity probably positively regulated by phosphorylation (PubMed:12231504, PubMed:27720609). Modulates expression of target genes, acting by binding to regulatory cAMP response elements (CRE) (PubMed:27720609, PubMed:12231504, PubMed:34260587). Acts downstream of the calcium-triggered CaMKK-CaMK1 signaling cascade, consisting of the protein kinase kinase ckk-1 and the protein kinase cmk-1 (PubMed:12231504, PubMed:27720609). Plays a role in learning and memory, feeding behavior, stress response, entry into the dauer stage and modulation of lifespan (PubMed:31413073, PubMed:21331044, PubMed:19035344, PubMed:27720609, PubMed:23013276, PubMed:34260587). Involved in commitment to the developmentally arrested larval state known as dauer, acting by positively regulating the expression of dauer-inhibiting TGF-beta-like daf-7 in the ASI neurons (PubMed:34260587). Plays a role in both associative and non- associative long-term memory (LTM) (PubMed:23013276, PubMed:31413073). Involved in modulating feeding behavior, acting by regulating transcription of tryptophan hydroxylase tph-1 in serotonergic ADF neurons (PubMed:19035344). Regulates transcription of genes involved in endoplasmic reticulum (ER) stress (PubMed:21331044). Involved in modulation of lifespan, in response to raised temperature, but independently of the heat-shock response pathway, acting by regulating transcription of FMRFamide-like neuropeptides flp-6 in the AFD neuron (PubMed:27720609, PubMed:21331044). FUNCTION: [Isoform e]: Plays a role in associative long-term memory (LTM) and learning; perhaps required at the time of acquisition and/or the consolidation phase of memory formation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family.


FUNCTION: May have antimicrobial activity against the Gram-negative bacterium E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ranatuerin subfamily.


FUNCTION: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule attachments that are not under tension. Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore Note=Associates with the mitotic spindle and on elongated and disassembling spindles. Also associated with the kinetochore (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.


FUNCTION: Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. SIMILARITY: Belongs to the ataxin-10 family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0496 family.


FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.


FUNCTION: Catalyzes the reversible NAD(+)-dependent oxidative deamination of L-phenylalanine to phenylpyruvate. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. SIMILARITY: Belongs to the thiamine-monophosphate kinase family.


FUNCTION: [Nociceptin]: Ligand of the opioid receptor-like receptor OPRL1. It may act as a transmitter in the brain by modulating nociceptive and locomotor behavior. May be involved in neuronal differentiation and development. When administered intracerebroventricularly, nociceptin induces hyperalgesia and decreases locomotor activity. FUNCTION: [Orphanin FQ2]: Has potent analgesic activity. FUNCTION: [Nocistatin]: Blocks nociceptin action in pain transmission by inhibiting nociceptin-induced hyperalgesia and allodynia. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the opioid neuropeptide precursor family.


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 NdhO subunit family.


FUNCTION: May play a role in cellular stress response. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: May have antimicrobial properties, like most ant linear peptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ponericin-G family.


FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:19944711). Shows activity on L-Leu (PubMed:19944711). Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions (By similarity). In addition, this protein inhibits dose-dependently the growth of Gram-positive, Gram- negative bacteria and yeast, probably by the generation of hydrogen peroxide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily.


FUNCTION: Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily.


FUNCTION: Probable member of the two-component regulatory system YxjM/YxjL. May activate YxjL by phosphorylation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Odorant signal transduction is probably mediated by a G- protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGA2 subfamily.


FUNCTION: May be involved in nucleotide excision repair (By similarity). Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a ubiquitin receptor that associates with the 26S proteasomal docking subunit RPN10 for the indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP) (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RAD23 family.


FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RraB family.


FUNCTION: [Movement protein P3N-PIPO]: Allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (By similarity). FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity). SUBCELLULAR LOCATION: Host cell junction, host plasmodesma. SIMILARITY: Belongs to the potyviridae P3N-PIPO polyprotein family.


FUNCTION: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the PsaE family.


SIMILARITY: Belongs to the UPF0319 family.


FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities (PubMed:35398258). The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble get3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WRB/GET1 family.


FUNCTION: Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:9427408, PubMed:15292137). Pilot protein that is required for the proper localization of the secretin YscC/SctC in the outer membrane (PubMed:9427408, PubMed:15292137). Also required for efficient oligomerization of YscC/SctC and stabilization of the oligomers (PubMed:15292137). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Note=Association with the outer membrane is a prerequisite for function in the biogenesis of YscC/SctC. SIMILARITY: Belongs to the ExsB/YscW family.


FUNCTION: Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re- initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SeqA family.


FUNCTION: E2 conjugating enzyme responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATG3 family.


FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family.


FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.


FUNCTION: Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids (PubMed:19218247). Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH (PubMed:14672942). Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens (PubMed:10998348). Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3- alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha- androstane-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:15929998, PubMed:17034817, PubMed:17442338, PubMed:8573067). Also specifically able to produce 17beta-hydroxy-5alpha-androstan-3-one/5alphaDHT (PubMed:10998348). May also reduce conjugated steroids such as 5alpha- dihydrotestosterone sulfate (PubMed:19218247). Displays affinity for bile acids (PubMed:8486699). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the aldo/keto reductase family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Dehydrogenase that converts trans-4-L-hydroxyproline to delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using ubiquinone-10 as the terminal electron acceptor. Can also use proline as a substrate but with a very much lower efficiency. Does not react with other diastereomers of Hyp: trans-4-D-hydroxyproline and cis-4-L- hydroxyproline. Ubiquininone analogs such as menadione, duroquinone and ubiquinone-1 react more efficiently than oxygen as the terminal electron acceptor during catalysis. SIMILARITY: Belongs to the proline oxidase family.


FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1- hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. SIMILARITY: Belongs to the rhamnulokinase family.


FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. SIMILARITY: Belongs to the nitrate reductase family.


FUNCTION: May be involved in a redox system involving ascorbic acid. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the multicopper oxidase family.


FUNCTION: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (By similarity). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (By similarity). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (By similarity). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (By similarity). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (By similarity). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (By similarity). SUBCELLULAR LOCATION: Nucleus speckle Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.


FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the cla gene cluster that produces clavatol and ortho-quinone methide (PubMed:30811183). The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones (PubMed:30811183). The non-reducing PKS claF is responsible for the formation of clavatol from successive condensations of 3 malonyl-CoA units, presumably with a simple acetyl- CoA starter unit, and 2 methylation steps (PubMed:30811183). The esterase claE probably collaborates with claF by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (By similarity). The clavatol oxidase claD then converts clavatol to hydroxyclavatol (PubMed:30811183). Spontaneous dehydration of hydroxyclavatol leads to the accumulation of the highly active ortho-quinone methide (PubMed:30811183, PubMed:31860310). On the other hand, the PKS-NRPS hybrid traA is involved in the formation of crustosic acid, with the help of traB and traD (PubMed:30811183). The polyketide synthase module (PKS) of traA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl- CoA starter unit with 3 malonyl-CoA units (PubMed:30811183). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with L-malic acid (PubMed:30811183). Because traA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase traG (By similarity). Crustosic acid undergoes decarboxylation and isomerization to the terrestric acid, catalyzed by the 2-oxoglutarate-dependent dioxygenase traH (PubMed:30811183). Both acids are further converted to the 2 gamma-butyrolactones (R)-5-methyltetronic acid and (S)-5- carboxylmethyltetronic acid, with involvement of the cytochrome P450 monooxygenase claJ (PubMed:30811183). Spontaneous addition of the methide to these gamma-butyrolactones leads to peniphenone D and penilactone D, which undergo again stereospecific attacking by methide to give penilactones A and B (PubMed:30811183, PubMed:31860310). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.


FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: In the C-terminal section; belongs to the pectinesterase family. SIMILARITY: In the N-terminal section; belongs to the PMEI family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. P subfamily.


FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity). SIMILARITY: Belongs to the dihydrofolate reductase family.


FUNCTION: Responsible for plasticity of the cell wall. SUBCELLULAR LOCATION: Secreted, cell wall.


FUNCTION: Catalyzes the conversion of dihydroorotate to orotate (PubMed:2996629). Participates in the pyrimidine biosynthetic pathway (PubMed:2996629). SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.


SIMILARITY: Belongs to the universal ribosomal protein uS11 family.


SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion system (TTSS). SIMILARITY: Belongs to the NopP family.


FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ADP-dependent glucokinase family.


FUNCTION: [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:15472229, PubMed:18674515, PubMed:18719240, PubMed:23756265, PubMed:23288867, PubMed:24641623). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:23756265). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol and estrone (PubMed:15472229, PubMed:18719240, PubMed:23288867). Contributes to bile acid (BA) detoxification by catalyzing the glucuronidation of BA substrates, which are natural detergents for dietary lipids absorption (PubMed:23756265). Involved in the glucuronidation of calcidiol, which is the major circulating form of vitamin D3, essential for the regulation of calcium and phosphate homeostasis (PubMed:24641623). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonists losartan, candesartan and zolarsartan, which can inhibit the effect of angiotensin II (PubMed:18674515). FUNCTION: [Isoform 2]: Lacks UDP-glucuronosyltransferase (UGT) activity but acts as a negative regulator of isoform 1. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. May play an essential role in the transition from the vegetative to the reproductive phase of development. May be a positive regulator of ABA signaling. SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GyaR subfamily.


FUNCTION: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. SIMILARITY: Belongs to the HAUS3 family.


FUNCTION: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. FUNCTION: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Loosely bound to the thylakoid inner membrane surface. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Loosely bound to the thylakoid inner membrane surface. SIMILARITY: Belongs to the plastocyanin family.


SIMILARITY: Belongs to the UPF0210 family.


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. TatA could form the protein-conducting channel of the Tat system. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatA/E family.


SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the flagella basal body rod proteins family.


FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L- glutamate and formamide. SIMILARITY: Belongs to the arginase family.


FUNCTION: Interferon-stimulated protein that positively regulates RNA virus-triggered innate immune signaling. Mechanistically, promotes 'Lys-27'-linked polyubiquitination of MAVS through TRIM21 leading to enhanced the IFN signaling pathway.


FUNCTION: Supports cell migration. May be involved in urothelial cell- matrix interactions. May be involved in tumor progression. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.


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. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS. SUBCELLULAR LOCATION: Virion Host nucleus Host mitochondrion. SIMILARITY: Belongs to the influenza viruses PB2 family.


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, PSMB7 displays a trypsin-like activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. SIMILARITY: Belongs to the peptidase T1B family.


FUNCTION: Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta- anomer, accelerating the equilibrium between the alpha- and beta- anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the NanM family.


FUNCTION: Membrane-bound UDP-glucosyltransferase (UGT) which catalyzes the C-glucosylation of kermesate and flavokermesate to produce carminate and flavokermesate 7-C-beta-D-glucoside (dcll) respectively (PubMed:29215010). Carminate is used as a deterrent against insect predators (PubMed:29215010). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=Localization to the endoplasmic reticulum membrane is critical for its activity. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the xylose isomerase family.


FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family.


FUNCTION: May regulate the expression of phage structural components with protein P13.


FUNCTION: Could be involved in defense against microbial infections. Protects the epithelia from external environment. SUBCELLULAR LOCATION: Secreted.


FUNCTION: May be involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RecA family. RAD51 subfamily.


FUNCTION: Peptide with nanomolar affinity for human melanocortin receptors. The natural disulfide pairing being unknown, the activity of all three possible peptides (with the cysteine pairings 'bead (I-II, III-IV), 'globular' (I-III, II-IV), and 'ribbon' (I-IV, II-III)) have been tested. All three isomers show similar affinities on each human melanocortin subtype (MC1R (~500 nM), MC3R (~100 nM), MC4R (~50 nM), and MC5R (~50 nM)). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Guanylyltransferase that catalyzes the activation of phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via the condensation of PEP with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor. SIMILARITY: Belongs to the CofC family.


FUNCTION: Cardioactive peptide. Corazonin is probably involved in the physiological regulation of the heart beat (By similarity). SUBCELLULAR LOCATION: [Corazonin]: Secreted. SUBCELLULAR LOCATION: [Corazonin precursor-related peptide]: Secreted. SIMILARITY: Belongs to the corazonin family.


FUNCTION: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbZ family.


FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume, membrane potential stabilization, signal transduction and transepithelial transport. Involved in the regulation of aldosterone production. The opening of CLCN2 channels at hyperpolarized membrane potentials in the glomerulosa causes cell membrane depolarization, activation of voltage- gated Ca2+ channels and increased expression of aldosterone synthase, the rate-limiting enzyme for aldosterone biosynthesis (PubMed:29403011, PubMed:29403012). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC- 2/CLCN2 subfamily.


FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain development and for the development of pharyngeal arches. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALTA1 family.


SIMILARITY: Belongs to the UPF0178 family.


FUNCTION: Transcription activator. Together with BRN1 and SMB, regulates cellular maturation of root cap. Promotes the expression of genes involved in secondary cell walls (SCW) biosynthesis. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Probable lipid hydrolase. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.


FUNCTION: Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase. Required for error-free repair of spontaneous and induced DNA lesions to protect the genome from mutation. FUNCTION: Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase. Required for error-free repair of spontaneous and induced DNA lesions to protect the genome from mutation (By similarity). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SHU2 family.