FUNCTION: Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects (PubMed:22923679). Catalyzes S-adenosylmethionine-dependent regioselective 4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and, with a lower efficiency, cirsimaritin (CIRM), sakuranetin (NAR7Me), ladanein (LAD) and genkwanin (GENK) (PubMed:22923679). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.


FUNCTION: Histone acetyltransferase which may be involved in transcriptional activation (PubMed:12397079, PubMed:22020126). May influence the function of ATM (PubMed:15923642). As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac (PubMed:16227571, PubMed:16543150, PubMed:21217699, PubMed:22547026, PubMed:22020126). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852, PubMed:22547026). That activity is less specific than the one of the MSL complex (PubMed:20018852, PubMed:22547026). Can also acetylate TP53/p53 at 'Lys-120'. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the MYST (SAS/MOZ) family.


FUNCTION: Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA- binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post- transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript. SIMILARITY: Belongs to the aconitase/IPM isomerase family.


FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and for the docking of ODA in ciliary axoneme. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme.


FUNCTION: Central component of the spindle assembly checkpoint. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MAD1 family.


FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:28596365). Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity (By similarity). Plays a redundant role with PCGF5 as part of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females (PubMed:28596365). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm Note=Recruited by the non- coding RNA Xist to specific nuclear foci that probably correspond to the inactivated X chromosome.


FUNCTION: Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: This toxin binds to the surface of glioma cells, and inhibits their proliferation without having effects on normal brain cells. In this context, this toxin has been described as a chloride channel inhibitor (probably ClC-3/CLCN3) by causing its internalization via caveolae (PubMed:16520829). It has also been described to selectively interact with MMP2 (in complex with MT1-MMP (MMP14) and TIMP2), to inhibit its enzymatic activity and to decrease its presence at the cell surface (PubMed:12454020). Additionnally, annexin A2 that is expressed on the surface of multiple human tumor cell lines and vascular endothelial cells in culture may be another molecular target, since surface binding of this peptide to the pancreatic tumor cell line Panc- 1 is dependent on the expression of annexin A2 using siRNA-mediated specific knockdown of annexin A2 levels (PubMed:20018898). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family.


FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Dosage dependent suppressor of PKC1 deletion and MPK1 deletion. Involved in cell lysis.


FUNCTION: Exhibits antimicrobial activity against the Gram-positive bacteria B.subtilis IFO 3134, K.varians MAFF 118076 and S.aureus ATCC 6538P, the Gram-negative bacteria A.tumefaciens MAFF 1001, B.bacteriovorus MAFF 106101 and K.pneumoniae MAFF 519002, and the yeasts C.krusei MAFF 114085, K.thermotolerans MAFF 113848 and T.delbrueckii MAFF 113811. SUBCELLULAR LOCATION: Secreted.


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


FUNCTION: Alpha subunit of nicotinic acetylcholine receptor (nAChR) (PubMed:15280391, PubMed:15990870, PubMed:20027209). Probably acts in cholinergic motoneurons to regulate presynaptic neurotransmitter release, thereby ensuring normal level of excitation of cholinergic motoneurons during locomotion (PubMed:20027209). Involved in nAChR sensitivity to nicotine and levamisole (PubMed:15280391, PubMed:15990870). SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily.


FUNCTION: Able to transport with low efficiency all natural purines as well as purine analogs. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.


FUNCTION: Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Upon expression in E.coli functions weakly as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Has no wax synthase activity. SIMILARITY: Belongs to the long-chain O-acyltransferase family.


FUNCTION: Transport of lipophilic molecules, possible pheromone- carrier. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Involved in recruitment of Pol III to the preinitiation complex. Involved in the configuration of an initiation-competent form of RNA polymerase. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family.


FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Plays an important role in causing fusarium head blight (FHB) on cereal crops. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.


FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin specifically inhibits mammalian Nav1.8/SCN10A sodium currents (IC(50)=2.11 uM) without inducing a shift in the current-voltage relationship of this channel (PubMed:32758497). In vivo, shows potent analgesic activity in a mice hotplate analgesic assay (PubMed:28219625). In addition, this toxin has better analgesic effects than Ziconotide, an analgesic drug (PubMed:28219625). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily.


FUNCTION: Catalyzes the condensation of 4-hydroxybenzoate (HB) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylphenol 5'-phosphate (beta-RFH-P) (PubMed:21634403). Also catalyzes the condensation of 4-aminobenzoate (pABA) with PRPP to produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P) (PubMed:15262968, PubMed:21634403). Only 4-hydroxybenzoate is known to be biosynthesized by methanogenic archaea, but 4-aminobenzoate can be used as substrate by growing methanogens when it is present in the growth medium (PubMed:21634403). SIMILARITY: Belongs to the beta-RFA-P synthase family.


FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3- methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism (By similarity). Vital for adult survival. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the AccD/PCCB family.


FUNCTION: Glucosyltransferase acting preferentially on aromatic substrates of the phenylpropanoid types. The best substrates are scopoletin and esculetin. Required for full resistance to virus. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Has hemolytic activity against human erythrocytes (HC50=14.3 uM). Has antibacterial activity against the Gram-positive bacterium S.aureus ATCC 25923 (MIC=64 uM) and the Gram-negative bacterium E.coli ATCC 25922 (MIC=64 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Ocellatin subfamily.


SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family.


FUNCTION: Telomeric DNA-binding protein, which binds to single-stranded C-rich repeat sequences, with high specificity to the 5'-GCCTAA-3' sequence (PubMed:18329362, PubMed:23390606). Repeat sequence binding can be at the 5' or 3' telomeric end (PubMed:18329362). May have a role in protecting the 5' end of the C-rich strand of the telomere (PubMed:23390606). Acts redundantly with pot-2 to negatively regulate telomerase-mediated telomere extension (PubMed:18329362, PubMed:23390606, PubMed:24297748). Also regulates telomere length by the telomerase-independent telomere maintenance pathway called ALT (alternative lengthening of telomeres) (PubMed:23390606, PubMed:22547822, PubMed:24297748). Through sun-1, anchors telomeres to the nuclear envelope in embryos (PubMed:24297748). SUBCELLULAR LOCATION: Nucleus Nucleus envelope Chromosome, telomere Note=More highly expressed in meiotic pachytene nuclei than in diakinesis-stage oocyte nuclei (PubMed:23390606). Also expressed in mitotic nuclei (PubMed:23390606). SIMILARITY: Belongs to the telombin family.


FUNCTION: Secreted cytokine-like protein (PubMed:12847263). Binds to the scavenger receptor MARCO (PubMed:12847263). Can also bind to pathogens including the Gram-positive bacterium L.monocytogenes, the Gram-negative bacterium P.aeruginosa, and yeast (PubMed:12847263). Strongly inhibits phospholipase A2 (PLA2G1B) activity (PubMed:24213919). Seems to have anti-inflammatory effects in respiratory epithelium (By similarity). Also has anti-fibrotic activity in lung (PubMed:24213919). May play a role in fetal lung development and maturation (PubMed:24213919). Promotes branching morphogenesis during early stages of lung development (PubMed:24213919). In the pituitary, may inhibit production of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secretoglobin family. UGRP subfamily.


FUNCTION: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks, nicked Holliday junctions and also intact Holliday junctions with a reduced efficiency. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. Plays a role in DNA repair and in genotoxic stress-induced homologous recombination (HR) in somatic cells. Mediates a subset of meiotic recombination events that are insensitive to crossover interference. Together with SEND1, essential for the resolution of toxic replication structures to ensure genome stability, and to maintain telomere integrity and replication (PubMed:26704385). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus. SIMILARITY: Belongs to the XPF family.


FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of aurovertins, fungal polyketides that exhibit potent inhibition of adenosine triphosphate synthase (PubMed:26340065). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-3 subfamily.


FUNCTION: tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the exportin family.


FUNCTION: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.


FUNCTION: Probably part of an ABC transporter complex. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein SsuA/TauA family.


FUNCTION: Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LZTFL1 family.


FUNCTION: Required for the assembly of axonemal inner and outer dynein arms. Involved in preassembly of dyneins into complexes before their transport into cilia (By similarity). SUBCELLULAR LOCATION: Cytoplasm Dynein axonemal particle. SIMILARITY: Belongs to the DNAAF3 family.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS8 family.


FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus. SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Nucleus. Apical cell membrane. Note=Nuclear, in a punctate pattern. Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes.


FUNCTION: Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N- succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta- D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4- carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate (PubMed:15182182). Influences the affinity of glutamyl-- tRNA ligase for its substrates and increases its thermostability. SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.


FUNCTION: Involved in olefin biosynthesis. Catalyzes the reversible stereospecific NADPH-dependent reduction of 2-alkyl-3-oxoalkanoic acids to 2-alkyl-3-hydroxyalkanoic acids. In the oxidative direction, syn-2- decyl-3-hydroxytetradecanoic acid is the preferred substrate. In the reductive direction, (2R/S)-2-hexyl-3-ketodecanoic acid is accepted as substrate. SIMILARITY: Belongs to the 3-beta-HSD family.


FUNCTION: Catalyzes the carboxylation of oleanolic acid at the C-23 position to form gypsogenic acid. Involved in the hemolytic saponin biosynthetic pathway. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Component of the MIS complex, a complex that mediates N6- methyladenosine (m6A) methylation on some mRNAs during meiosis and is required for sporulation. In the complex, mediates the entry of the MIS complex in nucleolus, where methylation takes place. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Mediates localization of the MIS complex to the nucleolus during the period of m6A mRNA accumulation.


FUNCTION: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone. Active against both saturated and unsaturated long-chain fatty acyl-CoAs. Protects cells against lipotoxicity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.


FUNCTION: Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213). SIMILARITY: Belongs to the GST superfamily.


FUNCTION: Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54.


FUNCTION: Depressant insect beta-toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage- independently at site-4 of sodium channels (Nav) and block action potentials, primarily by depolarizing the axonal membrane and suppressing the sodium current. This depressant toxin is active only on insects. It is found in a relatively small amount in the venom. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.


FUNCTION: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for myristoyl-ACP. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the acyl-ACP thioesterase family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.


SIMILARITY: Belongs to the IIV-6 219L family.


FUNCTION: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space Lysosome Melanosome Note=While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. SIMILARITY: Belongs to the peptidase C26 family.


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


FUNCTION: Auxin transporter regulating intracellular auxin homeostasis and metabolism (PubMed:19506555, PubMed:20439545). Mediates the auxin transport from the cytosol into the lumen of the endoplasmic reticulum (PubMed:19506555). May also act as an auxin efflux carrier when located to the cell membrane (PubMed:24692422). PIN5 and PIN8 may have an antagonistic/compensatory activity (PubMed:22760640, PubMed:22990451). Involved in unfolded protein response (UPR) activation (PubMed:24180465). Involved in the control of vein patterning (PubMed:24304505). Promotes vein formation (PubMed:26560462). PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells (PubMed:26560462). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Along the root developmental zones, the localization gradually shifted from cell membrane localization in the meristematic epidermal cells to internal localization in the older elongating epidermal cells. Localizes to the cell membrane in the pavement and guard cells of the cotyledon and to internal compartments in the vascular tissues. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.


FUNCTION: Recruits the lipid transfer protein Vps13 to mitochondria thereby promoting vacuole-mitochondria contacts (PubMed:28864540, PubMed:30018089, PubMed:34830155). Involved in mitochondrial lipid homeostasis (PubMed:23781023, PubMed:28864540). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein.


FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria (By similarity). FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family.


FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex. SIMILARITY: Belongs to the CENP-O/MCM21 family.


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


FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin- dependent kinase cdk8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.


FUNCTION: Multifunctional cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24568283). Within the pathway, the multifunctional cytochrome P450 monooxygenase af510 acts as a 2,4,6- trichlorophenol monooxygenase that first performs the C-H hydroxylation at the bridgehead C5 position to yield 5R-hydroxyl-beta-trans- bergamotene (PubMed:24568283). Subsequently, a four electron oxidation initiated at C-9 coupled to cleavage of the cyclobutane C5-C8 bond of the bicyclo[3.1.1] core yields the epoxyketone intermediate 5-keto- cordycol (PubMed:24568283). An additional epoxidation reaction also catalyzed by af510 then furnishes the characteristic bisepoxide ketone 5-keto-demethoxyfumagillol (PubMed:24568283). The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans- bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto- fumagillol, which is then stereoselectively reduced by the keto- reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy- seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (PubMed:24568283) (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Has omega-amidase activity (PubMed:19596042, PubMed:28373563). The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively (PubMed:19596042). Can also hydrolyze gamma-monomethyl-alpha- ketoglutarate in vitro (PubMed:19596042). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family.


FUNCTION: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. MITRAC complexes regulate both translation of mitochondrial encoded components and assembly of nuclear-encoded components imported in mitochondrion. Required for efficient translation of MT-CO1 and mitochondrial respiratory chain complex IV assembly. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the COA3 family.


FUNCTION: Binds pheromones, the pheromones are released from the saliva of males and affect the sexual behavior of females. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. Part of the cryptic P4-like prophage CP4-57, it excises the prophage when overexpressed, which also requires integration host factor (encoded by ihfA and ihfB) (PubMed:7511583). Overexpression of AlpA leads to excision of the CP4-57 prophage, which inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans-translation (PubMed:7511582). SIMILARITY: Belongs to the 'phage' integrase family.


FUNCTION: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family.


FUNCTION: Catalyzes the sequential condensation of three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for the biosynthesis of terpenenoids. SIMILARITY: Belongs to the FPP/GGPP synthase family.


FUNCTION: Catalyzes the reversible phosphorolysis of sucrose 6(F)- phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6- phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, can also reversibly act on sucrose in vitro (PubMed:24599311). Is also able to catalyze transglycosylation reactions in vitro (PubMed:26074151). SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose phosphorylase subfamily.


FUNCTION: Glutamate-gated receptor that probably acts as non-selective cation channel (Probable). May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells (Probable). Could play a role in calcium unloading from the xylem vessels (PubMed:11158446). Acts as negative regulator of lateral root initiation and development (PubMed:23590882). May restrict primordia numbers and position along the root axis by a signaling process originating in the phloem (PubMed:23590882). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes to the plasma membrane. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family.


SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family.


FUNCTION: Transports dicarboxylates across the inner membranes of mitochondria by a counter-exchange mechanism. Can transport 2- oxoadipate (2-oxohexanedioate), 2-oxoglutarate, adipate (hexanedioate), glutarate, and to a lesser extent, pimelate (heptanedioate), 2- oxopimelate (2-oxoheptanedioate), 2-aminoadipate (2-aminohexanedioate), oxaloacetate, and citrate. Plays a central role in catabolism of lysine, hydroxylysine, and tryptophan, by transporting common metabolite intermediates (such as 2-oxoadipate) into the mitochondria, where it is converted into acetyl-CoA and can enter the citric acid (TCA) cycle. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down- regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12- signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion Note=Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.


FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PSMG2 family.


FUNCTION: Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family.


FUNCTION: RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by NOLA1/GAR1 to yield mature H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding with DKC1/NOLA4 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the cytoplasm and the nucleus. Absent from the nucleolus (By similarity). SIMILARITY: Belongs to the NAF1 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family.


FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15- hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4- dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Cytoplasm, perinuclear region Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. SIMILARITY: Belongs to the MAPEG family.


FUNCTION: Chaperone involved in tail fiber assembly and retraction. Acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. During phage assembly, twelve fibritin molecules attach to the phage neck via gp13: six molecules forming the collar and six molecules forming the whiskers. SUBCELLULAR LOCATION: Virion Note=Localizes to the neck.


FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post- fusion hairpin state. During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs at the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein may trigger p53-dependent apoptosis. FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. FUNCTION: [Fusion glycoprotein F2]: Major determinant of the species specificity of RSV infection. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein seems to trigger p53-dependent apoptosis. SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass membrane protein Note=Localized at the host apical membrane. SUBCELLULAR LOCATION: [Fusion glycoprotein F2]: Virion membrane Host cell membrane Note=Localized at the host apical membrane. SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.


FUNCTION: Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis. SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass type III membrane protein Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. SIMILARITY: Belongs to the gammacoronaviruses E protein family.


FUNCTION: Catalyzes the phosphorylation of L-fuculose. SIMILARITY: Belongs to the FGGY kinase family.


FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. SIMILARITY: Belongs to the NDK family.


FUNCTION: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scolopendra toxin 8 family.


FUNCTION: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Predominantly recruits 2 dyneins, which increases both the force and speed of the microtubule motor (PubMed:25035494, PubMed:33734450). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell (PubMed:32073997). FUNCTION: (Microbial infection) May serve as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Golgi apparatus Note=Enriched at the cis-face of the Golgi complex. Localizes to microtubule asters in prophase (PubMed:11238449). Localizes to the manchette in elongating spermatids (By similarity). SIMILARITY: Belongs to the hook family.


FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.


FUNCTION: Receptor for IL27. Requires IL6ST/GP130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1-type immune responses. Also appears to be involved in innate defense mechanisms. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily.


FUNCTION: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities (PubMed:22921072). In the first step, the non-reducing polyketide synthase azaA forms the hexaketide precursor from successive condensations of five malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (PubMed:22921072). The reactive polyketide chain then undergoes a PT- mediated C2-C7 cyclization to afford the aromatic ring and is eventually released as an aldehyde through the R-domain (PubMed:22921072). The putative ketoreductase azaE is proposed to catalyze the reduction of the terminal ketone resulting in the early culture product FK17-P2a (PubMed:22921072). The monooxygenase azaH was demonstrated to be the only enzyme required to convert FK17-P2a to azanigerone E (PubMed:22921072). AzaH first hydroxylates the benzaldehyde intermediate FK17-P2a at C4, which triggers the formation of the pyran-ring to afford azanigerone E (PubMed:22921072). In parallel, the 2,4-dimethylhexanoyl chain is synthesized by the HR-PKS azaB and is proposed to be transferred to the C4-hydroxyl of azanigerone E by the acyltransferase azaD directly from the ACP domain of azaB (PubMed:22921072). Alternatively, the 2,4-dimethyl-hexanoyl chain may be offloaded from the HR-PKS as a carboxylic acid and converted to an acyl-CoA by azaF (PubMed:22921072). The resulting acyl- CoA molecule could then be taken up as a substrate by AzaD to form azanigerone B (PubMed:22921072). To yield the carboxylic acid substituent in azanigerone A, the hydroxypropyl side chain of azanigerone B would need to undergo a C-C oxidative cleavage catalyzed by cytochrome P450 AzaI (PubMed:22921072). AzaI is proposed to act on a vicinal diol that leads to a C-C bond scission either through an alkoxyradical intermediate or a peroxy complex (PubMed:22921072). In the biosynthesis of azanigerone A, azanigerone B first undergoes hydroxylation at C10, possibly catalyzed by one of the two FAD- dependent monooxygenases encoded in the cluster, azaG or azaL, resulting in the vicinal diol azanigerone C (PubMed:22921072). Oxidative cleavage of azanigerone C by azaI would yield the corresponding aldehyde derivative of azanigerone A (PubMed:22921072). Finally, the dehydrogenase azaJ is proposed to convert the aldehyde functional group into the carboxylic acid, completing the conversion from azanigerone B to azanigerone A (PubMed:22921072). Alternatively, the oxidation of aldehyde to carboxylic acid may be catalyzed by the same P450 enzyme azaI via consecutive oxidation or by endogenous alcohol dehydrogenase (PubMed:22921072). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions (By similarity). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Presumably involved in regulating the intracellular acetyl- CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.


FUNCTION: Methyltransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (PubMed:28529508). The first step of the pathway is the synthesis of 3,5- dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (By similarity). DMAO is then converted to farnesyl- DMAO by the prenyltransferase adrG (By similarity). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (By similarity). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (By similarity). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily.


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


FUNCTION: Catalyzes the conversion of L-ornithine into L-proline with release of ammonia. Is likely involved in the L-ornithine degradation pathway that allows P.putida to utilize this compound as sole carbon and nitrogen source. SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin family.


FUNCTION: Shows weak esterase activity with the p-nitrophenol-linked aliphatic ester pNP-butyrate. Does not exhibit cutinase activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family.


FUNCTION: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CidA/LrgA family. CidA subfamily.


FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N- acetylserotonin, the penultimate step in the synthesis of melatonin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily.


FUNCTION: Has apoptosis-inducing activity. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins (By similarity). Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre- mRNAs (By similarity). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (By similarity). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (By similarity). Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Cytoplasm, cytoskeleton Note=A small fraction is also associated with the cytoskeleton. SIMILARITY: Belongs to the pICln (TC 1.A.47) family.


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


FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.


FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein Note=Trans cisternae of Golgi stack. SIMILARITY: Belongs to the glycosyltransferase 7 family.


FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the enhancer of polycomb family.


FUNCTION: Plays a role as an effector of the ADP-ribosylation factor- like protein 2, ARL2. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, cilium basal body Note=Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). SIMILARITY: Belongs to the ARL2BP family.


FUNCTION: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.


FUNCTION: Involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria (PubMed:30606802). Specifically methylates the 1-OH position of 3,3'-di-O-methyl-4alpha-mannobiose, a probable early precursor of MMP, yielding the reducing end dimannoside of MMP (PubMed:30606802). SIMILARITY: Belongs to the methyltransferase superfamily.


FUNCTION: Part of the ABC transporter complex AraFGH involved in arabinose import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Arabinose importer (TC 3.A.1.2.2) family.


FUNCTION: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels. May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases. FUNCTION: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels (PubMed:28398555). May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases (By similarity). FUNCTION: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels (By similarity). May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases (PubMed:15336960). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Association with membranes is calcium-dependent (PubMed:8360179, PubMed:1543495). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Association with membranes is calcium-dependent (By similarity). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Association with membranes is calcium-dependent (By similarity). Enriched in the perinuclear region, probably at the trans Golgi network in response to calcium (PubMed:28398555). SIMILARITY: Belongs to the recoverin family.


SIMILARITY: Belongs to the recoverin family.


FUNCTION: Involved in storage lipid mobilization during the growth of higher plant seedling. SUBCELLULAR LOCATION: Glyoxysome. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.


FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily.


FUNCTION: Catalyzes the addition of a mannose residue from GDP-D- mannose to GlcAGroAc2 to generate 1,2-di-O-C16/C18:1-(alpha-D- mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic acid)-(1-3)- glycerol(ManGlcAGroAc2). SIMILARITY: Belongs to the glycosyltransferase group 1 family.


FUNCTION: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity). In airway epithelial cells, binding of denatonium increases the intracellular calcium ion concentration and stimulates ciliary beat frequency (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell projection, cilium membrane. Note=In airway epithelial cells, localizes to motile cilia. SIMILARITY: Belongs to the G-protein coupled receptor T2R family.


FUNCTION: Global transcriptional regulator that plays a key role in stress response and exerts either positive or negative regulation of genes. Acts by interacting with the C-terminal domain of the alpha subunit of the RNA polymerase (RNAP). This interaction can enhance binding of RNAP to the promoter region of target genes and stimulate their transcription, or block interaction of RNAP with activator. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ArsC family. Spx subfamily.


FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1 and CXCL8. SUBCELLULAR LOCATION: Secreted.


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). 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 T1A family.


SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf15 family.


FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. SIMILARITY: Belongs to the CobB/CbiA family.


FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity). FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EF-Ts family. SIMILARITY: Belongs to the EF-Ts family.


FUNCTION: SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light. FUNCTION: SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light (By similarity). SIMILARITY: Belongs to the alpha/beta-type SASP family.


FUNCTION: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MdcC family.


FUNCTION: Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the amphiregulin family.


FUNCTION: May form complexes with phosphorylated ligands by interfering with kinases and their effectors. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family.


FUNCTION: Monoheme cytochrome that function as the electron transport subunit of sulfide dehydrogenase. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: Involved in one of the last steps of the biosynthesis of chlorophyll a. Catalyzes the esterification of chlorophillide a or b with a preference for geranylgeranyldiphosphate (GGPP) rather than for phytyldiphosphate (PhyPP). SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. Chlorophyll synthase subfamily.


FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks neuronal alpha-3-beta-2/CHRNA3-CHRNB2 (human and rat), alpha-7/CHRNA7 (human and rat), and alpha-3-beta-4/CHRNA3-CHRNB4 (human) nAChRs (PubMed:8206995, PubMed:15609996, PubMed:19131337). Acts voltage-independently (PubMed:15609996). Competes with alpha- bungarotoxin for binding to the receptor (PubMed:12384509, PubMed:15609996). Binds to a different site than alpha-conotoxin ImII (PubMed:15609996). Is highly active against the neuromuscular receptor in frog (PubMed:8206995). Also exhibits inhibition of D.melanogaster alpha-7 nAChRs (PubMed:25466886). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily.


FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaD is not essential for flagellar synthesis and motility. FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaD is not essential for flagellar synthesis and motility (By similarity). SUBCELLULAR LOCATION: Secreted Bacterial flagellum. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the bacterial flagellin family.


FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'- nitrosonornicotine (NNN) (Ref.3, PubMed:17102129, PubMed:16192354). Catalyzes the demethylation of nicotine to form nornicotine (Ref.3, PubMed:17102129, PubMed:16192354). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family. CYP82E2 subfamily.


FUNCTION: Probably involved in DNA replication. Binds the origin of replication (ori) (By similarity). SIMILARITY: Belongs to the herpesviridae OriBP family.


FUNCTION: Has reversible, light-dependent DNA-binding activity. Upon illumination an internal FMN-protein adduct is formed which changes the protein conformation so that the previously sequestered DNA-binding domain is free to bind DNA. Binds to sequences within in its own promoter when illuminated but not when it has been incubated in the dark.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the complex I NDUFA4 subunit family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.


FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20 (H4K20me3) which represents a specific tag for epigenetic transcriptional repression. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily.


FUNCTION: Chitin-binding protein which functions in defense against chitin-containing fungal pathogens.


FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 4 family.


FUNCTION: Snake venom phospholipase A2 (PLA2) that has enzymatic activity but is non-toxic. Displays low binding affinity and enzymatic activity on phosphatidylserine-containing vesicles and HEK-293 plasma membranes, in contrast to ammodytoxins that have high activity on these phospholipids. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. MdtH (TC 2.A.1.2.21) subfamily.


FUNCTION: Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling. In response to cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+) refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)- dependent SOCE activity: possibly act by facilitating the deoligomerization of STIM to efficiently turn off ORAI when the endoplasmic reticulum lumen is filled with the appropriate Ca(2+) levels, and thus preventing the overload of the cell with excessive Ca(2+) ions. SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=Translocates to the endoplasmic reticulum-plasma membrane (ER-PM) region in a STIM1-dependent manner following cytosolic Ca(2+) elevation. SIMILARITY: Belongs to the SARAF family.


FUNCTION: Regulates focal adhesion turnover resulting in changes in focal adhesion size, cell adhesion and cell spreading, potentially via transcriptional modulation of beta-integrins (By similarity). Required to maintain gingival epithelial barrier function (By similarity). Required for cardiac sodium current propagation and electrical synchrony in cardiac myocytes (By similarity). Required for the formation of desmosome cell junctions in cardiomyocytes, thereby required for the correct formation of the heart, specifically trabeculation and formation of the atria walls (PubMed:15479741). Loss of desmosome cell junctions leads to mis-localization of DSP and DSG2 resulting in disruption of cell-cell adhesion and disordered intermediate filaments (PubMed:15479741). Modulates profibrotic gene expression in cardiomyocytes via regulation of DSP expression and subsequent activation of downstream TGFB1 and MAPK14/p38 MAPK signaling (By similarity). May play a role in junctional plaques (By similarity). SUBCELLULAR LOCATION: Nucleus Cell junction, desmosome Cell junction Cytoplasm Note=Colocalizes with CTNNA3 and SCN5A/Nav1.5 at intercalated disks in the heart. SIMILARITY: Belongs to the beta-catenin family.


FUNCTION: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere- associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the CENP-U/AME1 family.


FUNCTION: Hydroxymethylglutaryl-CoA synthase-like protein; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype (PubMed:24611558). AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) (PubMed:22846083). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment (PubMed:22846083). The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8- hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety (PubMed:10432635, PubMed:10975654, PubMed:22846083). Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes (PubMed:20348386). The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated (PubMed:10432635, PubMed:10975654, PubMed:22846083). The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK- toxin, probably via the catalysis of a side reaction of EDA or its precursor (PubMed:24611558). SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family.


SUBCELLULAR LOCATION: Lipid droplet Membrane; Multi-pass membrane protein Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. SIMILARITY: Belongs to the oleosin family.


FUNCTION: Macronuclear replacement variant which replaces conventional H3 in a subset of nucleosomes. 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. Functions redundantly to H3.4. H3.3 deposition into chromatin is mainly transcription-associated and DNA replication- independent, but it can also enter a replication-coupled pathway. Although not essential for vegetative growth, minor H3 variants are required for producing viable conjugation progeny by affecting late developmental stages of conjugation (By similarity). SUBCELLULAR LOCATION: Nucleus. Chromosome Note=Localizes mainly to the large, transcriptionally active, somatic macronucleus (MAC) and only faintly to the small, transcriptionally inert, germ line micronucleus (MIC). SIMILARITY: Belongs to the histone H3 family.


FUNCTION: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily.


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 PetN family.


FUNCTION: Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity (PubMed:15496142, PubMed:19826488, PubMed:19420222, PubMed:20145209, PubMed:27708256, PubMed:25489052, PubMed:29754825, PubMed:20154145, PubMed:32042062). Acetylates amino termini that are devoid of initiator methionine (PubMed:19420222). The alpha (N-terminal) acetyltransferase activity may be important for vascular, hematopoietic and neuronal growth and development. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation (PubMed:12464182). Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration (PubMed:19826488). Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and suppressing cancer development (PubMed:20145209). Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to preferential binding to co-chaperone HOPX (PubMed:27708256). Acetylates HIST1H4A (PubMed:29754825). Acts as a negative regulator of sister chromatid cohesion during mitosis (PubMed:27422821). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Also present in the free cytosolic and cytoskeleton-bound polysomes. SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.


SIMILARITY: To A.aeolicus AQ_423.


FUNCTION: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18. SUBCELLULAR LOCATION: Virion Host nucleus Note=Present in about 10 copies per virion. SIMILARITY: Belongs to the peptidase C5 family.


FUNCTION: Sialidase is able to release sialic acid from a wide variety of natural substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 33 family.


FUNCTION: Could function in transport of proteins into the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion outer membrane. SIMILARITY: Belongs to the metaxin family.


FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Membrane; Peripheral membrane protein; Cytoplasmic side Perikaryon Cell projection, dendrite Nucleus Note=Detected in Purkinje cell soma and dendrites. Associated with Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected in the nucleus after heterologous expression. Recruited to the cell membrane in the presence of GNAO1.


FUNCTION: Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the lipid A palmitoyltransferase family.


FUNCTION: During the asexual blood stage, plays an essential role in the export of several proteins into the host erythrocytes by cleaving the pentameric localization motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located downstream of the N-terminal secretory signal sequence (PubMed:24983235). Specifically, cleaves after the leucine residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins including EMP1 (By similarity). Also, by regulating protein export, plays an essential role in gametocyte development and thus parasite transmission to the mosquito vector (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase A1 family.


FUNCTION: May function as a transcriptional regulator that controls feoABC expression. FUNCTION: May function as a transcriptional regulator that controls feoABC expression. SIMILARITY: Belongs to the FeoC family. SIMILARITY: Belongs to the FeoC family.


FUNCTION: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). This subunit forms the outer membrane channel (By similarity). SUBCELLULAR LOCATION: Cell outer membrane Note=Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane. SIMILARITY: Belongs to the bacterial secretin family. GSP D subfamily.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the CarA family.


FUNCTION: Possesses kinase activity in vitro. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the OS-9 family.


FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly nuclear.


FUNCTION: Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5- trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone. SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.


FUNCTION: Probable flavin reductase in the luminescent systems of different marine bacteria. SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family.


FUNCTION: Plays a role in regulating magnetite crystal size; partially redundant function with MamF. SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the magnetosome MamF/MmsF protein family.


FUNCTION: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore.


FUNCTION: Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family.


FUNCTION: Involved in protein export. Participates in an early event of protein translocation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecG family.


FUNCTION: May be involved in regulation of NF-kappa-B signaling. May be involved in copper-dependent atp7a trafficking between the trans-Golgi network and vesicles in the cell periphery (By similarity). SUBCELLULAR LOCATION: Endosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the CCDC22 family.


FUNCTION: Involved in the replication of mitochondrial DNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the DNA polymerase type-A family.


FUNCTION: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the small GTPase superfamily. Rho family.


SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.


FUNCTION: Involved in sporulation and affects the sphingolipid composition of the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Concentrates within cortical patches at the membrane. SIMILARITY: Belongs to the SUR7 family.


FUNCTION: Involved in the biosynthetic pathway of cholesterol. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.


FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 35 (Jztx-27) subfamily.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cL38 family.


FUNCTION: SNARE promoting fusion of transport vesicles with target membranes. Together with SNARE STX6, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting. SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane protein Golgi apparatus membrane; Single-pass type IV membrane protein Endomembrane system; Single-pass type IV membrane protein; Cytoplasmic side Early endosome membrane; Single-pass type IV membrane protein Recycling endosome membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family.


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


SIMILARITY: Belongs to the UPF0736 family.


FUNCTION: Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A, regardless of whether the CoA is presented in the free thiol form or as an acetyl thioester, to a serine residue of a broad range of acceptors including the acyl carrier domain of FASN. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.


FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3- phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase. SIMILARITY: Belongs to the RuBisCO large chain family. Type III subfamily.


FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons (PubMed:26641313). Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine (PubMed:26641313). MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal (PubMed:26641313). The catalytic subunit MsrP is non- stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide (PubMed:26641313). Can catalyze the reduction of a variety of substrates in vitro, including dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide (PubMed:15355966). Cannot reduce cyclic N-oxides (PubMed:15355966). Shows no activity as sulfite oxidase (PubMed:15355966). SUBCELLULAR LOCATION: Periplasm Note=Is attached to the inner membrane when interacting with the MsrQ subunit. SIMILARITY: Belongs to the MsrP family.


FUNCTION: cCF10 is involved in the conjugative transfer of the hemolysin plasmid pCF10.


FUNCTION: Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. FUNCTION: This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy. SUBCELLULAR LOCATION: Host membrane. SIMILARITY: Belongs to the channel forming colicin family.


FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including sclareol, a diterpene-diol that is used as fragrance and flavoring, and has anticancer effects (able to kill leukemic and colon cancer cells by apoptosis) (Probable). Sclareol can also be used as synthesis precursor of ambergris substitution fragance products such as ambrox (Probable). Terpene synthase that produces 8-hydroxycopalyl diphosphate from geranylgeranyl diphosphate (GGPP) (PubMed:23113661, PubMed:22959531). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family.


FUNCTION: Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division (By similarity). SIMILARITY: Belongs to the NPR3 family.


FUNCTION: Stimulates insulin release. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Tryptophillin subfamily.


FUNCTION: Probably implicated in the export process of the lantibiotic nisin. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Nisin exporter (TC 3.A.1.111.3) family.


FUNCTION: Has antibacterial activity against the Gram-positive bacterium S.aureus 1056 MRSA (MIC=1.25 ug/ml) and the Gram-negative bacterium E.coli O157:H7 (MIC=0.96 ug/ml). Has antifungal activity against the yeast C.albicans 3153A (MIC=6.20 ug/ml). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium- iron protein.


FUNCTION: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing. Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules. Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10. Also involved in the alternative splicing of several genes including TJP1. Binds the pre- mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs (By similarity). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RRM RBM47 family.


FUNCTION: Fallaxidin-2.1 shows no antibacterial activity against Gram- positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction. FUNCTION: Fallaxidin-3.2 shows antibacterial activity against the Gram- positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=500 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram- negative bacteria E.cloacae and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.


FUNCTION: Serine/threonine kinase that may play a role in mediating the growth-factor and stress induced activation of the transcription factor CREB. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AMY1 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-4 integral membrane protein family.


FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cell projection, cilium Note=Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. SIMILARITY: Belongs to the TBCC family.


FUNCTION: Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for phototropic responses. Regulates a wide range of physiological activities in plants that maximize the efficiency of photosynthesis, such as chloroplast relocations, stomata opening, and leaf expansion (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Probable component of primosome involved in the initiation of DNA replication.


FUNCTION: Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre- rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre- ribosomal RNA by the RNA exosome. Positively regulates dimethylation of two adjacent adenosines in the loop of a conserved hairpin near the 3'- end of 18S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the PNO1 family.


FUNCTION: Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ9 subfamily.


FUNCTION: Involved in the biogenesis of the plastid translation machinery by promoting the splicing of group II introns in chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. P subfamily.


FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues (PubMed:16468985). In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins (PubMed:17082771). One function of the proteasome is to contribute to M.tuberculosis ability to resist killing by host macrophages, since the core proteasome is essential for persistence of the pathogen during the chronic phase of infection in mice (PubMed:18059281). Likely functions to recycle amino acids under nutrient starvation, thereby enabling the cell to maintain basal metabolic activities (PubMed:20711362) (By similarity). The mechanism of protection against bactericidal chemistries of the host's immune response probably involves the degradation of proteins that are irreversibly oxidized, nitrated, or nitrosated. A proteolysis- independent activity of the proteasome core is required for optimal growth of M.tuberculosis in mouse lungs and for RNI resistance; in contrast, long-term survival of M.tuberculosis in stationary phase and during starvation in vitro and in the chronic phase of mouse infection required a proteolytically active proteasome (PubMed:20711362). FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1B family.


FUNCTION: Involved in uptake of biotin and desthiobiotin with the concomitant entry of protons. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Allantoate permease family.